Canmetcon
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Identification
HMDB Protein ID HMDBP01476
Secondary Accession Numbers
  • 6772
Name Casein kinase II subunit alpha'
Synonyms
  1. CK II alpha'
Gene Name CSNK2A2
Protein Type Enzyme
Biological Properties
General Function Involved in protein kinase activity
Specific Function Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. The alpha and alpha' chains contain the catalytic site. Participates in Wnt signaling. CK2 phosphorylates 'Ser-392' of p53/TP53 following UV irradiation
Pathways Not Available
Reactions Not Available
GO Classification
Function
binding
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
kinase activity
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
adenyl ribonucleotide binding
atp binding
protein kinase activity
protein serine/threonine kinase activity
Process
phosphorus metabolic process
phosphate metabolic process
metabolic process
cellular metabolic process
protein amino acid phosphorylation
phosphorylation
Cellular Location Not Available
Gene Properties
Chromosome Location Chromosome:1
Locus 16q21
SNPs CSNK2A2
Gene Sequence
>1053 bp
ATGCCCGGCCCGGCCGCGGGCAGCAGGGCCCGGGTCTACGCCGAGGTGAACAGTCTGAGG
AGCCGCGAGTACTGGGACTACGAGGCTCACGTCCCGAGCTGGGGTAATCAAGATGATTAC
CAACTGGTTCGAAAACTTGGTCGGGGAAAATATAGTGAAGTATTTGAGGCCATTAATATC
ACCAACAATGAGAGAGTGGTTGTAAAAATCCTGAAGCCAGTGAAGAAAAAGAAGATAAAA
CGAGAGGTTAAGATTCTGGAGAACCTTCGTGGTGGAACAAATATCATTAAGCTGATTGAC
ACTGTAAAGGACCCCGTGTCAAAGACACCAGCTTTGGTATTTGAATATATCAATAATACA
GATTTTAAGCAACTCTACCAGATCCTGACAGACTTTGATATCCGGTTTTATATGTATGAA
CTACTTAAAGCTCTGGATTACTGCCACAGCAAGGGAATCATGCACAGGGATGTGAAACCT
CACAATGTCATGATAGATCACCAACAGAAAAAGCTGCGACTGATAGATTGGGGTCTGGCA
GAATTCTATCATCCTGCTCAGGAGTACAATGTTCGTGTAGCCTCAAGGTACTTCAAGGGA
CCAGAGCTCCTCGTGGACTATCAGATGTATGATTATAGCTTGGACATGTGGAGTTTGGGC
TGTATGTTAGCAAGCATGATCTTTCGAAGGGAACCATTCTTCCATGGACAGGACAACTAT
GACCAGCTTGTTCGCATTGCCAAGGTTCTGGGTACAGAAGAACTGTATGGGTATCTGAAG
AAGTATCACATAGACCTAGATCCACACTTCAACGATATCCTGGGACAACATTCACGGAAA
CGCTGGGAAAACTTTATCCATAGTGAGAACAGACACCTTGTCAGCCCTGAGGCCCTAGAT
CTTCTGGACAAACTTCTGCGATACGACCATCAACAGAGACTGACTGCCAAAGAGGCCATG
GAGCACCCATACTTCTACCCTGTGGTGAAGGAGCAGTCCCAGCCTTGTGCAGACAATGCT
GTGCTTTCCAGTGGTCTCACGGCAGCACGATGA
Protein Properties
Number of Residues 350
Molecular Weight 41212.9
Theoretical pI 8.82
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Casein kinase II subunit alpha'
MPGPAAGSRARVYAEVNSLRSREYWDYEAHVPSWGNQDDYQLVRKLGRGKYSEVFEAINI
TNNERVVVKILKPVKKKKIKREVKILENLRGGTNIIKLIDTVKDPVSKTPALVFEYINNT
DFKQLYQILTDFDIRFYMYELLKALDYCHSKGIMHRDVKPHNVMIDHQQKKLRLIDWGLA
EFYHPAQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRREPFFHGQDNY
DQLVRIAKVLGTEELYGYLKKYHIDLDPHFNDILGQHSRKRWENFIHSENRHLVSPEALD
LLDKLLRYDHQQRLTAKEAMEHPYFYPVVKEQSQPCADNAVLSSGLTAAR
GenBank ID Protein 177838
UniProtKB/Swiss-Prot ID P19784
UniProtKB/Swiss-Prot Entry Name CSK22_HUMAN
PDB IDs Not Available
GenBank Gene ID M55268
GeneCard ID CSNK2A2
GenAtlas ID CSNK2A2
HGNC ID HGNC:2459
References
General References
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  2. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. doi: 10.1016/j.molcel.2008.07.007. [PubMed:18691976 ]
  4. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. doi: 10.1074/mcp.M800588-MCP200. Epub 2009 Apr 15. [PubMed:19369195 ]
  5. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed:17344846 ]
  6. Keller DM, Zeng X, Wang Y, Zhang QH, Kapoor M, Shu H, Goodman R, Lozano G, Zhao Y, Lu H: A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1. Mol Cell. 2001 Feb;7(2):283-92. [PubMed:11239457 ]
  7. 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. [PubMed:12393879 ]
  8. Lozeman FJ, Litchfield DW, Piening C, Takio K, Walsh KA, Krebs EG: Isolation and characterization of human cDNA clones encoding the alpha and the alpha' subunits of casein kinase II. Biochemistry. 1990 Sep 11;29(36):8436-47. [PubMed:2174700 ]