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O54833 (CSK22_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Casein kinase II subunit alpha'

Short name=CK II alpha'
EC=2.7.11.1
Gene names
Name:Csnk2a2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length350 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins By similarity.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Constitutively active protein kinase whose activity is not directly affected by phosphorylation. Seems to be regulated by level of expression and localization By similarity.

Subunit structure

Heterotetramer composed of two catalytic subunits (alpha chain and/or alpha' chain) and two regulatory subunits (beta chains). The tetramer can exist as a combination of 2 alpha/2 beta, 2 alpha'/2 beta or 1 alpha/1 alpha'/2 beta subunits. Also part of a CK2-SPT16-SSRP1 complex composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, which forms following UV irradiation. Interacts with RNPS1 By similarity.

Disruption phenotype

Infertile male mice with oligospermia and globozoospermia. Ref.4

Miscellaneous

Can use both ATP and GTP as phosphoryl donors. Phosphorylation by casein kinase 2 has been estimated to represent up to one quarter of the eukaryotic phosphoproteome.

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CK2 subfamily.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 350350Casein kinase II subunit alpha'
PRO_0000085892

Regions

Domain40 – 325286Protein kinase
Nucleotide binding46 – 549ATP By similarity

Sites

Active site1571Proton acceptor By similarity
Binding site691ATP By similarity

Amino acid modifications

Modified residue131Phosphotyrosine By similarity
Modified residue181Phosphoserine By similarity
Modified residue211Phosphoserine By similarity
Modified residue971N6-acetyllysine By similarity
Modified residue2881Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
O54833 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: C5FA314617627F5B

FASTA35041,215
        10         20         30         40         50         60 
MPGPAAGSRA RVYAEVNSLR SREYWDYEAH VPSWGNQDDY QLVRKLGRGK YSEVFEAINI 

        70         80         90        100        110        120 
TNNERVVVKI LKPVKKKKIK REVKILENLR GGTNIIKLID TVKDPVSKTP ALVFEYINNT 

       130        140        150        160        170        180 
DFKQLYQILT DFDIRFYMYE LLKALDYCHS KGIMHRDVKP HNVMIDHQQK KLRLIDWGLA 

       190        200        210        220        230        240 
EFYHPAQEYN VRVASRYFKG PELLVDYQMY DYSLDMWSLG CMLASMIFRK EPFFHGQDNY 

       250        260        270        280        290        300 
DQLVRIAKVL GTDELYGYLK KYHIDLDPHF NDILGQHSRK RWENFIHSEN RHLVSPEALD 

       310        320        330        340        350 
LLDKLLRYDH QQRLTAKEAM EHPYFYPVVK EQSQPCAENT VLSSGLTAAR 

« Hide

References

« Hide 'large scale' references
[1]"Murine protein kinase CK2 alpha': cDNA and genomic cloning and chromosomal mapping."
Xu X., Rich E.S. Jr., Seldin D.C.
Genomics 48:79-86(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
[2]"Protein kinase CK2alpha' is induced by serum as a delayed early gene and cooperates with Ha-ras in fibroblast transformation."
Orlandini M., Semplici F., Ferruzzi R., Meggio F., Pinna L.A., Oliviero S.
J. Biol. Chem. 273:21291-21297(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: 129.
Tissue: Mammary gland.
[4]"Globozoospermia in mice lacking the casein kinase II alpha' catalytic subunit."
Xu X., Toselli P.A., Russell L.D., Seldin D.C.
Nat. Genet. 23:118-121(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF012251 mRNA. Translation: AAC53552.1.
AJ001420 mRNA. Translation: CAA04753.1.
BC057862 mRNA. Translation: AAH57862.1.
RefSeqNP_034104.1. NM_009974.3.
XP_006530703.1. XM_006530640.1.
UniGeneMm.440348.
Mm.51136.

3D structure databases

ProteinModelPortalO54833.
SMRO54833. Positions 8-332.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198946. 5 interactions.
IntActO54833. 5 interactions.
MINTMINT-4092108.

Chemistry

BindingDBO54833.
ChEMBLCHEMBL5326.

PTM databases

PhosphoSiteO54833.

Proteomic databases

PaxDbO54833.
PRIDEO54833.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000056919; ENSMUSP00000055919; ENSMUSG00000046707.
GeneID13000.
KEGGmmu:13000.
UCSCuc009myk.2. mouse.

Organism-specific databases

CTD1459.
MGIMGI:88547. Csnk2a2.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233021.
HOVERGENHBG107282.
InParanoidO54833.
KOK03097.
OMAPSWGNQD.
OrthoDBEOG7QG446.
PhylomeDBO54833.
TreeFamTF300483.

Enzyme and pathway databases

BRENDA2.7.11.1. 3474.

Gene expression databases

ArrayExpressO54833.
BgeeO54833.
CleanExMM_CSNK2A2.
GenevestigatorO54833.

Family and domain databases

InterProIPR011009. 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]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCSNK2A2. mouse.
NextBio282812.
PROO54833.
SOURCESearch...

Entry information

Entry nameCSK22_MOUSE
AccessionPrimary (citable) accession number: O54833
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: June 1, 1998
Last modified: April 16, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot