ID SRC_RSVH1 STANDARD; PRT; 526 AA. AC P25020; DT 01-MAR-1992 (Rel. 21, Created) DT 01-MAR-1992 (Rel. 21, 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 H-19). OC Viruses; Retroid viruses; Retroviridae; Avian type C retroviruses. OX NCBI_TaxID=11887; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90067864; PubMed=2587228; RA Bodor J., Poliak E., Pichrtova J., Geryk J., Svoboda J.; RT "Complete nucleotide sequence of LTR, v-src, LTR provirus H-19."; RL Nucleic Acids Res. 17:8869-8869(1989). 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 -!- 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; X15345; CAA33404.1; -. DR PIR; S09609; OKFVYR. 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 Transferase; Phosphorylation; ATP-binding; Myristate; KW SH3 domain; SH2 domain. FT LIPID 2 2 MYRISTATE (BY SIMILARITY). 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-) (BY SIMILARITY). SQ SEQUENCE 526 AA; 59075 MW; 33B212BCC943C6AF CRC64; MGSSKSKPKD PSQRRRSLEP PDSTHHGGFP ASQTPDETAA PDAHRNPSRS FGTVATEPKL FWGFNTSDTV TSPQRAGALA GGVTTFVALY DYESWTETDL SFKKGERLQI VNNTEGDWWL AHSLTTGQTG YIPSNYVAPS DSIQAEEWYF GKITRRESER LLLNPENPRG TFLVRKSETA KGAYCLSVSD FDNAKGPNVK HYKICKLYSG GFYITSRTQF GSLQQLVAYY SKHADGLCHR LTNVCPTSKP QTQGLAKDAW EIPRESLRLE AKLGQGCFGE VWMGTWNGTT RVAIKTLKPG TMSPEAFLQE AQVMKKLRHE KLVQLYAVVS EEPIYIVIEY MSKGSLLDFL KGEMGKYLRL PQLVDMAAQI ASGMAYVERM NYVHRDLRAA NILVGENLVC KVADFGLARL IEDNEYTARQ GAKFPIKWTA PEAALYGRFT IKSDVWSFGI LLTELTTKGR VPYPGMVNRE VLDQVERAYR MPCPPECPES LHDLMCQCWR KDPEERPTFK YLQAQLLPAC VLEVAE //