ID SRC_RSVSR STANDARD; PRT; 526 AA. AC P00524; DT 21-JUL-1986 (Rel. 01, Created) DT 01-JUL-1989 (Rel. 11, Last sequence update) DT 15-JUL-1998 (Rel. 36, 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 Schmidt-Ruppin). OC Viruses; Retroid viruses; Retroviridae; Avian type C retroviruses. OX NCBI_TaxID=11889; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89160256; PubMed=2537953; RA Barnier J.V., Dezelee P., Marx M., Calothy G.; RT "Nucleotide sequence of the src gene of the Schmidt-Ruppin strain of RT Rous sarcoma virus type E."; RL Nucleic Acids Res. 17:1252-1252(1989). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=83141780; PubMed=6298633; RA Czernilofsky A.P., Levinson A.D., Varmus H.E., Bishop J.M., RA Tischer E., Goodman H.; RT "Corrections to the nucleotide sequence of the src gene of Rous RT sarcoma virus."; RL Nature 301:736-738(1983). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=83155664; PubMed=6299580; RA Takeya T., Hanafusa H.; RT "Structure and sequence of the cellular gene homologous to the RSV src RT gene and the mechanism for generating the transforming virus."; RL Cell 32:881-890(1983). RN [4] 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). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 148-245 (SH2 DOMAIN). RX MEDLINE=92357140; PubMed=1379696; RA Waksman G., Kominos D., Robertson S.C., Pant N., Baltimore D., RA Birge R.B., Cowburn D., Hanafusa H., Mayer B.J., Overduin M., RA Resh M.D., Rios C.B., Silverman L., Kuriyan J.; RT "Crystal structure of the phosphotyrosine recognition domain SH2 of v- RT src complexed with tyrosine-phosphorylated peptides."; RL Nature 358:646-653(1992). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 144-247 (SH2 DOMAIN). RX MEDLINE=93201600; PubMed=7680960; RA Waksman G., Shoelson S.E., Pant N., Cowburn D., Kuriyan J.; RT "Binding of a high affinity phosphotyrosyl peptide to the Src SH2 RT domain: crystal structures of the complexed and peptide-free forms."; RL Cell 72:779-790(1993). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 146-247 (SH2 DOMAIN). RX MEDLINE=98038574; PubMed=9371236; RA Plummer M.S., Holland D.R., Shahripour A., Lunney E.A., Fergus J.H., RA Marks J.S., McConnell P., Mueller W.T., Sawyer T.K.; RT "Design, synthesis, and cocrystal structure of a nonpeptide Src SH2 RT domain ligand."; RL J. Med. Chem. 40:3719-3725(1997). 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; L29199; AAA42563.1; -. DR EMBL; X13745; CAA32012.1; -. DR EMBL; V01169; CAA24495.1; -. DR PIR; A00631; TVFV60. DR PDB; 1SHA; 31-OCT-93. DR PDB; 1SHB; 31-OCT-93. DR PDB; 1SPR; 31-MAY-94. DR PDB; 1SPS; 31-JUL-94. DR PDB; 1SKJ; 25-FEB-98. 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; 3D-structure. 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-). FT CONFLICT 10 10 G -> D (IN REF. 2 AND 3). FT CONFLICT 63 63 D -> G (IN REF. 2). FT CONFLICT 96 96 I -> T (IN REF. 3). FT CONFLICT 124 124 V -> L (IN REF. 2). FT CONFLICT 301 301 T -> N (IN REF. 3). FT CONFLICT 320 320 K -> E (IN REF. 2 AND 3). FT CONFLICT 496 496 S -> C (IN REF. 2 AND 3). FT TURN 147 148 FT STRAND 149 149 FT HELIX 155 162 FT TURN 163 163 FT TURN 165 166 FT TURN 169 170 FT STRAND 172 176 FT TURN 181 182 FT STRAND 184 192 FT TURN 193 195 FT STRAND 196 206 FT TURN 208 209 FT STRAND 212 213 FT TURN 216 217 FT STRAND 219 220 FT HELIX 223 230 FT TURN 231 232 FT TURN 235 236 FT STRAND 244 244 SQ SEQUENCE 526 AA; 58953 MW; 85D356B6B8ECB14D CRC64; MGSSKSKPKG PSQRRRSLEP PDSTHHGGFP ASQTPNKTAA PDTHRTPSRS FGTVATEPKL FGDFNTSDTV TSPQRAGALA GGVTTFVALY DYESWIETDL SFKKGERLQI VNNTEGNWWL AHSVTTGQTG YIPSNYVAPS DSIQAEEWYF GKITRRESER LLLNPENPRG TFLVRESETT KGAYCLSVSD FDNAKGLNVK HYKIRKLDSG GFYITSRTQF SSLQQLVAYY SKHADGLCHR LTNVCPTSKP QTQGLAKDAW EIPRESLRLE VKLGQGCFGE VWMGTWNGTT RVAIKTLKPG TMSPEAFLQE AQVMKKLRHK KLVQLYAVVS EEPIYIVIEY MSKGSLLDFL KGEMGKYLRL PQLVDMAAQI ASGMAYVERM NYVHRDLRAA NILVGENLVC KVADFGLARL IEDNEYTARQ GAKFPIKWTA PEAALYGRFT IKSDVWSFGI LLTELTTKGR VPYPGMGNGE VLDRVERGYR MPCPPECPES LHDLMSQCWR RDPEERPTFE YLQAQLLPAC VLEVAE //