Reviewed, UniProtKB/Swiss-Prot O42844 (KCC2_SCHPO)

Names and origin

Protein names

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

Gene names

Name:	cmk2
ORF Names:	SPAC23A1.06c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	504 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Has a role in the regulation of G2/M transition during mitosis. Ref.2 Ref.3
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Interacts with sty1. Ref.3
Subcellular location	Cytoplasm. Ref.2 Ref.3
Post-translational modification	Autophosphorylated. Ref.2 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
Cellular component	Cytoplasm
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	DNA replication checkpoint Ref.2 Inferred from mutant phenotype. Source: GeneDB_SPombe G2/M transition of mitotic cell cycle Inferred from mutant phenotype. Source: GeneDB_SPombe cellular response to oxidative stress Inferred from mutant phenotype. Source: GeneDB_SPombe negative regulation of cell cycle Ref.2 Inferred from mutant phenotype. Source: GeneDB_SPombe protein amino acid phosphorylation Inferred from mutant phenotype. Source: GeneDB_SPombe regulation of G2/M transition of mitotic cell cycle Ref.2 Inferred from mutant phenotype. Source: GeneDB_SPombe stress-activated protein kinase signaling pathway Ref.3 Inferred from genetic interaction. Source: GeneDB_SPombe
Cellular component	cell septum Ref.3 Inferred from direct assay. Source: GeneDB_SPombe cytoplasm Ref.3 Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calcium ion binding Traceable author statement. Source: GeneDB_SPombe calmodulin binding Traceable author statement. Source: GeneDB_SPombe calmodulin-dependent protein kinase activity Inferred from mutant phenotype. Source: GeneDB_SPombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 504	504	Calcium/calmodulin-dependent protein kinase type II		PRO_0000086104
Regions
	Domain	65 – 351	287	Protein kinase
	Nucleotide binding	71 – 79	9	ATP By similarity
	Region	366 – ?		Calmodulin-binding Potential
Sites
	Active site	188	1	Proton acceptor By similarity
	Binding site	94	1	ATP By similarity
Amino acid modifications
	Modified residue	252	1	Phosphothreonine Ref.4

Sequences

	Sequence		Length	Mass (Da)
	O42844-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 90929078D9F0DEBB	FASTA	504	56,609
	10 20 30 40 50 60 MSILAGFKNL LKHSKSSKGR SNASKSVDVS VNRDVAAYTE LAAKNVNAGG DEEIRVANYP 70 80 90 100 110 120 GLEKYQLIEN LGDGAFSQVY KAYSIDRKEH VAVKVIRKYE MNKKQRQGVF KEVNIMRRVK 130 140 150 160 170 180 HKNVVNLFDF VETEDFYHLV MELAEGGELF HQIVNFTYFS ENLARHIIIQ VAEAVKHLHD 190 200 210 220 230 240 VCGIVHRDIK PENLLFQPIE YLPSQNYTPP SLEPNKLDEG MFLEGIGAGG IGRILIADFG 250 260 270 280 290 300 FSKVVWNSKT ATPCGTVGYA APEIVNDELY SKNVDMWAMG CVLHTMLCGF PPFFDENIKD 310 320 330 340 350 360 LASKVVNGEF EFLSPWWDDI SDSAKDLITH LLTVDPRERY DIHQFFQHPW IKGESKMPEN 370 380 390 400 410 420 FTYKPKLHGT PGGPKLSLPR SLVSKGEIDI PTTPIKSATH PLLSSYSEPK TPGVSSVHEA 430 440 450 460 470 480 MGVAYDIRRL NHLGFSPEQL SKKSMNTGSI KELILDEETT TDDDDYIISS FPLNDTLGSE 490 500 GKDPFSLNLK ESSLYSRRSA KRVN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[2]	"Cmk2, a novel serine/threonine kinase in fission yeast." Alemany V., Sanchez-Piris M., Bachs O., Aligue R. FEBS Lett. 524:79-86(2002) [PubMed: 12135745] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
[3]	"Mkp1 and Mkp2, two MAPKAP-kinase homologues in Schizosaccharomyces pombe, interact with the MAP kinase Sty1." Asp E., Sunnerhagen P. Mol. Genet. Genomics 268:585-597(2003) [PubMed: 12589433] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STY1.
[4]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-252, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329670 Genomic DNA. Translation: CAA16980.1.
PIR	T38226.
RefSeq	NP_594436.1.
3D structure databases
HSSP	HSSP built from PDB template 1A06 based on UniProtKB Q63450.
ModBase	Search...
Protein-protein interaction databases
STRING	O42844.
Genome annotation databases
GeneID	2541982.
GenomeReviews	Gene locus cmk2 in contig CU329670_GR.
KEGG	spo:SPAC23A1.06c.
NMPDR	fig|4896.1.peg.4406.
Organism-specific databases
GeneDB_Spombe	SPAC23A1.06c.
Phylogenomic databases
OMA	TWIRIVA.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-002544-MON.
BRENDA	2.7.11.17. 653.
Gene expression databases
ArrayExpress	O42844.
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. 2 hits. [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...

Entry information

Entry name

KCC2_SCHPO

Accession

Primary (citable) accession number: O42844

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 13, 2002
Last sequence update:	June 1, 1998
Last modified:	November 3, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)