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  7. Casein kinase II subunit alpha'

Tchem Casein kinase II subunit alpha'

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. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV.

This gene encodes the alpha', or alpha 2, catalytic subunit of the protein kinase enzyme, casein kinase 2 (CK2). Casein kinase 2 is a serine/threonine protein kinase that phosphorylates acidic proteins such as casein. It is involved in various cellular processes, including cell cycle control, apoptosis, and circadian rhythms. This heterotetrameric kinase includes two catalytic subunits, either alpha or alpha', and two regulatory beta subunits. The closely related gene paralog encoding the alpha, or alpha 1 subunit (CSNK2A1, Gene ID: 1457) is found on chromosome 20. An intronic variant in this gene (alpha 2) may be associated with leukocyte telomere length in a South Asian population. A related transcribed pseudogene is found on chromosome 11. [provided by RefSeq, Aug 2017]

 Comments

Property Summary

Ligand Count 98
NCBI Gene PubMed Count 174
PubMed Score 221.26
PubTator Score 26.07

Knowledge Summary

Patent (7,051)

TINX Plot

  Disease (5)

Disease Target Count Z-score Confidence
Carcinoma, Squamous Cell 110 0.0 0.0
Skin Neoplasms 69 0.0 0.0
Disease Target Count
Squamous cell carcinoma 129
Disease Target Count Z-score Confidence
Carcinoma 11493 0.0 0.5
Disease Target Count Z-score Confidence
Cancer 2499 3.373 1.7

Expression

  Differential Expression (5)

Disease log2 FC p
diabetes mellitus -1.100 1.4e-03
intraductal papillary-mucinous carcinoma... -1.100 5.5e-03
intraductal papillary-mucinous neoplasm ... -1.100 1.3e-02
ovarian cancer -1.700 9.6e-08
psoriasis 1.200 5.0e-03

Synonym

Accession P19784 CK II alpha'
Symbols CK2A2
CSNK2A1
CK2alpha'

Gene

CSNK2A2

PDB

3E3B   3OFM   3U87   5M4U   5M56  

  Ortholog (1)

Species Source Disease
Chimp OMA EggNOG

 Collection (2)

 UniProt Keyword (16)

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 GO Function (3)

 GO Component (6)

 GO Process (15)

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 Compartment GO Term (25)

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 MGI Phenotype (2)

 GWAS Trait (1)

 HCA RNA Cell Line (56)

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Pathway (49)

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Protein-protein Interaction (28)

PCGF3   DDX41   PHRF1   NKAP   LUC7L2   KMT2A   CDC5L   BCR   CDK11B   ZNF687   C18orf25   ZMYND8   EIF3J   RYBP   AUTS2   FBRS   CSNK2A1   RNF111   ZNF592   RNF2   RING1   GPATCH2   HAGHL   FBRSL1   TSPYL2   XPC   ZNF106   HIRIP3  

Ligand (98)

Structure of CHEMBL3699249

CHEMBL3699249
pIC50 7.60

Structure of CHEMBL1928905

CHEMBL1928905
pKi 7.62

Structure of CHEMBL1233807

CHEMBL1233807
pKi 7.68

Structure of CHEMBL3699246

CHEMBL3699246
pIC50 7.68

Structure of CHEMBL595730

CHEMBL595730
pKi 7.68

Structure of CHEMBL3699298

CHEMBL3699298
pIC50 7.71

Structure of CHEMBL3759193

CHEMBL3759193
pIC50 7.72

Structure of CHEMBL3699299

CHEMBL3699299
pIC50 7.80

Structure of CHEMBL3699243

CHEMBL3699243
pIC50 7.81

Structure of CHEMBL475251

CHEMBL475251
pKd 7.85

Structure of CHEMBL3758777

CHEMBL3758777
pIC50 7.85

Structure of CHEMBL3758895

CHEMBL3758895
pIC50 7.89

Structure of CHEMBL3760064

CHEMBL3760064
pIC50 7.92

Structure of CHEMBL3758270

CHEMBL3758270
pIC50 7.92

Structure of CHEMBL2087023

CHEMBL2087023
pIC50 7.96

Structure of CHEMBL3760009

CHEMBL3760009
pIC50 7.96

Structure of CHEMBL3759349

CHEMBL3759349
pIC50 7.96

Structure of CHEMBL1230165

CHEMBL1230165
pIC50 7.96

Structure of CHEMBL3758519

CHEMBL3758519
pIC50 8.00

Structure of CHEMBL3759755

CHEMBL3759755
pIC50 8.00

Gene RIF (54)

AA Sequence 

MPGPAAGSRARVYAEVNSLRSREYWDYEAHVPSWGNQDDYQLVRKLGRGKYSEVFEAINITNNERVVVKI      1 - 70
LKPVKKKKIKREVKILENLRGGTNIIKLIDTVKDPVSKTPALVFEYINNTDFKQLYQILTDFDIRFYMYE     71 - 140
LLKALDYCHSKGIMHRDVKPHNVMIDHQQKKLRLIDWGLAEFYHPAQEYNVRVASRYFKGPELLVDYQMY    141 - 210
DYSLDMWSLGCMLASMIFRREPFFHGQDNYDQLVRIAKVLGTEELYGYLKKYHIDLDPHFNDILGQHSRK    211 - 280
RWENFIHSENRHLVSPEALDLLDKLLRYDHQQRLTAKEAMEHPYFYPVVKEQSQPCADNAVLSSGLTAAR    281 - 350
//

Text Mined References (189)

PMID Year Title