CSK22_HUMAN
ID CSK22_HUMAN Reviewed; 350 AA.
AC P19784;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 221.
DE RecName: Full=Casein kinase II subunit alpha';
DE Short=CK II alpha';
DE EC=2.7.11.1;
GN Name=CSNK2A2; Synonyms=CK2A2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2174700; DOI=10.1021/bi00488a034;
RA Lozeman F.J., Litchfield D.W., Piening C., Takio K., Walsh K.A.,
RA Krebs E.G.;
RT "Isolation and characterization of human cDNA clones encoding the alpha and
RT the alpha' subunits of casein kinase II.";
RL Biochemistry 29:8436-8447(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, AND INTERACTION WITH SSRP1 AND SUPT16H.
RX PubMed=11239457; DOI=10.1016/s1097-2765(01)00176-9;
RA Keller D.M., Zeng X., Wang Y., Zhang Q.H., Kapoor M., Shu H., Goodman R.,
RA Lozano G., Zhao Y., Lu H.;
RT "A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16,
RT and SSRP1.";
RL Mol. Cell 7:283-292(2001).
RN [4]
RP FUNCTION IN CELL CYCLE.
RX PubMed=11704824; DOI=10.1038/sj.onc.1204894;
RA Sayed M., Pelech S., Wong C., Marotta A., Salh B.;
RT "Protein kinase CK2 is involved in G2 arrest and apoptosis following
RT spindle damage in epithelial cells.";
RL Oncogene 20:6994-7005(2001).
RN [5]
RP INTERACTION WITH SSRP1 AND SUPT16H.
RX PubMed=12393879; DOI=10.1074/jbc.m209820200;
RA Keller D.M., Lu H.;
RT "p53 serine 392 phosphorylation increases after UV through induction of the
RT assembly of the CK2.hSPT16.SSRP1 complex.";
RL J. Biol. Chem. 277:50206-50213(2002).
RN [6]
RP FUNCTION IN APOPTOSIS.
RX PubMed=16193064; DOI=10.1038/sj.emboj.7600827;
RA Shin S., Lee Y., Kim W., Ko H., Choi H., Kim K.;
RT "Caspase-2 primes cancer cells for TRAIL-mediated apoptosis by processing
RT procaspase-8.";
RL EMBO J. 24:3532-3542(2005).
RN [7]
RP REVIEW ON FUNCTION.
RX PubMed=12631575; DOI=10.1096/fj.02-0473rev;
RA Meggio F., Pinna L.A.;
RT "One-thousand-and-one substrates of protein kinase CK2?";
RL FASEB J. 17:349-368(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-21 AND SER-288, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP REVIEW ON STRUCTURE.
RX PubMed=19387553; DOI=10.1007/s00018-009-9149-8;
RA Niefind K., Raaf J., Issinger O.G.;
RT "Protein kinase CK2 in health and disease: Protein kinase CK2: from
RT structures to insights.";
RL Cell. Mol. Life Sci. 66:1800-1816(2009).
RN [10]
RP REVIEW ON FUNCTION.
RX PubMed=19387552; DOI=10.1007/s00018-009-9150-2;
RA St-Denis N.A., Litchfield D.W.;
RT "Protein kinase CK2 in health and disease: From birth to death: the role of
RT protein kinase CK2 in the regulation of cell proliferation and survival.";
RL Cell. Mol. Life Sci. 66:1817-1829(2009).
RN [11]
RP REVIEW ON FUNCTION.
RX PubMed=19387551; DOI=10.1007/s00018-009-9151-1;
RA Filhol O., Cochet C.;
RT "Protein kinase CK2 in health and disease: Cellular functions of protein
RT kinase CK2: a dynamic affair.";
RL Cell. Mol. Life Sci. 66:1830-1839(2009).
RN [12]
RP REVIEW ON FUNCTION IN REGULATION OF HSP90.
RX PubMed=19387550; DOI=10.1007/s00018-009-9152-0;
RA Miyata Y.;
RT "Protein kinase CK2 in health and disease: CK2: the kinase controlling the
RT Hsp90 chaperone machinery.";
RL Cell. Mol. Life Sci. 66:1840-1849(2009).
RN [13]
RP REVIEW ON FUNCTION IN WNT SIGNALING.
RX PubMed=19387549; DOI=10.1007/s00018-009-9153-z;
RA Dominguez I., Sonenshein G.E., Seldin D.C.;
RT "Protein kinase CK2 in health and disease: CK2 and its role in Wnt and NF-
RT kappaB signaling: linking development and cancer.";
RL Cell. Mol. Life Sci. 66:1850-1857(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-13; SER-18; SER-21 AND
RP SER-288, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-97, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 1-334 IN COMPLEX WITH INHIBITOR.
RX PubMed=19193990; DOI=10.1107/s1744309108043194;
RA Nakaniwa T., Kinoshita T., Sekiguchi Y., Tada T., Nakanishi I., Kitaura K.,
RA Suzuki Y., Ohno H., Hirasawa A., Tsujimoto G.;
RT "Structure of human protein kinase CK2 alpha 2 with a potent indazole-
RT derivative inhibitor.";
RL Acta Crystallogr. F 65:75-79(2009).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
RX PubMed=21241709; DOI=10.1016/j.jmb.2011.01.020;
RA Bischoff N., Olsen B., Raaf J., Bretner M., Issinger O.G., Niefind K.;
RT "Structure of the human protein kinase CK2 catalytic subunit CK2alpha' and
RT interaction thermodynamics with the regulatory subunit CK2beta.";
RL J. Mol. Biol. 407:1-12(2011).
RN [20]
RP VARIANT [LARGE SCALE ANALYSIS] ALA-188.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Catalytic subunit of a constitutively active
CC serine/threonine-protein kinase complex that phosphorylates a large
CC number of substrates containing acidic residues C-terminal to the
CC phosphorylated serine or threonine. Regulates numerous cellular
CC processes, such as cell cycle progression, apoptosis and transcription,
CC as well as viral infection. May act as a regulatory node which
CC integrates and coordinates numerous signals leading to an appropriate
CC cellular response. During mitosis, functions as a component of the
CC p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains
CC cyclin-B-CDK1 activity and G2 arrest in response to spindle damage.
CC Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-
CC 392' of p53/TP53 following UV irradiation. Can also negatively regulate
CC apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the
CC apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage
CC and activation by CASP8, and inhibits the dimerization of CASP2 and
CC activation of CASP8. Regulates transcription by direct phosphorylation
CC of RNA polymerases I, II, III and IV. Also phosphorylates and regulates
CC numerous transcription factors including NF-kappa-B, STAT1, CREB1,
CC IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90
CC and its co-chaperones FKBP4 and CDC37, which is essential for chaperone
CC function. Regulates Wnt signaling by phosphorylating CTNNB1 and the
CC transcription factor LEF1. Acts as an ectokinase that phosphorylates
CC several extracellular proteins. During viral infection, phosphorylates
CC various proteins involved in the viral life cycles of EBV, HSV, HBV,
CC HCV, HIV, CMV and HPV. {ECO:0000269|PubMed:11239457,
CC ECO:0000269|PubMed:11704824, ECO:0000269|PubMed:16193064}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- ACTIVITY REGULATION: Constitutively active protein kinase whose
CC activity is not directly affected by phosphorylation. Seems to be
CC regulated by level of expression and localization (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Heterotetramer composed of two catalytic subunits (alpha chain
CC and/or alpha' chain) and two regulatory subunits (beta chains). The
CC tetramer can exist as a combination of 2 alpha/2 beta, 2 alpha'/2 beta
CC or 1 alpha/1 alpha'/2 beta subunits. Also part of a CK2-SPT16-SSRP1
CC complex composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, which
CC forms following UV irradiation (PubMed:11239457, PubMed:12393879).
CC Interacts with CSNKA2IP (via C-terminus) (By similarity). Interacts
CC with SIRT6; preventing CSNK2A2 localization to the nucleus (By
CC similarity). Interacts with RNPS1. {ECO:0000250|UniProtKB:O54833,
CC ECO:0000269|PubMed:11239457, ECO:0000269|PubMed:12393879,
CC ECO:0000269|PubMed:19193990}.
CC -!- INTERACTION:
CC P19784; P68400: CSNK2A1; NbExp=10; IntAct=EBI-347451, EBI-347804;
CC P19784; P67870: CSNK2B; NbExp=14; IntAct=EBI-347451, EBI-348169;
CC P19784; O60282: KIF5C; NbExp=4; IntAct=EBI-347451, EBI-717170;
CC P19784; Q9NRD5: PICK1; NbExp=5; IntAct=EBI-347451, EBI-79165;
CC P19784; Q8WV44: TRIM41; NbExp=7; IntAct=EBI-347451, EBI-725997;
CC P19784; Q9BS34: ZNF670; NbExp=4; IntAct=EBI-347451, EBI-745276;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O54833}. Cytoplasm
CC {ECO:0000250|UniProtKB:O54833}. Note=Interaction with SIRT6 prevents
CC translocation into the nucleus. {ECO:0000250|UniProtKB:O54833}.
CC -!- MISCELLANEOUS: Can use both ATP and GTP as phosphoryl donors.
CC Phosphorylation by casein kinase 2 has been estimated to represent up
CC to one quarter of the eukaryotic phosphoproteome.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CK2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; M55268; AAA51548.1; -; mRNA.
DR EMBL; BC008812; AAH08812.1; -; mRNA.
DR CCDS; CCDS10794.1; -.
DR PIR; B35838; B35838.
DR RefSeq; NP_001887.1; NM_001896.2.
DR PDB; 3E3B; X-ray; 3.20 A; X=1-334.
DR PDB; 3OFM; X-ray; 2.00 A; A=1-350.
DR PDB; 3U87; X-ray; 2.90 A; A/B=327-350.
DR PDB; 5M4U; X-ray; 2.19 A; A=1-350.
DR PDB; 5M56; X-ray; 2.24 A; A/B=1-350.
DR PDB; 5OOI; X-ray; 2.00 A; A/B=1-350.
DR PDB; 5Y9M; X-ray; 2.01 A; A/X=1-334.
DR PDB; 5YF9; X-ray; 1.89 A; B/X=1-334.
DR PDB; 5YWM; X-ray; 1.94 A; X=1-334.
DR PDB; 6HMB; X-ray; 1.04 A; A=1-350.
DR PDB; 6HMC; X-ray; 1.03 A; A=1-350.
DR PDB; 6HMD; X-ray; 1.00 A; A=1-350.
DR PDB; 6HMQ; X-ray; 0.97 A; A=1-346.
DR PDB; 6L20; X-ray; 3.09 A; A/D/G/J=1-333.
DR PDB; 6QY8; X-ray; 1.70 A; A/B/C/D=1-335.
DR PDB; 6QY9; X-ray; 1.50 A; A=1-335.
DR PDB; 6TE2; X-ray; 0.92 A; A=1-350.
DR PDB; 6TEW; X-ray; 1.08 A; A=1-350.
DR PDB; 6TGU; X-ray; 0.83 A; A=1-350.
DR PDB; 7A1B; X-ray; 1.29 A; A=1-350.
DR PDB; 7A1Z; X-ray; 1.02 A; A=1-350.
DR PDB; 7A22; X-ray; 1.01 A; A=1-350.
DR PDB; 7A2H; X-ray; 1.01 A; A=1-350.
DR PDB; 7AT9; X-ray; 1.05 A; A=1-350.
DR PDB; 7ATV; X-ray; 0.98 A; A=1-350.
DR PDBsum; 3E3B; -.
DR PDBsum; 3OFM; -.
DR PDBsum; 3U87; -.
DR PDBsum; 5M4U; -.
DR PDBsum; 5M56; -.
DR PDBsum; 5OOI; -.
DR PDBsum; 5Y9M; -.
DR PDBsum; 5YF9; -.
DR PDBsum; 5YWM; -.
DR PDBsum; 6HMB; -.
DR PDBsum; 6HMC; -.
DR PDBsum; 6HMD; -.
DR PDBsum; 6HMQ; -.
DR PDBsum; 6L20; -.
DR PDBsum; 6QY8; -.
DR PDBsum; 6QY9; -.
DR PDBsum; 6TE2; -.
DR PDBsum; 6TEW; -.
DR PDBsum; 6TGU; -.
DR PDBsum; 7A1B; -.
DR PDBsum; 7A1Z; -.
DR PDBsum; 7A22; -.
DR PDBsum; 7A2H; -.
DR PDBsum; 7AT9; -.
DR PDBsum; 7ATV; -.
DR AlphaFoldDB; P19784; -.
DR SMR; P19784; -.
DR BioGRID; 107842; 350.
DR ComplexPortal; CPX-2428; Casein kinase II complex, CSNK2A2 variant.
DR ComplexPortal; CPX-2437; Casein kinase II complex, CSNK2A1-CNSK2A2 variant.
DR CORUM; P19784; -.
DR DIP; DIP-318N; -.
DR IntAct; P19784; 268.
DR MINT; P19784; -.
DR STRING; 9606.ENSP00000262506; -.
DR BindingDB; P19784; -.
DR ChEMBL; CHEMBL4070; -.
DR DrugBank; DB07546; [1-(6-{6-[(1-methylethyl)amino]-1H-indazol-1-yl}pyrazin-2-yl)-1H-pyrrol-3-yl]acetic acid.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; P19784; -.
DR GuidetoPHARMACOLOGY; 1550; -.
DR GlyGen; P19784; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P19784; -.
DR MetOSite; P19784; -.
DR PhosphoSitePlus; P19784; -.
DR SwissPalm; P19784; -.
DR BioMuta; CSNK2A2; -.
DR DMDM; 125266; -.
DR SWISS-2DPAGE; P19784; -.
DR EPD; P19784; -.
DR jPOST; P19784; -.
DR MassIVE; P19784; -.
DR MaxQB; P19784; -.
DR PaxDb; P19784; -.
DR PeptideAtlas; P19784; -.
DR PRIDE; P19784; -.
DR ProteomicsDB; 53686; -.
DR Antibodypedia; 15225; 333 antibodies from 34 providers.
DR DNASU; 1459; -.
DR Ensembl; ENST00000262506.8; ENSP00000262506.3; ENSG00000070770.10.
DR GeneID; 1459; -.
DR KEGG; hsa:1459; -.
DR MANE-Select; ENST00000262506.8; ENSP00000262506.3; NM_001896.4; NP_001887.1.
DR UCSC; uc002enc.4; human.
DR CTD; 1459; -.
DR DisGeNET; 1459; -.
DR GeneCards; CSNK2A2; -.
DR HGNC; HGNC:2459; CSNK2A2.
DR HPA; ENSG00000070770; Tissue enhanced (testis).
DR MIM; 115442; gene.
DR neXtProt; NX_P19784; -.
DR OpenTargets; ENSG00000070770; -.
DR PharmGKB; PA26959; -.
DR VEuPathDB; HostDB:ENSG00000070770; -.
DR eggNOG; KOG0668; Eukaryota.
DR GeneTree; ENSGT00390000004215; -.
DR OMA; NSKEKCI; -.
DR OrthoDB; 1098380at2759; -.
DR PhylomeDB; P19784; -.
DR TreeFam; TF300483; -.
DR BRENDA; 2.7.11.1; 2681.
DR PathwayCommons; P19784; -.
DR Reactome; R-HSA-1483191; Synthesis of PC.
DR Reactome; R-HSA-201688; WNT mediated activation of DVL.
DR Reactome; R-HSA-2514853; Condensation of Prometaphase Chromosomes.
DR Reactome; R-HSA-445144; Signal transduction by L1.
DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-HSA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR Reactome; R-HSA-8934903; Receptor Mediated Mitophagy.
DR Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway.
DR SignaLink; P19784; -.
DR SIGNOR; P19784; -.
DR BioGRID-ORCS; 1459; 19 hits in 1122 CRISPR screens.
DR ChiTaRS; CSNK2A2; human.
DR EvolutionaryTrace; P19784; -.
DR GeneWiki; CSNK2A2; -.
DR GenomeRNAi; 1459; -.
DR Pharos; P19784; Tchem.
DR PRO; PR:P19784; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P19784; protein.
DR Bgee; ENSG00000070770; Expressed in secondary oocyte and 202 other tissues.
DR ExpressionAtlas; P19784; baseline and differential.
DR Genevisible; P19784; HS.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005956; C:protein kinase CK2 complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IGI:ARUK-UCL.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; TAS:ARUK-UCL.
DR GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; IGI:ARUK-UCL.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:ARUK-UCL.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; HMP:ParkinsonsUK-UCL.
DR GO; GO:1903146; P:regulation of autophagy of mitochondrion; HMP:ParkinsonsUK-UCL.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR GO; GO:1905818; P:regulation of chromosome separation; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd14132; STKc_CK2_alpha; 1.
DR InterPro; IPR045216; CK2_alpha.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24054; PTHR24054; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Apoptosis; ATP-binding; Cell cycle; Cytoplasm;
KW Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transcription; Transcription regulation;
KW Transferase; Wnt signaling pathway.
FT CHAIN 1..350
FT /note="Casein kinase II subunit alpha'"
FT /id="PRO_0000085891"
FT DOMAIN 40..325
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 157
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 46..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 13
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195"
FT MOD_RES 97
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195"
FT VARIANT 188
FT /note="E -> A (in dbSNP:rs55911801)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040416"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:6TGU"
FT TURN 14..19
FT /evidence="ECO:0007829|PDB:6TGU"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:6TGU"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:6TGU"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:6HMD"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:6TGU"
FT STRAND 40..48
FT /evidence="ECO:0007829|PDB:6TGU"
FT STRAND 50..59
FT /evidence="ECO:0007829|PDB:6TGU"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:6TGU"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:6TGU"
FT HELIX 76..88
FT /evidence="ECO:0007829|PDB:6TGU"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:6TGU"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:6TGU"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:6TGU"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:6TGU"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:6TGU"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:6TGU"
FT HELIX 131..150
FT /evidence="ECO:0007829|PDB:6TGU"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:6TGU"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:6TGU"
FT TURN 167..170
FT /evidence="ECO:0007829|PDB:6TGU"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:6TGU"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:6TE2"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:6TGU"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:6TGU"
FT HELIX 213..228
FT /evidence="ECO:0007829|PDB:6TGU"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:6TGU"
FT HELIX 239..250
FT /evidence="ECO:0007829|PDB:6TGU"
FT HELIX 252..262
FT /evidence="ECO:0007829|PDB:6TGU"
FT HELIX 268..272
FT /evidence="ECO:0007829|PDB:6TGU"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:6TGU"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:6TGU"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:6TGU"
FT HELIX 296..305
FT /evidence="ECO:0007829|PDB:6TGU"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:6TGU"
FT HELIX 316..320
FT /evidence="ECO:0007829|PDB:6TGU"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:6TGU"
FT HELIX 326..332
FT /evidence="ECO:0007829|PDB:6TGU"
SQ SEQUENCE 350 AA; 41213 MW; 3ECB92F6BD3DD7F1 CRC64;
MPGPAAGSRA RVYAEVNSLR SREYWDYEAH VPSWGNQDDY QLVRKLGRGK YSEVFEAINI
TNNERVVVKI LKPVKKKKIK REVKILENLR GGTNIIKLID TVKDPVSKTP ALVFEYINNT
DFKQLYQILT DFDIRFYMYE LLKALDYCHS KGIMHRDVKP HNVMIDHQQK KLRLIDWGLA
EFYHPAQEYN VRVASRYFKG PELLVDYQMY DYSLDMWSLG CMLASMIFRR EPFFHGQDNY
DQLVRIAKVL GTEELYGYLK KYHIDLDPHF NDILGQHSRK RWENFIHSEN RHLVSPEALD
LLDKLLRYDH QQRLTAKEAM EHPYFYPVVK EQSQPCADNA VLSSGLTAAR
