Reviewed, UniProtKB/Swiss-Prot P22517 (KCC2_YEAST)

Names and origin

Protein names

Recommended name:
    Calcium/calmodulin-dependent protein kinase II
    EC=2.7.11.17

Gene names

Name:	CMK2
Ordered Locus Names:	YOL016C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	447 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Important in cellular regulation.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Multimeric.
Miscellaneous	Present with 7500 molecules/cell in log phase SD medium. Ref.4
Sequence similarities	Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Ligand	ATP-binding Calmodulin-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein amino acid phosphorylation Ref.2 Inferred from direct assay. Source: SGD signal transduction Ref.2 Non-traceable author statement. Source: SGD
Cellular component	cytoplasm Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calmodulin binding Inferred from electronic annotation. Source: UniProtKB-KW calmodulin-dependent protein kinase activity Ref.2 Inferred from direct assay. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARO8	P53090	1	EBI-9600,EBI-2042933
RNR1	P21524	1	EBI-9600,EBI-15234
RNR2	P09938	1	EBI-9600,EBI-15240

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 447	447	Calcium/calmodulin-dependent protein kinase II		PRO_0000086105
Regions
	Domain	47 – 309	263	Protein kinase
	Nucleotide binding	53 – 61	9	ATP By similarity
	Region	323 – 334	12	Calmodulin-binding By similarity
Sites
	Active site	171	1	Proton acceptor By similarity
	Binding site	76	1	ATP By similarity
Amino acid modifications
	Modified residue	68	1	Phosphoserine Ref.8
	Modified residue	316	1	Phosphothreonine; by autocatalysis By similarity
	Modified residue	367	1	Phosphoserine Ref.5 Ref.7
	Modified residue	371	1	Phosphoserine Ref.8 Ref.5
	Modified residue	379	1	Phosphoserine Ref.8 Ref.7
	Modified residue	387	1	Phosphoserine; by autocatalysis By similarity
	Modified residue	443	1	Phosphoserine Ref.8 Ref.6
Experimental info
	Sequence conflict	282	1	V → A in CAA40281. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P22517-1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 5990740B980B8312	FASTA	447	50,447
	10 20 30 40 50 60 MPKESEVINS EFHVDVQDPE RLNGHPVAKF INKLSGQPES YVNRTNYIFG RTLGAGSFGV 70 80 90 100 110 120 VRQARKLSTN EDVAIKILLK KALQGNNVQL QMLYEELSIL QKLSHPNIVS FKDWFESKDK 130 140 150 160 170 180 FYIVTQLATG GELFDRILSR GKFTEVDAVE IIVQILGAVE YMHSKNVVHR DLKPENVLYV 190 200 210 220 230 240 DKSENSPLVI ADFGIAKQLK GEEDLIYKAA GSLGYVAPEV LTQDGHGKPC DIWSIGVITY 250 260 270 280 290 300 TLLCGYSPFI AESVEGFMEE CTASRYPVTF HMPYWDNISI DVKRFILKAL RLNPADRPTA 310 320 330 340 350 360 TELLDDPWIT SKRVETSNIL PDVKKGFSLR KKLRDAIEIV KLNNRIKRLR NMYSLGDDGD 370 380 390 400 410 420 NDIEENSLNE SLLDGVTHSL DDLRLQSQKK GGELTEEQMK LKSALTKDAF VQIVKAATKN 430 440 KHKVLAGEEE DDSKKTLHDD RESKSED

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2026147] [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: 2061341] [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: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367 AND SER-371, MASS SPECTROMETRY.
[6]	"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: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443, MASS SPECTROMETRY.
[7]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367 AND SER-379, MASS SPECTROMETRY.
[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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68; SER-371; SER-379 AND SER-443, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X56961 Genomic DNA. Translation: CAA40281.1. D90376 Genomic DNA. Translation: BAA14384.1. Z74758 Genomic DNA. Translation: CAA99015.1.
PIR	B40896.
RefSeq	NP_014626.1.
3D structure databases
HSSP	HSSP built from PDB template 1KWP based on UniProtKB P49137.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:2306N.
IntAct	P22517. 14 interactions.
STRING	P22517.
Proteomic databases
PeptideAtlas	P22517.
PRIDE	P22517.
Genome annotation databases
Ensembl	YOL016C; YOL016C; YOL016C; Saccharomyces cerevisiae. [Genome view]
GeneID	854144.
GenomeReviews	Gene locus YOL016C in contig Y13140_GR.
KEGG	sce:YOL016C.
NMPDR	fig|4932.3.peg.5720.
Organism-specific databases
CYGD	YOL016c.
SGD	S000005376. CMK2.
Phylogenomic databases
HOGENOM	P22517.
OMA	RESKSED.
Enzyme and pathway databases
BRENDA	2.7.11.17. 250.
Gene expression databases
ArrayExpress	P22517.
Genevestigator	P22517.
GermOnline	YOL016C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	975888.

Entry information

Entry name

KCC2_YEAST

Accession

Primary (citable) accession number: P22517

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	November 1, 1997
Last modified:	November 3, 2009
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)