ID FYN_HUMAN STANDARD; PRT; 536 AA. AC P06241; DT 01-JAN-1988 (Rel. 06, Created) DT 01-FEB-1994 (Rel. 28, 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) DE (SYN) (SLK). GN FYN. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86287278; PubMed=3526330; RA Semba K., Nishizawa M., Miyajima N., Yoshida M.C., Sukegawa J., RA Yamanashi Y., Sasaki M., Yamamoto T., Toyoshima K.; RT "Yes-related protooncogene, syn, belongs to the protein-tyrosine RT kinase family."; RL Proc. Natl. Acad. Sci. U.S.A. 83:5459-5463(1986). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=87089775; PubMed=3099169; RA Kawakami T., Pennington C.Y., Robbins K.C.; RT "Isolation and oncogenic potential of a novel human src-like gene."; RL Mol. Cell. Biol. 6:4195-4201(1986). RN [3] RP MYRISTOYLATION, AND PHOSPHORYLATION AT TYR-530. RX MEDLINE=91016431; PubMed=1699196; RA Peters D.J., McGrew B.R., Perron D.C., Liptak L.M., Laudano A.P.; RT "In vivo phosphorylation and membrane association of the fyn proto- RT oncogene product in IM-9 human lymphoblasts."; RL Oncogene 5:1313-1319(1990). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF SH3 DOMAIN. RX MEDLINE=93327750; PubMed=7687536; RA Noble M.E.M., Musacchio A., Saraste M., Courtneidge S.A., RA Wierenga R.K.; RT "Crystal structure of the SH3 domain in human Fyn; comparison of the RT three-dimensional structures of SH3 domains in tyrosine kinases and RT spectrin."; RL EMBO J. 12:2617-2624(1993). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 80-141. RX MEDLINE=95393198; PubMed=7664083; RA Musacchio A., Saraste M., Wilmanns M.; RT "High-resolution crystal structures of tyrosine kinase SH3 domains RT complexed with proline-rich peptides."; RL Nat. Struct. Biol. 1:546-551(1994). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 84-140 IN COMPLEX WITH NEF. RX MEDLINE=96279837; PubMed=8681387; RA Lee C.H., Saksela K., Mirza U.A., Chait B.T., Kuriyan J.; RT "Crystal structure of the conserved core of HIV-1 Nef complexed with a RT Src family SH3 domain."; RL Cell 85:931-942(1996). RN [7] RP STRUCTURE BY NMR OF SH3 DOMAIN. RX MEDLINE=96399716; PubMed=8805554; RA Morton C.J., Pugh D.J.R., Brown E.L.J., Kahmann J.D., Renzoni D.A.C., RA Campbell I.D.; RT "Solution structure and peptide binding of the SH3 domain from human RT Fyn."; RL Structure 4:705-714(1996). RN [8] RP STRUCTURE BY NMR. RX MEDLINE=97121261; PubMed=8961927; RA Renzoni D.A., Pugh D.J., Siligardi G., Das P., Morton C.J., Rossi C., RA Waterfield M.D., Campbell I.D., Ladbury J.E.; RT "Structural and thermodynamic characterization of the interaction of RT the SH3 domain from Fyn with the proline-rich binding site on the p85 RT subunit of PI3-kinase."; RL Biochemistry 35:15646-15653(1996). RN [9] RP STRUCTURE BY NMR OF SH2 DOMAIN. RX MEDLINE=98035454; PubMed=9351806; RA Mulhern T.D., Shaw G.L., Morton C.J., Day A.J., Campbell I.D.; RT "The SH2 domain from the tyrosine kinase Fyn in complex with a RT phosphotyrosyl peptide reveals insights into domain stability and RT binding specificity."; RL Structure 5:1313-1323(1997). RN [10] RP BINDING OF SH3 DOMAIN TO PI 3-KINASE. RX MEDLINE=93348274; PubMed=8394019; RA Prasad K.V., Janssen O., Kapeller R., Raab M., Cantley L.C., RA Rudd C.E.; RT "Src-homology 3 domain of protein kinase p59fyn mediates binding to RT phosphatidylinositol 3-kinase in T cells."; RL Proc. Natl. Acad. Sci. U.S.A. 90:7366-7370(1993). 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; M14333; AAC08285.1; -. DR EMBL; M14676; AAA36615.1; -. DR PIR; A24314; TVHUSY. DR PIR; A25389; TVHUSR. DR PDB; 1SHF; 31-OCT-93. DR PDB; 1FYN; 08-NOV-96. DR PDB; 1NYF; 08-NOV-96. DR PDB; 1NYG; 08-NOV-96. DR PDB; 1EFN; 11-JAN-97. DR PDB; 1A0N; 25-FEB-98. DR PDB; 1AOT; 14-JAN-98. DR PDB; 1AOU; 14-JAN-98. DR PDB; 1AZG; 25-FEB-98. DR MIM; 137025; -. 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; 3D-structure. FT INIT_MET 0 0 FT LIPID 1 1 MYRISTATE. FT LIPID 2 2 PALMITATE (BY SIMILARITY). FT LIPID 5 5 PALMITATE (BY SIMILARITY). FT DOMAIN 81 142 SH3. FT DOMAIN 148 245 SH2. FT DOMAIN 270 523 PROTEIN KINASE. FT MOD_RES 11 11 PHOSPHORYLATION (BY PKC) (BY SIMILARITY). FT NP_BIND 276 284 ATP (BY SIMILARITY). FT BINDING 298 298 ATP (BY SIMILARITY). FT ACT_SITE 389 389 BY SIMILARITY. FT MOD_RES 419 419 PHOSPHORYLATION (AUTO-) (BY SIMILARITY). FT MOD_RES 530 530 PHOSPHORYLATION. FT CONFLICT 183 183 A -> S (IN REF. 2). FT CONFLICT 436 436 A -> R (IN REF. 2). FT STRAND 85 88 FT STRAND 92 92 FT STRAND 99 99 FT STRAND 102 102 FT TURN 104 105 FT STRAND 107 112 FT STRAND 118 123 FT TURN 124 126 FT STRAND 129 133 FT HELIX 134 136 FT STRAND 137 139 SQ SEQUENCE 536 AA; 60630 MW; 57436625365A0977 CRC64; GCVQCKDKEA TKLTEERDGS LNQSSGYRYG TDPTPQHYPS FGVTSIPNYN NFHAAGGQGL TVFGGVNSSS HTGTLRTRGG TGVTLFVALY DYEARTEDDL SFHKGEKFQI LNSSEGDWWE ARSLTTGETG YIPSNYVAPV DSIQAEEWYF GKLGRKDAER QLLSFGNPRG TFLIRESETT KGAYSLSIRD WDDMKGDHVK HYKIRKLDNG GYYITTRAQF ETLQQLVQHY SERAAGLCCR LVVPCHKGMP RLTDLSVKTK DVWEIPRESL QLIKRLGNGQ FGEVWMGTWN GNTKVAIKTL KPGTMSPESF LEEAQIMKKL KHDKLVQLYA VVSEEPIYIV TEYMNKGSLL DFLKDGEGRA LKLPNLVDMA AQVAAGMAYI ERMNYIHRDL RSANILVGNG LICKIADFGL ARLIEDNEYT ARQGAKFPIK WTAPEAALYG RFTIKSDVWS FGILLTELVT KGRVPYPGMN NREVLEQVER GYRMPCPQDC PISLHELMIH CWKKDPEERP TFEYLQSFLE DYFTATEPQY QPGENL //