DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structural and functional integration of the PLCγ interaction domains critical for regulatory mechanisms and signaling deregulation. Structural and functional integration of the PLCγ interaction domains critical for regulatory mechanisms and signaling deregulation. Structure (London, England : 1993) 2012 imex curation Bunney TD., Esposito D., Mas-Droux C., Lamber E., Baxendale RW., Martins M., Cole A., Svergun D., Driscoll PC., Katan M. Only protein-protein interactions in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Bunney TD., Esposito D., Mas-Droux C., Lamber E., Baxendale RW., Martins M., Cole A., Svergun D., Driscoll PC., Katan M. DIP original experiment: DIP-251325X Structure (London, England : 1993) 2012 IMEx Structural and functional integration of the PLCγ interaction domains critical for regulatory mechanisms and signaling deregulation. Structural and functional integration of the PLCγ interaction domains critical for regulatory mechanisms and signaling deregulation. Structural and functional integration of the PLCγ interaction domains critical for regulatory mechanisms and signaling deregulation. Structure (London, England : 1993) 2012 imex curation Bunney TD., Esposito D., Mas-Droux C., Lamber E., Baxendale RW., Martins M., Cole A., Svergun D., Driscoll PC., Katan M. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Bunney TD., Esposito D., Mas-Droux C., Lamber E., Baxendale RW., Martins M., Cole A., Svergun D., Driscoll PC., Katan M. DIP original experiment: DIP-251324X Structure (London, England : 1993) 2012 IMEx Structural and functional integration of the PLCγ interaction domains critical for regulatory mechanisms and signaling deregulation. Structural and functional integration of the PLCγ interaction domains critical for regulatory mechanisms and signaling deregulation. Structural and functional integration of the PLCγ interaction domains critical for regulatory mechanisms and signaling deregulation. Structure (London, England : 1993) 2012 imex curation Bunney TD., Esposito D., Mas-Droux C., Lamber E., Baxendale RW., Martins M., Cole A., Svergun D., Driscoll PC., Katan M. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Bunney TD., Esposito D., Mas-Droux C., Lamber E., Baxendale RW., Martins M., Cole A., Svergun D., Driscoll PC., Katan M. DIP original experiment: DIP-251327X Structure (London, England : 1993) 2012 IMEx Structural and functional integration of the PLCγ interaction domains critical for regulatory mechanisms and signaling deregulation. Structural and functional integration of the PLCγ interaction domains critical for regulatory mechanisms and signaling deregulation. Structural and functional integration of the PLCγ interaction domains critical for regulatory mechanisms and signaling deregulation. Structure (London, England : 1993) 2012 imex curation Bunney TD., Esposito D., Mas-Droux C., Lamber E., Baxendale RW., Martins M., Cole A., Svergun D., Driscoll PC., Katan M. Only protein-protein interactions in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Bunney TD., Esposito D., Mas-Droux C., Lamber E., Baxendale RW., Martins M., Cole A., Svergun D., Driscoll PC., Katan M. DIP original experiment: DIP-251326X Structure (London, England : 1993) 2012 IMEx Structural and functional integration of the PLCγ interaction domains critical for regulatory mechanisms and signaling deregulation. Structural and functional integration of the PLCγ interaction domains critical for regulatory mechanisms and signaling deregulation. Structural and functional integration of the PLCγ interaction domains critical for regulatory mechanisms and signaling deregulation. Structure (London, England : 1993) 2012 imex curation Bunney TD., Esposito D., Mas-Droux C., Lamber E., Baxendale RW., Martins M., Cole A., Svergun D., Driscoll PC., Katan M. Only protein-protein interactions in vitro In vitro protein kinase assay protein kinase assay predetermined predetermined participant predetermined Bunney TD., Esposito D., Mas-Droux C., Lamber E., Baxendale RW., Martins M., Cole A., Svergun D., Driscoll PC., Katan M. DIP original experiment: DIP-251323X Structure (London, England : 1993) 2012 IMEx Structural and functional integration of the PLCγ interaction domains critical for regulatory mechanisms and signaling deregulation. pgfrb_human Platelet-derived growth factor receptor beta CD140 antigen-like family member B PDGFRB Beta-type platelet-derived growth factor receptor PDGFR Platelet-derived growth factor receptor 1 Beta platelet-derived growth factor receptor PDGFR1 protein protein human Homo sapiens Human MRLPGAMPALALKGELLLLSLLLLLEPQISQGLVVTPPGPELVLNVSSTFVLTCSGSAPVVWERMSQEPPQEMAKAQDGTFSSVLTLTNLTGLDTGEYFCTHNDSRGLETDERKRLYIFVPDPTVGFLPNDAEELFIFLTEITEITIPCRVTDPQLVVTLHEKKGDVALPVPYDHQRGFSGIFEDRSYICKTTIGDREVDSDAYYVYRLQVSSINVSVNAVQTVVRQGENITLMCIVIGNEVVNFEWTYPRKESGRLVEPVTDFLLDMPYHIRSILHIPSAELEDSGTYTCNVTESVNDHQDEKAINITVVESGYVRLLGEVGTLQFAELHRSRTLQVVFEAYPPPTVLWFKDNRTLGDSSAGEIALSTRNVSETRYVSELTLVRVKVAEAGHYTMRAFHEDAEVQLSFQLQINVPVRVLELSESHPDSGEQTVRCRGRGMPQPNIIWSACRDLKRCPRELPPTLLGNSSEEESQLETNVTYWEEEQEFEVVSTLRLQHVDRPLSVRCTLRNAVGQDTQEVIVVPHSLPFKVVVISAILALVVLTIISLIILIMLWQKKPRYEIRWKVIESVSSDGHEYIYVDPMQLPYDSTWELPRDQLVLGRTLGSGAFGQVVEATAHGLSHSQATMKVAVKMLKSTARSSEKQALMSELKIMSHLGPHLNVVNLLGACTKGGPIYIITEYCRYGDLVDYLHRNKHTFLQHHSDKRRPPSAELYSNALPVGLPLPSHVSLTGESDGGYMDMSKDESVDYVPMLDMKGDVKYADIESSNYMAPYDNYVPSAPERTCRATLINESPVLSYMDLVGFSYQVANGMEFLASKNCVHRDLAARNVLICEGKLVKICDFGLARDIMRDSNYISKGSTFLPLKWMAPESIFNSLYTTLSDVWSFGILLWEIFTLGGTPYPELPMNEQFYNAIKRGYRMAQPAHASDEIYEIMQKCWEEKFEIRPPFSQLVLLLERLLGEGYKKKYQQVDEEFLRSDHPAILRSQARLPGFHGLRSPLDTSSVLYTAVQPNEGDNDYIIPLPDPKPEVADEGPLEGSPSLASSTLNEVNTSSTISCDSPLEPQDEPEPEPQLELQVEPEPELEQLPDSGCPAPRAEAEDSFL DIP protein P09619 original sequence version: 176 DIP protein P09619 original sequence version: 185 DIP protein P09619 original sequence version: 114 DIP protein P09619 original sequence version: 162 DIP protein P09619 original sequence version: 150 DIP protein P09619 original sequence version: 165 DIP protein P09619 original sequence version: 161 038C15E531D6E89D plcg1_human 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 PLC-148 PLC1 Phospholipase C-II PLCG1 Phosphoinositide phospholipase C-gamma-1 Phospholipase C-gamma-1 protein protein human Homo sapiens Human MAGAASPCANGCGPGAPSDAEVLHLCRSLEVGTVMTLFYSKKSQRPERKTFQVKLETRQITWSRGADKIEGAIDIREIKEIRPGKTSRDFDRYQEDPAFRPDQSHCFVILYGMEFRLKTLSLQATSEDEVNMWIKGLTWLMEDTLQAPTPLQIERWLRKQFYSVDRNREDRISAKDLKNMLSQVNYRVPNMRFLRERLTDLEQRSGDITYGQFAQLYRSLMYSAQKTMDLPFLEASTLRAGERPELCRVSLPEFQQFLLDYQGELWAVDRLQVQEFMLSFLRDPLREIEEPYFFLDEFVTFLFSKENSVWNSQLDAVCPDTMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMGCRCIELDCWDGPDGMPVIYHGHTLTTKIKFSDVLHTIKEHAFVASEYPVILSIEDHCSIAQQRNMAQYFKKVLGDTLLTKPVEISADGLPSPNQLKRKILIKHKKLAEGSAYEEVPTSMMYSENDISNSIKNGILYLEDPVNHEWYPHYFVLTSSKIYYSEETSSDQGNEDEEEPKEVSSSTELHSNEKWFHGKLGAGRDGRHIAERLLTEYCIETGAPDGSFLVRESETFVGDYTLSFWRNGKVQHCRIHSRQDAGTPKFFLTDNLVFDSLYDLITHYQQVPLRCNEFEMRLSEPVPQTNAHESKEWYHASLTRAQAEHMLMRVPRDGAFLVRKRNEPNSYAISFRAEGKIKHCRVQQEGQTVMLGNSEFDSLVDLISYYEKHPLYRKMKLRYPINEEALEKIGTAEPDYGALYEGRNPGFYVEANPMPTFKCAVKALFDYKAQREDELTFIKSAIIQNVEKQEGGWWRGDYGGKKQLWFPSNYVEEMVNPVALEPEREHLDENSPLGDLLRGVLDVPACQIAIRPEGKNNRLFVFSISMASVAHWSLDVAADSQEELQDWVKKIREVAQTADARLTEGKIMERRKKIALELSELVVYCRPVPFDEEKIGTERACYRDMSSFPETKAEKYVNKAKGKKFLQYNRLQLSRIYPKGQRLDSSNYDPLPMWICGSQLVALNFQTPDKPMQMNQALFMTGRHCGYVLQPSTMRDEAFDPFDKSSLRGLEPCAISIEVLGARHLPKNGRGIVCPFVEIEVAGAEYDSTKQKTEFVVDNGLNPVWPAKPFHFQISNPEFAFLRFVVYEEDMFSDQNFLAQATFPVKGLKTGYRAVPLKNNYSEDLELASLLIKIDIFPAKENGDLSPFSGTSLRERGSDASGQLFHGRAREGSFESRYQQPFEDFRISQEHLADHFDSRERRAPRRTRVNGDNRL DIP protein P19174 original sequence version: 144 DIP protein P19174 original sequence version: 152 DIP protein P19174 original sequence version: 181 DIP protein P19174 original sequence version: 169 AE05ABE2A18EDDAC 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-plcg1-12 5 7 enzyme target enzyme target substrate substrate unspecified role unspecified role pY186/Y472/Y481/Y771/Y775/Y783/Y959/Y977/Y1254 pY186/Y472/Y481/Y771/Y775/Y783/Y959/Y977/Y1254 optyr O4'-phospho-L-tyrosine (2S)-2-amino-3-(4-phosphonooxyphenyl)propanoic acid 2-azanyl-3-(4-phosphonooxyphenyl)propanoic acid MOD_RES Phosphotyrosine O4-phosphotyrosine tyrosine phosphate 2-amino-3-(4-hydroxyphenyl)propanoic acid 4'-phosphate O4'-phospho-L-tyrosine O4'-phosphorylated L-tyrosine OPTyr Phospho Phospho Tyrosinyl Phosphorylation phosphorylationy modified residue ms mass detection of residue modification modified residue ms certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain human Homo sapiens Human 8 enzyme enzyme unspecified role unspecified role Kinase domain Region 456-774 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli phosphorylation phosphorylation reaction phosphorylation fgfr1-plcg1-13 1 7 unspecified role unspecified role prey prey P19174:p.Arg586Leu R586L mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain R L This feature has been corrected as a result of our quality control procedures. The original label was 'R586L'. Wed May 02 18:01:00 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg586leu' Tue Jun 30 16:33:01 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg586Leu' human Homo sapiens Human 8 unspecified role unspecified role bait bait Kinase domain Region 456-774 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P11362:p.[Leu457Val;Tyr463Phe;Cys488Ala;Tyr583Phe;Cys584Ser;Tyr585Phe] L457V/Y463F/C488A/Y583F/C584S/Y585F mutation mutation certain certain sequence position certain certain certain sequence position certain Y F certain certain sequence position certain certain certain sequence position certain C S certain certain sequence position certain certain certain sequence position certain Y F certain certain sequence position certain certain certain sequence position certain C A certain certain sequence position certain certain certain sequence position certain Y F certain certain sequence position certain certain certain sequence position certain L V This feature has been corrected as a result of our quality control procedures. The original label was 'L457V/Y463F/C488A/Y583F/C584S/Y585F'. Wed May 02 17:02:08 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu457val,tyr463phe,cys488ala,tyr583phe,cys584ser,tyr585phe' Tue Jun 30 19:37:54 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Leu457Val;Tyr463Phe;Cys488Ala;Tyr583Phe;Cys584Ser;Tyr585Phe]' pY653/Y654/Y766 pY653/Y654/Y766 optyr O4'-phospho-L-tyrosine (2S)-2-amino-3-(4-phosphonooxyphenyl)propanoic acid 2-azanyl-3-(4-phosphonooxyphenyl)propanoic acid MOD_RES Phosphotyrosine O4-phosphotyrosine tyrosine phosphate 2-amino-3-(4-hydroxyphenyl)propanoic acid 4'-phosphate O4'-phospho-L-tyrosine O4'-phosphorylated L-tyrosine OPTyr Phospho Phospho Tyrosinyl Phosphorylation phosphorylationy certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain StrepII-tag StrepII-tag strep ii tag strep ii tag Strep (II) Strep II Strep (II) Strep II n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli direct interaction direct interaction pdgfrb-plcg1-6 2 6 unspecified role unspecified role unspecified role unspecified role Region 1018-1029 Region 1018-1029 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain pY1021 pY1021 optyr O4'-phospho-L-tyrosine (2S)-2-amino-3-(4-phosphonooxyphenyl)propanoic acid 2-azanyl-3-(4-phosphonooxyphenyl)propanoic acid MOD_RES Phosphotyrosine O4-phosphotyrosine tyrosine phosphate 2-amino-3-(4-hydroxyphenyl)propanoic acid 4'-phosphate O4'-phospho-L-tyrosine O4'-phosphorylated L-tyrosine OPTyr Phospho Phospho Tyrosinyl Phosphorylation phosphorylationy certain certain sequence position certain certain certain sequence position certain in vitro In vitro 7 unspecified role unspecified role unspecified role unspecified role nSH2-cSH2 domain Region 545-790 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction fgfr1-plcg1-14 3 7 unspecified role unspecified role unspecified role unspecified role nSH2-cSH2 domain Region 545-790 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain P19174:p.[Tyr771Phe;Tyr775Phe] Y771F/Y775F 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 This feature has been corrected as a result of our quality control procedures. The original label was 'Y771F/Y775F'. Wed May 02 15:11:28 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr771phe,tyr775phe' 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.[Tyr771Phe;Tyr775Phe]' pY783 pY783 optyr O4'-phospho-L-tyrosine (2S)-2-amino-3-(4-phosphonooxyphenyl)propanoic acid 2-azanyl-3-(4-phosphonooxyphenyl)propanoic acid MOD_RES Phosphotyrosine O4-phosphotyrosine tyrosine phosphate 2-amino-3-(4-hydroxyphenyl)propanoic acid 4'-phosphate O4'-phospho-L-tyrosine O4'-phosphorylated L-tyrosine OPTyr Phospho Phospho Tyrosinyl Phosphorylation phosphorylationy certain certain sequence position certain certain certain sequence position certain decreasing-ptm ptm decreasing an interaction decreasing-ptm ecolx Escherichia coli 8 unspecified role unspecified role unspecified role unspecified role Kinase domain Region 456-774 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P11362:p.[Leu457Val;Tyr463Phe;Cys488Ala;Tyr583Phe;Cys584Ser;Tyr585Phe;Tyr653Phe;Tyr654Phe] L457V/Y463F/C488A/Y583F/C584S/Y585F/Y653F/Y654F 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 C S certain certain sequence position certain certain certain sequence position certain Y F certain certain sequence position certain certain certain sequence position certain C A certain certain sequence position certain certain certain sequence position certain Y F certain certain sequence position certain certain certain sequence position certain L V This feature has been corrected as a result of our quality control procedures. The original label was 'L457V/Y463F/C488A/Y583F/C584S/Y585F/Y653F/Y654F'. Wed May 02 19:48:43 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu457val,tyr463phe,cys488ala,tyr583phe,cys584ser,tyr585phe,tyr653phe,tyr654phe' Tue Jun 30 18:58:47 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Leu457Val;Tyr463Phe;Cys488Ala;Tyr583Phe;Cys584Ser;Tyr585Phe;Tyr653Phe;Tyr654Phe]' pY766 pY766 optyr O4'-phospho-L-tyrosine (2S)-2-amino-3-(4-phosphonooxyphenyl)propanoic acid 2-azanyl-3-(4-phosphonooxyphenyl)propanoic acid MOD_RES Phosphotyrosine O4-phosphotyrosine tyrosine phosphate 2-amino-3-(4-hydroxyphenyl)propanoic acid 4'-phosphate O4'-phospho-L-tyrosine O4'-phosphorylated L-tyrosine OPTyr Phospho Phospho Tyrosinyl Phosphorylation phosphorylationy certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction fgfr1-plcg1-15 4 7 unspecified role unspecified role prey prey Region 488-933 Region 488-933 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P19174:p.Tyr783Phe Y783F mutation increasing strength mutation increasing interaction strength mutation increasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain Y F This feature has been corrected as a result of our quality control procedures. The original label was 'Y783F'. Wed May 02 20:28:41 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr783phe' Tue Jun 30 18:18:15 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr783Phe' ecolx Escherichia coli 8 unspecified role unspecified role bait bait Kinase domain Region 456-774 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P11362:p.[Leu457Val;Tyr463Phe;Cys488Ala;Tyr583Phe;Cys584Ser;Tyr585Phe] L457V/Y463F/C488A/Y583F/C584S/Y585F mutation mutation certain certain sequence position certain certain certain sequence position certain Y F certain certain sequence position certain certain certain sequence position certain C S certain certain sequence position certain certain certain sequence position certain Y F certain certain sequence position certain certain certain sequence position certain C A certain certain sequence position certain certain certain sequence position certain Y F certain certain sequence position certain certain certain sequence position certain L V This feature has been corrected as a result of our quality control procedures. The original label was 'L457V/Y463F/C488A/Y583F/C584S/Y585F'. Wed May 02 15:05:53 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu457val,tyr463phe,cys488ala,tyr583phe,cys584ser,tyr585phe' Tue Jun 30 17:36:23 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Leu457Val;Tyr463Phe;Cys488Ala;Tyr583Phe;Cys584Ser;Tyr585Phe]' pY653/Y654/Y766 pY653/Y654/Y766 optyr O4'-phospho-L-tyrosine (2S)-2-amino-3-(4-phosphonooxyphenyl)propanoic acid 2-azanyl-3-(4-phosphonooxyphenyl)propanoic acid MOD_RES Phosphotyrosine O4-phosphotyrosine tyrosine phosphate 2-amino-3-(4-hydroxyphenyl)propanoic acid 4'-phosphate O4'-phospho-L-tyrosine O4'-phosphorylated L-tyrosine OPTyr Phospho Phospho Tyrosinyl Phosphorylation phosphorylationy certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain StrepII-tag StrepII-tag strep ii tag strep ii tag Strep (II) Strep II Strep (II) Strep II n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli direct interaction direct interaction