YPK1_YEAST
ID YPK1_YEAST Reviewed; 680 AA.
AC P12688; D6VX69;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 222.
DE RecName: Full=Serine/threonine-protein kinase YPK1;
DE EC=2.7.11.1;
DE AltName: Full=Sphingosine-like immunosuppressant resistant protein 2;
DE AltName: Full=Yeast protein kinase 1;
GN Name=YPK1; Synonyms=SLI2; OrderedLocusNames=YKL126W;
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].
RX PubMed=2850145; DOI=10.1089/dna.1.1988.7.469;
RA Maurer R.A.;
RT "Isolation of a yeast protein kinase gene by screening with a mammalian
RT protein kinase cDNA.";
RL DNA 7:469-474(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 DISCUSSION OF SEQUENCE, AND FUNCTION.
RX PubMed=8437590; DOI=10.1007/bf00277146;
RA Chen P.C., Lee K.S., Levin D.E.;
RT "A pair of putative protein kinase genes (YPK1 and YPK2) is required for
RT cell growth in Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 236:443-447(1993).
RN [5]
RP PHOSPHORYLATION AT THR-504 BY PKH1.
RX PubMed=10074427; DOI=10.1016/s0960-9822(99)80088-8;
RA Casamayor A., Torrance P.D., Kobayashi T., Thorner J., Alessi D.R.;
RT "Functional counterparts of mammalian protein kinases PDK1 and SGK in
RT budding yeast.";
RL Curr. Biol. 9:186-197(1999).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-376.
RX PubMed=10825204; DOI=10.1128/mcb.20.12.4411-4419.2000;
RA Sun Y., Taniguchi R., Tanoue D., Yamaji T., Takematsu H., Mori K.,
RA Fujita T., Kawasaki T., Kozutsumi Y.;
RT "Sli2 (Ypk1), a homologue of mammalian protein kinase SGK, is a downstream
RT kinase in the sphingolipid-mediated signaling pathway of yeast.";
RL Mol. Cell. Biol. 20:4411-4419(2000).
RN [7]
RP INVOLVEMENT IN ENDOCYTOSIS, AND MUTAGENESIS OF LYS-376; ASP-488; GLY-490;
RP THR-504 AND THR-662.
RX PubMed=11807089; DOI=10.1083/jcb.200107135;
RA deHart A.K.A., Schnell J.D., Allen D.A., Hicke L.;
RT "The conserved Pkh-Ypk kinase cascade is required for endocytosis in
RT yeast.";
RL J. Cell Biol. 156:241-248(2002).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, ACTIVATION BY PKH1, AND MUTAGENESIS OF
RP LYS-376.
RX PubMed=12221112; DOI=10.1091/mbc.e02-04-0201;
RA Roelants F.M., Torrance P.D., Bezman N., Thorner J.;
RT "Pkh1 and Pkh2 differentially phosphorylate and activate Ypk1 and Ykr2 and
RT define protein kinase modules required for maintenance of cell wall
RT integrity.";
RL Mol. Biol. Cell 13:3005-3028(2002).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [10]
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 [11]
RP INVOLVEMENT IN MYRIOCIN RESISTANCE.
RX PubMed=15025559; DOI=10.1042/bj20040108;
RA Momoi M., Tanoue D., Sun Y., Takematsu H., Suzuki Y., Suzuki M., Suzuki A.,
RA Fujita T., Kozutsumi Y.;
RT "SLI1 (YGR212W) is a major gene conferring resistance to the sphingolipid
RT biosynthesis inhibitor ISP-1, and encodes an ISP-1 N-acetyltransferase in
RT yeast.";
RL Biochem. J. 381:321-328(2004).
RN [12]
RP FUNCTION, PHOSPHORYLATION, AND MUTAGENESIS OF LYS-376; ASP-488; THR-504 AND
RP THR-662.
RX PubMed=15470109; DOI=10.1099/mic.0.27286-0;
RA Roelants F.M., Torrance P.D., Thorner J.;
RT "Differential roles of PDK1- and PDK2-phosphorylation sites in the yeast
RT AGC kinases Ypk1, Pkc1 and Sch9.";
RL Microbiology 150:3289-3304(2004).
RN [13]
RP MUTAGENESIS OF LYS-376; GLY-490; THR-504 AND THR-662.
RX PubMed=15820214; DOI=10.1016/j.abb.2005.02.030;
RA Tanoue D., Kobayashi T., Sun Y., Fujita T., Takematsu H., Kozutsumi Y.;
RT "The requirement for the hydrophobic motif phosphorylation of Ypk1 in yeast
RT differs depending on the downstream events, including endocytosis, cell
RT growth, and resistance to a sphingolipid biosynthesis inhibitor, ISP-1.";
RL Arch. Biochem. Biophys. 437:29-41(2005).
RN [14]
RP ACTIVITY REGULATION, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT THR-504 AND
RP THR-662 BY PKH1, AND MUTAGENESIS OF LYS-376; THR-504 AND THR-662.
RX PubMed=15840588; DOI=10.1074/jbc.m502972200;
RA Liu K., Zhang X., Lester R.L., Dickson R.C.;
RT "The sphingoid long chain base phytosphingosine activates AGC-type protein
RT kinases in Saccharomyces cerevisiae including Ypk1, Ypk2, and Sch9.";
RL J. Biol. Chem. 280:22679-22687(2005).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57; SER-644 AND SER-653, 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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170 AND SER-653, AND
RP IDENTIFICATION BY 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57; SER-61; SER-64; SER-71;
RP SER-170; THR-502; THR-504; SER-644; SER-653 AND SER-671, AND IDENTIFICATION
RP BY MASS 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 [19]
RP FUNCTION, AND PHOSPHORYLATION BY FPK1.
RX PubMed=19966303; DOI=10.1073/pnas.0912497106;
RA Roelants F.M., Baltz A.G., Trott A.E., Fereres S., Thorner J.;
RT "A protein kinase network regulates the function of aminophospholipid
RT flippases.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:34-39(2010).
CC -!- FUNCTION: Plays an essential role in the proliferation of yeast cells.
CC Involved in a signaling pathway, required for optimal cell wall
CC integrity, that acts in parallel with the PKC1-SLT2-dependent pathway.
CC Downstream kinase in the sphingolipid-mediated signaling pathway. Its
CC phosphorylation is regulated by the intracellular sphingolipid
CC concentration. Cooperates with SLI1 in mediating resistance to the
CC sphingolipid biosynthesis inhibitor drug myriocin (ISP-1). Its kinase
CC activity is essential for the resistance. Required for both receptor-
CC mediated and fluid-phase endocytosis, but is not necessary for receptor
CC phosphorylation or ubiquitination. Necessary for the internalization of
CC plasma membrane proteins carrying different types of internalization
CC signals. Acts downstream of the PKH kinases to control endocytosis by
CC phosphorylating components of the endocytic machinery. Phosphorylation
CC of residue Thr-504 in the activation loop is essential for activity.
CC phosphorylates and down-regulates flippase activator FPK1.
CC {ECO:0000269|PubMed:10825204, ECO:0000269|PubMed:12221112,
CC ECO:0000269|PubMed:15470109, ECO:0000269|PubMed:19966303,
CC ECO:0000269|PubMed:8437590}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- ACTIVITY REGULATION: Activated by phytosphingosine (PHS), a sphingoid
CC long chain base. Activated by PKH1 phosphorylation.
CC {ECO:0000269|PubMed:15840588}.
CC -!- INTERACTION:
CC P12688; P53739: FPK1; NbExp=2; IntAct=EBI-29473, EBI-9813;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10825204,
CC ECO:0000269|PubMed:12221112, ECO:0000269|PubMed:14562095}. Cell
CC membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305};
CC Cytoplasmic side {ECO:0000305}. Note=Intracellular localization is
CC regulated by the intracellular sphingolipid levels. During the yeast
CC cell cycle, distributed both on the plasma membrane and in the cytosol.
CC Greater accumulation was detected on the plasma membrane, such as in
CC the budding area, a daughter cell and the neck region of the mother
CC cell in the S phase, and the septum between a mother cell and a
CC daughter cell in the G2 phase.
CC -!- PTM: Autophosphorylated. Autophosphorylation is stimulated by PHS.
CC Phosphorylated by PKH1. PHS stimulates phosphorylation by PKH1. The N-
CC terminal half is phosphorylated by FPK1. {ECO:0000269|PubMed:10074427,
CC ECO:0000269|PubMed:15470109, ECO:0000269|PubMed:15840588,
CC ECO:0000269|PubMed:19966303}.
CC -!- MISCELLANEOUS: Present with 2950 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. RAC subfamily. {ECO:0000305}.
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DR EMBL; M21307; AAA34880.1; -; Genomic_DNA.
DR EMBL; Z28126; CAA81967.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09035.1; -; Genomic_DNA.
DR PIR; S37955; S37955.
DR RefSeq; NP_012796.1; NM_001179692.1.
DR AlphaFoldDB; P12688; -.
DR SMR; P12688; -.
DR BioGRID; 34010; 166.
DR DIP; DIP-4869N; -.
DR IntAct; P12688; 22.
DR MINT; P12688; -.
DR STRING; 4932.YKL126W; -.
DR iPTMnet; P12688; -.
DR MaxQB; P12688; -.
DR PaxDb; P12688; -.
DR PRIDE; P12688; -.
DR EnsemblFungi; YKL126W_mRNA; YKL126W; YKL126W.
DR GeneID; 853733; -.
DR KEGG; sce:YKL126W; -.
DR SGD; S000001609; YPK1.
DR VEuPathDB; FungiDB:YKL126W; -.
DR eggNOG; KOG0598; Eukaryota.
DR GeneTree; ENSGT00940000175269; -.
DR HOGENOM; CLU_000288_120_2_1; -.
DR InParanoid; P12688; -.
DR OMA; SWKRLLM; -.
DR BioCyc; YEAST:G3O-31908-MON; -.
DR BRENDA; 2.7.11.1; 984.
DR Reactome; R-SCE-1257604; PIP3 activates AKT signaling.
DR Reactome; R-SCE-1358803; Downregulation of ERBB2:ERBB3 signaling.
DR Reactome; R-SCE-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR Reactome; R-SCE-165158; Activation of AKT2.
DR Reactome; R-SCE-198323; AKT phosphorylates targets in the cytosol.
DR Reactome; R-SCE-198693; AKT phosphorylates targets in the nucleus.
DR Reactome; R-SCE-203615; eNOS activation.
DR Reactome; R-SCE-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-SCE-392451; G beta:gamma signalling through PI3Kgamma.
DR Reactome; R-SCE-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR Reactome; R-SCE-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-SCE-6804757; Regulation of TP53 Degradation.
DR Reactome; R-SCE-6804758; Regulation of TP53 Activity through Acetylation.
DR Reactome; R-SCE-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-SCE-9031628; NGF-stimulated transcription.
DR PRO; PR:P12688; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P12688; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019887; F:protein kinase regulator activity; IMP:CACAO.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:SGD.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0071311; P:cellular response to acetate; IMP:SGD.
DR GO; GO:0070941; P:eisosome assembly; IGI:SGD.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006650; P:glycerophospholipid metabolic process; IMP:SGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0061093; P:negative regulation of phospholipid translocation; IMP:SGD.
DR GO; GO:0090155; P:negative regulation of sphingolipid biosynthetic process; IMP:SGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0060237; P:regulation of fungal-type cell wall organization; IMP:SGD.
DR GO; GO:0000749; P:response to pheromone triggering conjugation with cellular fusion; IMP:SGD.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Cell wall biogenesis/degradation; Cytoplasm;
KW Endocytosis; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..680
FT /note="Serine/threonine-protein kinase YPK1"
FT /id="PRO_0000086835"
FT DOMAIN 347..602
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 603..673
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 470
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 353..361
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 57
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 502
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 504
FT /note="Phosphothreonine; by PKH1"
FT /evidence="ECO:0000269|PubMed:10074427,
FT ECO:0000269|PubMed:15840588, ECO:0007744|PubMed:19779198"
FT MOD_RES 644
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 662
FT /note="Phosphothreonine; by PKH1"
FT /evidence="ECO:0000269|PubMed:15840588"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 376
FT /note="K->A,R: No kinase activity. ATP-binding defect.
FT Internalization defects."
FT /evidence="ECO:0000269|PubMed:10825204,
FT ECO:0000269|PubMed:11807089, ECO:0000269|PubMed:12221112,
FT ECO:0000269|PubMed:15470109, ECO:0000269|PubMed:15820214,
FT ECO:0000269|PubMed:15840588"
FT MUTAGEN 488
FT /note="D->A: Catalytically inactive. Internalization
FT defects."
FT /evidence="ECO:0000269|PubMed:11807089,
FT ECO:0000269|PubMed:15470109"
FT MUTAGEN 490
FT /note="G->R: Reduced sphingolipid biosynthesis inhibitor
FT drug myriocin (ISP-1) resistance. Defective in growth and
FT endocytosis."
FT /evidence="ECO:0000269|PubMed:11807089,
FT ECO:0000269|PubMed:15820214"
FT MUTAGEN 504
FT /note="T->A,D,E: Reduced sphingolipid biosynthesis
FT inhibitor drug myriocin (ISP-1) resistance. Defective in
FT growth and endocytosis."
FT /evidence="ECO:0000269|PubMed:11807089,
FT ECO:0000269|PubMed:15470109, ECO:0000269|PubMed:15820214,
FT ECO:0000269|PubMed:15840588"
FT MUTAGEN 504
FT /note="T->A,D: No phosphorylation; when associated with A-
FT 662 or D-662."
FT /evidence="ECO:0000269|PubMed:11807089,
FT ECO:0000269|PubMed:15470109, ECO:0000269|PubMed:15820214,
FT ECO:0000269|PubMed:15840588"
FT MUTAGEN 662
FT /note="T->A,D: No phosphorylation; when associated with A-
FT 504 or D-504."
FT /evidence="ECO:0000269|PubMed:11807089,
FT ECO:0000269|PubMed:15470109, ECO:0000269|PubMed:15820214,
FT ECO:0000269|PubMed:15840588"
FT MUTAGEN 662
FT /note="T->A: No phosphorylation. Reduced sphingolipid
FT biosynthesis inhibitor drug myriocin (ISP-1) resistance. No
FT defect in growth or endocytosis."
FT /evidence="ECO:0000269|PubMed:11807089,
FT ECO:0000269|PubMed:15470109, ECO:0000269|PubMed:15820214,
FT ECO:0000269|PubMed:15840588"
FT CONFLICT 201
FT /note="P -> L (in Ref. 2; AAA34880)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="M -> I (in Ref. 2; AAA34880)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 680 AA; 76480 MW; 00112BBB849CD2B5 CRC64;
MYSWKSKFKF GKSKEEKEAK HSGFFHSSKK EEQQNNQATA GEHDASITRS SLDRKGTINP
SNSSVVPVRV SYDASSSTST VRDSNGGNSE NTNSSQNLDE TANIGSTGTP NDATSSSGMM
TIKVYNGDDF ILPFPITSSE QILNKLLASG VPPPHKEISK EVDALIAQLS RVQIKNQGPA
DEDLISSESA AKFIPSTIML PGSSTLNPLL YFTIEFDNTV ATIEAEYGTI AKPGFNKIST
FDVTRKLPYL KIDVFARIPS ILLPSKTWQQ EMGLQDEKLQ TIFDKINSNQ DIHLDSFHLP
INLSFDSAAS IRLYNHHWIT LDNGLGKINI SIDYKPSRNK PLSIDDFDLL KVIGKGSFGK
VMQVRKKDTQ KVYALKAIRK SYIVSKSEVT HTLAERTVLA RVDCPFIVPL KFSFQSPEKL
YFVLAFINGG ELFYHLQKEG RFDLSRARFY TAELLCALDN LHKLDVVYRD LKPENILLDY
QGHIALCDFG LCKLNMKDDD KTDTFCGTPE YLAPELLLGL GYTKAVDWWT LGVLLYEMLT
GLPPYYDEDV PKMYKKILQE PLVFPDGFDR DAKDLLIGLL SRDPTRRLGY NGADEIRNHP
FFSQLSWKRL LMKGYIPPYK PAVSNSMDTS NFDEEFTREK PIDSVVDEYL SESVQKQFGG
WTYVGNEQLG SSMVQGRSIR
