Casein kinase II subunit alpha

Details

Name
Casein kinase II subunit alpha
Synonyms
  • 2.7.11.1
  • CK II alpha
  • CK2A1
Gene Name
CSNK2A1
Organism
Humans
Amino acid sequence
>lcl|BSEQ0002405|Casein kinase II subunit alpha
MSGPVPSRARVYTDVNTHRPREYWDYESHVVEWGNQDDYQLVRKLGRGKYSEVFEAINIT
NNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLADIVKDPVSRTPALVFEHVNNTD
FKQLYQTLTDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAE
FYHPGQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYD
QLVRIAKVLGTEDLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDF
LDKLLRYDHQSRLTAREAMEHPYFYTVVKDQARMGSSSMPGGSTPVSSANMMSGISSVPT
PSPLGPLAGSPVIAAANPLGMPVPAAAGAQQ
Number of residues
391
Molecular Weight
45143.25
Theoretical pI
7.86
GO Classification
Functions
ATP binding / Hsp90 protein binding / protein N-terminus binding / protein serine/threonine kinase activity
Processes
axon guidance / chaperone-mediated protein folding / mitotic cell cycle / mitotic spindle checkpoint / negative regulation of cysteine-type endopeptidase activity involved in apoptotic process / positive regulation of cell growth / positive regulation of cell proliferation / positive regulation of protein catabolic process / positive regulation of Wnt signaling pathway / protein phosphorylation / regulation of transcription, DNA-templated / rhythmic process / signal transduction / transcription, DNA-templated / Wnt signaling pathway
Components
cytosol / nucleus / NuRD complex / plasma membrane / Sin3 complex
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. Phosphorylates PML at 'Ser-565' and primes it for ubiquitin-mediated degradation. Plays an important role in the circadian clock function by phosphorylating ARNTL/BMAL1 at 'Ser-90' which is pivotal for its interaction with CLOCK and which controls CLOCK nuclear entry (PubMed:11239457, PubMed:11704824, PubMed:16193064, PubMed:19188443, PubMed:20625391, PubMed:22406621). Phosphorylates CCAR2 at 'Thr-454' in gastric carcinoma tissue (PubMed:24962073).
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Nucleus
Gene sequence
>lcl|BSEQ0010842|Casein kinase II subunit alpha (CSNK2A1)
ATGTCGGGACCCGTGCCAAGCAGGGCCAGAGTTTACACAGATGTTAATACACACAGACCT
CGAGAATACTGGGATTACGAGTCACATGTGGTGGAATGGGGAAATCAAGATGACTACCAG
CTGGTTCGAAAATTAGGCCGAGGTAAATACAGTGAAGTATTTGAAGCCATCAACATCACA
AATAATGAAAAAGTTGTTGTTAAAATTCTCAAGCCAGTAAAAAAGAAGAAAATTAAGCGT
GAAATAAAGATTTTGGAGAATTTGAGAGGAGGTCCCAACATCATCACACTGGCAGACATT
GTAAAAGACCCTGTGTCACGAACCCCCGCCTTGGTTTTTGAACACGTAAACAACACAGAC
TTCAAGCAATTGTACCAGACGTTAACAGACTATGATATTCGATTTTACATGTATGAGATT
CTGAAGGCCCTGGATTATTGTCACAGCATGGGAATTATGCACAGAGATGTCAAGCCCCAT
AATGTCATGATTGATCATGAGCACAGAAAGCTACGACTAATAGACTGGGGTTTGGCTGAG
TTTTATCATCCTGGCCAAGAATATAATGTCCGAGTTGCTTCCCGATACTTCAAAGGTCCT
GAGCTACTTGTAGACTATCAGATGTACGATTATAGTTTGGATATGTGGAGTTTGGGTTGT
ATGCTGGCAAGTATGATCTTTCGGAAGGAGCCATTTTTCCATGGACATGACAATTATGAT
CAGTTGGTGAGGATAGCCAAGGTTCTGGGGACAGAAGATTTATATGACTATATTGACAAA
TACAACATTGAATTAGATCCACGTTTCAATGATATCTTGGGCAGACACTCTCGAAAGCGA
TGGGAACGCTTTGTCCACAGTGAAAATCAGCACCTTGTCAGCCCTGAGGCCTTGGATTTC
CTGGACAAACTGCTGCGATATGACCACCAGTCACGGCTTACTGCAAGAGAGGCAATGGAG
CACCCCTATTTCTACACTGTTGTGAAGGACCAGGCTCGAATGGGTTCATCTAGCATGCCA
GGGGGCAGTACGCCCGTCAGCAGCGCCAATATGATGTCAGGGATTTCTTCAGTGCCAACC
CCTTCACCCCTTGGACCTCTGGCAGGCTCACCAGTGATTGCTGCTGCCAACCCCCTTGGG
ATGCCTGTTCCAGCTGCCGCTGGCGCTCAGCAGTAA
Chromosome Location
20
Locus
20p13
External Identifiers
ResourceLink
UniProtKB IDP68400
UniProtKB Entry NameCSK21_HUMAN
GenBank Protein ID598147
GenBank Gene IDJ02853
GenAtlas IDCSNK2A1
HGNC IDHGNC:2457
General References
  1. Meisner H, Heller-Harrison R, Buxton J, Czech MP: Molecular cloning of the human casein kinase II alpha subunit. Biochemistry. 1989 May 2;28(9):4072-6. [PubMed:2752008]
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  8. Bosc DG, Slominski E, Sichler C, Litchfield DW: Phosphorylation of casein kinase II by p34cdc2. Identification of phosphorylation sites using phosphorylation site mutants in vitro. J Biol Chem. 1995 Oct 27;270(43):25872-8. [PubMed:7592773]
  9. 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]
  10. Sayed M, Pelech S, Wong C, Marotta A, Salh B: Protein kinase CK2 is involved in G2 arrest and apoptosis following spindle damage in epithelial cells. Oncogene. 2001 Oct 25;20(48):6994-7005. [PubMed:11704824]
  11. 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]
  12. Shin S, Lee Y, Kim W, Ko H, Choi H, Kim K: Caspase-2 primes cancer cells for TRAIL-mediated apoptosis by processing procaspase-8. EMBO J. 2005 Oct 19;24(20):3532-42. Epub 2005 Sep 29. [PubMed:16193064]
  13. Trembley JH, Tatsumi S, Sakashita E, Loyer P, Slaughter CA, Suzuki H, Endo H, Kidd VJ, Mayeda A: Activation of pre-mRNA splicing by human RNPS1 is regulated by CK2 phosphorylation. Mol Cell Biol. 2005 Feb;25(4):1446-57. [PubMed:15684395]
  14. 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]
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  22. MacPherson MR, Molina P, Souchelnytskyi S, Wernstedt C, Martin-Perez J, Portillo F, Cano A: Phosphorylation of serine 11 and serine 92 as new positive regulators of human Snail1 function: potential involvement of casein kinase-2 and the cAMP-activated kinase protein kinase A. Mol Biol Cell. 2010 Jan 15;21(2):244-53. doi: 10.1091/mbc.E09-06-0504. Epub 2009 Nov 18. [PubMed:19923321]
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  27. Bae JS, Park SH, Kim KM, Kwon KS, Kim CY, Lee HK, Park BH, Park HS, Lee H, Moon WS, Chung MJ, Sylvester KG, Jang KY: CK2alpha phosphorylates DBC1 and is involved in the progression of gastric carcinoma and predicts poor survival of gastric carcinoma patients. Int J Cancer. 2015 Feb 15;136(4):797-809. doi: 10.1002/ijc.29043. Epub 2014 Jul 1. [PubMed:24962073]
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03127BenzamidineexperimentalunknownDetails
DB04395Phosphoaminophosphonic Acid-Adenylate EsterexperimentalunknownDetails
DB04462Tetrabromo-2-BenzotriazoleexperimentalunknownDetails
DB02709Resveratrolapproved, experimental, investigationalunknownDetails
DB04720S-METHYL-4,5,6,7-TETRABROMO-BENZIMIDAZOLEexperimentalunknownDetails
DB07715EmodininvestigationalunknownDetails
DB078023,8-DIBROMO-7-HYDROXY-4-METHYL-2H-CHROMEN-2-ONEexperimentalunknownDetails
DB030351,8-Di-Hydroxy-4-Nitro-AnthraquinoneexperimentalunknownDetails
DB01765(5-Oxo-5,6-Dihydro-Indolo[1,2-a]Quinazolin-7-Yl)-Acetic AcidexperimentalunknownDetails
DB04719DIMETHYL-(4,5,6,7-TETRABROMO-1H-BENZOIMIDAZOL-2-YL)-AMINEexperimentalunknownDetails
DB04721N1,N2-ETHYLENE-2-METHYLAMINO-4,5,6,7-TETRABROMO-BENZIMIDAZOLEexperimentalunknownDetails
DB021701,8-Di-Hydroxy-4-Nitro-Xanthen-9-OneexperimentalunknownDetails
DB039245,8-Di-Amino-1,4-Dihydroxy-AnthraquinoneexperimentalunknownDetails
DB0833819-(cyclopropylamino)-4,6,7,15-tetrahydro-5H-16,1-(azenometheno)-10,14-(metheno)pyrazolo[4,3-o][1,3,9]triazacyclohexadecin-8(9H)-oneexperimentalunknownDetails
DB08340N,N'-DIPHENYLPYRAZOLO[1,5-A][1,3,5]TRIAZINE-2,4-DIAMINEexperimentalunknownDetails
DB083454-(2-(1H-IMIDAZOL-4-YL)ETHYLAMINO)-2-(PHENYLAMINO)PYRAZOLO[1,5-A][1,3,5]TRIAZINE-8-CARBONITRILEexperimentalunknownDetails
DB083532-(CYCLOHEXYLMETHYLAMINO)-4-(PHENYLAMINO)PYRAZOLO[1,5-A][1,3,5]TRIAZINE-8-CARBONITRILEexperimentalunknownDetails
DB083542-(4-CHLOROBENZYLAMINO)-4-(PHENYLAMINO)PYRAZOLO[1,5-A][1,3,5]TRIAZINE-8-CARBONITRILEexperimentalunknownDetails
DB083602-(4-ETHYLPIPERAZIN-1-YL)-4-(PHENYLAMINO)PYRAZOLO[1,5-A][1,3,5]TRIAZINE-8-CARBONITRILEexperimentalunknownDetails
DB08362N-(3-(8-CYANO-4-(PHENYLAMINO)PYRAZOLO[1,5-A][1,3,5]TRIAZIN-2-YLAMINO)PHENYL)ACETAMIDEexperimentalunknownDetails
DB084735,6-dichloro-1-beta-D-ribofuranosyl-1H-benzimidazoleexperimentalunknownDetails
DB086601,2,5,8-tetrahydroxyanthracene-9,10-dioneexperimentalunknownDetails
DB08846Ellagic AcidinvestigationalunknowninhibitorDetails
DB00171ATPinvestigational, nutraceuticalunknownDetails
DB04216Quercetinexperimental, investigationalunknownDetails
DB12010Fostamatinibapproved, investigationalunknowninhibitorDetails