ID YES_XIPHE STANDARD; PRT; 544 AA. AC P27447; DT 01-AUG-1992 (Rel. 23, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 01-NOV-1995 (Rel. 32, Last annotation update) DE PROTO-ONCOGENE TYROSINE-PROTEIN KINASE YES (EC 2.7.1.112) (P61-YES) DE (C-YES). GN YES. OS Xiphophorus helleri. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Atherinomorpha; OC Cyprinodontiformes; Poeciliidae; Xiphophorus. OX NCBI_TaxID=8084; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=RIO LANCETILLA; RX MEDLINE=91187435; PubMed=1707152; RA Hannig G., Ottilie S., Schartl M.; RT "Conservation of structure and expression of the c-yes and fyn genes RT in lower vertebrates."; RL Oncogene 6:361-369(1991). 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; X54970; CAA38714.1; -. DR HSSP; P12931; 1FMK. 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 Proto-oncogene; Tyrosine-protein kinase; Phosphorylation; KW Transferase; ATP-binding; Myristate; SH3 domain; SH2 domain. FT LIPID 2 2 MYRISTATE (BY SIMILARITY). FT DOMAIN 92 153 SH3 (BY SIMILARITY). FT DOMAIN 159 256 SH2. FT DOMAIN 278 531 PROTEIN KINASE. FT NP_BIND 284 292 ATP (BY SIMILARITY). FT BINDING 306 306 ATP (BY SIMILARITY). FT ACT_SITE 397 397 BY SIMILARITY. FT MOD_RES 427 427 PHOSPHORYLATION (AUTO-) (BY SIMILARITY). SQ SEQUENCE 544 AA; 61288 MW; 7D41818B3E7086EF CRC64; MGCVRSKEAK GPALKYQPDN SNVVPVSAHL GHYGPEPTIM GQSPAMKTQN NSHPTALSPF GGVSSPMTPF GGASTSFTSV TVNNPFPAVI TGGVTFFVAL YDYEARTSDD LSFRKGDRFQ IINNTEGDWW EARSINTGEN GYIPSNYVAP ADSIQSEEWY FGKLSRKDTE RLLLLPGNER GTFLIRESET TKGAYSLSLR DWDETKGDNC KHYKIRKLDN GGYYITTRTQ FMSLQMLVKH YTEHVDGLCY KLTTVCPQVK PQTQGIAKDA WEIPRESLRL DVRLGQGCFG EVWMGTWNGT TKVAIKTLKP GTMSPEAFLE EAQIMKKLRH DKLVPLYAVV SEEPIYIVTE FMGKGSLLDF LKEGDGKHLK LPQLVDMASQ IADGMAFIER MNYIHRDLRA ANILVADNLV CKIADFGLAR LIEDNEYTAR QGAKFPIKWT APEAALYGRF TIKSDVWSFG ILLTELVTKG RVPYPGMVNR EVLEQVDRGY RMPCPQGCPE SLHEMMRQCW KKEPDERPTF EYIQSFLEDY FTATEPQYQP GDNL //