MCK1_YEAST
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 03-AUG-2022, entry version 206.
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; 607.
DR DIP; DIP-5860N; -.
DR IntAct; P21965; 52.
DR MINT; P21965; -.
DR STRING; 4932.YNL307C; -.
DR iPTMnet; P21965; -.
DR MaxQB; P21965; -.
DR PaxDb; P21965; -.
DR PRIDE; P21965; -.
DR EnsemblFungi; YNL307C_mRNA; YNL307C; YNL307C.
DR GeneID; 855409; -.
DR KEGG; sce:YNL307C; -.
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; WYGPFAI; -.
DR BioCyc; YEAST:G3O-33294-MON; -.
DR BRENDA; 2.7.11.26; 984.
DR Reactome; R-SCE-3371453; Regulation of HSF1-mediated heat shock response.
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:0030163; P:protein catabolic process; IMP:SGD.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd14137; STKc_GSK3; 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 Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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
