Casein kinase II subunit alpha'

Details

Name
Casein kinase II subunit alpha'
Synonyms
  • 2.7.11.1
  • CK II alpha'
  • CK2A2
Gene Name
CSNK2A2
Organism
Humans
Amino acid sequence
>lcl|BSEQ0012773|Casein kinase II subunit alpha'
MPGPAAGSRARVYAEVNSLRSREYWDYEAHVPSWGNQDDYQLVRKLGRGKYSEVFEAINI
TNNERVVVKILKPVKKKKIKREVKILENLRGGTNIIKLIDTVKDPVSKTPALVFEYINNT
DFKQLYQILTDFDIRFYMYELLKALDYCHSKGIMHRDVKPHNVMIDHQQKKLRLIDWGLA
EFYHPAQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRREPFFHGQDNY
DQLVRIAKVLGTEELYGYLKKYHIDLDPHFNDILGQHSRKRWENFIHSENRHLVSPEALD
LLDKLLRYDHQQRLTAKEAMEHPYFYPVVKEQSQPCADNAVLSSGLTAAR
Number of residues
350
Molecular Weight
41212.925
Theoretical pI
8.82
GO Classification
Functions
ATP binding / protein N-terminus binding / protein serine/threonine kinase activity
Processes
apoptotic process / axon guidance / mitotic cell cycle / mitotic spindle checkpoint / positive regulation of protein targeting to mitochondrion / regulation of mitophagy / regulation of transcription, DNA-templated / transcription, DNA-templated / Wnt signaling pathway
Components
cytosol / nucleus
General Function
Protein serine/threonine kinase activity
Specific 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. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0012774|Casein kinase II subunit alpha' (CSNK2A2)
ATGCCCGGCCCGGCCGCGGGCAGCAGGGCCCGGGTCTACGCCGAGGTGAACAGTCTGAGG
AGCCGCGAGTACTGGGACTACGAGGCTCACGTCCCGAGCTGGGGTAATCAAGATGATTAC
CAACTGGTTCGAAAACTTGGTCGGGGAAAATATAGTGAAGTATTTGAGGCCATTAATATC
ACCAACAATGAGAGAGTGGTTGTAAAAATCCTGAAGCCAGTGAAGAAAAAGAAGATAAAA
CGAGAGGTTAAGATTCTGGAGAACCTTCGTGGTGGAACAAATATCATTAAGCTGATTGAC
ACTGTAAAGGACCCCGTGTCAAAGACACCAGCTTTGGTATTTGAATATATCAATAATACA
GATTTTAAGCAACTCTACCAGATCCTGACAGACTTTGATATCCGGTTTTATATGTATGAA
CTACTTAAAGCTCTGGATTACTGCCACAGCAAGGGAATCATGCACAGGGATGTGAAACCT
CACAATGTCATGATAGATCACCAACAGAAAAAGCTGCGACTGATAGATTGGGGTCTGGCA
GAATTCTATCATCCTGCTCAGGAGTACAATGTTCGTGTAGCCTCAAGGTACTTCAAGGGA
CCAGAGCTCCTCGTGGACTATCAGATGTATGATTATAGCTTGGACATGTGGAGTTTGGGC
TGTATGTTAGCAAGCATGATCTTTCGAAGGGAACCATTCTTCCATGGACAGGACAACTAT
GACCAGCTTGTTCGCATTGCCAAGGTTCTGGGTACAGAAGAACTGTATGGGTATCTGAAG
AAGTATCACATAGACCTAGATCCACACTTCAACGATATCCTGGGACAACATTCACGGAAA
CGCTGGGAAAACTTTATCCATAGTGAGAACAGACACCTTGTCAGCCCTGAGGCCCTAGAT
CTTCTGGACAAACTTCTGCGATACGACCATCAACAGAGACTGACTGCCAAAGAGGCCATG
GAGCACCCATACTTCTACCCTGTGGTGAAGGAGCAGTCCCAGCCTTGTGCAGACAATGCT
GTGCTTTCCAGTGGTCTCACGGCAGCACGATGA
Chromosome Location
16
Locus
16q21
External Identifiers
ResourceLink
UniProtKB IDP19784
UniProtKB Entry NameCSK22_HUMAN
GenBank Protein ID177838
GenBank Gene IDM55268
HGNC IDHGNC:2459
General References
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  5. Keller DM, Lu H: p53 serine 392 phosphorylation increases after UV through induction of the assembly of the CK2.hSPT16.SSRP1 complex. J Biol Chem. 2002 Dec 20;277(51):50206-13. Epub 2002 Oct 21. [Article]
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  13. Dominguez I, Sonenshein GE, Seldin DC: Protein kinase CK2 in health and disease: CK2 and its role in Wnt and NF-kappaB signaling: linking development and cancer. Cell Mol Life Sci. 2009 Jun;66(11-12):1850-7. doi: 10.1007/s00018-009-9153-z. [Article]
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  17. Nakaniwa T, Kinoshita T, Sekiguchi Y, Tada T, Nakanishi I, Kitaura K, Suzuki Y, Ohno H, Hirasawa A, Tsujimoto G: Structure of human protein kinase CK2 alpha 2 with a potent indazole-derivative inhibitor. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Feb 1;65(Pt 2):75-9. doi: 10.1107/S1744309108043194. Epub 2009 Jan 31. [Article]
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB07546[1-(6-{6-[(1-methylethyl)amino]-1H-indazol-1-yl}pyrazin-2-yl)-1H-pyrrol-3-yl]acetic acidexperimentalunknownDetails
DB12010Fostamatinibapproved, investigationalunknowninhibitorDetails