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/ Molecular basis of gain-of-function LEOPARD syndrome-associated SHP2 mutations. Molecular basis of gain-of-function LEOPARD syndrome-associated SHP2 mutations. Biochemistry 2014 imex curation 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 29-Mar-2021: Contacted by IntAct-Help. Only protein-protein interactions imex curation 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 Accepted 2021-FEB-02 AT 08:42 GMT AT 08:42 GMT by PPORRAS Biochemistry 2014 Only protein-protein interactions imex curation imex curation Molecular basis of gain-of-function LEOPARD syndrome-associated SHP2 mutations. Molecular basis of gain-of-function LEOPARD syndrome-associated SHP2 mutations. Biochemistry 2014 imex curation 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 29-Mar-2021: Contacted by IntAct-Help. Only protein-protein interactions imex curation 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 Accepted 2021-FEB-02 AT 08:42 GMT AT 08:42 GMT by PPORRAS Biochemistry 2014 Only protein-protein interactions imex curation imex curation spy1_human Protein sprouty homolog 1 SPRY1 protein protein human Homo sapiens Human MDPQNQHGSGSSLVVIQQPSLDSRQRLDYEREIQPTAILSLDQIKAIRGSNEYTEGPSVVKRPAPRTAPRQEKHERTHEIIPINVNNNYEHRHTSHLGHAVLPSNARGPILSRSTSTGSAASSGSNSSASSEQGLLGRSPPTRPVPGHRSERAIRTQPKQLIVDDLKGSLKEDLTQHKFICEQCGKCKCGECTAPRTLPSCLACNRQCLCSAESMVEYGTCMCLVKGIFYHCSNDDEGDSYSDNPCSCSQSHCCSRYLCMGAMSLFLPCLLCYPPAKGCLKLCRRCYDWIHRPGCRCKNSNTVYCKLESCPSRGQGKPS 40E2D4D12816E057 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 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 4-nitrophenyl phosphate(2−) 4-nitrophenyl phosphate(2−) small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) paxi_human Paxillin PXN protein protein human Homo sapiens Human MDDLDALLADLESTTSHISKRPVFLSEETPYSYPTGNHTYQEIAVPPPVPPPPSSEALNGTILDPLDQWQPSSSRFIHQQPQSSSPVYGSSAKTSSVSNPQDSVGSPCSRVGEEEHVYSFPNKQKSAEPSPTVMSTSLGSNLSELDRLLLELNAVQHNPPGFPADEANSSPPLPGALSPLYGVPETNSPLGGKAGPLTKEKPKRNGGRGLEDVRPSVESLLDELESSVPSPVPAITVNQGEMSSPQRVTSTQQQTRISASSATRELDELMASLSDFKIQGLEQRADGERCWAAGWPRDGGRSSPGGQDEGGFMAQGKTGSSSPPGGPPKPGSQLDSMLGSLQSDLNKLGVATVAKGVCGACKKPIAGQVVTAMGKTWHPEHFVCTHCQEEIGSRNFFERDGQPYCEKDYHNLFSPRCYYCNGPILDKVVTALDRTWHPEHFFCAQCGAFFGPEGFHEKDGKAYCRKDYFDMFAPKCGGCARAILENYISALNTLWHPECFVCRECFTPFVNGSFFEHDGQPYCEVHYHERRGSLCSGCQKPITGRCITAMAKKFHPEHFVCAFCLKQLNKGTFKEQNDKPYCQNCFLKLFC DIP protein P49023 original sequence version: 115 DIP protein P49023 original sequence version: 126 DIP protein P49023 original sequence version: 169 DIP protein P49023 original sequence version: 140 DIP protein P49023 original sequence version: 175 ABF6C0BE5939623F 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 E0FAC78772B6677B 4_nitrophenyl phosphate(2)-ptpn11-1 1 6 enzyme target enzyme target substrate substrate neutral component neutral component purified purified chemical synthesis Chemical synthesis (Chemical synthesis) 5 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 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 Q06124-2:p.Tyr279Cys mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain Y C Tue Jun 30 15:40:17 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr279Cys' Q06124-2:p.Ala461Thr mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain A T 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.Ala461Thr' Q06124-2:p.Gly464Ala mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain G A Tue Jun 30 18:55:15 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly464Ala' Q06124-2:p.Thr468Met mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain T M Tue Jun 30 19:39:41 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr468Met' 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 R L Tue Jun 30 16:55:19 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg498Leu' Q06124-2:p.Gln506Pro mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain Q P Tue Jun 30 15:42:10 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln506Pro' Q06124-2:p.Gln510Glu mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain Q E Tue Jun 30 17:18:13 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln510Glu' ecoli Escherichia coli (strain K12) dephosphorylation dephosphorylation reaction dephosphorylation Table 1 4_nitrophenyl phosphate(2)-ptpn11-2 1 6 enzyme target enzyme target substrate substrate neutral component neutral component purified purified chemical synthesis Chemical synthesis (Chemical synthesis) 5 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 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 Q06124-2:p.Tyr279Cys mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain Y C Tue Jun 30 19:51:47 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr279Cys' Q06124-2:p.Ala461Thr mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain A T Tue Jun 30 18:22:14 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ala461Thr' Q06124-2:p.Gly464Ala mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain G A Tue Jun 30 19:36:52 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly464Ala' Q06124-2:p.Thr468Met mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain T M Tue Jun 30 16:15:59 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr468Met' Q06124-2:p.Arg498Leu mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain R L Tue Jun 30 19:53:13 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg498Leu' Q06124-2:p.Gln506Pro mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain Q P Tue Jun 30 17:50:35 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln506Pro' Q06124-2:p.Gln510Glu mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain Q E Tue Jun 30 19:46:41 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln510Glu' ecoli Escherichia coli (strain K12) dephosphorylation dephosphorylation reaction dephosphorylation Table 1 egfr-ptpn11-4 1 5 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 Q06124-2:p.Tyr279Cys mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain Y C Tue Jun 30 16:21:00 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr279Cys' Q06124-2:p.Thr468Met mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain T M Tue Jun 30 20:06:12 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr468Met' catalytic domain 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 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 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 prerequisite-ptm prerequisite-ptm prerequisite ptm required ptm prerequisite-ptm required-ptm chemical synthesis Chemical synthesis (Chemical synthesis) dephosphorylation dephosphorylation reaction dephosphorylation Table 2 ptpn11-spry1-2 1 3 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 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 prerequisite-ptm prerequisite-ptm prerequisite ptm required ptm prerequisite-ptm required-ptm chemical synthesis Chemical synthesis (Chemical synthesis) 5 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 region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Q06124-2:p.Tyr279Cys mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain Y C Tue Jun 30 17:00:31 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr279Cys' Q06124-2:p.Thr468Met mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain T M Tue Jun 30 18:08:45 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr468Met' catalytic domain binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) dephosphorylation dephosphorylation reaction dephosphorylation Table 2 ptpn11-pxn-1 1 5 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 region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Q06124-2:p.Tyr279Cys mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain Y C Tue Jun 30 18:50:23 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr279Cys' Q06124-2:p.Thr468Met mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain T M Tue Jun 30 17:36:22 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr468Met' catalytic domain binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 7 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 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 chemical synthesis Chemical synthesis (Chemical synthesis) dephosphorylation dephosphorylation reaction dephosphorylation Table 2 gab1-ptpn11-38 1 5 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 region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Q06124-2:p.Tyr279Cys mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain Y C Tue Jun 30 16:43:08 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr279Cys' Q06124-2:p.Thr468Met mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain T M Tue Jun 30 17:14:23 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr468Met' catalytic domain binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 8 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 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 prerequisite-ptm prerequisite-ptm prerequisite ptm required ptm prerequisite-ptm required-ptm chemical synthesis Chemical synthesis (Chemical synthesis) dephosphorylation dephosphorylation reaction dephosphorylation Table 2 4_nitrophenyl phosphate(2)-ptpn11-3 1 5 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 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 Q06124-2:p.Glu76Lys mutation mutation certain certain sequence position certain certain certain sequence position certain E K Tue Jun 30 18:30:41 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu76Lys' ecoli Escherichia coli (strain K12) 6 enzyme target enzyme target substrate substrate neutral component neutral component purified purified chemical synthesis Chemical synthesis (Chemical synthesis) 5 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 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 Q06124-2:p.Tyr279Cys mutation increasing rate mutation increasing interaction rate mutation increasing rate certain certain sequence position certain certain certain sequence position certain Y C 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 Tue Jun 30 16:52:03 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr279Cys' Q06124-2:p.Gly464Ala mutation increasing rate mutation increasing interaction rate mutation increasing rate certain certain sequence position certain certain certain sequence position certain G A 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 Tue Jun 30 16:55:11 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly464Ala' Q06124-2:p.Thr468Met mutation increasing rate mutation increasing interaction rate mutation increasing rate certain certain sequence position certain certain certain sequence position certain T M 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 Tue Jun 30 17:51:34 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr468Met' Q06124-2:p.Arg498Leu mutation increasing rate mutation increasing interaction rate mutation increasing rate certain certain sequence position certain certain certain sequence position certain R L 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 Tue Jun 30 19:42:58 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg498Leu' Q06124-2:p.Gln506Pro mutation increasing rate mutation increasing interaction rate mutation increasing rate certain certain sequence position certain certain certain sequence position certain Q P 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 Tue Jun 30 17:31:10 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln506Pro' Q06124-2:p.Gln510Glu mutation increasing rate mutation increasing interaction rate mutation increasing rate certain certain sequence position certain certain certain sequence position certain Q E 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 Tue Jun 30 20:12:25 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln510Glu' ecoli Escherichia coli (strain K12) dephosphorylation dephosphorylation reaction dephosphorylation 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 2 5 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 Y C certain certain sequence position certain certain certain sequence position certain C S Q06124-2:p.Cys459Ser mutation increasing strength mutation increasing interaction strength mutation increasing strength certain certain sequence position certain certain certain sequence position certain C S 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 Q06124-2:p.Tyr279Cys mutation increasing strength mutation increasing interaction strength mutation increasing strength certain certain sequence position certain certain certain sequence position certain Y C Tue Jun 30 16:07:01 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr279Cys' Q06124-2:p.Ala461Thr mutation increasing strength mutation increasing interaction strength mutation increasing strength certain certain sequence position certain certain certain sequence position certain A T Tue Jun 30 17:25:00 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ala461Thr' Q06124-2:p.Gly464Ala mutation increasing strength mutation increasing interaction strength mutation increasing strength certain certain sequence position certain certain certain sequence position certain G A Tue Jun 30 18:56:29 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly464Ala' Q06124-2:p.Thr468Met mutation increasing strength mutation increasing interaction strength mutation increasing strength certain certain sequence position certain certain certain sequence position certain T M Tue Jun 30 18:12:39 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr468Met' Q06124-2:p.Arg498Leu mutation increasing strength mutation increasing interaction strength mutation increasing strength certain certain sequence position certain certain certain sequence position certain R L Tue Jun 30 17:46:24 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg498Leu' Q06124-2:p.Gln506Pro mutation increasing strength mutation increasing interaction strength mutation increasing strength certain certain sequence position certain certain certain sequence position certain Q P Tue Jun 30 20:14:51 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln506Pro' Q06124-2:p.Gln510Glu mutation increasing strength mutation increasing interaction strength mutation increasing strength certain certain sequence position certain certain certain sequence position certain Q E Tue Jun 30 17:24:29 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln510Glu' Q06124-2:p.Glu76Lys mutation increasing strength mutation increasing interaction strength mutation increasing strength certain certain sequence position certain certain certain sequence position certain E K Tue Jun 30 19:08:35 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu76Lys' 8 unspecified role unspecified role prey prey living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level physical association physical association 6a, 6d, 7a, 7b EGF HGF