YPK2_YEAST
ID YPK2_YEAST Reviewed; 677 AA.
AC P18961; D6VZS6;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Serine/threonine-protein kinase YPK2/YKR2;
DE EC=2.7.11.1;
GN Name=YPK2; Synonyms=YKR2; OrderedLocusNames=YMR104C; ORFNames=YM9718.03C;
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=2663649; DOI=10.1016/0378-1119(89)90021-8;
RA Kubo K., Ohno S., Matsumoto S., Yahara I., Suzuki K.;
RT "A novel yeast gene coding for a putative protein kinase.";
RL Gene 76:177-180(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [4]
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION BY PKH2, ACTIVATION BY
RP PKH2, AND MUTAGENESIS OF LYS-373.
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 [6]
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 [7]
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 [8]
RP ACTIVATION BY PHS, AND MUTAGENESIS OF LYS-373.
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 [9]
RP FUNCTION, PHOSPHORYLATION AT THR-501 BY PKH2, PHOSPHORYLATION AT SER-641
RP AND THR-659 BY TOR2, REGULATION BY TOR2, AND MUTAGENESIS OF ASP-239;
RP SER-641 AND THR-659.
RX PubMed=16055732; DOI=10.1128/mcb.25.16.7239-7248.2005;
RA Kamada Y., Fujioka Y., Suzuki N.N., Inagaki F., Wullschleger S.,
RA Loewith R., Hall M.N., Ohsumi Y.;
RT "Tor2 directly phosphorylates the AGC kinase Ypk2 to regulate actin
RT polarization.";
RL Mol. Cell. Biol. 25:7239-7248(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641 AND SER-650, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-63, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-63; SER-72; THR-499 AND
RP SER-669, AND IDENTIFICATION 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).
CC -!- FUNCTION: May act as a downstream kinase in the sphingolipid-mediated
CC signaling pathway. Plays an essential role in the proliferation of
CC yeast cells. Involved in a signaling pathway, required for optimal cell
CC wall integrity, that acts in parallel with the PKC1-SLT2-dependent
CC pathway. A substrate of TOR complex 2 (TORC2) and required for TORC2 to
CC regulate spatial aspects of cell growth. Phosphorylation of residue
CC Thr-501 is indispensable for function. {ECO:0000269|PubMed:12221112,
CC ECO:0000269|PubMed:16055732, 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 PKH2 phosphorylation. Kinase activity is
CC regulated by TOR2 via direct phosphorylation of Ser-641 and Thr-659.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
CC -!- PTM: Autophosphorylated (By similarity). Phosphorylated by PKH2 and
CC TOR2. {ECO:0000250, ECO:0000269|PubMed:12221112,
CC ECO:0000269|PubMed:16055732}.
CC -!- MISCELLANEOUS: Present with 1310 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}.
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; M24929; AAA78259.1; -; Genomic_DNA.
DR EMBL; Z49702; CAA89740.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10000.1; -; Genomic_DNA.
DR PIR; JS0178; JS0178.
DR RefSeq; NP_013822.1; NM_001182604.1.
DR AlphaFoldDB; P18961; -.
DR SMR; P18961; -.
DR BioGRID; 35279; 120.
DR DIP; DIP-4438N; -.
DR IntAct; P18961; 18.
DR MINT; P18961; -.
DR STRING; 4932.YMR104C; -.
DR iPTMnet; P18961; -.
DR MaxQB; P18961; -.
DR PaxDb; P18961; -.
DR PRIDE; P18961; -.
DR EnsemblFungi; YMR104C_mRNA; YMR104C; YMR104C.
DR GeneID; 855130; -.
DR KEGG; sce:YMR104C; -.
DR SGD; S000004710; YPK2.
DR VEuPathDB; FungiDB:YMR104C; -.
DR eggNOG; KOG0598; Eukaryota.
DR GeneTree; ENSGT00940000175269; -.
DR HOGENOM; CLU_000288_120_2_1; -.
DR InParanoid; P18961; -.
DR OMA; HEHEHHI; -.
DR BioCyc; YEAST:G3O-32802-MON; -.
DR BRENDA; 2.7.11.1; 984.
DR PRO; PR:P18961; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P18961; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0070941; P:eisosome assembly; IGI:SGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0060237; P:regulation of fungal-type cell wall organization; IGI: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 shape; Cell wall biogenesis/degradation; Cytoplasm;
KW Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..677
FT /note="Serine/threonine-protein kinase YPK2/YKR2"
FT /id="PRO_0000086836"
FT DOMAIN 344..599
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 600..670
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 467
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 350..358
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 373
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 63
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 66
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P12688"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 499
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 501
FT /note="Phosphothreonine; by PKH2"
FT /evidence="ECO:0000269|PubMed:16055732"
FT MOD_RES 641
FT /note="Phosphoserine; by TOR2"
FT /evidence="ECO:0000269|PubMed:16055732,
FT ECO:0007744|PubMed:17330950"
FT MOD_RES 650
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 659
FT /note="Phosphothreonine; by TOR2"
FT /evidence="ECO:0000269|PubMed:16055732"
FT MOD_RES 669
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 239
FT /note="D->A: Rescues growth of cells compromised in TORC2,
FT but not TORC1 function. Restores SLT2 activation and
FT suppresses actin cytoskeleton organization defect in TOR2
FT mutant cells."
FT /evidence="ECO:0000269|PubMed:16055732"
FT MUTAGEN 373
FT /note="K->R,A: No kinase activity."
FT /evidence="ECO:0000269|PubMed:12221112,
FT ECO:0000269|PubMed:15840588"
FT MUTAGEN 641
FT /note="S->A: Reduced kinase activity; when associated with
FT A-659."
FT /evidence="ECO:0000269|PubMed:16055732"
FT MUTAGEN 659
FT /note="T->A: Reduced kinase activity; when associated with
FT A-641."
FT /evidence="ECO:0000269|PubMed:16055732"
SQ SEQUENCE 677 AA; 76664 MW; E1FAB0295386A113 CRC64;
MHSWRISKFK LGRSKEDDGS SEDENEKSWG NGLFHFHHGE KHHDGSPKNH NHEHEHHIRK
INTNETLPSS LSSPKLRNDA SFKNPSGIGN DNSKASERKA SQSSTETQGP SSESGLMTVK
VYSGKDFTLP FPITSNSTIL QKLLSSGILT SSSNDASEVA AIMRQLPRYK RVDQDSAGEG
LIDRAFATKF IPSSILLPGS TNSSPLLYFT IEFDNSITTI SPDMGTMEQP VFNKISTFDV
TRKLRFLKID VFARIPSLLL PSKNWQQEIG EQDEVLKEIL KKINTNQDIH LDSFHLPLNL
KIDSAAQIRL YNHHWISLER GYGKLNITVD YKPSKNKPLS IDDFDLLKVI GKGSFGKVMQ
VRKKDTQKIY ALKALRKAYI VSKCEVTHTL AERTVLARVD CPFIVPLKFS FQSPEKLYLV
LAFINGGELF YHLQHEGRFS LARSRFYIAE LLCALDSLHK LDVIYRDLKP ENILLDYQGH
IALCDFGLCK LNMKDNDKTD TFCGTPEYLA PEILLGQGYT KTVDWWTLGI LLYEMMTGLP
PYYDENVPVM YKKILQQPLL FPDGFDPAAK DLLIGLLSRD PSRRLGVNGT DEIRNHPFFK
DISWKKLLLK GYIPPYKPIV KSEIDTANFD QEFTKEKPID SVVDEYLSAS IQKQFGGWTY
IGDEQLGDSP SQGRSIS
