IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Poly(A) nuclease interacts with the C-terminal domain of polyadenylate-binding protein domain from poly(A)-binding protein. Poly(A) nuclease interacts with the C-terminal domain of polyadenylate-binding protein domain from poly(A)-binding protein. J. Biol. Chem. (0021-9258) 2007 imex curation Siddiqui N., Mangus D.A., Chang T.C., Palermino J.M., Shyu A.B., Gehring K. kalle.gehring@mcgill.ca 13-Jan-2014: Contacted by IntAct-Help. Only protein-protein interactions baker's yeast-l40 Saccharomyces cerevisiae l40 l40 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Siddiqui N., Mangus D.A., Chang T.C., Palermino J.M., Shyu A.B., Gehring K. kalle.gehring@mcgill.ca Accepted 2013-NOV-29 by PPORRAS J. Biol. Chem. (0021-9258) 2007 Only protein-protein interactions imex curation Poly(A) nuclease interacts with the C-terminal domain of polyadenylate-binding protein domain from poly(A)-binding protein. Poly(A) nuclease interacts with the C-terminal domain of polyadenylate-binding protein domain from poly(A)-binding protein. J. Biol. Chem. (0021-9258) 2007 imex curation Siddiqui N., Mangus D.A., Chang T.C., Palermino J.M., Shyu A.B., Gehring K. kalle.gehring@mcgill.ca 13-Jan-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Siddiqui N., Mangus D.A., Chang T.C., Palermino J.M., Shyu A.B., Gehring K. Protein sample preparations for the PABC domains from yeast and human PABP are described in PMID:11940585 and PMID:11287632, respectively. kalle.gehring@mcgill.ca Accepted 2013-NOV-29 by PPORRAS J. Biol. Chem. (0021-9258) 2007 Only protein-protein interactions imex curation Poly(A) nuclease interacts with the C-terminal domain of polyadenylate-binding protein domain from poly(A)-binding protein. Poly(A) nuclease interacts with the C-terminal domain of polyadenylate-binding protein domain from poly(A)-binding protein. J. Biol. Chem. (0021-9258) 2007 imex curation Siddiqui N., Mangus D.A., Chang T.C., Palermino J.M., Shyu A.B., Gehring K. kalle.gehring@mcgill.ca 13-Jan-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro pull down pull down autoradiography autoradiography Siddiqui N., Mangus D.A., Chang T.C., Palermino J.M., Shyu A.B., Gehring K. kalle.gehring@mcgill.ca Accepted 2013-NOV-29 by PPORRAS J. Biol. Chem. (0021-9258) 2007 Only protein-protein interactions imex curation Poly(A) nuclease interacts with the C-terminal domain of polyadenylate-binding protein domain from poly(A)-binding protein. Poly(A) nuclease interacts with the C-terminal domain of polyadenylate-binding protein domain from poly(A)-binding protein. J. Biol. Chem. (0021-9258) 2007 imex curation Siddiqui N., Mangus D.A., Chang T.C., Palermino J.M., Shyu A.B., Gehring K. kalle.gehring@mcgill.ca 13-Jan-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Siddiqui N., Mangus D.A., Chang T.C., Palermino J.M., Shyu A.B., Gehring K. Protein sample preparation for the PABC domain from yeast PABP is described in PMID:11940585. kalle.gehring@mcgill.ca Accepted 2013-NOV-29 by PPORRAS J. Biol. Chem. (0021-9258) 2007 Only protein-protein interactions imex curation pan3_yeast PAN2-PAN3 deadenylation complex subunit PAN3 PAN3 ECM35 PAB1P-dependent poly(A)-specific ribonuclease Poly(A)-nuclease deadenylation complex subunit 3 YKL025C protein protein yeast Saccharomyces cerevisiae Baker's yeast MDKINPDWAKDIPCRNITIYGYCKKEKEGCPFKHSDNTTATTINDVPPPIDVGEATTPTMTSVPKFNAKVSASFTPMTVGSDSLTTVTNTTSAATNATGNIAMAATSATASTVNPMINPIVNSSLVNNNNNNSNISISIPTTASSSNYDPFNAPIFTPSSTSSIHTNANAHSFPFPSIANSGGININATDDNSNNMSMANNVPPPMQPPPIESSNLKYPRIYPPPHSLLQYHLYAPEQPSSLKSLLKPNERSADQLFIPNNIREDLTKKNLSILQVFPSSGKVIPSIVQDYFNLVPLNFNNNDFLNKTTLFKVFSNYDGKAYVLKRLPNIDKSMNPNKISKIYQIWSKINCTNLIKFRDIFQTTKFGDLSICLVFDYYPNSLSLYDYHFVNFPKFPITNNYLWIYLVQLTNVINSIHSQNLSIGNTLNWRKVLITGDPGRIKLSHCNFMDLLFNDDTDTVVSSGGSTIEGQQQLDYKYLGELLFNLSINIENSNNNTAPKEYRLEEITPQSIDDMRQIDDKFKDVLKYLISDNGDSKKSIHDLTSHFYDKMFMVLESSQTYTEYMESVLSRELENGRLFRLVNKLNCIFGRIESRIDINWSESGTKFPIILFYDYVFHQVDSNGKPIMDLTHVLRCLNKLDAGIQEKLMLVTPDELNCIIISYKELKDLIESTFRSITQ DE03E15BF4A5DA7C DE03E15BF4A5DA7C parn_human Poly(A)-specific ribonuclease PARN PARN Polyadenylate-specific ribonuclease Deadenylating nuclease Deadenylation nuclease DAN protein protein human Homo sapiens Human MEIIRSNFKSNLHKVYQAIEEADFFAIDGEFSGISDGPSVSALTNGFDTPEERYQKLKKHSMDFLLFQFGLCTFKYDYTDSKYITKSFNFYVFPKPFNRSSPDVKFVCQSSSIDFLASQGFDFNKVFRNGIPYLNQEEERQLREQYDEKRSQANGAGALSYVSPNTSKCPVTIPEDQKKFIDQVVEKIEDLLQSEENKNLDLEPCTGFQRKLIYQTLSWKYPKGIHVETLETEKKERYIVISKVDEEERKRREQQKHAKEQEELNDAVGFSRVIHAIANSGKLVIGHNMLLDVMHTVHQFYCPLPADLSEFKEMTTCVFPRLLDTKLMASTQPFKDIINNTSLAELEKRLKETPFNPPKVESAEGFPSYDTASEQLHEAGYDAYITGLCFISMANYLGSFLSPPKIHVSARSKLIEPFFNKLFLMRVMDIPYLNLEGPDLQPKRDHVLHVTFPKEWKTSDLYQLFSAFGNIQISWIDDTSAFVSLSQPEQVKIAVNTSKYAESYRIQTYAEYMGRKQEEKQIKRKWTEDSWKEADSKRLNPQCIPYTLQNHYYRNNSFTAPSTVGKRNLSPSQEEAGLEDGVSGEISDTELEQTDSCAEPLSEGRKKAKKLKRMKKELSPAGSISKNSPATLFEVPDTW DIP protein O95453 original sequence version: 106 DIP protein O95453 original sequence version: 99 6994BE39384DF7AC pabp1_human Polyadenylate-binding protein 1 PABPC1 PAB1 PABP1 PABPC2 PABP protein protein human Homo sapiens Human MNPSAPSYPMASLYVGDLHPDVTEAMLYEKFSPAGPILSIRVCRDMITRRSLGYAYVNFQQPADAERALDTMNFDVIKGKPVRIMWSQRDPSLRKSGVGNIFIKNLDKSIDNKALYDTFSAFGNILSCKVVCDENGSKGYGFVHFETQEAAERAIEKMNGMLLNDRKVFVGRFKSRKEREAELGARAKEFTNVYIKNFGEDMDDERLKDLFGKFGPALSVKVMTDESGKSKGFGFVSFERHEDAQKAVDEMNGKELNGKQIYVGRAQKKVERQTELKRKFEQMKQDRITRYQGVNLYVKNLDDGIDDERLRKEFSPFGTITSAKVMMEGGRSKGFGFVCFSSPEEATKAVTEMNGRIVATKPLYVALAQRKEERQAHLTNQYMQRMASVRAVPNPVINPYQPAPPSGYFMAAIPQTQNRAAYYPPSQIAQLRPSPRWTAQGARPHPFQNMPGAIRPAAPRPPFSTMRPASSQVPRVMSTQRVANTSTQTMGPRPAAAAAAATPAVRTVPQYKYAAGVRNPQQHLNAQPQVTMQQPAVHVQGQEPLTASMLASAPPQEQKQMLGERLFPLIQAMHPTLAGKITGMLLEIDNSELLHMLESPESLRSKVDEAVAVLQAHQAKEAAQKAVNSATGVPTV DIP protein P11940 original sequence version: 187 DIP protein P11940 original sequence version: 181 DIP protein P11940-1 original sequence version: 136 DIP protein P11940 original sequence version: 148 DIP protein P11940 original sequence version: 172 2EB1B02A346132EE pabp_yeast Polyadenylate-binding protein, cytoplasmic and nuclear PAB1 ARS consensus-binding protein ACBP-67 Polyadenylate tail-binding protein YER165W protein protein yeast Saccharomyces cerevisiae Baker's yeast MADITDKTAEQLENLNIQDDQKQAATGSESQSVENSSASLYVGDLEPSVSEAHLYDIFSPIGSVSSIRVCRDAITKTSLGYAYVNFNDHEAGRKAIEQLNYTPIKGRLCRIMWSQRDPSLRKKGSGNIFIKNLHPDIDNKALYDTFSVFGDILSSKIATDENGKSKGFGFVHFEEEGAAKEAIDALNGMLLNGQEIYVAPHLSRKERDSQLEETKAHYTNLYVKNINSETTDEQFQELFAKFGPIVSASLEKDADGKLKGFGFVNYEKHEDAVKAVEALNDSELNGEKLYVGRAQKKNERMHVLKKQYEAYRLEKMAKYQGVNLFVKNLDDSVDDEKLEEEFAPYGTITSAKVMRTENGKSKGFGFVCFSTPEEATKAITEKNQQIVAGKPLYVAIAQRKDVRRSQLAQQIQARNQMRYQQATAAAAAAAAGMPGQFMPPMFYGVMPPRGVPFNGPNPQQMNPMGGMPKNGMPPQFRNGPVYGVPPQGGFPRNANDNNQFYQQKQRQALGEQLYKKVSAKTSNEEAAGKITGMILDLPPQEVFPLLESDELFEQHYKEASAAYESFKKEQEQQTEQA 4F97E494753E17C7 4F97E494753E17C7 pan3_human PAN2-PAN3 deadenylation complex subunit PAN3 PAN3 PAB1P-dependent poly(A)-specific ribonuclease Poly(A)-nuclease deadenylation complex subunit 3 protein protein human Homo sapiens Human MNSGGGLPPPSAAASPSSSSLAAAVAVVAPPGVGGVPGGAAVGVKLKYCRYYAKDKTCFYGEECQFLHEDPAAGAAPGLGLHSNSVPLALAGAPVAGFPPGAVAGGGAGPPPGPKKPDLGDPGTGAAAGGGGSSGGLDGPRLAIPGMDGGALTDTSLTDSYFSTSFIGVNGFGSPVETKYPLMQRMTNSSSSPSLLNDSAKPYSAHDPLTSPASSLFNDFGALNISQRRKPRKYRLGMLEERLVPMGSKARKAKNPIGCLADRCKSGVPINMVWWNRVTENNLQTPNPTASEFIPKGGSTSRLSNVSQSNMSAFSQVFSHPSMGSPATAGLAPGMSLSAGSSPLHSPKITPHTSPAPRRRSHTPNPASYMVPSSASTSVNNPVSQTPSSGQVIQKETVGGTTYFYTDTTPAPLTGMVFPNYHIYPPTAPHVAYMQPKANAPSFFMADELRQELINRHLITMAQIDQADMPAVPTEVDSYHSLFPLEPLPPPNRIQKSSNFGYITSCYKAVNSKDDLPYCLRRIHGFRLVNTKCMVLVDMWKKIQHSNIVTLREVFTTKAFAEPSLVFAYDFHAGGETMMSRHFNDPNADAYFTKRKWGQHEGPLPRQHAGLLPESLIWAYIVQLSSALRTIHTAGLACRVMDPTKILITGKTRLRVNCVGVFDVLTFDNSQNNNPLALMAQYQQADLISLGKVVLALACNSLAGIQRENLQKAMELVTINYSSDLKNLILYLLTDQNRMRSVNDIMPMIGARFYTQLDAAQMRNDVIEEDLAKEVQNGRLFRLLAKLGTINERPEFQKDPTWSETGDRYLLKLFRDHLFHQVTEAGAPWIDLSHIISCLNKLDAGVPEKISLISRDEKSVLVVTYSDLKRCFENTFQELIAAANGQL DIP protein Q58A45 original sequence version: 90 4883F859D2A642D2 pabpc1-pan3 3 9 unspecified role unspecified role prey prey region 35s radiolabel 35s radiolabel 35S s35 radiolabelled S35 s35 radiolabelled 35S S35 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Q58A45:p.Phe293Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain F A Wed May 02 19:14:03 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe293ala' Tue Jun 30 19:34:11 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe293Ala' in vitro In vitro 7 unspecified role unspecified role bait bait region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined pabp_hyd domain sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecobb Escherichia coli (strain B / BL21) physical association physical association Fig. 4a pabpc1-parn 3 7 unspecified role unspecified role bait bait region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined region required to bind necessary binding region required to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecobb Escherichia coli (strain B / BL21) 6 unspecified role unspecified role prey prey region 35s radiolabel 35s radiolabel 35S s35 radiolabelled S35 s35 radiolabelled 35S S35 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined in vitro In vitro physical association physical association Fig. 4b pabpc1-pan3-1 4 7 unspecified role unspecified role neutral component neutral component pabp_hyd domain sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecobb Escherichia coli (strain B / BL21) 9 unspecified role unspecified role neutral component neutral component lig_pam2_1 motif sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain chemical synthesis Chemical synthesis (Chemical synthesis) 27 25 direct interaction direct interaction Fig. 2a Temp = 15C pabpc1-pan3-2 2 7 unspecified role unspecified role neutral component neutral component region 15n label 15n label 15N N15 15N N15 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined pabp_hyd domain sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 9 unspecified role unspecified role neutral component neutral component lig_pam2_1 motif sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain chemical synthesis Chemical synthesis (Chemical synthesis) 31 33 direct interaction direct interaction Fig. 2b, Fig. 3a pab1-pan3 4 8 unspecified role unspecified role neutral component neutral component pabp_hyd domain sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecobd Escherichia coli (strain B / BL21-DE3) 5 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain chemical synthesis Chemical synthesis (Chemical synthesis) 36 38 direct interaction direct interaction Fig 5a Temp = 15C pab1-pan3-1 2 5 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain chemical synthesis Chemical synthesis (Chemical synthesis) 8 unspecified role unspecified role neutral component neutral component pabp_hyd domain sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain region 15n label 15n label 15N N15 15N N15 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecobd Escherichia coli (strain B / BL21-DE3) 41 43 direct interaction direct interaction Fig. 3b, Fig. 5b pab1-pan3-2 2 8 unspecified role unspecified role neutral component neutral component pabp_hyd domain sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecobd Escherichia coli (strain B / BL21-DE3) 5 unspecified role unspecified role neutral component neutral component region 15n label 15n label 15N N15 15N N15 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecobd Escherichia coli (strain B / BL21-DE3) 47 50 direct interaction direct interaction Fig 6 pab1-pan3-3 1 8 unspecified role unspecified role bait bait pabp_hyd domain sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain 5 unspecified role unspecified role prey prey P36102:p.Phe151Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain F A Wed May 02 14:24:37 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe151ala' Tue Jun 30 17:14:44 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe151Ala' P36102:p.Asn152Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain N A Wed May 02 15:55:50 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asn152ala' Tue Jun 30 16:53:11 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asn152Ala' P36102:p.Phe156Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain F A Wed May 02 15:22:20 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe156ala' Tue Jun 30 17:06:06 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe156Ala' P36102:p.[Phe151Ala;Phe156Ala] mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain F A certain certain sequence position certain certain certain sequence position certain F A Wed May 02 16:40:07 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe151ala,phe156ala' Tue Jun 30 20:02:45 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Phe151Ala;Phe156Ala]' physical association physical association Fig. 7a pab1-pan3-4 4 5 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecobd Escherichia coli (strain B / BL21-DE3) 8 unspecified role unspecified role neutral component neutral component pabp_hyd domain sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecobd Escherichia coli (strain B / BL21-DE3) 63 61 direct interaction direct interaction Fig. 5a Temp = 15C