ID FYN_MOUSE STANDARD; PRT; 533 AA. AC P39688; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 01-OCT-2000 (Rel. 40, Last annotation update) DE PROTO-ONCOGENE TYROSINE-PROTEIN KINASE FYN (EC 2.7.1.112) (P59-FYN). GN FYN. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91175680; PubMed=2488273; RA Cooke M.P., Perlmutter R.M.; RT "Expression of a novel form of the fyn proto-oncogene in hematopoietic RT cells."; RL New Biol. 1:66-74(1989). RN [2] RP SEQUENCE FROM N.A. RA Lee C., Kim M.G., Jeon S.H., Park D.E., Park S.D., Seong R.H.; RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP PALMITOYLATION. RX MEDLINE=94019312; PubMed=8413237; RA Shenoy-Scaria A.M., Timson L.K., Kwong J., Shaw A.S., Lublin D.M.; RT "Palmitylation of an amino-terminal cysteine motif of protein tyrosine RT kinases p56lck and p59fyn mediates interaction with glycosyl- RT phosphatidylinositol-anchored proteins."; RL Mol. Cell. Biol. 13:6385-6392(1993). RN [4] RP PALMITOYLATION. RX MEDLINE=95071286; PubMed=7980442; RA Koegl M., Zlatkine P., Ley S.C., Courtneidge S.A., Magee A.I.; RT "Palmitoylation of multiple Src-family kinases at a homologous N- RT terminal motif."; RL Biochem. J. 303:749-753(1994). RN [5] RP PALMITOYLATION. RX MEDLINE=97345356; PubMed=9201723; RA Wolven A., Okamura H., Rosenblatt Y., Resh M.D.; RT "Palmitoylation of p59fyn is reversible and sufficient for plasma RT membrane association."; RL Mol. Biol. Cell 8:1159-1173(1997). RN [6] RP MYRISTOYLATION. RX MEDLINE=96251668; PubMed=8655574; RA Gauen L.K.T., Linder M.E., Shaw A.S.; RT "Multiple features of the p59fyn src homology 4 domain define a motif RT for immune-receptor tyrosine-based activation motif (ITAM) binding and RT for plasma membrane localization."; RL J. Cell Biol. 133:1007-1015(1996). CC -!- FUNCTION: IMPLICATED IN THE CONTROL OF CELL GROWTH. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP + CC PROTEIN TYROSINE PHOSPHATE. CC -!- SUBUNIT: ASSOCIATES THROUGH ITS SH3 DOMAIN, TO THE P85 SUBUNIT OF CC PHOSPHATIDYLINOSITOL 3-KINASE. INTERACTS WITH THE FYN-BINDING CC PROTEIN (FYB). 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; M27266; AAA37644.1; -. DR EMBL; U70324; AAB09568.1; -. DR PIR; A44991; A44991. DR HSSP; P06241; 1FYN. DR MGD; MGI:95602; Fyn. 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; Transferase; Tyrosine-protein kinase; Phosphorylation; KW ATP-binding; Myristate; SH3 domain; SH2 domain; Palmitate; KW Lipoprotein. FT INIT_MET 0 0 BY SIMILARITY. FT LIPID 1 1 MYRISTATE. FT LIPID 2 2 PALMITATE. FT LIPID 5 5 PALMITATE. FT DOMAIN 81 142 SH3. FT DOMAIN 148 245 SH2. FT DOMAIN 267 520 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-) (BY SIMILARITY). SQ SEQUENCE 533 AA; 59926 MW; EFBD703F15B2933C CRC64; GCVQCKDKEA AKLTEERDGS LNQSSGYRYG TDPTPQHYPS FGVTSIPNYN NFHAAGGQGL TVFGGVNSSS HTGTLRTRGG TGVTLFVALY DYEARTEDDL SFHKGEKFQI LNSSEGDWWE ARSLTTGETG YIPSNYVAPV DSIQAEEWYF GKLGRKDAER QLLSFGNPRG TFLIRESQTT KGAYSLSIRD WDDMKGDHVK HYKIRKLDNG GYYITTRAQF ETLQQLVQHY SEKADGLCFN LTVVSSSCTP QTSGLAKDAW EVARDSLFLE KKLGQGCFAE VWLGTWNGNT KVAIKTLKPG TMSPESFLEE AQIMKKLKHD KLVQLYAVVS EEPIYIVTEY MSKGSLLDFL KDGEGRALKL PNLVDMAAQV AAGMAYIERM NYIHRDLRSA NILVGNGLIC KIADFGLARL IEDNEYTARQ GAKFPIKWTA PEAALYGRFT IKSDVWSFGI LLTELVTKGR VPYPGMNNRE VLEQVERGYR MPCPQDCPIS LHELMIHCWK KDPEERPTFE YLQGFLEDYF TATEPQYQPG ENL //