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P22517

- KCC2_YEAST

UniProt

P22517 - KCC2_YEAST

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Protein

Calcium/calmodulin-dependent protein kinase II

Gene
CMK2, YOL016C
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 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 – 761ATP By similarity
Active sitei171 – 1711Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi53 – 619ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calmodulin-dependent protein kinase activity Source: SGD

GO - Biological processi

  1. protein phosphorylation Source: SGD
  2. 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.

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: Chromosome XV

Organism-specific databases

CYGDiYOL016c.
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 autocatalysis By similarity
Modified residuei353 – 3531Phosphotyrosine1 Publication
Modified residuei354 – 3541Phosphoserine1 Publication
Modified residuei367 – 3671Phosphoserine2 Publications
Modified residuei371 – 3711Phosphoserine1 Publication
Modified residuei387 – 3871Phosphoserine; by autocatalysis By similarity
Modified residuei443 – 4431Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP22517.
PaxDbiP22517.
PeptideAtlasiP22517.

Expressioni

Gene expression databases

GenevestigatoriP22517.

Interactioni

Subunit structurei

Multimeric.

Protein-protein interaction databases

BioGridi34387. 101 interactions.
DIPiDIP-2306N.
IntActiP22517. 6 interactions.
MINTiMINT-481301.
STRINGi4932.YOL016C.

Structurei

3D structure databases

ProteinModelPortaliP22517.
SMRiP22517. Positions 32-371.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini47 – 309263Protein kinaseAdd
BLAST

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00750000117487.
HOGENOMiHOG000233016.
KOiK08794.
OMAiWDNISID.
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_dom.
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

MPKESEVINS EFHVDVQDPE RLNGHPVAKF INKLSGQPES YVNRTNYIFG    50
RTLGAGSFGV VRQARKLSTN EDVAIKILLK KALQGNNVQL QMLYEELSIL 100
QKLSHPNIVS FKDWFESKDK FYIVTQLATG GELFDRILSR GKFTEVDAVE 150
IIVQILGAVE YMHSKNVVHR DLKPENVLYV DKSENSPLVI ADFGIAKQLK 200
GEEDLIYKAA GSLGYVAPEV LTQDGHGKPC DIWSIGVITY TLLCGYSPFI 250
AESVEGFMEE CTASRYPVTF HMPYWDNISI DVKRFILKAL RLNPADRPTA 300
TELLDDPWIT SKRVETSNIL PDVKKGFSLR KKLRDAIEIV KLNNRIKRLR 350
NMYSLGDDGD NDIEENSLNE SLLDGVTHSL DDLRLQSQKK GGELTEEQMK 400
LKSALTKDAF VQIVKAATKN KHKVLAGEEE DDSKKTLHDD RESKSED 447
Length:447
Mass (Da):50,447
Last modified:November 1, 1997 - v2
Checksum:i5990740B980B8312
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti282 – 2821V → A in CAA40281. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi B40896.
RefSeqi NP_014626.1. NM_001183270.1.

3D structure databases

ProteinModelPortali P22517.
SMRi P22517. Positions 32-371.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 34387. 101 interactions.
DIPi DIP-2306N.
IntActi P22517. 6 interactions.
MINTi MINT-481301.
STRINGi 4932.YOL016C.

Proteomic databases

MaxQBi P22517.
PaxDbi P22517.
PeptideAtlasi P22517.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YOL016C ; YOL016C ; YOL016C .
GeneIDi 854144.
KEGGi sce:YOL016C.

Organism-specific databases

CYGDi YOL016c.
SGDi S000005376. CMK2.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00750000117487.
HOGENOMi HOG000233016.
KOi K08794.
OMAi WDNISID.
OrthoDBi EOG793BK1.

Enzyme and pathway databases

BioCyci YEAST:G3O-33432-MONOMER.
BRENDAi 2.7.11.17. 984.

Miscellaneous databases

NextBioi 975888.
PROi P22517.

Gene expression databases

Genevestigatori P22517.

Family and domain databases

InterProi IPR020636. 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_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
PANTHERi PTHR24347. PTHR24347. 1 hit.
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: June 11, 2014
This is version 141 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.

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