KCC1_YEAST
ID KCC1_YEAST Reviewed; 446 AA.
AC P27466; D6VTP5;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Calcium/calmodulin-dependent protein kinase I;
DE EC=2.7.11.17;
GN Name=CMK1; OrderedLocusNames=YFR014C;
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=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
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-417; SER-420 AND SER-429, 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-429, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417; SER-418; SER-420 AND
RP SER-429, 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 1520 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}.
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; X57782; CAA40928.1; -; Genomic_DNA.
DR EMBL; D90375; BAA14383.1; -; Genomic_DNA.
DR EMBL; D50617; BAA09253.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12455.1; -; Genomic_DNA.
DR PIR; A40896; A40896.
DR RefSeq; NP_116669.1; NM_001179979.2.
DR AlphaFoldDB; P27466; -.
DR SMR; P27466; -.
DR BioGRID; 31166; 294.
DR DIP; DIP-2305N; -.
DR IntAct; P27466; 34.
DR MINT; P27466; -.
DR STRING; 4932.YFR014C; -.
DR iPTMnet; P27466; -.
DR MaxQB; P27466; -.
DR PaxDb; P27466; -.
DR PRIDE; P27466; -.
DR EnsemblFungi; YFR014C_mRNA; YFR014C; YFR014C.
DR GeneID; 850568; -.
DR KEGG; sce:YFR014C; -.
DR SGD; S000001910; CMK1.
DR VEuPathDB; FungiDB:YFR014C; -.
DR eggNOG; KOG0032; Eukaryota.
DR GeneTree; ENSGT00940000166992; -.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; P27466; -.
DR OMA; MLNERDD; -.
DR BioCyc; YEAST:G3O-30467-MON; -.
DR BRENDA; 2.7.11.17; 984.
DR PRO; PR:P27466; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P27466; protein.
DR GO; GO:0005737; C:cytoplasm; IDA: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; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IMP:SGD.
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 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 ATP-binding; Calmodulin-binding; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..446
FT /note="Calcium/calmodulin-dependent protein kinase I"
FT /id="PRO_0000086090"
FT DOMAIN 37..299
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..323
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT REGION 349..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 161
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 43..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 343
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P22517"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22517"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT CONFLICT 53..54
FT /note="QA -> VR (in Ref. 1; CAA40928)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="L -> V (in Ref. 1; CAA40928)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="R -> T (in Ref. 1; CAA40928)"
FT /evidence="ECO:0000305"
FT CONFLICT 199..202
FT /note="PAGS -> AGTA (in Ref. 1; CAA40928)"
FT /evidence="ECO:0000305"
FT CONFLICT 237..243
FT /note="SAFRAER -> ATIDRK (in Ref. 1; CAA40928)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="K -> Q (in Ref. 1; CAA40928)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 446 AA; 50296 MW; 586C31CED6311555 CRC64;
MDDKVSEKES SPKQTEEDSE GKMAHVQPAS YVNKKKYVFG KTLGAGTFGV VRQAKNTETG
EDVAVKILIK KALKGNKVQL EALYDELDIL QRLHHPNIVA FKDWFESKDK FYIITQLAKG
GELFDRILKK GKFTEEDAVR ILVEILSAVK YMHSQNIVHR DLKPENLLYI DKSDESPLVV
ADFGIAKRLK SDEELLYKPA GSLGYVAPEV LTQDGHGKPC DIWSIGVITY TLLCGYSAFR
AERVQDFLDE CTTGEYPVKF HRPYWDSVSN KAKQFILKAL NLDPSKRPTA AELLEDPWII
CTELKTHNLL PGLKEGLDAR QKFRNSVERV RLNMKIQKLR DLYLEQTESD SDFDEGSQAN
GSVPPLKATD TSQLSKKLSE EEQSKLKSEL TSKAFAQLVN TVLAEKEKFL NINRVCSSDS
DLPGSDIKSL DEAKEKPEGK DTKTEE
