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/ The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site. The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site. Cell (0092-8674) 2009 imex curation Bae JH., Lew ED., Yuzawa S., Tome F., Lax I., Schlessinger J. Synapse - Interactions of proteins with an established role in the presynapse. joseph.schlessinger@yale.edu 23-Feb-2010: Contacted by JYOTI. jyoti Only protein-protein interactions 6 in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Bae JH., Lew ED., Yuzawa S., Tome F., Lax I., Schlessinger J. Synapse - Interactions of proteins with an established role in the presynapse. joseph.schlessinger@yale.edu Accepted 2009-Not a month!-23 by JYOTI. 23-Feb-2010: Contacted by JYOTI. Cell (0092-8674) 2009 jyoti Only protein-protein interactions 6 imex curation The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site. The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site. Cell (0092-8674) 2009 imex curation Bae JH., Lew ED., Yuzawa S., Tome F., Lax I., Schlessinger J. Synapse - Interactions of proteins with an established role in the presynapse. joseph.schlessinger@yale.edu 23-Feb-2010: Contacted by JYOTI. jyoti Only protein-protein interactions 6 in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Bae JH., Lew ED., Yuzawa S., Tome F., Lax I., Schlessinger J. Synapse - Interactions of proteins with an established role in the presynapse. Chemically synthesied FGFR peptide is conserved across multiple species so I have therefore matched the species to the other protein in the entry. joseph.schlessinger@yale.edu Accepted 2009-Not a month!-23 by JYOTI. 23-Feb-2010: Contacted by JYOTI. Cell (0092-8674) 2009 jyoti Only protein-protein interactions 6 imex curation The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site. The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site. Cell (0092-8674) 2009 imex curation Bae JH., Lew ED., Yuzawa S., Tome F., Lax I., Schlessinger J. Synapse - Interactions of proteins with an established role in the presynapse. joseph.schlessinger@yale.edu 23-Feb-2010: Contacted by JYOTI. jyoti Only protein-protein interactions 6 rat-l6 Rattus norvegicus l6 Rat L6 myotube cell line anti bait coip anti bait coimmunoprecipitation anti bait coip predetermined predetermined participant predetermined Bae JH., Lew ED., Yuzawa S., Tome F., Lax I., Schlessinger J. Synapse - Interactions of proteins with an established role in the presynapse. Chemically synthesied FGFR peptide is conserved across multiple species so I have therefore matched the species to the other protein in the entry. joseph.schlessinger@yale.edu Accepted 2009-Not a month!-23 by JYOTI. 23-Feb-2010: Contacted by JYOTI. Cell (0092-8674) 2009 jyoti Only protein-protein interactions 6 imex curation plcg1_rat 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 Phosphoinositide phospholipase C-gamma-1 Phospholipase C-gamma-1 Plcg1 protein protein rat Rattus norvegicus (Rat) Rat MAGVGTPCANGCGPSAPSEAEVLHLCRSLEVGTVMTLFYSKKSQRPERKTFQVKLETRQITWSRGADKIEGSIDIREIKEIRPGKTSRDFDRYQEDPAFRPDQSHCFVILYGMEFRLKTLSLQATSEDEVNMWIKGLTWLMEDTLQAATPLQIERWLRKQFYSVDRNREDRISAKDLKNMLSQVNYRVPNMRFLRERLTDFEQRSGDITYGQFAQLYRSLMYSAQKTMDLPFLETNTLRTGERPELCQVSLSEFQQFLLEYQGELWAVDRLQVQEFMLSFLRDPLREIEEPYFFLDELVTFLFSKENSVWNSQLDAVCPETMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMGCRCIELDCWDGPDGMPVIYHGHTLTTKIKFSDVLHTIKEHAFVASEYPVILSIEDHCSIAQQRNMAQHFRKVLGDTLLTKPVDIAADGLPSPNQLKRKILIKHKKLAEGSAYEEVPTSVMYSENDISNSIKNGILYLEDPVNHEWYPHYFVLTSSKIYYSEETSSDQGNEDEEEPKEASGSTELHSSEKWFHGKLGAGRDGRHIAERLLTEYCIETGAPDGSFLVRESETFVGDYTLSFWRNGKVQHCRIHSRQDAGTPKFFLTDNLVFDSLYDLITHYQQVPLRCNEFEMRLSEPVPQTNAHESKEWYHASLTRAQAEHMLMRVPRDGAFLVRKRNEPNSYAISFRAEGKIKHCRVQQEGQTVMLGNSEFDSLVDLISYYEKHPLYRKMKLRYPINEEALEKIGTAEPDYGALYEGRNPGFYVEANPMPTFKCAVKALFDYKAQREDELTFTKSAIIQNVEKQDGGWWRGDYGGKKQLWFPSNYVEEMINPAILEPEREHLDENSPLGDLLRGVLDVPACQIAIRPEGKNNRLFVFSISMPSVAQWSLDVAADSQEELQDWVKKIREVAQTADARLTEGKMMERRKKIALELSELVVYCRPVPFDEEKIGTERACYRDMSSFPETKAEKYVNKAKGKKFLQYNRLQLSRIYPKGQRLDSSNYDPLPMWICGSQLVALNFQTPDKPMQMNQALFMAGGHCGYVLQPSTMRDEAFDPFDKSSLRGLEPCVICIEVLGARHLPKNGRGIVCPFVEIEVAGAEYDSTKQKTEFVVDNGLNPVWPAKPFHFQISNPEFAFLRFVVYEEDMFSDQNFLAQATFPVKGLKTGYRAVPLKNNYSEDLELASLLIKIDIFPAKENGDLSPFSGTSLRERASDASSQLFHVRAREGSFEARYQQPFEDFRISQEHLADHFDSRERRAPRRTRVNGDNRL DIP protein P10686 original sequence version: 98 DIP protein P10686 original sequence version: 127 BB3240C27972CE3B fgfr1_rat Fibroblast growth factor receptor 1 Fgfr1 Flg MFR Proto-oncogene c-Fgr Basic fibroblast growth factor receptor 1 protein protein rat Rattus norvegicus (Rat) Rat MWGWRGLLFWAVLVTATLCTARPAPTLPEQAQPWGVPVEVESLLVHPGDLLQLRCRLRDDVQSINWLRDGVQLAESNRTRITGEEVEVRDSIPADSGLYACVTNSPSGSDTTYFSVNVSDALPSSEDDDDDDDSSSEEKETDNTKPNRRPVAPYWTSPEKMEKKLHAVPAAKTVKFKCPSSGTPSPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVALGSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYDQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVLEALEERPAVMTSPLYLEIIIYCTGAFLISCMVGSVIIYKMKSGTKKSDFHSQMAVHKLAKSIPLRRQVTVSADSSASMNSGVLLVRPSRLSSSGTPMLAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPNPGVPVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWNAVPSQRPTFKQLVEDLDRIVALTSNQEYLDLSMPLDQDSPSFPDTRSSTCSSGEDSVFSHEPFPEEPCLPRHPTQLANGGLNRR E59D924D0A1DE5C5 fgfr1_human Fibroblast growth factor receptor 1 FGFR1 FGFBR FLG FLT2 Fms-like tyrosine kinase 2 Proto-oncogene c-Fgr BFGFR CEK HBGFR Basic fibroblast growth factor receptor 1 N-sam protein protein human Homo sapiens Human MWSWKCLLFWAVLVTATLCTARPSPTLPEQAQPWGAPVEVESFLVHPGDLLQLRCRLRDDVQSINWLRDGVQLAESNRTRITGEEVEVQDSVPADSGLYACVTSSPSGSDTTYFSVNVSDALPSSEDDDDDDDSSSEEKETDNTKPNRMPVAPYWTSPEKMEKKLHAVPAAKTVKFKCPSSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVALGSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVLEALEERPAVMTSPLYLEIIIYCTGAFLISCMVGSVIVYKMKSGTKKSDFHSQMAVHKLAKSIPLRRQVTVSADSSASMNSGVLLVRPSRLSSSGTPMLAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVALTSNQEYLDLSMPLDQYSPSFPDTRSSTCSSGEDSVFSHEPLPEEPCLPRHPAQLANGGLKRR DIP protein P11362 original sequence version: 154 DIP protein P11362 original sequence version: 160 DIP protein P11362 original sequence version: 180 DIP protein P11362 original sequence version: 170 93A01B5D78C3E72C fgfr1-plcg1-1 1 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 P11362:p.[Tyr463Phe;Tyr583Phe;Tyr585Phe] mutation mutation certain certain sequence position certain certain certain sequence position certain Y F certain certain sequence position certain certain certain sequence position certain Y F certain certain sequence position certain certain certain sequence position certain Y F Fri Jul 22 11:04:41 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr583phe,tyr585phe,tyr463phe' Wed May 02 18:01:14 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr463phe,tyr583phe,tyr585phe' Tue Jun 30 16:07:40 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Tyr463Phe;Tyr583Phe;Tyr585Phe]' ecoli Escherichia coli (strain K12) 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 ecoli Escherichia coli (strain K12) 12 9 direct interaction direct interaction Crystal Structure of Activated FGFR1 in Complex with a PLCγ Fragment Fig. 2, 2.5A R-factor: 24.9%, Free R-factor: 28.9% fgfr1-plcg1-2 2 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) 4 unspecified role unspecified role neutral component neutral component n-terminal sh2 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 15 17 direct interaction direct interaction ITC curves for the interaction of the SH2 domains of PLCγ with either an FGFR1-derived phosphopeptide Fig. 6, Supp. Table 2 fgfr1-plcg1-3 2 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) 4 unspecified role unspecified role neutral component neutral component c-terminal sh2 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 22 20 direct interaction direct interaction ITC curves for the interaction of the SH2 domains of PLCγ with either an FGFR1-derived phosphopeptide Fig. 6, Supp. Table 2 fgfr1-plcg1-4 2 4 unspecified role unspecified role neutral component neutral component n-terminal sh2 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 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 P11362:p.[Tyr463Phe;Tyr583Phe;Tyr585Phe;Tyr730Phe] mutation mutation certain certain sequence position certain certain certain sequence position certain Y F certain certain sequence position certain certain certain sequence position certain Y F certain certain sequence position certain certain certain sequence position certain Y F certain certain sequence position certain certain certain sequence position certain Y F Fri Jul 22 11:13:16 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr463phe,tyr585phe,tyr583phe,tyr730phe' Wed May 02 20:12:06 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr463phe,tyr583phe,tyr585phe,tyr730phe' Tue Jun 30 19:34:42 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Tyr463Phe;Tyr583Phe;Tyr585Phe;Tyr730Phe]' ecoli Escherichia coli (strain K12) 25 27 direct interaction direct interaction In stark contrast, the N-SH2 domain binds 10�40 times more tightly to FGFR1-3P than the binding of the N-SH2 or C-SH2 domain to the pY766 peptide, with a dissociation constant of 33 � 1 nM. Fig. 6, Supp. Table 2 fgfr1-plcg1-5 2 4 unspecified role unspecified role neutral component neutral component c-terminal sh2 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 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 P11362:p.[Tyr463Phe;Tyr583Phe;Tyr585Phe;Tyr730Phe] mutation mutation certain certain sequence position certain certain certain sequence position certain Y F certain certain sequence position certain certain certain sequence position certain Y F certain certain sequence position certain certain certain sequence position certain Y F certain certain sequence position certain certain certain sequence position certain Y F Fri Jul 22 10:52:00 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr463phe,tyr585phe,tyr583phe,tyr730phe' Wed May 02 20:01:25 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr463phe,tyr583phe,tyr585phe,tyr730phe' Tue Jun 30 17:59:48 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Tyr463Phe;Tyr583Phe;Tyr585Phe;Tyr730Phe]' ecoli Escherichia coli (strain K12) 31 33 direct interaction direct interaction The C-SH2 domain binds to the intact FGFR1-3P kinase domain with a similar dissociation constant of 0.5 μM. Fig. 6, Supp. Table 2 fgfr1-plcg1-6 3 4 unspecified role unspecified role prey prey 6 unspecified role unspecified role bait bait P11362:p.Arg609Val mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R V Wed May 02 18:00:42 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg609val' Tue Jun 30 20:21:26 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg609Val' P11362:p.Asp755Val mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain D V Wed May 02 17:14:28 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp755val' Tue Jun 30 18:58:28 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp755Val' P11362:p.Tyr766Phe mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Y F Wed May 02 18:48:59 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr766phe' Tue Jun 30 20:07:13 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr766Phe' P11362:p.[Arg609Val;Asp755Val] mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R V certain certain sequence position certain certain certain sequence position certain D V Wed May 02 16:44:05 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg609val,asp755val' Tue Jun 30 18:16:44 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Arg609Val;Asp755Val]' P11362:p.[Val636Asp;Val758Asp] mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain V D certain certain sequence position certain certain certain sequence position certain V D Wed May 02 15:17:56 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'val636asp,val758asp' Tue Jun 30 17:35:43 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Val636Asp;Val758Asp]' physical association physical association Lysates from FGF1-stimulated or unstimulated cells were subjected to immunoprecipitation with anti-FGFR1 antibodies or anti-PLCγ antibodies followed by immunoblotting with anti-PLCγ antibodies. Fig. 7A Fibroblast growth factor (FGF)