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Protein

Calcium/calmodulin-dependent protein kinase II

Gene

CMK2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Important in cellular regulation.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei76 – 761ATPPROSITE-ProRule annotation
Active sitei171 – 1711Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi53 – 619ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • calmodulin-dependent protein kinase activity Source: SGD

GO - Biological processi

  • protein phosphorylation Source: SGD
  • signal transduction Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Calmodulin-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33432-MONOMER.
BRENDAi2.7.11.17. 984.
ReactomeiREACT_336144. CREB phosphorylation through the activation of CaMKII.
REACT_353242. HSF1-dependent transactivation.

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium/calmodulin-dependent protein kinase II (EC:2.7.11.17)
Gene namesi
Name:CMK2
Ordered Locus Names:YOL016C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XV

Organism-specific databases

CYGDiYOL016c.
EuPathDBiFungiDB:YOL016C.
SGDiS000005376. CMK2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 447447Calcium/calmodulin-dependent protein kinase IIPRO_0000086105Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei316 – 3161Phosphothreonine; by autocatalysisBy similarity
Modified residuei353 – 3531Phosphotyrosine1 Publication
Modified residuei354 – 3541Phosphoserine1 Publication
Modified residuei367 – 3671Phosphoserine2 Publications
Modified residuei371 – 3711Phosphoserine1 Publication
Modified residuei387 – 3871Phosphoserine; by autocatalysisBy similarity
Modified residuei443 – 4431Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP22517.
PaxDbiP22517.
PeptideAtlasiP22517.

Interactioni

Subunit structurei

Multimeric.

Protein-protein interaction databases

BioGridi34387. 100 interactions.
DIPiDIP-2306N.
IntActiP22517. 6 interactions.
MINTiMINT-481301.

Structurei

3D structure databases

ProteinModelPortaliP22517.
SMRiP22517. Positions 1-376.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini47 – 309263Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni323 – 33412Calmodulin-bindingBy similarityAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118944.
HOGENOMiHOG000233016.
InParanoidiP22517.
KOiK08794.
OMAiGKNATDH.
OrthoDBiEOG793BK1.

Family and domain databases

InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 1 hit.
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P22517-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKESEVINS EFHVDVQDPE RLNGHPVAKF INKLSGQPES YVNRTNYIFG
60 70 80 90 100
RTLGAGSFGV VRQARKLSTN EDVAIKILLK KALQGNNVQL QMLYEELSIL
110 120 130 140 150
QKLSHPNIVS FKDWFESKDK FYIVTQLATG GELFDRILSR GKFTEVDAVE
160 170 180 190 200
IIVQILGAVE YMHSKNVVHR DLKPENVLYV DKSENSPLVI ADFGIAKQLK
210 220 230 240 250
GEEDLIYKAA GSLGYVAPEV LTQDGHGKPC DIWSIGVITY TLLCGYSPFI
260 270 280 290 300
AESVEGFMEE CTASRYPVTF HMPYWDNISI DVKRFILKAL RLNPADRPTA
310 320 330 340 350
TELLDDPWIT SKRVETSNIL PDVKKGFSLR KKLRDAIEIV KLNNRIKRLR
360 370 380 390 400
NMYSLGDDGD NDIEENSLNE SLLDGVTHSL DDLRLQSQKK GGELTEEQMK
410 420 430 440
LKSALTKDAF VQIVKAATKN KHKVLAGEEE DDSKKTLHDD RESKSED
Length:447
Mass (Da):50,447
Last modified:November 1, 1997 - v2
Checksum:i5990740B980B8312
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti282 – 2821V → A in CAA40281 (PubMed:2026147).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56961 Genomic DNA. Translation: CAA40281.1.
D90376 Genomic DNA. Translation: BAA14384.1.
Z74758 Genomic DNA. Translation: CAA99015.1.
BK006948 Genomic DNA. Translation: DAA10766.1.
PIRiB40896.
RefSeqiNP_014626.1. NM_001183270.1.

Genome annotation databases

EnsemblFungiiYOL016C; YOL016C; YOL016C.
GeneIDi854144.
KEGGisce:YOL016C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56961 Genomic DNA. Translation: CAA40281.1.
D90376 Genomic DNA. Translation: BAA14384.1.
Z74758 Genomic DNA. Translation: CAA99015.1.
BK006948 Genomic DNA. Translation: DAA10766.1.
PIRiB40896.
RefSeqiNP_014626.1. NM_001183270.1.

3D structure databases

ProteinModelPortaliP22517.
SMRiP22517. Positions 1-376.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34387. 100 interactions.
DIPiDIP-2306N.
IntActiP22517. 6 interactions.
MINTiMINT-481301.

Proteomic databases

MaxQBiP22517.
PaxDbiP22517.
PeptideAtlasiP22517.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOL016C; YOL016C; YOL016C.
GeneIDi854144.
KEGGisce:YOL016C.

Organism-specific databases

CYGDiYOL016c.
EuPathDBiFungiDB:YOL016C.
SGDiS000005376. CMK2.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118944.
HOGENOMiHOG000233016.
InParanoidiP22517.
KOiK08794.
OMAiGKNATDH.
OrthoDBiEOG793BK1.

Enzyme and pathway databases

BioCyciYEAST:G3O-33432-MONOMER.
BRENDAi2.7.11.17. 984.
ReactomeiREACT_336144. CREB phosphorylation through the activation of CaMKII.
REACT_353242. HSF1-dependent transactivation.

Miscellaneous databases

NextBioi975888.
PROiP22517.

Family and domain databases

InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 1 hit.
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Multiple Ca2+/calmodulin-dependent protein kinase genes in a unicellular eukaryote."
    Pausch M.H., Kaim D., Kunisawa R., Admon A., Thorner J.
    EMBO J. 10:1511-1522(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Two yeast genes encoding calmodulin-dependent protein kinases. Isolation, sequencing and bacterial expressions of CMK1 and CMK2."
    Ohya Y., Kawasaki H., Suzuki K., Londesborough J., Anraku Y.
    J. Biol. Chem. 266:12784-12794(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  7. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-353; SER-354; SER-367 AND SER-371, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiKCC2_YEAST
AccessioniPrimary (citable) accession number: P22517
Secondary accession number(s): D6W250
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: November 1, 1997
Last modified: July 22, 2015
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 7500 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.