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/ Distinct functional domains in nesprin-1alpha and nesprin-2beta bind directly to emerin and both interactions are disrupted in X-linked Emery-Dreifuss muscular dystrophy. Distinct functional domains in nesprin-1alpha and nesprin-2beta bind directly to emerin and both interactions are disrupted in X-linked Emery-Dreifuss muscular dystrophy. Experimental cell research 2007 imex curation Wheeler MA., Davies JD., Zhang Q., Emerson LJ., Hunt J., Shanahan CM., Ellis JA. Cardiac - Interactions involving cardiac related proteins Dear checker -please check the identifiers below - as the names of the protein isoforms given in this publication do not correspond to the UniProt names, and while I repeated the Blasts of protein sequences from GRCh37 assembly more than once, the results differed on occasion.... Ensembl identifiers were located from the GRCh37 assembly. ENST00000313630: Q8NF91-3 (called Nesprin 1-alpha here). ENST00000312125:Q8WXH0-3 (called Nesprin 2-beta here) ENSP00000345521:Q8WXH0-5 (called Nesprin 2-alpha here) juliet.ellis@kcl.ac.uk Only protein-protein interactions imex curation in vitro In vitro pull down pull down weight autoradiogra molecular weight estimation by autoradiography weight autoradiogra Wheeler MA., Davies JD., Zhang Q., Emerson LJ., Hunt J., Shanahan CM., Ellis JA. Cardiac - Interactions involving cardiac related proteins The 1–169(208) mutation has a two nucleotide deletion (CT of Proline 169, CCT codon sequence) which results in a frameshift, with a new C-terminal protein sequence and premature truncation of the protein. The sequence of the mutation from Patient LB1520 (here called the 1–169(208) mutation) was found from partly from Figure 2A Reference 32 (Cartegni et al., -1997) and to find the N-terminal region of the frameshifted region by translating the nucleotide sequence after the deletion of the two nucleotide base pairs -CT from the aa 169 Proline residue. (see Bione S et al/. -1994, pmid:7894480) Amino acid 208 now corresponds to a STOP codon. Dear checker -please check the identifiers below - as the names of the protein isoforms given in this publication do not correspond to the UniProt names, and while I repeated the Blasts of protein sequences from GRCh37 assembly more than once, the results differed on occasion.... Ensembl identifiers were located from the GRCh37 assembly. ENST00000313630: Q8NF91-3 (called Nesprin 1-alpha here). ENST00000312125:Q8WXH0-3 (called Nesprin 2-beta here) ENSP00000345521:Q8WXH0-5 (called Nesprin 2-alpha here) juliet.ellis@kcl.ac.uk Accepted 2015-MAY-08 by ORCHARD Experimental cell research 2007 Only protein-protein interactions imex curation imex curation I assume the corrections were both for Figure 7- which would mean(EBI-10760546) - the second EBI number you gave was for Fig6 -EBI-10760483- which does not use the Emerin mutation. As you can see I have worked out the exact mutation sequence - the complete translated sequence I worked out using the sequence from Ensembl (and Bione Reference) which gives the same sequence for the C terminal region as given for Fig 2A in Ref 32-Cartegni - so is most likely correct. I dont like to enter aas 1-208 as sufficient to bind - as they are using the full length protein here apart from this mutant. However the feature I have enters would assume the sequence continues after residue 207 in an "unmutated" form- which is incorrect - dont know how we can show the protein stops at aa 207. Distinct functional domains in nesprin-1alpha and nesprin-2beta bind directly to emerin and both interactions are disrupted in X-linked Emery-Dreifuss muscular dystrophy. Distinct functional domains in nesprin-1alpha and nesprin-2beta bind directly to emerin and both interactions are disrupted in X-linked Emery-Dreifuss muscular dystrophy. Experimental cell research 2007 imex curation Wheeler MA., Davies JD., Zhang Q., Emerson LJ., Hunt J., Shanahan CM., Ellis JA. Cardiac - Interactions involving cardiac related proteins Dear checker -please check the identifiers below - as the names of the protein isoforms given in this publication do not correspond to the UniProt names, and while I repeated the Blasts of protein sequences from GRCh37 assembly more than once, the results differed on occasion.... Ensembl identifiers were located from the GRCh37 assembly. ENST00000313630: Q8NF91-3 (called Nesprin 1-alpha here). ENST00000312125:Q8WXH0-3 (called Nesprin 2-beta here) ENSP00000345521:Q8WXH0-5 (called Nesprin 2-alpha here) juliet.ellis@kcl.ac.uk Only protein-protein interactions imex curation in vitro In vitro far western blotting far western blotting Affinity blotting Affinity blotting western blot western blot Immuno blot Immuno blot Wheeler MA., Davies JD., Zhang Q., Emerson LJ., Hunt J., Shanahan CM., Ellis JA. Cardiac - Interactions involving cardiac related proteins Dear checker -please check the identifiers below - as the names of the protein isoforms given in this publication do not correspond to the UniProt names, and while I repeated the Blasts of protein sequences from GRCh37 assembly more than once, the results differed on occasion.... Ensembl identifiers were located from the GRCh37 assembly. ENST00000313630: Q8NF91-3 (called Nesprin 1-alpha here). ENST00000312125:Q8WXH0-3 (called Nesprin 2-beta here) ENSP00000345521:Q8WXH0-5 (called Nesprin 2-alpha here) juliet.ellis@kcl.ac.uk Accepted 2015-MAY-08 by ORCHARD Experimental cell research 2007 Only protein-protein interactions imex curation imex curation I assume the corrections were both for Figure 7- which would mean(EBI-10760546) - the second EBI number you gave was for Fig6 -EBI-10760483- which does not use the Emerin mutation. As you can see I have worked out the exact mutation sequence - the complete translated sequence I worked out using the sequence from Ensembl (and Bione Reference) which gives the same sequence for the C terminal region as given for Fig 2A in Ref 32-Cartegni - so is most likely correct. I dont like to enter aas 1-208 as sufficient to bind - as they are using the full length protein here apart from this mutant. However the feature I have enters would assume the sequence continues after residue 207 in an "unmutated" form- which is incorrect - dont know how we can show the protein stops at aa 207. Distinct functional domains in nesprin-1alpha and nesprin-2beta bind directly to emerin and both interactions are disrupted in X-linked Emery-Dreifuss muscular dystrophy. Distinct functional domains in nesprin-1alpha and nesprin-2beta bind directly to emerin and both interactions are disrupted in X-linked Emery-Dreifuss muscular dystrophy. Experimental cell research 2007 imex curation Wheeler MA., Davies JD., Zhang Q., Emerson LJ., Hunt J., Shanahan CM., Ellis JA. Cardiac - Interactions involving cardiac related proteins Dear checker -please check the identifiers below - as the names of the protein isoforms given in this publication do not correspond to the UniProt names, and while I repeated the Blasts of protein sequences from GRCh37 assembly more than once, the results differed on occasion.... Ensembl identifiers were located from the GRCh37 assembly. ENST00000313630: Q8NF91-3 (called Nesprin 1-alpha here). ENST00000312125:Q8WXH0-3 (called Nesprin 2-beta here) ENSP00000345521:Q8WXH0-5 (called Nesprin 2-alpha here) juliet.ellis@kcl.ac.uk Only protein-protein interactions imex curation mouse-c2c12 Mouse C3H muscle myoblast c2c12 Mouse C3H muscle myoblast fluorescence imaging fluorescence microscopy fluorescence imaging immunocytochemistry immunocytochemistry Wheeler MA., Davies JD., Zhang Q., Emerson LJ., Hunt J., Shanahan CM., Ellis JA. Cardiac - Interactions involving cardiac related proteins Dear checker -please check the identifiers below - as the names of the protein isoforms given in this publication do not correspond to the UniProt names, and while I repeated the Blasts of protein sequences from GRCh37 assembly more than once, the results differed on occasion.... Ensembl identifiers were located from the GRCh37 assembly. ENST00000313630: Q8NF91-3 (called Nesprin 1-alpha here). ENST00000312125:Q8WXH0-3 (called Nesprin 2-beta here) ENSP00000345521:Q8WXH0-5 (called Nesprin 2-alpha here) juliet.ellis@kcl.ac.uk Accepted 2015-MAY-08 by ORCHARD Experimental cell research 2007 Only protein-protein interactions imex curation imex curation I assume the corrections were both for Figure 7- which would mean(EBI-10760546) - the second EBI number you gave was for Fig6 -EBI-10760483- which does not use the Emerin mutation. As you can see I have worked out the exact mutation sequence - the complete translated sequence I worked out using the sequence from Ensembl (and Bione Reference) which gives the same sequence for the C terminal region as given for Fig 2A in Ref 32-Cartegni - so is most likely correct. I dont like to enter aas 1-208 as sufficient to bind - as they are using the full length protein here apart from this mutant. However the feature I have enters would assume the sequence continues after residue 207 in an "unmutated" form- which is incorrect - dont know how we can show the protein stops at aa 207. q8nf91-3 Nesprin-1 Enaptin Myocyte nuclear envelope protein 1 Nuclear envelope spectrin repeat protein 1 Synaptic nuclear envelope protein 1 Alpha SYNE1 C6orf98 KIAA0796 KIAA1262 KIAA1756 MYNE1 KASH domain-containing protein 1 protein protein human Homo sapiens Human MGERLAKASHESKASEIEYKLGKVNDRWQHLLDLIAARVKKLKETLVAVQQLDKNMSSLRTWLAHIESELAKPIVYDSCNSEEIQRKLNEQQELQRDIEKHSTGVASVLNLCEVLLHDCDACATDAECDSIQQATRNLDRRWRNICAMSMERRLKIEETWRLWQKFLDDYSRFEDWLKSSERTAAFPSSSGVIYTVAKEELKKFEAFQRQVHECLTQLELINKQYRRLARENRTDSACSLKQMVHEGNQRWDNLQKRVTSILRRLKHFIGQREEFETARDSILVWLTEMDLQLTNIEHFSECDVQAKIKQLKAFQQEISLNHNKIEQIIAQGEQLIEKSEPLDAAIIEEELDELRRYCQEVFGRVERYHKKLIRLPLPDDEHDLSDRELELEDSAALSDLHWHDRSADSLLSPQPSSNLSLSLAQPLRSERSGRDTPASVDSIPLEWDHDYDLSRDLESAMSRALPSEDEEGQDDKDFYLRGAVGLSDVMIPESPEAYVKLTENAIKNTSGDHSALESQIRQLGKALDDSRFQIQQTENIIRSKTPTGPELDTSYKGYMKLLGECSSSIDSVKRLEHKLKEEEESLPGFVNLHSTETQTAGVIDRWELLQAQALSKELRMKQNLQKWQQFNSDLNSIWAWLGDTEEELEQLQRLELSTDIQTIELQIKKLKELQKAVDHRKAIILSINLCSPEFTQADSKESRDLQDRLSQMNGRWDRVCSLLEEWRGLLQDALMQCQGFHEMSHGLLLMLENIDRRKNEIVPIDSNLDAEILQDHHKQLMQIKHELLESQLRVASLQDMSCQLLVNAEGTDCLEAKEKVHVIGNRLKLLLKEVSRHIKELEKLLDVSSSQQDLSSWSSADELDTSGSVSPTSGRSTPNRQKTPRGKCSLSQPGPSVSSPHSRSTKGGSDSSLSEPGPGRSGRGFLFRVLRAALPLQLLLLLLIGLACLVPMSEEDYSCALSNNFARSFHPMLRYTNGPPPL 332A6E5ABA5A2248 emd_human Emerin EDMD STA EMD protein protein human Homo sapiens Human MDNYADLSDTELTTLLRRYNIPHGPVVGSTRRLYEKKIFEYETQRRRLSPPSSSAASSYSFSDLNSTRGDADMYDLPKKEDALLYQSKGYNDDYYEESYFTTRTYGEPESAGPSRAVRQSVTSFPDADAFHHQVHDDDLLSSSEEECKDRERPMYGRDSAYQSITHYRPVSASRSSLDLSYYPTSSSTSFMSSSSSSSSWLTRRAIRPENRAPGAGLGQDRQVPLWGQLLLFLVFVIVLFFIYHFMQAEEGNPF DIP protein P50402 original sequence version: 95 DIP protein P50402 original sequence version: 125 EB62EDD59B7A044F q8wxh0-3 Nesprin-2 Nuclear envelope spectrin repeat protein 2 Nucleus and actin connecting element protein Synaptic nuclear envelope protein 2 JAM19 epsilon2 SYNE2 KIAA1011 NUA KASH domain-containing protein 2 protein protein human Homo sapiens Human MSNLRTWLARIESELSKPVVYDVCDDQEIQKRLAEQQDLQRDIEQHSAGVESVFNICDVLLHDSDACANETECDSIQQTTRSLDRRWRNICAMSMERRMKIEETWRLWQKFLDDYSRFEDWLKSAERTAACPNSSEVLYTSAKEELKRFEAFQRQIHERLTQLELINKQYRRLARENRTDTASRLKQMVHEGNQRWDNLQRRVTAVLRRLRHFTNQREEFEGTRESILVWLTEMDLQLTNVEHFSESDADDKMRQLNGFQQEITLNTNKIDQLIVFGEQLIQKSEPLDAVLIEDELEELHRYCQEVFGRVSRFHRRLTSCTPGLEDEKEASENETDMEDPREIQTDSWRKRGESEEPSSPQSLCHLVAPGHERSGCETPVSVDSIPLEWDHTGDVGGSSSHEEDEEGPYYSALSGKSISDGHSWHVPDSPSCPEHHYKQMEGDRNVPPVPPASSTPYKPPYGKLLLPPGTDGGKEGPRVLNGNPQQEDGGLAGITEQQSGAFDRWEMIQAQELHNKLKIKQNLQQLNSDISAITTWLKKTEAELEMLKMAKPPSDIQEIELRVKRLQEILKAFDTYKALVVSVNVSSKEFLQTESPESTELQSRLRQLSLLWEAAQGAVDSWRGGLRQSLMQCQDFHQLSQNLLLWLASAKNRRQKAHVTDPKADPRALLECRRELMQLEKELVERQPQVDMLQEISNSLLIKGHGEDCIEAEEKVHVIEKKLKQLREQVSQDLMALQGTQNPASPLPSFDEVDSGDQPPATSVPAPRAKQFRAVRTTEGEEETESRVPGSTRPQRSFLSRVVRAALPLQLLLLLLLLLACLLPSSEEDYSCTQANNFARSFYPMLRYTNGPPPT Produced by exon skipping that results in a frameshift. 554952A1E70DF621 emd_mouse Emerin Emd Sta protein protein mouse Mus musculus Mouse MDDYAVLSDTELAAVLRQYNIPHGPIVGSTRKLYEKKIFEYETQRRRLLPPNSSSSSFSYQFSDLDSAAVDSDMYDLPKKEDALLYQSKDYNDDYYEESYLTTKTYGEPESVGMSKSFRQPGTSLVDADTFHHQVRDDIFSSLEEEGKDRERLIYGQDSAYQSIAHYRPISNVSRSSLGLSYYPTSSTSSVSSSSSSPSSWLTRRAIRPEKQAPAAALGQDRQVPLWGQLLLFLVFAAFLLFVYYSIQAEEGNPFWMDP 645B021541063502 emd-syne1-2 2 5 unspecified role unspecified role bait bait c_terminus his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range N/A sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 4 unspecified role unspecified role prey prey delta_tm sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain c_terminus his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range ecoli Escherichia coli (strain K12) 11 13 physical association physical association 3A Full-length nesprin-2beta-deltaTM has a higher affinity than full-length nesprin-1alpha- deltaTM for emerin. emd-syne2-1 2 5 unspecified role unspecified role bait bait c_terminus his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 6 unspecified role unspecified role prey prey delta_tm sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain c_terminus his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range ecoli Escherichia coli (strain K12) 18 20 physical association physical association 3Ai Full-length nesprin-2beta-deltaTM has a higher affinity than full-length nesprin-1alpha- deltaTM for emerin. emd-syne1-4 2 5 unspecified role unspecified role bait bait c_terminus his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 4 unspecified role unspecified role prey prey region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n_terminus gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) 27 25 physical association physical association 3B/C/D Full-length nesprin-2beta-deltaTM has a higher affinity than full-length nesprin-1alpha- deltaTM for emerin. The authors state that the binding site for both Nesprins lies between emerin residues 140 and 176. (data not shown) emd-syne2-2 2 5 unspecified role unspecified role bait bait c_terminus his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 6 unspecified role unspecified role prey prey region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n_terminus gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) 32 34 physical association physical association 3B/C/Di Full-length nesprin-2beta-deltaTM has a higher affinity than full-length nesprin-1alpha- deltaTM for emerin. emd-syne1-5 1 5 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 P50402:p.Pro183His mutation increasing strength mutation increasing interaction strength mutation increasing strength certain certain sequence position certain certain certain sequence position certain P H Wed May 02 15:38:15 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'pro183his' Tue Jun 30 19:56:05 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Pro183His' P50402:p.Pro183Thr mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength certain certain sequence position certain certain certain sequence position certain P T Wed May 02 15:45:49 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'pro183thr' Tue Jun 30 16:37:53 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Pro183Thr' 169-207 binding region binding-associated region binding region substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain PVSASRSSLDLSYYPTSSSTSFMSSSSSSSSWLTRRAIR RRFSLQELPGPVLLSYFLLHLFYVLLIIFLFMAHPPCHPA This mutation involves a frameshift at residue 169 that results in the addition of a novel transmembrane region immediately followed by a premature stop codon at residue 208. Region substitution leads to an increase in interaction strength. P50402:p.Gln133His mutation increasing strength mutation increasing interaction strength mutation increasing strength certain certain sequence position certain certain certain sequence position certain Q H Wed May 02 17:02:51 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gln133his' Tue Jun 30 19:08:03 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln133His' in vitro In vitro 4 unspecified role unspecified role bait bait region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n_terminus gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) physical association physical association 4B, 6A,7A syne1-emd-2 1 5 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 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 4 unspecified role unspecified role prey prey delta_tm_region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 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 49 51 physical association physical association 5A emd-syne1-6 1 5 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 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 6 unspecified role unspecified role prey prey delta_tm_region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 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 58 56 physical association physical association 5A-2 syne1-emd-3 1 5 competitor competitor competitor prey prey 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) 5 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 4 unspecified role unspecified role bait bait region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n_terminus gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) physical association physical association 6A have left this as a "phys.assoc" on purpose -more appropriate. syne2-emd-1 1 5 stimulator stimulator prey prey 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) 5 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 6 unspecified role unspecified role bait bait region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n_terminus gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) association association 6A-2 Prior incubation with the emerin peptide did not block binding for nesprin-2beta, in fact an increase in binding was observed. syne1-emd-4 1 5 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 P50402:p.Pro183His mutation increasing strength mutation increasing interaction strength mutation increasing strength certain certain sequence position certain certain certain sequence position certain P H Wed May 02 17:29:23 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'pro183his' Tue Jun 30 17:00:54 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Pro183His' P50402:p.Pro183Thr mutation increasing strength mutation increasing interaction strength mutation increasing strength certain certain sequence position certain certain certain sequence position certain P T Wed May 02 18:03:25 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'pro183thr' Tue Jun 30 16:58:01 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Pro183Thr' 169-207 binding region binding-associated region binding region substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain PVSASRSSLDLSYYPTSSSTSFMSSSSSSSSWLTRRAIR RRFSLQELPGPVLLSYFLLHLFYVLLIIFLFMAHPPCHPA This mutation involves a frameshift at residue 169 that results in the addition of a novel transmembrane region immediately followed by a premature stop codon at residue 208. Region substitution leads to an increase in interaction strength. in vitro In vitro 6 unspecified role unspecified role bait bait region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n_terminus gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) physical association physical association 4B, 6A,7A-2 emd-syne1-8 3 4 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 n_terminus gfp tag green fluorescent protein tag GFP green fluorescent protein GFP green fluorescent protein gfp tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range 7 unspecified role unspecified role neutral component neutral component colocalization colocalization 8 emd-syne1-7 3 7 unspecified role unspecified role neutral component neutral component 6 tag fluorescence tag visualisation by fluorescence tag fluorescence immunocytochemistry immunocytochemistry unspecified role unspecified role neutral component neutral component n_terminus gfp tag green fluorescent protein tag GFP green fluorescent protein GFP green fluorescent protein gfp tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range N/A sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain colocalization colocalization 8-2