ID   KCC2_YEAST              Reviewed;         447 AA.
AC   P22517; D6W250;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   27-MAR-2024, entry version 206.
DE   RecName: Full=Calcium/calmodulin-dependent protein kinase II;
DE            EC=2.7.11.17;
GN   Name=CMK2; OrderedLocusNames=YOL016C;
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=2026147; DOI=10.1002/j.1460-2075.1991.tb07671.x;
RA   Pausch M.H., Kaim D., Kunisawa R., Admon A., Thorner J.;
RT   "Multiple Ca2+/calmodulin-dependent protein kinase genes in a unicellular
RT   eukaryote.";
RL   EMBO J. 10:1511-1522(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2061341; DOI=10.1016/s0021-9258(18)98968-4;
RA   Ohya Y., Kawasaki H., Suzuki K., Londesborough J., Anraku Y.;
RT   "Two yeast genes encoding calmodulin-dependent protein kinases. Isolation,
RT   sequencing and bacterial expressions of CMK1 and CMK2.";
RL   J. Biol. Chem. 266:12784-12794(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(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   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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367 AND SER-371, 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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443, AND IDENTIFICATION BY
RP   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   [8]
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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-353; SER-354; SER-367 AND
RP   SER-371, 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: Important in cellular regulation.
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=2.7.11.17;
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=2.7.11.17;
CC   -!- SUBUNIT: Multimeric.
CC   -!- MISCELLANEOUS: Present with 7500 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. CaMK subfamily. {ECO:0000305}.
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DR   EMBL; X56961; CAA40281.1; -; Genomic_DNA.
DR   EMBL; D90376; BAA14384.1; -; Genomic_DNA.
DR   EMBL; Z74758; CAA99015.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10766.1; -; Genomic_DNA.
DR   PIR; B40896; B40896.
DR   RefSeq; NP_014626.1; NM_001183270.1.
DR   AlphaFoldDB; P22517; -.
DR   SMR; P22517; -.
DR   BioGRID; 34387; 154.
DR   DIP; DIP-2306N; -.
DR   IntAct; P22517; 8.
DR   MINT; P22517; -.
DR   STRING; 4932.YOL016C; -.
DR   iPTMnet; P22517; -.
DR   MaxQB; P22517; -.
DR   PaxDb; 4932-YOL016C; -.
DR   PeptideAtlas; P22517; -.
DR   EnsemblFungi; YOL016C_mRNA; YOL016C; YOL016C.
DR   GeneID; 854144; -.
DR   KEGG; sce:YOL016C; -.
DR   AGR; SGD:S000005376; -.
DR   SGD; S000005376; CMK2.
DR   VEuPathDB; FungiDB:YOL016C; -.
DR   eggNOG; KOG0032; Eukaryota.
DR   GeneTree; ENSGT00940000166992; -.
DR   HOGENOM; CLU_000288_63_0_1; -.
DR   InParanoid; P22517; -.
DR   OMA; HDWFESR; -.
DR   OrthoDB; 1121238at2759; -.
DR   BioCyc; YEAST:G3O-33432-MONOMER; -.
DR   BRENDA; 2.7.11.17; 984.
DR   BioGRID-ORCS; 854144; 0 hits in 13 CRISPR screens.
DR   PRO; PR:P22517; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; P22517; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IDA: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:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:SGD.
DR   CDD; cd05117; STKc_CAMK; 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   PANTHER; PTHR24347:SF433; CALCIUM_CALMODULIN-DEPENDENT PROTEIN KINASE I-RELATED; 1.
DR   PANTHER; PTHR24347; SERINE/THREONINE-PROTEIN KINASE; 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   ATP-binding; Calmodulin-binding; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..447
FT                   /note="Calcium/calmodulin-dependent protein kinase II"
FT                   /id="PRO_0000086105"
FT   DOMAIN          47..309
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          323..334
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          421..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        171
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         53..61
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         76
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         316
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         353
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         354
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         367
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         371
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         387
FT                   /note="Phosphoserine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         443
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   CONFLICT        282
FT                   /note="V -> A (in Ref. 1; CAA40281)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   447 AA;  50447 MW;  5990740B980B8312 CRC64;
     MPKESEVINS EFHVDVQDPE RLNGHPVAKF INKLSGQPES YVNRTNYIFG RTLGAGSFGV
     VRQARKLSTN EDVAIKILLK KALQGNNVQL QMLYEELSIL QKLSHPNIVS FKDWFESKDK
     FYIVTQLATG GELFDRILSR GKFTEVDAVE IIVQILGAVE YMHSKNVVHR DLKPENVLYV
     DKSENSPLVI ADFGIAKQLK GEEDLIYKAA GSLGYVAPEV LTQDGHGKPC DIWSIGVITY
     TLLCGYSPFI AESVEGFMEE CTASRYPVTF HMPYWDNISI DVKRFILKAL RLNPADRPTA
     TELLDDPWIT SKRVETSNIL PDVKKGFSLR KKLRDAIEIV KLNNRIKRLR NMYSLGDDGD
     NDIEENSLNE SLLDGVTHSL DDLRLQSQKK GGELTEEQMK LKSALTKDAF VQIVKAATKN
     KHKVLAGEEE DDSKKTLHDD RESKSED
//