{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P68400","secondaryAccessions":["B4DYS6","D3DVV8","P19138","P20426","Q14013","Q5U065"],"uniProtkbId":"CSK21_HUMAN","entryAudit":{"firstPublicDate":"2004-11-23","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2004-11-23","entryVersion":213,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Casein kinase II subunit alpha"},"shortNames":[{"value":"CK II alpha"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20545769"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22017874"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22325354"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30699359"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31439799"}],"value":"2.7.11.1"}]}},"genes":[{"geneName":{"value":"CSNK2A1"},"synonyms":[{"value":"CK2A1"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19139"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11239457"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11704824"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16193064"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18411307"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18583988"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18678890"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19188443"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20545769"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20625391"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21482717"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22017874"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22184066"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22325354"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22406621"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23123191"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24962073"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26811421"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28512243"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30699359"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30765518"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30898438"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31439799"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35597237"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38334665"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"12631575"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19387549"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19387550"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19387551"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19387552"}],"value":"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)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17989"},{"database":"Rhea","id":"RHEA-COMP:9863"},{"database":"Rhea","id":"RHEA-COMP:11604"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29999"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:83421"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.1","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18411307"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18583988"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18678890"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20545769"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20625391"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21482717"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22017874"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22184066"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23123191"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28512243"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30699359"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30898438"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31439799"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:17990"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18411307"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18583988"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18678890"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20545769"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21482717"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23123191"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28512243"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30699359"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30898438"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31439799"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35597237"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:46608"},{"database":"Rhea","id":"RHEA-COMP:11060"},{"database":"Rhea","id":"RHEA-COMP:11605"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30013"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:61977"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.11.1","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18411307"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18583988"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18678890"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20625391"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22325354"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31439799"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:46609"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18411307"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18583988"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18678890"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31439799"}]}]},{"texts":[{"value":"Constitutively active protein kinase whose activity is not directly affected by phosphorylation. Seems to be regulated by level of expression and localization"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11092945"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11239457"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11574463"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12393879"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15684395"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19923321"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20625391"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22406621"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24962073"}],"value":"Heterotetramer composed of two catalytic subunits (alpha chain and/or alpha' chain) and two regulatory subunits (beta chains). The tetramer can exist as a combination of 2 alpha/2 beta, 2 alpha'/2 beta or 1 alpha/1 alpha'/2 beta subunits. Also part of a CK2-SPT16-SSRP1 complex composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, which forms following UV irradiation. Interacts with RNPS1. Interacts with SNAI1. Interacts with PML (isoform PML-12). Interacts with CCAR2. Interacts with HIRIP3 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