ID KSYK_RAT STANDARD; PRT; 629 AA. AC Q64725; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE TYROSINE-PROTEIN KINASE SYK (EC 2.7.1.112) (SPLEEN TYROSINE KINASE). GN SYK. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Mammalia; OC Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 95279402. RA ROWLEY R.B., BOLEN J.B., FARGNOLI J.; RT "Molecular cloning of rodent p72Syk. Evidence of alternative mRNA RT splicing."; RL J. Biol. Chem. 270:12659-12664(1995). CC -!- FUNCTION: MAY PARTICIPATE IN SIGNALING PATHWAYS. PLAYS A ROLE IN CC LYMPHOCYTE ACTIVATION. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP + PROTEIN CC TYROSINE PHOSPHATE. CC -!- ALTERNATIVE PRODUCTS: TWO FORMS, SYKB AND SYKA, ARE FORMED BY CC ALTERNATIVE SPLCING OF SYK. THE SEQUENCE SHOWN IS THAT OF SYKB. CC -!- PTM: AUTOPHOSPHORYLATED (BY SIMILARITY). CC -!- SIMILARITY: CONTAINS 2 SH2 DOMAINS. CC -!- SIMILARITY: TO OTHER PROTEIN-TYROSINE KINASES IN THE CATALYTIC CC DOMAIN. BELONGS TO THE SYK/ZAP-70 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 -------------------------------------------------------------------------- CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U21684; AAA75167.1; -. DR EMBL; U21683; AAA75166.1; -. DR HSSP; P43405; 1CSY. DR PFAM; PF00017; SH2; 2. DR PFAM; PF00069; pkinase; 1. 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; 2. KW Transferase; Tyrosine-protein kinase; ATP-binding; Phosphorylation; KW SH2 domain; Alternative splicing. FT DOMAIN 14 106 SH2. FT DOMAIN 167 258 SH2. FT DOMAIN 365 625 PROTEIN KINASE. FT NP_BIND 371 379 ATP (BY SIMILARITY). FT BINDING 396 396 ATP (BY SIMILARITY). FT ACT_SITE 488 488 BY SIMILARITY. FT MOD_RES 519 519 PHOSPHORYLATION (AUTO-) (BY SIMILARITY). FT VARSPLIC 277 299 MISSING (IN FORM SYKA). SQ SEQUENCE 629 AA; 71528 MW; 86C26196 CRC32; MAGNAVDNAN HLTYFFGNIT REEAEDYLVQ GGMTDGLYLL RQSRNYLGGF ALSVAHNRKA HHYTIERELN GTYAISGGRA HASPADLCHY HSQEPEGLVC LLKKPFNRPP GVQPKTGPFE DLKENLIREY VKQTWNLQGQ ALEQAIISQK PQLEKLIATT AHEKMPWFHG NISRDESEQT VLIGSKTNGK FLIRARDNNG SFALCLLHEG KVLHYRIDRD KTGKLSIPEG KKFDTLWQLV EHYSYKPDGL LRVLTVPCQK IGVQMGHPGS SNAHPVTWSP GGIISRIKSY SFPKPGHKKP PPPQGSRPES TVSFNPYEPT GGAWGPDRGL QREALPMDTE VYESPYADPE EIRPKEVYLD RKLLTLEDNE LGSGNFGTVK KGYYQMKKVV KTVAVKILKN EANDPALKDE LLAEANVMQQ LDNPYIVRMI GICEAESWML VMEMAAWGPL NKYLQQNRHI KDKNIIELVH QVSMGMKYLE ESNFVHRDLA ARNVLLVTQH YAKISDFGLS KALRADENYY KAQTHGKWPV KWYAPECINY FKFSSKSDVW SFGVLMWEAF SYGQKPYRGM KGSEVTAMLE KGERMGCPPG CPREMYDLMF LCWTYDVENR PGFAAVELRL RNYYYDVVN //