ID SRC_RSVP STANDARD; PRT; 526 AA. AC P00526; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 01-NOV-1995 (Rel. 32, Last annotation update) DE TYROSINE-PROTEIN KINASE TRANSFORMING PROTEIN SRC (EC 2.7.1.112) (P60- DE SRC). GN V-SRC. OS Rous sarcoma virus (strain Prague C). OC Viruses; Retroid viruses; Retroviridae; Avian type C retroviruses. OX NCBI_TaxID=11888; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=83155662; PubMed=6299578; RA Schwartz D., Tizard R., Gilbert W.; RT "Nucleotide sequence of Rous sarcoma virus."; RL Cell 32:853-869(1983). RN [2] RP PHOSPHORYLATION AT TYR-416. RX MEDLINE=81220979; PubMed=6264320; RA Neil J.C., Ghysdael J., Vogt P.K., Smart J.E.; RT "Homologous tyrosine phosphorylation sites in transformation-specific RT gene products of distinct avian sarcoma viruses."; RL Nature 291:675-677(1981). CC -!- FUNCTION: THIS PHOSPHOPROTEIN, REQUIRED FOR BOTH THE INITIATION CC AND THE MAINTENANCE OF NEOPLASTIC TRANSFORMATION, IS A PROTEIN CC KINASE THAT CATALYZES THE PHOSPHORYLATION OF TYROSINE RESIDUES CC IN VITRO. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP + CC PROTEIN TYROSINE PHOSPHATE. CC -!- MISCELLANEOUS: AS A RESULT OF BASE VARIATIONS, RESIDUES 242 AND CC 288 MAY BE REPLACED BY THR AND GLY, RESPECTIVELY. 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; J02342; AAB59935.1; -. DR PIR; A00632; TVFVR. DR HSSP; P00523; 2PTK. 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 Tyrosine-protein kinase; Transforming protein; Oncogene; KW Transferase; Phosphorylation; ATP-binding; Myristate; KW SH3 domain; SH2 domain. FT LIPID 2 2 MYRISTATE. FT DOMAIN 81 142 SH3. FT DOMAIN 148 245 SH2. FT DOMAIN 267 517 PROTEIN KINASE. FT NP_BIND 273 281 ATP (BY SIMILARITY). FT BINDING 295 295 ATP (BY SIMILARITY). FT ACT_SITE 386 386 BY SIMILARITY. FT MOD_RES 416 416 PHOSPHORYLATION (AUTO-). SQ SEQUENCE 526 AA; 59130 MW; 12C12DE33FFFAB11 CRC64; MGSSKSKPKD PSQRRHSLEP PDSTHHGGFP ASQTPDETAA PDAHRNPSRS FGTVATEPKL FWGFNTSDTV TSPQRAGALA GGVTTFVALY DYESWTETDL SFKKGERLQI VNNTEGDWWL AHSLTTGQTG YIPSNYVAPS DSIQAEEWYF GKITRRESER LLLNPENPRG TFLVRKSETA KGAYCLSVSD FDNAKGPNVK HYKIYKLYSG GFYITSRTQF GSLQQLVAYY SKHADGLCHR LANVCPTSKP QTQGLAKDAW EIPRESLRLE AKLGQGCFGE VWMGTWNDTT RVAIKTLKPG TMSPEAFLQE AQVMKKLRHE KLVQLYAVVS EEPIYIVIEY MSKGSLLDFL KGEMGKYLRL PQLVDMAAQI ASGMAYVERM NYVHRDLRAA NILVGENLVC KVADFGLARL IEDNEYTARQ GAKFPIKWTA PEAALYGRFT IKSDVWSFGI LLTELTTKGR VPYPGMVNRE VLDQVERGYR MPCPPECPES LHDLMCQCWR KDPEERPTFK YLQAQLLPAC VLEVAE //