true2006-10-312024-03-27168LCB5_YEASTThe nucleotide sequence of Saccharomyces cerevisiae chromosome XII.Johnston M.Hillier L.W.Riles L.Albermann K.Andre B.Ansorge W.Benes V.Brueckner M.Delius H.Dubois E.Duesterhoeft A.Entian K.-D.Floeth M.Goffeau A.Hebling U.Heumann K.Heuss-Neitzel D.Hilbert H.Hilger F.Kleine K.Koetter P.Louis E.J.Messenguy F.Mewes H.-W.Miosga T.Moestl D.Mueller-Auer S.Nentwich U.Obermaier B.Piravandi E.Pohl T.M.Portetelle D.Purnelle B.Rechmann S.Rieger M.Rinke M.Rose M.Scharfe M.Scherens B.Scholler P.Schwager C.Schwarz S.Underwood A.P.Urrestarazu L.A.Vandenbol M.Verhasselt P.Vierendeels F.Voet M.Volckaert G.Voss H.Wambutt R.Wedler E.Wedler H.Zimmermann F.K.Zollner A.Hani J.Hoheisel J.D.1997Nature38787-90NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]ATCC 204508 / S288cThe reference genome sequence of Saccharomyces cerevisiae: Then and now.Engel S.R.Dietrich F.S.Fisk D.G.Binkley G.Balakrishnan R.Costanzo M.C.Dwight S.S.Hitz B.C.Karra K.Nash R.S.Weng S.Wong E.D.Lloyd P.Skrzypek M.S.Miyasato S.R.Simison M.Cherry J.M.doi:10.1534/g3.113.0089952014G3 (Bethesda)4389-398GENOME REANNOTATIONThe LCB4 (YOR171c) and LCB5 (YLR260w) genes of Saccharomyces encode sphingoid long chain base kinases.Nagiec M.M.Skrzypek M.S.Nagiec E.E.Lester R.L.Dickson R.C.doi:10.1074/jbc.273.31.194371998J. Biol. Chem.27319437-19442FUNCTIONCATALYTIC ACTIVITYBIOPHYSICOCHEMICAL PROPERTIESAccumulation of phosphorylated sphingoid long chain bases results in cell growth inhibition in Saccharomyces cerevisiae.Kim S.Fyrst H.Saba J.D.doi:10.1093/genetics/156.4.15192000Genetics1561519-1529FUNCTIONRole for de novo sphingoid base biosynthesis in the heat-induced transient cell cycle arrest of Saccharomyces cerevisiae.Jenkins G.M.Hannun Y.A.doi:10.1074/jbc.m0074252002001J. Biol. Chem.2768574-8581FUNCTIONCalcium influx and signaling in yeast stimulated by intracellular sphingosine 1-phosphate accumulation.Birchwood C.J.Saba J.D.Dickson R.C.Cunningham K.W.doi:10.1074/jbc.m0102212002001J. Biol. Chem.27611712-11718FUNCTIONLcb4p is a key regulator of ceramide synthesis from exogenous long chain sphingoid base in Saccharomyces cerevisiae.Funato K.Lombardi R.Vallee B.Riezman H.doi:10.1074/jbc.m2099252002003J. Biol. Chem.2787325-7334FUNCTIONSUBCELLULAR LOCATIONGlobal analysis of protein expression in yeast.Ghaemmaghami S.Huh W.-K.Bower K.Howson R.W.Belle A.Dephoure N.O'Shea E.K.Weissman J.S.doi:10.1038/nature020462003Nature425737-741LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.Li X.Gerber S.A.Rudner A.D.Beausoleil S.A.Haas W.Villen J.Elias J.E.Gygi S.P.doi:10.1021/pr060559j2007J. Proteome Res.61190-1197IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]ADR376A multidimensional chromatography technology for in-depth phosphoproteome analysis.Albuquerque C.P.Smolka M.B.Payne S.H.Bafna V.Eng J.Zhou H.doi:10.1074/mcp.m700468-mcp2002008Mol. Cell. Proteomics71389-1396IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution.Holt L.J.Tuch B.B.Villen J.Johnson A.D.Gygi S.P.Morgan D.O.doi:10.1126/science.11728672009Science3251682-1686IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Identification of the phytosphingosine metabolic pathway leading to odd-numbered fatty acids.Kondo N.Ohno Y.Yamagata M.Obara T.Seki N.Kitamura T.Naganuma T.Kihara A.doi:10.1038/ncomms63382014Nat. Commun.55338FUNCTIONCATALYTIC ACTIVITY1851LCB5EukaryotaSphingolipid de novo biosynthesisAssociation of TriC/CCT with target proteins during biosynthesisVEGFR2 mediated cell proliferationExtra-nuclear estrogen signalingPKR-mediated signaling0 hits in 10 CRISPR screensProteinATP-NAD_kinase_NDiacylglycerol_kinase_cat_domNAD/diacylglycerol_kinase_sfLD11247P-RELATEDSPHINGOSINE KINASEDAGK_catDAGKcNAD kinase/diacylglycerol kinase-likeDAGKSphingoid long chain base kinase 5LCB kinase 52.7.1.91Sphinganine kinase 5LCB5YLR260WCatalyzes the phosphorylation of the sphingoid long chain bases dihydrosphingosine (DHS or sphinganine) and phytosphingosine (PHS) to form dihydrosphingosine 1-phosphate (DHS-1P) and phytosphingosine 1-phosphate (PHS-1P) respectively (PubMed:9677363, PubMed:11102354, PubMed:12493772, PubMed:25345524). Redundant to LCB4, is only responsible for few percent of the total activity (PubMed:9677363). Involved in the biosynthesis of sphingolipids and ceramides (PubMed:9677363, PubMed:25345524). Involved in heat-induced transient cell cycle arrest (PubMed:11056159). Accumulation of phosphorylated sphingoid long chain bases (LCBPs) stimulates calcium influx and activates calcineurin signaling (PubMed:11102354, PubMed:11278643). Involved in heat-stress resistance (PubMed:11056159).2 uM for dihydrosphingosinePresent with 1760 molecules/cell in log phase SD medium.Sphingoid long chain base kinase 5775661687DAGKc266405Disordered20Disordered101130Disordered180207Disordered506525Basic residues19Basic and acidic residues194Acidic residues522Proton donor/acceptor335276278308333336340366368434440652654S-palmitoyl cysteine; by AKR191S-palmitoyl cysteine; by AKR194substrate1996-11-011775663855628d63da911fb68c52be5c94d980MTLKPSKRRKGRSRHSRKKQITSAILTEEGIMIKAKPSSPYTYANRMADKRSRSSIDNISRTSFQSNISRTSFQSNSDNNSIFETASLISCVTCLSDTDTIDRSETSTTDTSKDDLSANPKLHYPSVNGQLPANTVIPYGRILDARYIEKEPLHYYDANSSPSSPLSSSMSNISEKCDLDELESSQKKERKGNSLSRGSNSSSSLLTSRSPFTKLVEVIFARPRRHDVVPKRVSLYIDYKPHSSSHLKEEDDLVEEILKRSYKNTRRNKSIFVIINPFGGKGKAKKLFMTKAKPLLLASRCSIEVVYTKYPGHAIEIAREMDIDKYDTIACASGDGIPHEVINGLYQRPDHVKAFNNIAITEIPCGSGNAMSVSCHWTNNPSYSTLCLIKSIETRIDLMCCSQPSYAREHPKLSFLSQTYGLIAETDINTEFIRWMGPARFELGVAFNIIQKKKYPCEIYVKYAAKSKNELKNHYLEHKNKGSLEFQHITMNKDNEDCDNYNYENEYETENEDEDEDADADDEDSHLISRDLADSSADQIKEEDFKIKYPLDEGIPSDWERLDPNISNNLGIFYTGKMPYVAADTKFFPAALPSDGTMDMVITDARTSLTRMAPILLGLDKGSHVLQPEVLHSKILAYKIIPKLGNGLFSVDGEKFPLEPLQVEIMPRLCKTLLRNGRYVDTDFDSMtruetruetruetruetruetruetruetruetruetruetruetruetruetruetrue