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/ Structures of lung cancer-derived EGFR mutants and inhibitor complexes: mechanism of activation and insights into differential inhibitor sensitivity. Structures of lung cancer-derived EGFR mutants and inhibitor complexes: mechanism of activation and insights into differential inhibitor sensitivity. Cancer Cell (1535-6108) 2007 imex curation Yun CH., Boggon TJ., Li Y., Woo MS., Greulich H., Meyerson M., Eck MJ. Cancer - Interactions investigated in the context of cancer eck@red.dfci.harvard.edu 10-APR-2007: Contacted by JYOTI. Only protein-protein interactions 1 in vitro In vitro enzymatic study enzymatic study predetermined predetermined participant predetermined Yun CH., Boggon TJ., Li Y., Woo MS., Greulich H., Meyerson M., Eck MJ. Cancer - Interactions investigated in the context of cancer eck@red.dfci.harvard.edu Accepted 2007-APR-29 by DAVET. 10-APR-2007: Contacted by JYOTI. Cancer Cell (1535-6108) 2007 Only protein-protein interactions 1 imex curation tyr1197_autophos_pep Peptide based on human EGFR Tyr1197 autophosphorylation site peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) RAHEEIYHFFFAKKK An amino acid sequence which is not represented in UniProt F5144B7993F18B5B egfr_human Epidermal growth factor receptor ERBB1 EGFR Receptor tyrosine-protein kinase erbB-1 Proto-oncogene c-ErbB-1 ERBB HER1 protein protein human Homo sapiens Human MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTEDSIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPSRDPHYQDPHSTAVGNPEYLNTVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRVAPQSSEFIGA DIP protein P00533 original sequence version: 213 DIP protein P00533 original sequence version: 214 DIP protein P00533 original sequence version: 119 DIP protein P00533 original sequence version: 207 DIP protein P00533 original sequence version: 132 DIP protein P00533-1 original sequence version: 197 DIP protein P00533 original sequence version: 163 DIP protein P00533-1 original sequence version: 159 DIP protein P00533 original sequence version: 184 DIP protein P00533-1 original sequence version: 174 DIP protein P00533-1 original sequence version: 191 DIP protein P00533 original sequence version: 218 DIP protein P00533 original sequence version: 221 DIP protein P00533-1 original sequence version: 221 DIP protein P00533 original sequence version: 226 DIP protein P00533 original sequence version: 166 DIP protein P00533-1 original sequence version: 166 DIP protein P00533 original sequence version: 194 DIP protein P00533-1 original sequence version: 194 DIP protein P00533-1 original sequence version: 224 DIP protein P00533 original sequence version: 189 DIP protein P00533-1 original sequence version: 207 DIP protein P00533 original sequence version: 177 DIP protein P00533 original sequence version: 168 D8A2A50B4EFB6ED2 egfr-tyr1197_autopho 1 3 enzyme enzyme unspecified role unspecified role region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P00533:p.Leu858Arg mutation increasing mutation increasing interaction mutation increasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain L R Wed May 02 16:24:21 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu858arg' Tue Jun 30 18:19:01 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu858Arg' P00533:p.Gly719Ser mutation increasing mutation increasing interaction mutation increasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain G S Wed May 02 16:46:26 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly719ser' Tue Jun 30 19:54:22 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly719Ser' spofr-sf_9 Spodoptera frugiperda insect cells Fall armyworm sf_9 insect cells Derived from pupal ovarian tissue of the fall armyworm Cloned from the parent cell line, IPLB-SF-21-AE (SF-21) derived from immature ovaries of fall armyworm Spodoptera frugiperda pupae cells are susceptible to Baculovirus infection 2 enzyme target enzyme target substrate substrate unspecified role unspecified role chemical synthesis Chemical synthesis (Chemical synthesis) phosphorylation phosphorylation reaction phosphorylation S1 The increased catalytic activity of the mutants, as compared with the wild-type enzyme, likely results from a shift of the equilibrium toward the active conformation of the enzyme It is proposed by the authors that the mutants have increased activity due to a shift of the equilibrium towards the active conformation. The peptide based on human EGFR Tyr1197 autophosphorylation site is phosphorylated by EGFR.