LCB4_YEAST
ID LCB4_YEAST Reviewed; 624 AA.
AC Q12246; D6W2M7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Sphingoid long chain base kinase 4 {ECO:0000303|PubMed:9677363};
DE Short=LCB kinase 4 {ECO:0000303|PubMed:9677363};
DE EC=2.7.1.91 {ECO:0000269|PubMed:25345524, ECO:0000269|PubMed:9677363};
DE AltName: Full=Sphinganine kinase 4 {ECO:0000305};
GN Name=LCB4 {ECO:0000303|PubMed:9677363};
GN OrderedLocusNames=YOR171C {ECO:0000312|SGD:S000005697}; ORFNames=O3615;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8972579;
RX DOI=10.1002/(sici)1097-0061(199612)12:15<1563::aid-yea44>3.0.co;2-m;
RA Madania A., Poch O., Tarassov I.A., Winsor B., Martin R.P.;
RT "Analysis of a 22,956 bp region on the right arm of Saccharomyces
RT cerevisiae chromosome XV.";
RL Yeast 12:1563-1573(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9677363; DOI=10.1074/jbc.273.31.19437;
RA Nagiec M.M., Skrzypek M.S., Nagiec E.E., Lester R.L., Dickson R.C.;
RT "The LCB4 (YOR171c) and LCB5 (YLR260w) genes of Saccharomyces encode
RT sphingoid long chain base kinases.";
RL J. Biol. Chem. 273:19437-19442(1998).
RN [5]
RP FUNCTION.
RX PubMed=11102354; DOI=10.1093/genetics/156.4.1519;
RA Kim S., Fyrst H., Saba J.D.;
RT "Accumulation of phosphorylated sphingoid long chain bases results in cell
RT growth inhibition in Saccharomyces cerevisiae.";
RL Genetics 156:1519-1529(2000).
RN [6]
RP FUNCTION.
RX PubMed=11795842; DOI=10.1007/s00294-001-0259-6;
RA Zhang X., Skrzypek M.S., Lester R.L., Dickson R.C.;
RT "Elevation of endogenous sphingolipid long-chain base phosphates kills
RT Saccharomyces cerevisiae cells.";
RL Curr. Genet. 40:221-233(2001).
RN [7]
RP FUNCTION.
RX PubMed=11056159; DOI=10.1074/jbc.m007425200;
RA Jenkins G.M., Hannun Y.A.;
RT "Role for de novo sphingoid base biosynthesis in the heat-induced transient
RT cell cycle arrest of Saccharomyces cerevisiae.";
RL J. Biol. Chem. 276:8574-8581(2001).
RN [8]
RP FUNCTION.
RX PubMed=11278643; DOI=10.1074/jbc.m010221200;
RA Birchwood C.J., Saba J.D., Dickson R.C., Cunningham K.W.;
RT "Calcium influx and signaling in yeast stimulated by intracellular
RT sphingosine 1-phosphate accumulation.";
RL J. Biol. Chem. 276:11712-11718(2001).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=12459470; DOI=10.1016/s0014-5793(02)03636-0;
RA Hait N.C., Fujita K., Lester R.L., Dickson R.C.;
RT "Lcb4p sphingoid base kinase localizes to the Golgi and late endosomes.";
RL FEBS Lett. 532:97-102(2002).
RN [10]
RP FUNCTION.
RX PubMed=11967828; DOI=10.1002/yea.861;
RA Ferguson-Yankey S.R., Skrzypek M.S., Lester R.L., Dickson R.C.;
RT "Mutant analysis reveals complex regulation of sphingolipid long chain base
RT phosphates and long chain bases during heat stress in yeast.";
RL Yeast 19:573-586(2002).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12493772; DOI=10.1074/jbc.m209925200;
RA Funato K., Lombardi R., Vallee B., Riezman H.;
RT "Lcb4p is a key regulator of ceramide synthesis from exogenous long chain
RT sphingoid base in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 278:7325-7334(2003).
RN [12]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [13]
RP PHOSPHORYLATION AT SER-451 AND SER-455, AND UBIQUITINATION.
RX PubMed=15598647; DOI=10.1074/jbc.m410908200;
RA Iwaki S., Kihara A., Sano T., Igarashi Y.;
RT "Phosphorylation by Pho85 cyclin-dependent kinase acts as a signal for the
RT down-regulation of the yeast sphingoid long-chain base kinase Lcb4 during
RT the stationary phase.";
RL J. Biol. Chem. 280:6520-6527(2005).
RN [14]
RP FUNCTION, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=16141212; DOI=10.1074/jbc.m503147200;
RA Sano T., Kihara A., Kurotsu F., Iwaki S., Igarashi Y.;
RT "Regulation of the sphingoid long-chain base kinase Lcb4p by ergosterol and
RT heme: studies in phytosphingosine-resistant mutants.";
RL J. Biol. Chem. 280:36674-36682(2005).
RN [15]
RP PALMITOYLATION AT CYS-43 AND CYS-46.
RX PubMed=16227572; DOI=10.1128/mcb.25.21.9189-9197.2005;
RA Kihara A., Kurotsu F., Sano T., Iwaki S., Igarashi Y.;
RT "Long-chain base kinase Lcb4 Is anchored to the membrane through its
RT palmitoylation by Akr1.";
RL Mol. Cell. Biol. 25:9189-9197(2005).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=17686782; DOI=10.1074/jbc.m701607200;
RA Iwaki S., Sano T., Takagi T., Osumi M., Kihara A., Igarashi Y.;
RT "Intracellular trafficking pathway of yeast long-chain base kinase Lcb4,
RT from its synthesis to its degradation.";
RL J. Biol. Chem. 282:28485-28492(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451; SER-454 AND SER-455, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111; SER-120; SER-154;
RP SER-451; SER-454; SER-455 AND SER-460, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [21]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-148, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [22]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=25345524; DOI=10.1038/ncomms6338;
RA Kondo N., Ohno Y., Yamagata M., Obara T., Seki N., Kitamura T.,
RA Naganuma T., Kihara A.;
RT "Identification of the phytosphingosine metabolic pathway leading to odd-
RT numbered fatty acids.";
RL Nat. Commun. 5:5338-5338(2014).
CC -!- FUNCTION: Catalyzes the phosphorylation of the sphingoid long chain
CC bases dihydrosphingosine (DHS or sphinganine) and phytosphingosine
CC (PHS) to form dihydrosphingosine 1-phosphate (DHS-1P) and
CC phytosphingosine 1-phosphate (PHS-1P) respectively (PubMed:9677363,
CC PubMed:11102354, PubMed:11795842, PubMed:16141212, PubMed:25345524).
CC Involved in the biosynthesis of sphingolipids and ceramides
CC (PubMed:12493772). Required with LCB3 for an effective incorporation of
CC DHS into ceramides through a phosphorylation-dephosphorylation cycle.
CC Involved in heat-induced transient cell cycle arrest (PubMed:11056159).
CC Accumulation of phosphorylated sphingoid long chain bases (LCBPs)
CC stimulates calcium influx and activates calcineurin signaling
CC (PubMed:11278643). Involved in heat-stress resistance
CC (PubMed:11967828). {ECO:0000269|PubMed:11056159,
CC ECO:0000269|PubMed:11102354, ECO:0000269|PubMed:11278643,
CC ECO:0000269|PubMed:11795842, ECO:0000269|PubMed:11967828,
CC ECO:0000269|PubMed:12493772, ECO:0000269|PubMed:16141212,
CC ECO:0000269|PubMed:25345524, ECO:0000269|PubMed:9677363}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4R)-hydroxysphinganine + ATP = (4R)-hydroxysphinganine 1-
CC phosphate + ADP + H(+); Xref=Rhea:RHEA:33563, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:64124, ChEBI:CHEBI:64795,
CC ChEBI:CHEBI:456216; EC=2.7.1.91;
CC Evidence={ECO:0000269|PubMed:25345524, ECO:0000269|PubMed:9677363};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33564;
CC Evidence={ECO:0000269|PubMed:25345524, ECO:0000269|PubMed:9677363};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sphingoid base + ATP = a sphingoid 1-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:51496, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:76941, ChEBI:CHEBI:84410, ChEBI:CHEBI:456216;
CC EC=2.7.1.91; Evidence={ECO:0000269|PubMed:9677363};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + sphinganine = ADP + H(+) + sphinganine 1-phosphate;
CC Xref=Rhea:RHEA:15465, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57817, ChEBI:CHEBI:57939, ChEBI:CHEBI:456216;
CC EC=2.7.1.91; Evidence={ECO:0000269|PubMed:9677363};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15466;
CC Evidence={ECO:0000269|PubMed:9677363};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.7 uM for sphinganine {ECO:0000269|PubMed:9677363};
CC KM=25 uM for ATP {ECO:0000269|PubMed:9677363};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12459470,
CC ECO:0000269|PubMed:16141212}; Peripheral membrane protein
CC {ECO:0000305}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12493772}; Peripheral membrane protein
CC {ECO:0000305}. Late endosome membrane {ECO:0000269|PubMed:12459470};
CC Peripheral membrane protein {ECO:0000305}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:12459470}; Peripheral membrane protein
CC {ECO:0000305}. Note=LCB4 is synthesized in the cytosol, palmitoylated
CC at the Golgi apparatus by AKR1, and then transported to the plasma
CC membrane (PM) via the late Sec pathway. Most of the LCB4 is delivered
CC further to the cortical ER (cER), which is closely adjacent to the PM.
CC In stationary phase, G1 cell cycle arrest causes ER-localized LCB4 to
CC be transported to the Golgi apparatus via the early Sec pathway, and
CC finally to the vacuole via the MVB pathway, where it is degraded.
CC {ECO:0000269|PubMed:17686782}.
CC -!- PTM: Phosphorylated by the cyclin-CDKs PCL1-PHO85 and PCL2-PHO85.
CC Phosphorylation is a prerequisite to ubiquitination. The
CC phosphorylation level depends on sterol composition and may also be
CC involved in subcellular location (PubMed:16141212).
CC {ECO:0000269|PubMed:15598647, ECO:0000269|PubMed:16141212}.
CC -!- PTM: Ubiquitinated. The ubiquitination leads to degradation in the
CC vacuole. {ECO:0000269|PubMed:15598647}.
CC -!- PTM: Palmitoylated by palmitoyltransferase AKR1; this anchors the
CC protein to the plasma membrane. {ECO:0000269|PubMed:16227572}.
CC -!- DISRUPTION PHENOTYPE: Completely abolishes the conversion of
CC phytosphingosin to glycerophospholipid. {ECO:0000269|PubMed:25345524}.
CC -!- MISCELLANEOUS: Present with 2840 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U55021; AAB47416.1; -; Genomic_DNA.
DR EMBL; Z75078; CAA99378.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10943.1; -; Genomic_DNA.
DR PIR; S67059; S67059.
DR RefSeq; NP_014814.1; NM_001183590.1.
DR AlphaFoldDB; Q12246; -.
DR SMR; Q12246; -.
DR BioGRID; 34565; 157.
DR DIP; DIP-2844N; -.
DR IntAct; Q12246; 3.
DR MINT; Q12246; -.
DR STRING; 4932.YOR171C; -.
DR SwissLipids; SLP:000000109; -.
DR iPTMnet; Q12246; -.
DR SwissPalm; Q12246; -.
DR MaxQB; Q12246; -.
DR PaxDb; Q12246; -.
DR PRIDE; Q12246; -.
DR EnsemblFungi; YOR171C_mRNA; YOR171C; YOR171C.
DR GeneID; 854342; -.
DR KEGG; sce:YOR171C; -.
DR SGD; S000005697; LCB4.
DR VEuPathDB; FungiDB:YOR171C; -.
DR eggNOG; KOG1116; Eukaryota.
DR GeneTree; ENSGT00940000167991; -.
DR HOGENOM; CLU_013399_0_2_1; -.
DR InParanoid; Q12246; -.
DR OMA; HYISIDG; -.
DR BioCyc; MetaCyc:YOR171C-MON; -.
DR BioCyc; YEAST:YOR171C-MON; -.
DR Reactome; R-SCE-1483206; Glycerophospholipid biosynthesis.
DR Reactome; R-SCE-1660661; Sphingolipid de novo biosynthesis.
DR SABIO-RK; Q12246; -.
DR PRO; PR:Q12246; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12246; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0017050; F:D-erythro-sphingosine kinase activity; IDA:SGD.
DR GO; GO:0001727; F:lipid kinase activity; IBA:GO_Central.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0008481; F:sphinganine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0019722; P:calcium-mediated signaling; IMP:SGD.
DR GO; GO:0016310; P:phosphorylation; IBA:GO_Central.
DR GO; GO:0006665; P:sphingolipid metabolic process; IDA:SGD.
DR GO; GO:0046512; P:sphingosine biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.50.10330; -; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR Pfam; PF00781; DAGK_cat; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF111331; SSF111331; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Endoplasmic reticulum; Endosome;
KW Golgi apparatus; Isopeptide bond; Kinase; Lipid metabolism; Lipoprotein;
KW Membrane; Nucleotide-binding; Palmitate; Phosphoprotein;
KW Reference proteome; Sphingolipid metabolism; Transferase; Ubl conjugation.
FT CHAIN 1..624
FT /note="Sphingoid long chain base kinase 4"
FT /id="PRO_0000255956"
FT DOMAIN 224..363
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT REGION 95..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 293
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 234..236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 266
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 291..294
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 324..326
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 392
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 398
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT BINDING 589..591
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 451
FT /note="Phosphoserine; by PHO85"
FT /evidence="ECO:0000269|PubMed:15598647,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 455
FT /note="Phosphoserine; by PHO85"
FT /evidence="ECO:0000269|PubMed:15598647,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT LIPID 43
FT /note="S-palmitoyl cysteine; by AKR1"
FT /evidence="ECO:0000269|PubMed:16227572"
FT LIPID 46
FT /note="S-palmitoyl cysteine; by AKR1"
FT /evidence="ECO:0000269|PubMed:16227572"
FT CROSSLNK 148
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
SQ SEQUENCE 624 AA; 69639 MW; E033A3BAC604D4BB CRC64;
MVVQKKLRAI LTDEGVLIKS QSHHMFNKHG QLRSGDSLSL LSCLSCLDDG TLSSDGGSFD
EDDSLELLPL NTTIPFNRIL NAKYVNVGQK GFNNGKISSN PFQTENLSSS SENDDVENHS
LSNDKAPVSE SQSFPKKDKW DTKTNTVKVS PDDSQDNSPS LGIKDNQQLI ELTFAVPKGH
DVIPQKLTLL IDHVSRKSRA NTGEENISSG TVEEILEKSY ENSKRNRSIL VIINPHGGKG
TAKNLFLTKA RPILVESGCK IEIAYTKYAR HAIDIAKDLD ISKYDTIACA SGDGIPYEVI
NGLYRRPDRV DAFNKLAVTQ LPCGSGNAMS ISCHWTNNPS YAALCLVKSI ETRIDLMCCS
QPSYMNEWPR LSFLSQTYGV IAESDINTEF IRWMGPVRFN LGVAFNIIQG KKYPCEVFVK
YAAKSKKELK VHFLENKDKN KGCLTFEPNP SPNSSPDLLS KNNINNSTKD ELSPNFLNED
NFKLKYPMTE PVPRDWEKMD SELTDNLTIF YTGKMPYIAK DTKFFPAALP ADGTIDLVIT
DARIPVTRMT PILLSLDKGS HVLEPEVIHS KILAYKIIPK VESGLFSVDG EKFPLEPLQV
EIMPMLCKTL LRNGRYIDTE FESM
