Casein kinase II subunit alpha

Details

Name
Casein kinase II subunit alpha
Kind
protein
Synonyms
  • 2.7.11.1
  • CK II alpha
  • CK2A1
Gene Name
CSNK2A1
UniProtKB Entry
P68400Swiss-Prot
Organism
Humans
NCBI Taxonomy ID
9606
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
identical protein binding / kinase activity / protein serine kinase activity
Processes
apoptotic process / DNA damage response / double-strand break repair / negative regulation of apoptotic signaling pathway / negative regulation of double-strand break repair via homologous recombination / negative regulation of proteasomal ubiquitin-dependent protein catabolic process / negative regulation of translation / peptidyl-serine phosphorylation / peptidyl-threonine phosphorylation / positive regulation of aggrephagy / positive regulation of cell population proliferation / protein stabilization / regulation of cell cycle / regulation of chromosome separation / symbiont-mediated disruption of host cell PML body
Components
nucleoplasm / PML body / protein kinase CK2 complex / Sin3-type complex
General 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 (PubMed:11239457, PubMed:11704824, PubMed:16193064, PubMed:18411307, PubMed:18583988, PubMed:18678890, PubMed:19188443, PubMed:20545769, PubMed:20625391, PubMed:22017874, PubMed:22406621, PubMed:24962073, PubMed:30898438, PubMed:31439799). Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection (PubMed:12631575, PubMed:19387551, PubMed:19387552). May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response (PubMed:12631575, PubMed:19387551, PubMed:19387552). 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 (PubMed:11704824, PubMed:19188443). Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation (PubMed:11239457). Phosphorylates a number of DNA repair proteins in response to DNA damage, such as MDC1, MRE11, RAD9A, RAD51 and HTATSF1, promoting their recruitment to DNA damage sites (PubMed:18411307, PubMed:18583988, PubMed:18678890, PubMed:20545769, PubMed:21482717, PubMed:22325354, PubMed:26811421, PubMed:28512243, PubMed:30898438, PubMed:35597237). Can also negatively regulate apoptosis (PubMed:16193064, PubMed:22184066). Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3 (PubMed:16193064). Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8 (PubMed:16193064). Phosphorylates YY1, protecting YY1 from cleavage by CASP7 during apoptosis (PubMed:22184066). Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV (PubMed:12631575, PubMed:19387550, PubMed:19387551, PubMed:19387552, PubMed:23123191). Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, ATF4, SRF, MAX, JUN, FOS, MYC and MYB (PubMed:12631575, PubMed:19387550, PubMed:19387551, PubMed:19387552, PubMed:23123191). Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function (PubMed:19387550). Mediates sequential phosphorylation of FNIP1, promoting its gradual interaction with Hsp90, leading to activate both kinase and non-kinase client proteins of Hsp90 (PubMed:30699359). Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1 (PubMed:19387549). Acts as an ectokinase that phosphorylates several extracellular proteins (PubMed:12631575, PubMed:19387550, PubMed:19387551, PubMed:19387552). During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV (PubMed:12631575, PubMed:19387550, PubMed:19387551, PubMed:19387552). Phosphorylates PML at 'Ser-565' and primes it for ubiquitin-mediated degradation (PubMed:20625391, PubMed:22406621). Plays an important role in the circadian clock function by phosphorylating BMAL1 at 'Ser-90' which is pivotal for its interaction with CLOCK and which controls CLOCK nuclear entry (By similarity). Phosphorylates CCAR2 at 'Thr-454' in gastric carcinoma tissue (PubMed:24962073). Phosphorylates FMR1, promoting FMR1-dependent formation of a membraneless compartment (PubMed:30765518, PubMed:31439799). May phosphorylate histone H2A on 'Ser-1' (PubMed:38334665)
Specific Function
ATP binding
Pfam Domain Function
Signal Regions
Not Available
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
GeneCard IDCSNK2A1
GenAtlas IDCSNK2A1
HGNC IDHGNC:2457
PDB ID(s)1JWH, 1NA7, 1PJK, 2PVR, 2ZJW, 3AMY, 3AT2, 3AT3, 3AT4, 3AXW, 3BQC, 3C13, 3FWQ, 3H30, 3JUH, 3MB6, 3MB7, 3NGA, 3NSZ, 3OWJ, 3OWK, 3OWL, 3PE1, 3PE2, 3PE4, 3Q04, 3Q9W, 3Q9X, 3Q9Y, 3Q9Z, 3QA0, 3R0T, 3RPS, 3TAX, 3U4U, 3U87, 3U9C, 3W8L, 3WAR, 3WIK, 3WIL, 3WOW, 4DGL, 4FBX, 4GRB, 4GUB, 4GYW, 4GYY, 4GZ3, 4IB5, 4KWP, 4MD7, 4MD8, 4MD9, 4NH1, 4RLL, 4UB7, 4UBA, 5B0X, 5CLP, 5CQU, 5CQW, 5CS6, 5CSH, 5CSP, 5CSV, 5CT0, 5CTP, 5CU0, 5CU2, 5CU3, 5CU4, 5CU6, 5CVF, 5CVG, 5CVH, 5CX9, 5H8B, 5H8E, 5H8G, 5HGV, 5KU8, 5KWH, 5M44, 5M4C, 5M4F, 5M4I, 5MMF, 5MMR, 5MO5, 5MO6, 5MO7, 5MO8, 5MOD, 5MOE, 5MOH, 5MOT, 5MOV, 5MOW, 5MP8, 5MPJ, 5N1V, 5N9K, 5N9L, 5N9N, 5NQC, 5OMY, 5ONI, 5OQU, 5ORH, 5ORJ, 5ORK, 5OS7, 5OS8, 5OSL, 5OSP, 5OSR, 5OSU, 5OSZ, 5OT5, 5OT6, 5OTD, 5OTH, 5OTI, 5OTL, 5OTO, 5OTP, 5OTQ, 5OTR, 5OTS, 5OTY, 5OTZ, 5OUE, 5OUL, 5OUM, 5OUU, 5OWH, 5OWL, 5OYF, 5T1H, 5VIE, 5VIF, 5ZN0, 5ZN1, 5ZN2, 5ZN3, 5ZN4, 5ZN5, 6A1C, 6E37, 6EHK, 6EHU, 6EII, 6FVF, 6FVG, 6GIH, 6GMD, 6HBN, 6HME, 6HNW, 6HNY, 6HOP, 6HOQ, 6HOR, 6HOT, 6HOU, 6JWA, 6L1Z, 6L21, 6L22, 6L23, 6L24, 6Q38, 6Q4Q, 6QY7, 6RB1, 6RCB, 6RCM, 6RFE, 6RFF, 6SPW, 6SPX, 6TEI, 6TLL, 6TLO, 6TLP, 6TLR, 6TLS, 6TLU, 6TLV, 6TLW, 6YPG, 6YPH, 6YPJ, 6YPK, 6YPN, 6YUL, 6YUM, 6YZH, 6Z19, 6Z83, 6Z84, 7A49, 7A4B, 7A4C, 7A4Q, 7AT5, 7AY9, 7AYA, 7B8H, 7B8I, 7BU4, 7L1X, 7PSU, 7QGB, 7QGC, 7QGD, 7QGE, 7QUX, 7X4H, 7Z39, 7ZWE, 7ZWG, 7ZY0, 7ZY2, 7ZY5, 7ZY8, 7ZYD, 7ZYK, 7ZYO, 7ZYR, 8AE7, 8AEC, 8AEK, 8AEM, 8BGC, 8C5Q, 8C6L, 8C6M, 8C6N, 8P05, 8P07, 8PVO, 8PVP, 8QWY, 8QWZ, 9EPV, 9EPW, 9EPX, 9EPY, 9EPZ, 9EQ0, 9EQ1
KEGG IDhsa:1457
IUPHAR/Guide To Pharmacology ID1549
NCBI Gene ID1457
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. [Article]
  2. 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. [Article]
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  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  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. [Article]
  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. [Article]
  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. [Article]
  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. [Article]
  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. [Article]
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  31. Ermakova I, Boldyreff B, Issinger OG, Niefind K: Crystal structure of a C-terminal deletion mutant of human protein kinase CK2 catalytic subunit. J Mol Biol. 2003 Jul 25;330(5):925-34. [Article]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
BenzamidineexperimentalunknowntargetDetails
Phosphoaminophosphonic Acid-Adenylate EsterexperimentalunknowntargetDetails
Tetrabromo-2-BenzotriazoleexperimentalyestargetinhibitorDetails
ResveratrolinvestigationalunknowntargetDetails
S-METHYL-4,5,6,7-TETRABROMO-BENZIMIDAZOLEexperimentalunknowntargetDetails
EmodininvestigationalyestargetinhibitorDetails
3,8-DIBROMO-7-HYDROXY-4-METHYL-2H-CHROMEN-2-ONEexperimentalunknowntargetDetails
1,8-Di-Hydroxy-4-Nitro-AnthraquinoneexperimentalunknowntargetDetails
(5-hydroxyindolo[1,2-a]quinazolin-7-yl)acetic acidexperimentalyestargetinhibitorDetails
DIMETHYL-(4,5,6,7-TETRABROMO-1H-BENZOIMIDAZOL-2-YL)-AMINEexperimentalunknowntargetDetails
N1,N2-ETHYLENE-2-METHYLAMINO-4,5,6,7-TETRABROMO-BENZIMIDAZOLEexperimentalunknowntargetDetails
1,8-Di-Hydroxy-4-Nitro-Xanthen-9-OneexperimentalunknowntargetDetails
5,8-Di-Amino-1,4-Dihydroxy-AnthraquinoneexperimentalunknowntargetDetails
19-(cyclopropylamino)-4,6,7,15-tetrahydro-5H-16,1-(azenometheno)-10,14-(metheno)pyrazolo[4,3-o][1,3,9]triazacyclohexadecin-8(9H)-oneexperimentalunknowntargetDetails
N,N'-DIPHENYLPYRAZOLO[1,5-A][1,3,5]TRIAZINE-2,4-DIAMINEexperimentalunknowntargetDetails
4-(2-(1H-IMIDAZOL-4-YL)ETHYLAMINO)-2-(PHENYLAMINO)PYRAZOLO[1,5-A][1,3,5]TRIAZINE-8-CARBONITRILEexperimentalunknowntargetDetails
2-(CYCLOHEXYLMETHYLAMINO)-4-(PHENYLAMINO)PYRAZOLO[1,5-A][1,3,5]TRIAZINE-8-CARBONITRILEexperimentalunknowntargetDetails
2-(4-CHLOROBENZYLAMINO)-4-(PHENYLAMINO)PYRAZOLO[1,5-A][1,3,5]TRIAZINE-8-CARBONITRILEexperimentalunknowntargetDetails
2-(4-ETHYLPIPERAZIN-1-YL)-4-(PHENYLAMINO)PYRAZOLO[1,5-A][1,3,5]TRIAZINE-8-CARBONITRILEexperimentalunknowntargetDetails
N-(3-(8-CYANO-4-(PHENYLAMINO)PYRAZOLO[1,5-A][1,3,5]TRIAZIN-2-YLAMINO)PHENYL)ACETAMIDEexperimentalunknowntargetDetails
DichlororibofuranosylbenzimidazoleexperimentalyestargetinhibitorDetails
QuinalizarinexperimentalunknowntargetDetails
Ellagic acidinvestigationalyestargetinhibitorDetails
ATPinvestigational, nutraceuticalunknowntargetDetails
Quercetinexperimental, investigationalunknowntargetDetails
Fostamatinibapproved, investigationalunknowntargetinhibitorDetails
ApigeninexperimentalyestargetinhibitorDetails
SilmitasertibinvestigationalyestargetinhibitorDetails