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/ Structural basis of binding of P-body-associated proteins GW182 and ataxin-2 by the Mlle domain of poly(A)-binding protein. Structural basis of binding of P-body-associated proteins GW182 and ataxin-2 by the Mlle domain of poly(A)-binding protein. J. Biol. Chem. (0021-9258) 2010 imex curation Kozlov G., Safaee N., Rosenauer A., Gehring K. kalle.gehring@mcgill.ca 09-Sep-2013: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Kozlov G., Safaee N., Rosenauer A., Gehring K. kalle.gehring@mcgill.ca Accepted 2013-AUG-29 by MGT 09-Sep-2013: Contacted by IntAct-Help. J. Biol. Chem. (0021-9258) 2010 Only protein-protein interactions imex curation Short label for the pabpc1 binding region feature has been changed to 'PABP_HYD domain'. The IPR002004 was already present in the xref for this feature, is this not the correct place then? I can delete the 'sufficient to bind' feature for Q9HCJ0 if you like, although I think the required and sufficient provide different and complementary types of data. Structural basis of binding of P-body-associated proteins GW182 and ataxin-2 by the Mlle domain of poly(A)-binding protein. Structural basis of binding of P-body-associated proteins GW182 and ataxin-2 by the Mlle domain of poly(A)-binding protein. J. Biol. Chem. (0021-9258) 2010 imex curation Kozlov G., Safaee N., Rosenauer A., Gehring K. kalle.gehring@mcgill.ca 09-Sep-2013: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr predetermined predetermined participant predetermined Kozlov G., Safaee N., Rosenauer A., Gehring K. This experiment is not described in the 'Experimental procedures' section, but its use is indicated as a footnote of Table 2. kalle.gehring@mcgill.ca Accepted 2013-AUG-29 by MGT 09-Sep-2013: Contacted by IntAct-Help. J. Biol. Chem. (0021-9258) 2010 Only protein-protein interactions imex curation Short label for the pabpc1 binding region feature has been changed to 'PABP_HYD domain'. The IPR002004 was already present in the xref for this feature, is this not the correct place then? I can delete the 'sufficient to bind' feature for Q9HCJ0 if you like, although I think the required and sufficient provide different and complementary types of data. Structural basis of binding of P-body-associated proteins GW182 and ataxin-2 by the Mlle domain of poly(A)-binding protein. Structural basis of binding of P-body-associated proteins GW182 and ataxin-2 by the Mlle domain of poly(A)-binding protein. J. Biol. Chem. (0021-9258) 2010 imex curation Kozlov G., Safaee N., Rosenauer A., Gehring K. kalle.gehring@mcgill.ca 09-Sep-2013: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Kozlov G., Safaee N., Rosenauer A., Gehring K. kalle.gehring@mcgill.ca Accepted 2013-AUG-29 by MGT 09-Sep-2013: Contacted by IntAct-Help. J. Biol. Chem. (0021-9258) 2010 Only protein-protein interactions imex curation Short label for the pabpc1 binding region feature has been changed to 'PABP_HYD domain'. The IPR002004 was already present in the xref for this feature, is this not the correct place then? I can delete the 'sufficient to bind' feature for Q9HCJ0 if you like, although I think the required and sufficient provide different and complementary types of data. Structural basis of binding of P-body-associated proteins GW182 and ataxin-2 by the Mlle domain of poly(A)-binding protein. Structural basis of binding of P-body-associated proteins GW182 and ataxin-2 by the Mlle domain of poly(A)-binding protein. J. Biol. Chem. (0021-9258) 2010 imex curation Kozlov G., Safaee N., Rosenauer A., Gehring K. kalle.gehring@mcgill.ca 09-Sep-2013: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Kozlov G., Safaee N., Rosenauer A., Gehring K. kalle.gehring@mcgill.ca Accepted 2013-AUG-29 by MGT 09-Sep-2013: Contacted by IntAct-Help. J. Biol. Chem. (0021-9258) 2010 Only protein-protein interactions imex curation Short label for the pabpc1 binding region feature has been changed to 'PABP_HYD domain'. The IPR002004 was already present in the xref for this feature, is this not the correct place then? I can delete the 'sufficient to bind' feature for Q9HCJ0 if you like, although I think the required and sufficient provide different and complementary types of data. atx2_human Ataxin-2 Spinocerebellar ataxia type 2 protein Trinucleotide repeat-containing gene 13 protein SCA2 TNRC13 ATXN2 ATX2 protein protein human Homo sapiens Human MRSAAAAPRSPAVATESRRFAAARWPGWRSLQRPARRSGRGGGGAAPGPYPSAAPPPPGPGPPPSRQSSPPSASDCFGSNGNGGGAFRPGSRRLLGLGGPPRPFVVLLLPLASPGAPPAAPTRASPLGARASPPRSGVSLARPAPGCPRPACEPVYGPLTMSLKPQQQQQQQQQQQQQQQQQQQQQQQPPPAAANVRKPGGSGLLASPAAAPSPSSSSVSSSSATAPSSVVAATSGGGRPGLGRGRNSNKGLPQSTISFDGIYANMRMVHILTSVVGSKCEVQVKNGGIYEGVFKTYSPKCDLVLDAAHEKSTESSSGPKREEIMESILFKCSDFVVVQFKDMDSSYAKRDAFTDSAISAKVNGEHKEKDLEPWDAGELTANEELEALENDVSNGWDPNDMFRYNEENYGVVSTYDSSLSSYTVPLERDNSEEFLKREARANQLAEEIESSAQYKARVALENDDRSEEEKYTAVQRNSSEREGHSINTRENKYIPPGQRNREVISWGSGRQNSPRMGQPGSGSMPSRSTSHTSDFNPNSGSDQRVVNGGVPWPSPCPSPSSRPPSRYQSGPNSLPPRAATPTRPPSRPPSRPSRPPSHPSAHGSPAPVSTMPKRMSSEGPPRMSPKAQRHPRNHRVSAGRGSISSGLEFVSHNPPSEAATPPVARTSPSGGTWSSVVSGVPRLSPKTHRPRSPRQNSIGNTPSGPVLASPQAGIIPTEAVAMPIPAASPTPASPASNRAVTPSSEAKDSRLQDQRQNSPAGNKENIKPNETSPSFSKAENKGISPVVSEHRKQIDDLKKFKNDFRLQPSSTSESMDQLLNKNREGEKSRDLIKDKIEPSAKDSFIENSSSNCTSGSSKPNSPSISPSILSNTEHKRGPEVTSQGVQTSSPACKQEKDDKEEKKDAAEQVRKSTLNPNAKEFNPRSFSQPKPSTTPTSPRPQAQPSPSMVGHQQPTPVYTQPVCFAPNMMYPVPVSPGVQPLYPIPMTPMPVNQAKTYRAVPNMPQQRQDQHHQSAMMHPASAAGPPIAATPPAYSTQYVAYSPQQFPNQPLVQHVPHYQSQHPHVYSPVIQGNARMMAPPTHAQPGLVSSSATQYGAHEQTHAMYACPKLPYNKETSPSFYFAISTGSLAQQYAHPNATLHPHTPHPQPSATPTGQQQSQHGGSHPAPSPVQHHQHQAAQALHLASPQQQSAIYHAGLAPTPPSMTPASNTQSPQNSFPAAQQTVFTIHPSHVQPAYTNPPHMAHVPQAHVQSGMVPSHPTAHAPMMLMTTQPPGGPQAALAQSALQPIPVSTTAHFPYMTHPSVQAHHQQQL DIP protein Q99700 original sequence version: 90 40A2883FF9D5D118 tnr6c_human Trinucleotide repeat-containing gene 6C protein TNRC6C KIAA1582 protein protein human Homo sapiens Human MATGSAQGNFTGHTKKTNGNNGTNGALVQSPSNQSALGAGGANSNGSAARVWGVATGSSSGLAHCSVSGGDGKMDTMIGDGRSQNCWGASNSNAGINLNLNPNANPAAWPVLGHEGTVATGNPSSICSPVSAIGQNMGNQNGNPTGTLGAWGNLLPQESTEPQTSTSQNVSFSAQPQNLNTDGPNNTNPMNSSPNPINAMQTNGLPNWGMAVGMGAIIPPHLQGLPGANGSSVSQVSGGSAEGISNSVWGLSPGNPATGNSNSGFSQGNGDTVNSALSAKQNGSSSAVQKEGSGGNAWDSGPPAGPGILAWGRGSGNNGVGNIHSGAWGHPSRSTSNGVNGEWGKPPNQHSNSDINGKGSTGWESPSVTSQNPTVQPGGEHMNSWAKAASSGTTASEGSSDGSGNHNEGSTGREGTGEGRRRDKGIIDQGHIQLPRNDLDPRVLSNTGWGQTPVKQNTAWEFEESPRSERKNDNGTEAWGCAATQASNSGGKNDGSIMNSTNTSSVSGWVNAPPAAVPANTGWGDSNNKAPSGPGVWGDSISSTAVSTAAAAKSGHAWSGAANQEDKSPTWGEPPKPKSQHWGDGQRSNPAWSAGGGDWADSSSVLGHLGDGKKNGSGWDADSNRSGSGWNDTTRSGNSGWGNSTNTKANPGTNWGETLKPGPQQNWASKPQDNNVSNWGGAASVKQTGTGWIGGPVPVKQKDSSEATGWEEPSPPSIRRKMEIDDGTSAWGDPSNYNNKTVNMWDRNNPVIQSSTTTNTTTTTTTTTSNTTHRVETPPPHQAGTQLNRSPLLGPGRKVSSGWGEMPNVHSKTENSWGEPSSPSTLVDNGTAAWGKPPSSGSGWGDHPAEPPVAFGRAGAPVAASALCKPASKSMQEGWGSGGDEMNLSTSQWEDEEGDVWNNAASQESTSSCSSWGNAPKKGLQKGMKTSGKQDEAWIMSRLIKQLTDMGFPREPAEEALKSNNMNLDQAMSALLEKKVDVDKRGLGVTDHNGMAAKPLGCRPPISKESSVDRPTFLDKDGGLVEEPTPSPFLPSPSLKLPLSHSALPSQALGGIASGLGMQNLNSSRQIPSGNLGMFGNSGAAQARTMQQPPQPPVQPLNSSQPSLRAQVPQFLSPQVQAQLLQFAAKNIGLNPALLTSPINPQHMTMLNQLYQLQLAYQRLQIQQQMLQAQRNVSGSMRQQEQQVARTITNLQQQIQQHQRQLAQALLVKQPPPPPPPPHLSLHPSAGKSAMDSFPSHPQTPGLPDLQTKEQQSSPNTFAPYPLAGLNPNMNVNSMDMTGGLSVKDPSQSQSRLPQWTHPNSMDNLPSAASPLEQNPSKHGAIPGGLSIGPPGKSSIDDSYGRYDLIQNSESPASPPVAVPHSWSRAKSDSDKISNGSSINWPPEFHPGVPWKGLQNIDPENDPDVTPGSVPTGPTINTTIQDVNRYLLKSGGKLSDIKSTWSSGPTSHTQASLSHELWKVPRNSTAPTRPPPGLTNPKPSSTWGASPLGWTSSYSSGSAWSTDTSGRTSSWLVLRNLTPQIDGSTLRTLCLQHGPLITFHLNLTQGNAVVRYSSKEEAAKAQKSLHMCVLGNTTILAEFAGEEEVNRFLAQGQALPPTSSWQSSSASSQPRLSAAGSSHGLVRSDAGHWNAPCLGGKGSSELLWGGVPQYSSSLWGPPSADDSRVIGSPTPLTTLLPGDLLSGESL DIP protein Q9HCJ0 original sequence version: 57 DIP protein Q9HCJ0-1 original sequence version: 56 DIP protein Q9HCJ0-1 original sequence version: 68 C8230D65BFB1DA0B 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 pabpc1-tnrc6c-1 1 GW182 6 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) 7 unspecified role unspecified role neutral component neutral component pabp_hyd domain 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) direct interaction direct interaction Fig. 1, Fig. 4, Table 1 working 22.1%, free 23.1% 1.50A atxn2-pabpc1-1 1 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) 7 unspecified role unspecified role neutral component neutral component pabp_hyd domain 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) direct interaction direct interaction Fig. 3, Fig. 4, Table 1 working 21.2%, free 24.5% 1.70A pabpc1-tnrc6c-2 4 GW182 6 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 region 15n label 15n label 15N N15 15N N15 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined chemical synthesis Chemical synthesis (Chemical synthesis) 7 unspecified role unspecified role neutral component neutral component pabp_hyd domain 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) direct interaction direct interaction Fig. 2b, Suppl. Fig. S1, Suppl. Fig. S2 pabpc1-tnrc6c-3 4 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 certain certain sequence position certain certain certain sequence position certain ecobd Escherichia coli (strain B / BL21-DE3) GW182 6 unspecified role unspecified role neutral component neutral component Q9HCJ0:p.Gly1392Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain G A Wed May 02 16:45:36 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly1392ala' Tue Jun 30 19:52:26 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly1392Ala' Q9HCJ0:p.Trp1395Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain W A Wed May 02 18:22:23 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp1395ala' Tue Jun 30 19:45:42 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp1395Ala' region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain chemical synthesis Chemical synthesis (Chemical synthesis) direct interaction direct interaction Fig. 2c, Table 2, Suppl. Fig. S3, Suppl. Fig. S4 NMR with the 1385-1399 fragment containing the gly1392ala and trp1395ala mutation showed Kd = 300 x10e-6 molar and Kd = 1400 x10e-6 molar, respectively. pabpc1-tnrc6c-4 3 7 unspecified role unspecified role neutral component neutral component pabp_hyd domain 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) GW182 6 unspecified role unspecified role neutral component neutral component Q9HCJ0:p.Trp1385Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain W A Wed May 02 20:23:22 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp1385ala' Tue Jun 30 19:30:14 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp1385Ala' Q9HCJ0:p.Pro1386Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain P A Wed May 02 17:27:12 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'pro1386ala' Tue Jun 30 18:01:10 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Pro1386Ala' Q9HCJ0:p.Pro1394Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain P A Wed May 02 17:38:39 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'pro1394ala' Tue Jun 30 17:24:18 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Pro1394Ala' region required to bind necessary binding region required to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain Q9HCJ0:p.Phe1389Ala mutation disrupting mutation disrupting interaction mutation disrupting alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain F A Wed May 02 15:41:26 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe1389ala' Tue Jun 30 19:54:01 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe1389Ala' chemical synthesis Chemical synthesis (Chemical synthesis) direct interaction direct interaction Fig 2a, Table 2 The fragment consisting of residues 1381-1393 showed no binding. For the trp1385ala mutant the Kd = 82x10e-6 molar. For the pro1386ala mutant the Kd = 18x10e-6 molar. For the pro1394ala mutant the Kd = 25x10e-6 molar. The phe1389ala mutant showed no binding. atxn2-pabpc1-3 2 7 unspecified role unspecified role unspecified role unspecified role 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) 5 unspecified role unspecified role unspecified role unspecified role 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) physical association physical association Table 2