ID YES_XENLA STANDARD; PRT; 537 AA. AC P10936; DT 01-JUL-1989 (Rel. 11, Created) DT 01-JUL-1989 (Rel. 11, 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 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=89296347; PubMed=2472592; RA Steele R.E., Irwin M.Y., Knudsen C.L., Collett J.W., Fero J.B.; RT "The yes proto-oncogene is present in amphibians and contributes to RT the maternal RNA pool in the oocyte."; RL Oncogene Res. 4:223-233(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; X14377; CAA32551.1; -. DR PIR; S08517; S08517. 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 Proto-oncogene; Tyrosine-protein kinase; Phosphorylation; KW Transferase; ATP-binding; Myristate; SH3 domain; SH2 domain. FT LIPID 2 2 MYRISTATE (BY SIMILARITY). FT DOMAIN 85 146 SH3. FT DOMAIN 152 249 SH2. FT DOMAIN 271 524 PROTEIN KINASE. FT NP_BIND 277 285 ATP (BY SIMILARITY). FT BINDING 299 299 ATP (BY SIMILARITY). FT ACT_SITE 390 390 BY SIMILARITY. FT MOD_RES 420 420 PHOSPHORYLATION (AUTO-) (BY SIMILARITY). SQ SEQUENCE 537 AA; 60357 MW; FF26F615940AC31B CRC64; MGCIKSKEDK GPSIKYRTEP KPDPGSQYGA DPTQATQSPG IKGPAPNFNS HSMTPFGGSS GITPFGGASS IFSPTPVPYP GGLTGGVTVF VALYDYEART TEDLSFRKGE RFQIINNTEG DWWEARSIAT GKTGYIPSNY VAPADSIQAE EWYFGKMGRK DAERLLLNPG NQRGTFLVRE SETTKGAYSL SIRDWDEVRG DNVKHYKIRK LDNGGYYITT RAQFESLQKL VKHYSEHADG LCYRLTTVCP SVKPQTQGLA KDAWEIPRES LRLDVKLGQG CFGEVWIGTW NGTTKVAIKT LKPGTMMPEA FLQEAQIMKK LRHDKLVPLY AVVSEEPIYI VTEYMIKGSL LDFLKEGNGK YLKLPQLVDM AAQIADGMAY IERMNYIHRD LRAANILVGD NLVCKIADFG LARLIEDNEY TARQGAKFPI KWTAPEAALY GRFTIKSDVW SFGILLTELV AKGRVPYPGM VNREVLEQVE RGYRMPCPQR CPESLHELMK LCWKKDPDER PTFEYIQSFL EDYFTATEPQ YQPGDNL //