ID SRC_MOUSE STANDARD; PRT; 540 AA. AC P05480; DT 01-NOV-1988 (Rel. 09, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE NEURONAL PROTO-ONCOGENE TYROSINE-PROTEIN KINASE SRC (EC 2.7.1.112) DE (P60-SRC) (C-SRC). GN SRC. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=BALB/C; RX MEDLINE=87263406; PubMed=2440106; RA Martinez R., Mathey-Prevot B., Bernards A., Baltimore D.; RT "Neuronal pp60c-src contains a six-amino acid insertion relative to RT its non-neuronal counterpart."; RL Science 237:411-415(1987). CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP + CC PROTEIN TYROSINE PHOSPHATE. CC -!- SIMILARITY: CONTAINS 1 SH2 DOMAIN. CC -!- SIMILARITY: CONTAINS 1 SH3 DOMAIN. CC -!- SIMILARITY: TO OTHER PROTEIN-TYROSINE KINASES IN THE CATALYTIC CC DOMAIN. BELONGS TO THE SRC SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M17031; AAA40135.1; -. DR PIR; A43610; A43610. DR HSSP; P12931; 1HCT. DR MGD; MGI:98397; Src. DR INTERPRO; IPR000719; -. DR INTERPRO; IPR000980; -. DR INTERPRO; IPR001245; -. DR INTERPRO; IPR001452; -. DR PFAM; PF00017; SH2; 1. DR PFAM; PF00018; SH3; 1. DR PFAM; PF00069; pkinase; 1. DR PRINTS; PR00109; TYRKINASE. DR PRINTS; PR00401; SH2DOMAIN. DR PRINTS; PR00452; SH3DOMAIN. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS50001; SH2; 1. DR PROSITE; PS50002; SH3; 1. KW Transferase; Tyrosine-protein kinase; Proto-oncogene; Phosphorylation; KW ATP-binding; Myristate; SH3 domain; SH2 domain. FT INIT_MET 0 0 BY SIMILARITY. FT LIPID 1 1 MYRISTATE (BY SIMILARITY). FT DOMAIN 82 149 SH3. FT DOMAIN 155 252 SH2. FT DOMAIN 274 527 PROTEIN KINASE. FT NP_BIND 280 288 ATP (BY SIMILARITY). FT BINDING 302 302 ATP (BY SIMILARITY). FT ACT_SITE 393 393 BY SIMILARITY. FT MOD_RES 423 423 PHOSPHORYLATION (AUTO-) (BY SIMILARITY). FT MOD_RES 534 534 PHOSPHORYLATION (BY SIMILARITY). SQ SEQUENCE 540 AA; 60487 MW; 424BA0EEE5D752AA CRC64; GSNKSKPKDA SQRRRSLEPS ENVHGAGGAF PASQTPSKPA SADGHRGPSA AFVPPAAEPK LFGGFNSSDT VTSPQRAGAL AGGVTTFVAL YDYESRTETD LSFKKGERLQ IVNNTRKVDV REGDWWLAHS LSTGQTGYIP SNYVAPSDSI QAEEWYFGKI TRRESERLLL NAENPRGTFL VRESETTKGA YCLSVSDFDN AKGLNVKHYK IRKLDSGGFY ITSRTQFNSL QQLVAYYSKH ADGLCHRLTT VCPTSKPQTQ GLAKDAWEIP RESLRLEVKL GQGCFGEVWM GTWNGTTRVA IKTLKPGTMS PEAFLQEAQV MKKLRHEKLV QLYAVVSEEP IYIVTEYMNK GSLLDFLKGE TGKYLRLPQL VDMSAQIASG MAYVERMNYV HRDLRAANIL VGENLVCKVA DFGLARLIED NEYTARQGAK FPIKWTAPEA ALYGRFTIKS DVWSFGILLT ELTTKGRVPY PGMVNREVLD QVERGYRMPC PPECPESLHD LMCQCWRKEP EERPTFEYLQ AFLEDYFTST EPQYQPGENL //