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 28-FEB-2003 (Rel. 41, 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; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95279402; PubMed=7759516; 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). RN [2] RP PHOSPHORYLATION OF TYR-317; TYR-342 AND TYR-346. RX MEDLINE=22191330; PubMed=12077122; RA Hong J.J., Yankee T.M., Harrison M.L., Geahlen R.L.; RT "Regulation of signaling in B cells through the phosphorylation of RT Syk on linker region tyrosines. A mechanism for negative signaling by RT the Lyn tyrosine kinase."; RL J. Biol. Chem. 277:31703-31714(2002). CC -!- FUNCTION: Positive effector of BCR-stimulated responses. Couples CC the B cell antigen receptor (BCR) to the mobilization of calcium CC ion either through a phosphoinositide 3-kinase-dependent pathway, CC when not phosphorylated on tyrosines of the linker region, or CC through a phospholipase C-gamma-dependent pathway, when CC phosphorylated on Tyr-342 and Tyr-346. Thus the differential CC phosphorylation of Syk can determine the pathway by which BCR is CC coupled to the regulation of intracellular calcium ion. CC -!- CATALYTIC ACTIVITY: ATP + a protein tyrosine = ADP + protein CC tyrosine phosphate. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=SykB; CC IsoId=Q64725-1; Sequence=Displayed; CC Name=SykA; CC IsoId=Q64725-2; Sequence=VSP_005011; CC -!- PTM: Autophosphorylated (By similarity). CC -!- PTM: Phosphorylation on Tyr-317 creates a binding site for c-Cbl, CC an adapter protein that serves as a negative regulator of BCR- CC stimulated calcium ion signaling. CC -!- PTM: Phosphorylation on Tyr-342 and Tyr-346 enhances the CC phosphorylation and activation of phospholipase C-gamma and the CC early phase of calcium ion mobilization via a phosphoinositide 3- CC kinase-independent pathway. CC -!- SIMILARITY: BELONGS TO THE TYR FAMILY OF PROTEIN KINASES. SYK/ZAP- CC 70 SUBFAMILY. CC -!- SIMILARITY: Contains 2 SH2 domains. 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; 1A81. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR000980; SH2. DR InterPro; IPR001245; Tyr_pkinase. DR Pfam; PF00017; SH2; 2. DR Pfam; PF00069; pkinase; 1. DR PRINTS; PR00401; SH2DOMAIN. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR ProDom; PD000093; SH2; 2. DR SMART; SM00252; SH2; 2. DR SMART; SM00219; TyrKc; 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; Repeat; Alternative splicing. FT DOMAIN 14 106 SH2 1. FT DOMAIN 167 258 SH2 2. FT DOMAIN 259 364 LINKER. 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 317 317 PHOSPHORYLATION (BY LYN). FT MOD_RES 342 342 PHOSPHORYLATION. FT MOD_RES 346 346 PHOSPHORYLATION. FT MOD_RES 519 519 PHOSPHORYLATION (AUTO-) (BY SIMILARITY). FT VARSPLIC 277 299 Missing (in isoform SykA). FT /FTId=VSP_005011. SQ SEQUENCE 629 AA; 71528 MW; 81169A643EC6A6FE CRC64; 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 //