Casein kinase II subunit alpha

Casein kinase II subunit alpha

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 threonine11239457,11704824,16193064,18411307,18583988,18678890,19188443,20545769,20625391,22017874,22406621,24962073,30898438,31439799. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection12631575,19387551,19387552. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response12631575,19387551,19387552. 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 damage11704824,19188443. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation11239457. 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 sites18411307,18583988,18678890,20545769,21482717,22325354,26811421,28512243,30898438,35597237. Can also negatively regulate apoptosis16193064,22184066. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL316193064. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP816193064. Phosphorylates YY1, protecting YY1 from cleavage by CASP7 during apoptosis22184066. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV12631575,19387550,19387551,19387552,23123191. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, ATF4, SRF, MAX, JUN, FOS, MYC and MYB12631575,19387550,19387551,19387552,23123191. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function19387550. Mediates sequential phosphorylation of FNIP1, promoting its gradual interaction with Hsp90, leading to activate both kinase and non-kinase client proteins of Hsp9030699359. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF119387549. Acts as an ectokinase that phosphorylates several extracellular proteins12631575,19387550,19387551,19387552. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV12631575,19387550,19387551,19387552. Phosphorylates PML at 'Ser-565' and primes it for ubiquitin-mediated degradation20625391,22406621. 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 tissue24962073. Phosphorylates FMR1, promoting FMR1-dependent formation of a membraneless compartment30765518,31439799. May phosphorylate histone H2A on 'Ser-1'38334665

Quoted from UniProt’s FUNCTION annotation for P68400 (reviewed). The superscript numbers are UniProt’s own PubMed citations, kept in the sentence and in order, each linking to the paper it names.

What it acts with

STRING’s highest-confidence human functional partners. The combined score mixes several kinds of evidence, so each channel is shown separately — a partner supported by experiment is a different claim from one supported only by text mining, and for a receptor this is where its coupling appears as evidence rather than as assertion.

Where it sits in the cell

• Nucleoplasm
• Primary ciliumadditional

Human Protein Atlas, by antibody immunofluorescence in cell lines — a different assay from the expression figures below, which are RNA.

UniProt, curated Nucleus