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/ http://www.ebi.ac.uk/ yu-2014-9 in vitro In vitro phosphatase assay phosphatase assay predetermined predetermined participant predetermined Yu ZH., Zhang RY., Walls CD., Chen L., Zhang S., Wu L., Liu S., Zhang ZY. Rare diseases - Interactions investigated in the context of Rare genetic disease EGFR, Sprouty1, Paxillin and Gab1 peptides used in phosphatase assay were found to align (100% homology) with human and also with other species like mouse, monkey, etc; we have chosen human over all other species zyzhang@iu.edu Biochemistry 2014 Only protein-protein interactions imex curation imex curation yu-2014-10 human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Yu ZH., Zhang RY., Walls CD., Chen L., Zhang S., Wu L., Liu S., Zhang ZY. Rare diseases - Interactions investigated in the context of Rare genetic disease zyzhang@iu.edu Biochemistry 2014 Only protein-protein interactions imex curation imex curation 4-nitrophenyl phosphate(2−) 4-nitrophenyl phosphate(2−) small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) q06124-2 Tyrosine-protein phosphatase non-receptor type 11 PTPN11 PTP2C SHPTP2 PTP2C Protein-tyrosine phosphatase 1D Protein-tyrosine phosphatase 2C SH-PTP2 SH-PTP3 protein protein human Homo sapiens Human MTSRRWFHPNITGVEAENLLLTRGVDGSFLARPSKSNPGDFTLSVRRNGAVTHIKIQNTGDYYDLYGGEKFATLAELVQYYMEHHGQLKEKNGDVIELKYPLNCADPTSERWFHGHLSGKEAEKLLTEKGKHGSFLVRESQSHPGDFVLSVRTGDDKGESNDGKSKVTHVMIRCQELKYDVGGGERFDSLTDLVEHYKKNPMVETLGTVLQLKQPLNTTRINAAEIESRVRELSKLAETTDKVKQGFWEEFETLQQQECKLLYSRKEGQRQENKNKNRYKNILPFDHTRVVLHDGDPNEPVSDYINANIIMPEFETKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRVIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYTLRELKLSKVGQGNTERTVWQYHFRTWPDHGVPSDPGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRSQRSGMVQTEAQYRFIYMAVQHYIETLQRRIEEEQKSKRKGHEYTNIKYSLADQTSGDQSPLPPCTPTPPCAEMREDSARVYENVGLMQQQKSFR 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 spy1_human Protein sprouty homolog 1 SPRY1 protein protein human Homo sapiens Human MDPQNQHGSGSSLVVIQQPSLDSRQRLDYEREIQPTAILSLDQIKAIRGSNEYTEGPSVVKRPAPRTAPRQEKHERTHEIIPINVNNNYEHRHTSHLGHAVLPSNARGPILSRSTSTGSAASSGSNSSASSEQGLLGRSPPTRPVPGHRSERAIRTQPKQLIVDDLKGSLKEDLTQHKFICEQCGKCKCGECTAPRTLPSCLACNRQCLCSAESMVEYGTCMCLVKGIFYHCSNDDEGDSYSDNPCSCSQSHCCSRYLCMGAMSLFLPCLLCYPPAKGCLKLCRRCYDWIHRPGCRCKNSNTVYCKLESCPSRGQGKPS paxi_human Paxillin PXN protein protein human Homo sapiens Human MDDLDALLADLESTTSHISKRPVFLSEETPYSYPTGNHTYQEIAVPPPVPPPPSSEALNGTILDPLDQWQPSSSRFIHQQPQSSSPVYGSSAKTSSVSNPQDSVGSPCSRVGEEEHVYSFPNKQKSAEPSPTVMSTSLGSNLSELDRLLLELNAVQHNPPGFPADEANSSPPLPGALSPLYGVPETNSPLGGKAGPLTKEKPKRNGGRGLEDVRPSVESLLDELESSVPSPVPAITVNQGEMSSPQRVTSTQQQTRISASSATRELDELMASLSDFKIQGLEQRADGERCWAAGWPRDGGRSSPGGQDEGGFMAQGKTGSSSPPGGPPKPGSQLDSMLGSLQSDLNKLGVATVAKGVCGACKKPIAGQVVTAMGKTWHPEHFVCTHCQEEIGSRNFFERDGQPYCEKDYHNLFSPRCYYCNGPILDKVVTALDRTWHPEHFFCAQCGAFFGPEGFHEKDGKAYCRKDYFDMFAPKCGGCARAILENYISALNTLWHPECFVCRECFTPFVNGSFFEHDGQPYCEVHYHERRGSLCSGCQKPITGRCITAMAKKFHPEHFVCAFCLKQLNKGTFKEQNDKPYCQNCFLKLFC gab1_human GRB2-associated-binding protein 1 Growth factor receptor bound protein 2-associated protein 1 GRB2-associated binder 1 GAB1 protein protein human Homo sapiens Human MSGGEVVCSGWLRKSPPEKKLKRYAWKRRWFVLRSGRLTGDPDVLEYYKNDHAKKPIRIIDLNLCQQVDAGLTFNKKEFENSYIFDINTIDRIFYLVADSEEEMNKWVRCICDICGFNPTEEDPVKPPGSSLQAPADLPLAINTAPPSTQADSSSATLPPPYQLINVPPHLETLGIQEDPQDYLLLINCQSKKPEPTRTHADSAKSTSSETDCNDNVPSHKNPASSQSKHGMNGFFQQQMIYDSPPSRAPSASVDSSLYNLPRSYSHDVLPKVSPSSTEADGELYVFNTPSGTSSVETQMRHVSISYDIPPTPGNTYQIPRTFPEGTLGQTSKLDTIPDIPPPRPPKPHPAHDRSPVETCSIPRTASDTDSSYCIPTAGMSPSRSNTISTVDLNKLRKDASSQDCYDIPRAFPSDRSSSLEGFHNHFKVKNVLTVGSVSSEELDENYVPMNPNSPPRQHSSSFTEPIQEANYVPMTPGTFDFSSFGMQVPPPAHMGFRSSPKTPPRRPVPVADCEPPPVDRNLKPDRKVKPAPLEIKPLPEWEELQAPVRSPITRSFARDSSRFPMSPRPDSVHSTTSSSDSHDSEENYVPMNPNLSSEDPNLFGSNSLDGGSSPMIKPKGDKQVEYLDLDLDSGKSTPPRKQKSSGSGSSVADERVDYVVVDQQKTLALKSTREAWTDGRQSTESETPAKSVK 4_nitrophenyl phosphate(2)-ptpn11-1 3670464 N/A 3670466 enzyme target enzyme target substrate substrate neutral component neutral component purified purified chemical synthesis Chemical synthesis (Chemical synthesis) N/A 3670467 enzyme enzyme neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false c-c terminal region 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 false Q06124-2:p.Tyr279Cys mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain false Q06124-2:p.Ala461Thr mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain false Q06124-2:p.Gly464Ala mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain false Q06124-2:p.Thr468Met mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain false Q06124-2:p.Arg498Leu mutation with no effect mutation with no effect mutation with no effect mutation not affecting interaction certain certain sequence position certain certain certain sequence position certain false Q06124-2:p.Gln506Pro mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain false Q06124-2:p.Gln510Glu mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) dephosphorylation dephosphorylation reaction dephosphorylation false false false 3670464 Table 1 4_nitrophenyl phosphate(2)-ptpn11-2 3670464 N/A 3670466 enzyme target enzyme target substrate substrate neutral component neutral component purified purified chemical synthesis Chemical synthesis (Chemical synthesis) N/A 3670467 enzyme enzyme neutral component neutral component purified purified catalytic domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false c-c terminal region 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 false Q06124-2:p.Tyr279Cys mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain false Q06124-2:p.Ala461Thr mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain false Q06124-2:p.Gly464Ala mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain false Q06124-2:p.Thr468Met mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain false Q06124-2:p.Arg498Leu mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain false Q06124-2:p.Gln506Pro mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain false Q06124-2:p.Gln510Glu mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) dephosphorylation dephosphorylation reaction dephosphorylation false false false 3670464 Table 1 egfr-ptpn11-4 3670464 N/A 3670467 enzyme enzyme neutral component neutral component purified purified c-c terminal region 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 false Q06124-2:p.Tyr279Cys mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain false Q06124-2:p.Thr468Met mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain false catalytic domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) N/A 3670468 enzyme target enzyme target substrate substrate unspecified role unspecified role purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false tyr1016 phosres phosphorylated residue PhosRes Phospho Phosphorylation Phosphorylation (O of Serine, Threonine, Tyrosine and Aspartate, N epsilon of Lysine) certain certain sequence position certain certain certain sequence position certain false chemical synthesis Chemical synthesis (Chemical synthesis) dephosphorylation dephosphorylation reaction dephosphorylation false false false 3670464 Table 2 ptpn11-spry1-2 3670464 N/A 3670469 enzyme target enzyme target substrate substrate neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false tyr53 phosres phosphorylated residue PhosRes Phospho Phosphorylation Phosphorylation (O of Serine, Threonine, Tyrosine and Aspartate, N epsilon of Lysine) certain certain sequence position certain certain certain sequence position certain false chemical synthesis Chemical synthesis (Chemical synthesis) N/A 3670467 enzyme enzyme neutral component neutral component purified purified c-c terminal region 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 false region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false Q06124-2:p.Tyr279Cys mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain false Q06124-2:p.Thr468Met mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain false catalytic domain binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) dephosphorylation dephosphorylation reaction dephosphorylation false false false 3670464 Table 2 ptpn11-pxn-1 3670464 N/A 3670467 enzyme enzyme neutral component neutral component purified purified c-c terminal region 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 false region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false Q06124-2:p.Tyr279Cys mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain false Q06124-2:p.Thr468Met mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain false catalytic domain binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) N/A 3670470 enzyme target enzyme target substrate substrate neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false tyr118 phosres phosphorylated residue PhosRes Phospho Phosphorylation Phosphorylation (O of Serine, Threonine, Tyrosine and Aspartate, N epsilon of Lysine) certain certain sequence position certain certain certain sequence position certain false chemical synthesis Chemical synthesis (Chemical synthesis) dephosphorylation dephosphorylation reaction dephosphorylation false false false 3670464 Table 2 gab1-ptpn11-38 3670464 N/A 3670467 enzyme enzyme neutral component neutral component purified purified c-c terminal region 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 false region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false Q06124-2:p.Tyr279Cys mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain false Q06124-2:p.Thr468Met mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain false catalytic domain binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) N/A 3670471 enzyme target enzyme target substrate substrate neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false tyr589 phosres phosphorylated residue PhosRes Phospho Phosphorylation Phosphorylation (O of Serine, Threonine, Tyrosine and Aspartate, N epsilon of Lysine) certain certain sequence position certain certain certain sequence position certain false chemical synthesis Chemical synthesis (Chemical synthesis) dephosphorylation dephosphorylation reaction dephosphorylation false false false 3670464 Table 2 4_nitrophenyl phosphate(2)-ptpn11-3 3670464 N/A 3670467 inhibitor inhibitor neutral component neutral component purified purified n-sh2 domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false c-terminal region 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 false Q06124-2:p.Glu76Lys mutation mutation certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) N/A 3670466 enzyme target enzyme target substrate substrate neutral component neutral component purified purified chemical synthesis Chemical synthesis (Chemical synthesis) N/A 3670467 enzyme enzyme neutral component neutral component purified purified catalytic domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false c-c terminal region 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 false Q06124-2:p.Tyr279Cys mutation increasing rate mutation increasing interaction rate mutation increasing rate certain certain sequence position certain certain certain sequence position certain false p.Tyr279Cys mutant was found to have increasing phosphatase activity, which is more due to the inefficient binding of N-SH2 construct with SHP2 compared to the wildtype; in other words, the mutation offers 'protective' effect, which allows less access for N-SH2 inhibition Q06124-2:p.Gly464Ala mutation increasing rate mutation increasing interaction rate mutation increasing rate certain certain sequence position certain certain certain sequence position certain false p.Gly464Ala mutant was found to have increasing phosphatase activity, which is more due to the inefficient binding of N-SH2 construct with SHP2 compared to the wildtype; in other words, the mutation offers 'protective' effect, which allows less access for N-SH2 inhibition Q06124-2:p.Thr468Met mutation increasing rate mutation increasing interaction rate mutation increasing rate certain certain sequence position certain certain certain sequence position certain false p.Thr468Met mutant was found to have increasing phosphatase activity, which is more due to the inefficient binding of N-SH2 construct with SHP2 compared to the wildtype; in other words, the mutation offers 'protective' effect, which allows less access for N-SH2 inhibition Q06124-2:p.Arg498Leu mutation increasing rate mutation increasing interaction rate mutation increasing rate certain certain sequence position certain certain certain sequence position certain false p.Arg498Leu mutant was found to have increasing phosphatase activity, which is more due to the inefficient binding of N-SH2 construct with SHP2 compared to the wildtype; in other words, the mutation offers 'protective' effect, which allows less access for N-SH2 inhibition Q06124-2:p.Gln506Pro mutation increasing rate mutation increasing interaction rate mutation increasing rate certain certain sequence position certain certain certain sequence position certain false p.Gln506Pro mutant was found to have increasing phosphatase activity, which is more due to the inefficient binding of N-SH2 construct with SHP2 compared to the wildtype; in other words, the mutation offers 'protective' effect, which allows less access for N-SH2 inhibition Q06124-2:p.Gln510Glu mutation increasing rate mutation increasing interaction rate mutation increasing rate certain certain sequence position certain certain certain sequence position certain false p.Gln510Glu mutant was found to have increasing phosphatase activity, which is more due to the inefficient binding of N-SH2 construct with SHP2 compared to the wildtype; in other words, the mutation offers 'protective' effect, which allows less access for N-SH2 inhibition ecoli Escherichia coli (strain K12) dephosphorylation dephosphorylation reaction dephosphorylation false false false 3670464 Table 5 The mutants were found to have increasing phosphatase activity, which is more due to the inefficient binding of N-SH2 construct with SHP2 compared to the wildtype; in other words, the mutations offers 'protective' effect, which allows less access for N-SH2 inhibition gab1-ptpn11-37 3670465 N/A 3670467 unspecified role unspecified role bait bait over-expressed over expressed level over-expressed living cell living cell Q06124-2:p.[Tyr279Cys;Cys459Ser] mutation increasing strength mutation increasing interaction strength mutation increasing strength certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false Q06124-2:p.Cys459Ser mutation increasing strength mutation increasing interaction strength mutation increasing strength certain certain sequence position certain certain certain sequence position certain false n-terminal region ha tag ha tag YPYDVPDYA epitope tag YPYDVPDYA epitope tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range false Q06124-2:p.Tyr279Cys mutation increasing strength mutation increasing interaction strength mutation increasing strength certain certain sequence position certain certain certain sequence position certain false Q06124-2:p.Ala461Thr mutation increasing strength mutation increasing interaction strength mutation increasing strength certain certain sequence position certain certain certain sequence position certain false Q06124-2:p.Gly464Ala mutation increasing strength mutation increasing interaction strength mutation increasing strength certain certain sequence position certain certain certain sequence position certain false Q06124-2:p.Thr468Met mutation increasing strength mutation increasing interaction strength mutation increasing strength certain certain sequence position certain certain certain sequence position certain false Q06124-2:p.Arg498Leu mutation increasing strength mutation increasing interaction strength mutation increasing strength certain certain sequence position certain certain certain sequence position certain false Q06124-2:p.Gln506Pro mutation increasing strength mutation increasing interaction strength mutation increasing strength certain certain sequence position certain certain certain sequence position certain false Q06124-2:p.Gln510Glu mutation increasing strength mutation increasing interaction strength mutation increasing strength certain certain sequence position certain certain certain sequence position certain false Q06124-2:p.Glu76Lys mutation increasing strength mutation increasing interaction strength mutation increasing strength certain certain sequence position certain certain certain sequence position certain false N/A 3670471 unspecified role unspecified role prey prey living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level physical association physical association false false false 6a, 6d, 7a, 7b EGF HGF