ID SRC_RAT STANDARD; PRT; 535 AA. AC Q9WUD9; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE PROTO-ONCOGENE TYROSINE-PROTEIN KINASE SRC (EC 2.7.1.112) (P60-SRC) DE (C-SRC). GN SRC. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SPRAGUE-DAWLEY; TISSUE=TESTIS; RA Stockand J.D., Al-Khalili O., Spier B.J., Eaton D.C.; RT "Rattus norvegicus proto-oncogene encoding tyrosine-protein kinase RT pp60-c-src."; RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases. 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; AF130457; AAD24180.1; -. 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 83 144 SH3. FT DOMAIN 150 247 SH2. FT DOMAIN 269 522 PROTEIN KINASE. FT NP_BIND 275 283 ATP (BY SIMILARITY). FT BINDING 297 297 ATP (BY SIMILARITY). FT ACT_SITE 388 388 BY SIMILARITY. FT MOD_RES 419 419 PHOSPHORYLATION (AUTO-) (BY SIMILARITY). FT MOD_RES 529 529 PHOSPHORYLATION (BY SIMILARITY). SQ SEQUENCE 535 AA; 59946 MW; AD083DD2357890EC CRC64; GSNKSKPKDA SQRRRSLEPA ENVHGAGGAF PASQTPSKPA SADGHRGPNA AFVPPAAAEP KLFGGFNSSD TVTSPQRAGP LAGGVTTFVA LYDYESRTET DLSFKKGERL QIVNNTEGDW WLAHSLSTGQ TGYIPSNYVA PFDSIQAEEW YFGKITRRES ERLLLNAENP RGTFLVRESE TTKGAYCLSV SDFDNAKGLN VKHYKIRKLD SGGFYITSRT QFNSLQQLVA YYSKHADGLC HRLTTVCPTS KPQTQGLAKD AWEIPRESLR LEVKLGQGCF GEVWMGTWNG TTRVAIKTLK PGTMSPEAFL QEAQVMKKLR HEKLVQLYAV VSEEPIYIVT EYMNKGSLLD FLKGETGKYL RLPQLVDMSA QIASGMAYVD RMNYVHRDLR AANILVGENL VCKVADFGLA RLIEDNEYTA RQGAKFPIKW TAPEAALYGR FTIKSDVWSF GILLTELTTK GRVPYPGMVN REVLDQVERG YRMPCPPECP ESLHDLMCQC WRKEPEERPT FEYLQAFLED YFTSTERQYQ PGENL //