ID SRC1_XENLA STANDARD; PRT; 531 AA. AC P13115; DT 01-JAN-1990 (Rel. 13, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 01-NOV-1995 (Rel. 32, Last annotation update) DE TYROSINE-PROTEIN KINASE SRC-1 (EC 2.7.1.112) (P60-SRC-1). GN SRC-1. OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus. OX NCBI_TaxID=8355; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89278134; PubMed=2499582; RA Steele R.E., Unger T.F., Mardis M.J., Fero J.B.; RT "The two Xenopus laevis SRC genes are co-expressed and each produces RT functional pp60src."; RL J. Biol. Chem. 264:10649-10653(1989). 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; M24704; AAA49962.1; -. DR PIR; A34104; A34104. 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; ATP-binding; Tyrosine-protein kinase; Phosphorylation; KW Myristate; SH3 domain; SH2 domain. FT INIT_MET 0 0 BY SIMILARITY. FT LIPID 1 1 MYRISTATE (BY SIMILARITY). FT DOMAIN 79 140 SH3. FT DOMAIN 146 243 SH2. FT DOMAIN 265 518 PROTEIN KINASE. FT NP_BIND 271 279 ATP (BY SIMILARITY). FT BINDING 293 293 ATP (BY SIMILARITY). FT ACT_SITE 384 384 BY SIMILARITY. FT MOD_RES 414 414 PHOSPHORYLATION (AUTO-) (BY SIMILARITY). SQ SEQUENCE 531 AA; 59725 MW; 19A8FFDC11E3BACE CRC64; GATKSKPREG GPRSRSLDIV EGSHQPFTSL SASQTPNKSL DSHRPPAQPF GGNCDLTPFG GINFSDTITS PQRTGPLAGG VTTFVALYDY ESRTETDLSF KKGERLQIVN NTEGDWWLAR SLSSGQTGYI PSNYVAPSDS IQAEEWYLGK ITRREAERLL LSLENPRGTF LVRESETTKG AYCLSVSDYD ANRGLNVKHY KIRKLDSGGF YITSRTQFSS LQQLVAYYSK HADGLCHRLT AVCPTAKPQT QGLSRDAWEI PRDSLRLELK LGQGCFGEVW MGTWNGTTRV AIKTLKPGTM SPEAFLQEAQ VMKKLRHEKL VQLYAVVSEE PIYIVTEYMS KGSLLDFLKG EMGRYLRLPQ LVDMAAQIAS GMAYVERMNY VHRDLRAANI LVGENLVCKV ADFGLARLIE DNEYTARQGA KFPIKWTAPE AALYGRFTIK SDVWSFGILL TELTTKGRVP YPGMVNREVL DQVERGYRMP CPPDCPESLH DLMFQCWRKD PEERPTFEYL QAFLEDYFTA TEPQYQPGDN L //