ID   MCK1_YEAST              Reviewed;         375 AA.
AC   P21965; D6W0N8;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   27-MAR-2024, entry version 215.
DE   RecName: Full=Protein kinase MCK1;
DE            EC=2.7.12.1;
DE   AltName: Full=Meiosis and centromere regulatory kinase;
GN   Name=MCK1; Synonyms=YPK1; OrderedLocusNames=YNL307C; ORFNames=N0392;
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], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=1701015; DOI=10.1128/mcb.10.12.6244-6256.1990;
RA   Dailey D., Schieven G.L., Lim M.-Y., Marquardt H., Gilmore T., Thorner J.,
RA   Martin G.S.;
RT   "Novel yeast protein kinase (YPK1 gene product) is a 40-kilodalton
RT   phosphotyrosyl protein associated with protein-tyrosine kinase activity.";
RL   Mol. Cell. Biol. 10:6244-6256(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2010083; DOI=10.1101/gad.5.4.533;
RA   Neigeborn L., Mitchell A.P.;
RT   "The yeast MCK1 gene encodes a protein kinase homolog that activates early
RT   meiotic gene expression.";
RL   Genes Dev. 5:533-548(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2010084; DOI=10.1101/gad.5.4.549;
RA   Shero J.H., Hieter P.;
RT   "A suppressor of a centromere DNA mutation encodes a putative protein
RT   kinase (MCK1).";
RL   Genes Dev. 5:549-560(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=S288c / FY1676;
RX   PubMed=7502583; DOI=10.1002/yea.320111109;
RA   Maftahi M., Nicaud J.-M., Levesque H., Gaillardin C.;
RT   "Sequencing analysis of a 24.7 kb fragment of yeast chromosome XIV
RT   identifies six known genes, a new member of the hexose transporter family
RT   and ten new open reading frames.";
RL   Yeast 11:1077-1085(1995).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8553702; DOI=10.1002/yea.320111311;
RA   Maurer K.C.T., Urbanus J.H.M., Planta R.J.;
RT   "Sequence analysis of a 30 kb DNA segment from yeast chromosome XIV
RT   carrying a ribosomal protein gene cluster, the genes encoding a plasma
RT   membrane protein and a subunit of replication factor C, and a novel
RT   putative serine/threonine protein kinase gene.";
RL   Yeast 11:1303-1310(1995).
RN   [8]
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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-199, AND IDENTIFICATION BY
RP   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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, 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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198; TYR-199 AND SER-202, AND
RP   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).
RN   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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).
CC   -!- FUNCTION: May be an autophosphorylating tyrosine kinase, a bifunctional
CC       (serine/tyrosine-specific) protein kinase, or a serine kinase that is a
CC       substrate for an associated tyrosine kinase. MCK1 is a transcriptional
CC       activator of IME1, it stimulates spore maturation, and play a positive
CC       regulatory role in both mitotic centromere function and activation of
CC       early meiotic gene expression.
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=2.7.12.1;
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=2.7.12.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC   -!- INTERACTION:
CC       P21965; Q00684: CDC14; NbExp=2; IntAct=EBI-10517, EBI-4192;
CC       P21965; P19812: UBR1; NbExp=3; IntAct=EBI-10517, EBI-19909;
CC   -!- PTM: Phosphorylated at tyrosine and serine.
CC   -!- MISCELLANEOUS: Present with 396 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; X55054; CAA38895.1; -; Genomic_DNA.
DR   EMBL; M55984; AAA34764.1; -; Genomic_DNA.
DR   EMBL; Z46259; CAA86388.1; -; Genomic_DNA.
DR   EMBL; Z71583; CAA96236.1; -; Genomic_DNA.
DR   EMBL; Z71582; CAA96235.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10254.1; -; Genomic_DNA.
DR   PIR; A39622; A39622.
DR   RefSeq; NP_014092.1; NM_001183145.1.
DR   AlphaFoldDB; P21965; -.
DR   SMR; P21965; -.
DR   BioGRID; 35532; 624.
DR   DIP; DIP-5860N; -.
DR   IntAct; P21965; 52.
DR   MINT; P21965; -.
DR   STRING; 4932.YNL307C; -.
DR   iPTMnet; P21965; -.
DR   MaxQB; P21965; -.
DR   PaxDb; 4932-YNL307C; -.
DR   PeptideAtlas; P21965; -.
DR   EnsemblFungi; YNL307C_mRNA; YNL307C; YNL307C.
DR   GeneID; 855409; -.
DR   KEGG; sce:YNL307C; -.
DR   AGR; SGD:S000005251; -.
DR   SGD; S000005251; MCK1.
DR   VEuPathDB; FungiDB:YNL307C; -.
DR   eggNOG; KOG0658; Eukaryota.
DR   GeneTree; ENSGT00520000055635; -.
DR   HOGENOM; CLU_000288_181_20_1; -.
DR   InParanoid; P21965; -.
DR   OMA; GPFAIKK; -.
DR   OrthoDB; 2872909at2759; -.
DR   BioCyc; YEAST:G3O-33294-MONOMER; -.
DR   BRENDA; 2.7.11.26; 984.
DR   Reactome; R-SCE-3371453; Regulation of HSF1-mediated heat shock response.
DR   BioGRID-ORCS; 855409; 1 hit in 13 CRISPR screens.
DR   PRO; PR:P21965; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P21965; Protein.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0030332; F:cyclin binding; IPI:SGD.
DR   GO; GO:0004857; F:enzyme inhibitor activity; IMP:SGD.
DR   GO; GO:0004672; F:protein kinase activity; HDA:SGD.
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:0004712; F:protein serine/threonine/tyrosine kinase activity; IDA:SGD.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IEA:RHEA.
DR   GO; GO:0030437; P:ascospore formation; IMP:SGD.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:SGD.
DR   GO; GO:0051321; P:meiotic cell cycle; IMP:SGD.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:SGD.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0030163; P:protein catabolic process; IMP:SGD.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   CDD; cd14137; STKc_GSK3; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR039192; STKc_GSK3.
DR   PANTHER; PTHR24057; GLYCOGEN SYNTHASE KINASE-3 ALPHA; 1.
DR   PANTHER; PTHR24057:SF4; PROTEIN KINASE MCK1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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   Acetylation; ATP-binding; Direct protein sequencing; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..375
FT                   /note="Protein kinase MCK1"
FT                   /id="PRO_0000086317"
FT   DOMAIN          35..327
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        164
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         41..49
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         68
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         198
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         199
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         202
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   375 AA;  43136 MW;  BCF0C776B6E3841B CRC64;
     MSTEEQNGVP LQRGSEFIAD DVTSNKSNNT RRMLVKEYRK IGRGAFGTVV QAYLTQDKKN
     WLGPFAIKKV PAHTEYKSRE LQILRIADHP NIVKLQYFFT HLSPQDNKVY QHLAMECLPE
     TLQIEINRYV TNKLEMPLKH IRLYTYQIAR GMLYLHGLGV CHRDIKPSNV LVDPETGVLK
     ICDFGSAKKL EHNQPSISYI CSRFYRAPEL IIGCTQYTTQ IDIWGLGCVM GEMLIGKAIF
     QGQEPLLQLR EIAKLLGPPD KRFIFFSNPA YDGPLFSKPL FSGSSQQRFE KYFGHSGPDG
     IDLLMKILVY EPQQRLSPRR ILAHQFFNEL RNDDTFLPRG FTEPIKLPNL FDFNDFELQI
     LGEFADKIKP TKVAE
//