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Serine/threonine-protein kinase YPK1 (EC 2.7.11.1) (Sphingosine-like immunosuppressant resistant protein 2) (Yeast protein kinase 1)

 YPK1_YEAST              Reviewed;         680 AA.
P12688; D6VX69;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 2.
30-AUG-2017, entry version 187.
RecName: Full=Serine/threonine-protein kinase YPK1;
EC=2.7.11.1;
AltName: Full=Sphingosine-like immunosuppressant resistant protein 2;
AltName: Full=Yeast protein kinase 1;
Name=YPK1; Synonyms=SLI2; OrderedLocusNames=YKL126W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2850145; DOI=10.1089/dna.1.1988.7.469;
Maurer R.A.;
"Isolation of a yeast protein kinase gene by screening with a
mammalian protein kinase cDNA.";
DNA 7:469-474(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8196765; DOI=10.1038/369371a0;
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M.,
Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C.,
Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G.,
Zimmermann J., Haasemann M., Becker I., Mewes H.-W.;
"Complete DNA sequence of yeast chromosome XI.";
Nature 369:371-378(1994).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
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.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
DISCUSSION OF SEQUENCE, AND FUNCTION.
PubMed=8437590; DOI=10.1007/BF00277146;
Chen P.C., Lee K.S., Levin D.E.;
"A pair of putative protein kinase genes (YPK1 and YPK2) is required
for cell growth in Saccharomyces cerevisiae.";
Mol. Gen. Genet. 236:443-447(1993).
[5]
PHOSPHORYLATION AT THR-504 BY PKH1.
PubMed=10074427; DOI=10.1016/S0960-9822(99)80088-8;
Casamayor A., Torrance P.D., Kobayashi T., Thorner J., Alessi D.R.;
"Functional counterparts of mammalian protein kinases PDK1 and SGK in
budding yeast.";
Curr. Biol. 9:186-197(1999).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-376.
PubMed=10825204; DOI=10.1128/MCB.20.12.4411-4419.2000;
Sun Y., Taniguchi R., Tanoue D., Yamaji T., Takematsu H., Mori K.,
Fujita T., Kawasaki T., Kozutsumi Y.;
"Sli2 (Ypk1), a homologue of mammalian protein kinase SGK, is a
downstream kinase in the sphingolipid-mediated signaling pathway of
yeast.";
Mol. Cell. Biol. 20:4411-4419(2000).
[7]
INVOLVEMENT IN ENDOCYTOSIS, AND MUTAGENESIS OF LYS-376; ASP-488;
GLY-490; THR-504 AND THR-662.
PubMed=11807089; DOI=10.1083/jcb.200107135;
deHart A.K.A., Schnell J.D., Allen D.A., Hicke L.;
"The conserved Pkh-Ypk kinase cascade is required for endocytosis in
yeast.";
J. Cell Biol. 156:241-248(2002).
[8]
FUNCTION, SUBCELLULAR LOCATION, ACTIVATION BY PKH1, AND MUTAGENESIS OF
LYS-376.
PubMed=12221112; DOI=10.1091/mbc.E02-04-0201;
Roelants F.M., Torrance P.D., Bezman N., Thorner J.;
"Pkh1 and Pkh2 differentially phosphorylate and activate Ypk1 and Ykr2
and define protein kinase modules required for maintenance of cell
wall integrity.";
Mol. Biol. Cell 13:3005-3028(2002).
[9]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[10]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[11]
INVOLVEMENT IN MYRIOCIN RESISTANCE.
PubMed=15025559; DOI=10.1042/BJ20040108;
Momoi M., Tanoue D., Sun Y., Takematsu H., Suzuki Y., Suzuki M.,
Suzuki A., Fujita T., Kozutsumi Y.;
"SLI1 (YGR212W) is a major gene conferring resistance to the
sphingolipid biosynthesis inhibitor ISP-1, and encodes an ISP-1 N-
acetyltransferase in yeast.";
Biochem. J. 381:321-328(2004).
[12]
FUNCTION, PHOSPHORYLATION, AND MUTAGENESIS OF LYS-376; ASP-488;
THR-504 AND THR-662.
PubMed=15470109; DOI=10.1099/mic.0.27286-0;
Roelants F.M., Torrance P.D., Thorner J.;
"Differential roles of PDK1- and PDK2-phosphorylation sites in the
yeast AGC kinases Ypk1, Pkc1 and Sch9.";
Microbiology 150:3289-3304(2004).
[13]
MUTAGENESIS OF LYS-376; GLY-490; THR-504 AND THR-662.
PubMed=15820214; DOI=10.1016/j.abb.2005.02.030;
Tanoue D., Kobayashi T., Sun Y., Fujita T., Takematsu H.,
Kozutsumi Y.;
"The requirement for the hydrophobic motif phosphorylation of Ypk1 in
yeast differs depending on the downstream events, including
endocytosis, cell growth, and resistance to a sphingolipid
biosynthesis inhibitor, ISP-1.";
Arch. Biochem. Biophys. 437:29-41(2005).
[14]
ENZYME REGULATION, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT THR-504 AND
THR-662 BY PKH1, AND MUTAGENESIS OF LYS-376; THR-504 AND THR-662.
PubMed=15840588; DOI=10.1074/jbc.M502972200;
Liu K., Zhang X., Lester R.L., Dickson R.C.;
"The sphingoid long chain base phytosphingosine activates AGC-type
protein kinases in Saccharomyces cerevisiae including Ypk1, Ypk2, and
Sch9.";
J. Biol. Chem. 280:22679-22687(2005).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57; SER-644 AND SER-653,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170 AND SER-653, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57; SER-61; SER-64;
SER-71; SER-170; THR-502; THR-504; SER-644; SER-653 AND SER-671, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[19]
FUNCTION, AND PHOSPHORYLATION BY FPK1.
PubMed=19966303; DOI=10.1073/pnas.0912497106;
Roelants F.M., Baltz A.G., Trott A.E., Fereres S., Thorner J.;
"A protein kinase network regulates the function of aminophospholipid
flippases.";
Proc. Natl. Acad. Sci. U.S.A. 107:34-39(2010).
-!- FUNCTION: Plays an essential role in the proliferation of yeast
cells. Involved in a signaling pathway, required for optimal cell
wall integrity, that acts in parallel with the PKC1-SLT2-dependent
pathway. Downstream kinase in the sphingolipid-mediated signaling
pathway. Its phosphorylation is regulated by the intracellular
sphingolipid concentration. Cooperates with SLI1 in mediating
resistance to the sphingolipid biosynthesis inhibitor drug
myriocin (ISP-1). Its kinase activity is essential for the
resistance. Required for both receptor-mediated and fluid-phase
endocytosis, but is not necessary for receptor phosphorylation or
ubiquitination. Necessary for the internalization of plasma
membrane proteins carrying different types of internalization
signals. Acts downstream of the PKH kinases to control endocytosis
by phosphorylating components of the endocytic machinery.
Phosphorylation of residue Thr-504 in the activation loop is
essential for activity. phosphorylates and down-regulates flippase
activator FPK1. {ECO:0000269|PubMed:10825204,
ECO:0000269|PubMed:12221112, ECO:0000269|PubMed:15470109,
ECO:0000269|PubMed:19966303, ECO:0000269|PubMed:8437590}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Activated by phytosphingosine (PHS), a
sphingoid long chain base. Activated by PKH1 phosphorylation.
{ECO:0000269|PubMed:15840588}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10825204,
ECO:0000269|PubMed:12221112, ECO:0000269|PubMed:14562095}. Cell
membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305};
Cytoplasmic side {ECO:0000305}. Note=Intracellular localization is
regulated by the intracellular sphingolipid levels. During the
yeast cell cycle, distributed both on the plasma membrane and in
the cytosol. Greater accumulation was detected on the plasma
membrane, such as in the budding area, a daughter cell and the
neck region of the mother cell in the S phase, and the septum
between a mother cell and a daughter cell in the G2 phase.
-!- PTM: Autophosphorylated. Autophosphorylation is stimulated by PHS.
Phosphorylated by PKH1. PHS stimulates phosphorylation by PKH1.
The N-terminal half is phosphorylated by FPK1.
{ECO:0000269|PubMed:10074427, ECO:0000269|PubMed:15470109,
ECO:0000269|PubMed:15840588, ECO:0000269|PubMed:19966303}.
-!- MISCELLANEOUS: Present with 2950 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. RAC subfamily. {ECO:0000305}.
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EMBL; M21307; AAA34880.1; -; Genomic_DNA.
EMBL; Z28126; CAA81967.1; -; Genomic_DNA.
EMBL; BK006944; DAA09035.1; -; Genomic_DNA.
PIR; S37955; S37955.
RefSeq; NP_012796.1; NM_001179692.1.
ProteinModelPortal; P12688; -.
SMR; P12688; -.
BioGrid; 34010; 118.
DIP; DIP-4869N; -.
IntAct; P12688; 19.
MINT; MINT-505912; -.
STRING; 4932.YKL126W; -.
iPTMnet; P12688; -.
MaxQB; P12688; -.
PRIDE; P12688; -.
EnsemblFungi; YKL126W; YKL126W; YKL126W.
GeneID; 853733; -.
KEGG; sce:YKL126W; -.
EuPathDB; FungiDB:YKL126W; -.
SGD; S000001609; YPK1.
GeneTree; ENSGT00890000139324; -.
HOGENOM; HOG000233033; -.
InParanoid; P12688; -.
KO; K13303; -.
OMA; NQGYTRS; -.
OrthoDB; EOG092C0HH3; -.
BioCyc; YEAST:G3O-31908-MONOMER; -.
BRENDA; 2.7.11.1; 984.
Reactome; R-SCE-114604; GPVI-mediated activation cascade.
Reactome; R-SCE-1257604; PIP3 activates AKT signaling.
Reactome; R-SCE-1358803; Downregulation of ERBB2:ERBB3 signaling.
Reactome; R-SCE-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
Reactome; R-SCE-165158; Activation of AKT2.
Reactome; R-SCE-166208; mTORC1-mediated signalling.
Reactome; R-SCE-198693; AKT phosphorylates targets in the nucleus.
Reactome; R-SCE-198753; ERK/MAPK targets.
Reactome; R-SCE-199418; Negative regulation of the PI3K/AKT network.
Reactome; R-SCE-203615; eNOS activation.
Reactome; R-SCE-211163; AKT-mediated inactivation of FOXO1A.
Reactome; R-SCE-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-SCE-375165; NCAM signaling for neurite out-growth.
Reactome; R-SCE-389357; CD28 dependent PI3K/Akt signaling.
Reactome; R-SCE-389513; CTLA4 inhibitory signaling.
Reactome; R-SCE-392451; G beta:gamma signalling through PI3Kgamma.
Reactome; R-SCE-444257; RSK activation.
Reactome; R-SCE-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
Reactome; R-SCE-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-SCE-6804757; Regulation of TP53 Degradation.
Reactome; R-SCE-6804758; Regulation of TP53 Activity through Acetylation.
Reactome; R-SCE-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-SCE-881907; Gastrin-CREB signalling pathway via PKC and MAPK.
PRO; PR:P12688; -.
Proteomes; UP000002311; Chromosome XI.
GO; GO:0005935; C:cellular bud neck; IDA:SGD.
GO; GO:0005829; C:cytosol; IDA:SGD.
GO; GO:0005886; C:plasma membrane; IDA:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019887; F:protein kinase regulator activity; IMP:CACAO.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:SGD.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0071311; P:cellular response to acetate; IMP:SGD.
GO; GO:0070941; P:eisosome assembly; IGI:SGD.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0006650; P:glycerophospholipid metabolic process; IMP:SGD.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0061093; P:negative regulation of phospholipid translocation; IMP:SGD.
GO; GO:0090157; P:negative regulation of sphingolipid biosynthesis involved in cellular sphingolipid homeostasis; IMP:SGD.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IGI:SGD.
GO; GO:0046777; P:protein autophosphorylation; IDA:SGD.
GO; GO:0006468; P:protein phosphorylation; IDA:SGD.
GO; GO:0060237; P:regulation of fungal-type cell wall organization; IMP:SGD.
GO; GO:0000749; P:response to pheromone involved in conjugation with cellular fusion; IMP:SGD.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR017892; Pkinase_C.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00433; Pkinase_C; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
ATP-binding; Cell membrane; Cell wall biogenesis/degradation;
Complete proteome; Cytoplasm; Endocytosis; Kinase; Membrane;
Nucleotide-binding; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 680 Serine/threonine-protein kinase YPK1.
/FTId=PRO_0000086835.
DOMAIN 347 602 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 603 673 AGC-kinase C-terminal.
NP_BIND 353 361 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 470 470 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 376 376 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 57 57 Phosphothreonine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
MOD_RES 61 61 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 64 64 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 71 71 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 170 170 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 502 502 Phosphothreonine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 504 504 Phosphothreonine; by PKH1.
{ECO:0000244|PubMed:19779198,
ECO:0000269|PubMed:10074427,
ECO:0000269|PubMed:15840588}.
MOD_RES 644 644 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
MOD_RES 653 653 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 662 662 Phosphothreonine; by PKH1.
{ECO:0000269|PubMed:15840588}.
MOD_RES 671 671 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MUTAGEN 376 376 K->A,R: No kinase activity. ATP-binding
defect. Internalization defects.
{ECO:0000269|PubMed:10825204,
ECO:0000269|PubMed:11807089,
ECO:0000269|PubMed:12221112,
ECO:0000269|PubMed:15470109,
ECO:0000269|PubMed:15820214,
ECO:0000269|PubMed:15840588}.
MUTAGEN 488 488 D->A: Catalytically inactive.
Internalization defects.
{ECO:0000269|PubMed:11807089,
ECO:0000269|PubMed:15470109}.
MUTAGEN 490 490 G->R: Reduced sphingolipid biosynthesis
inhibitor drug myriocin (ISP-1)
resistance. Defective in growth and
endocytosis.
{ECO:0000269|PubMed:11807089,
ECO:0000269|PubMed:15820214}.
MUTAGEN 504 504 T->A,D,E: Reduced sphingolipid
biosynthesis inhibitor drug myriocin
(ISP-1) resistance. Defective in growth
and endocytosis.
{ECO:0000269|PubMed:11807089,
ECO:0000269|PubMed:15470109,
ECO:0000269|PubMed:15820214,
ECO:0000269|PubMed:15840588}.
MUTAGEN 504 504 T->A,D: No phosphorylation; when
associated with A-662 or D-662.
{ECO:0000269|PubMed:11807089,
ECO:0000269|PubMed:15470109,
ECO:0000269|PubMed:15820214,
ECO:0000269|PubMed:15840588}.
MUTAGEN 662 662 T->A,D: No phosphorylation; when
associated with A-504 or D-504.
{ECO:0000269|PubMed:11807089,
ECO:0000269|PubMed:15470109,
ECO:0000269|PubMed:15820214,
ECO:0000269|PubMed:15840588}.
MUTAGEN 662 662 T->A: No phosphorylation. Reduced
sphingolipid biosynthesis inhibitor drug
myriocin (ISP-1) resistance. No defect in
growth or endocytosis.
{ECO:0000269|PubMed:11807089,
ECO:0000269|PubMed:15470109,
ECO:0000269|PubMed:15820214,
ECO:0000269|PubMed:15840588}.
CONFLICT 201 201 P -> L (in Ref. 2; AAA34880).
{ECO:0000305}.
CONFLICT 553 553 M -> I (in Ref. 2; AAA34880).
{ECO:0000305}.
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


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