Aliases for CSNK2A1 Gene
External Ids for CSNK2A1 Gene
Casein kinase II is a serine/threonine protein kinase that phosphorylates acidic proteins such as casein. It is involved in various cellular processes, including cell cycle control, apoptosis, and circadian rhythm. The kinase exists as a tetramer and is composed of an alpha, an alpha-prime, and two beta subunits. The alpha subunits contain the catalytic activity while the beta subunits undergo autophosphorylation. The protein encoded by this gene represents the alpha subunit. While this gene is found on chromosome 20, a related transcribed pseudogene is found on chromosome 11. Three transcript variants encoding two different proteins have been found for this gene. [provided by RefSeq, Jul 2014]
GeneCards Summary for CSNK2A1 Gene
CSNK2A1 (Casein Kinase 2, Alpha 1 Polypeptide) is a Protein Coding gene. Diseases associated with CSNK2A1 include malaria. Among its related pathways are L1CAM interactions and NF-KappaB Family Pathway. GO annotations related to this gene include protein serine/threonine kinase activity and beta-catenin binding. An important paralog of this gene is CSNK2A2.
UniProtKB/Swiss-Prot for CSNK2A1 Gene
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.
Casein kinase II (CK2) is a constitutively active, ubiquitously expressed serine/threonine protein kinase that is thought to have a regulatory function in cell proliferation, cell differentiation and apoptosis. CK2 functions as a tetrameric complex consisting of two regulatory beta-subunits and two catalytic units (alpha and alpha) in a homomeric or heteromeric conformation. Whilst the alpha- and alpha-subunits are catalytically identical, proteins that regulate CK2, such as cdc2 and Hsp90, preferentially bind to the alpha and not the alpha-subunit. CK2 can phosphorylate a number of key intracellular signaling proteins implicated in tumor suppression (p53 and PTEN) and tumorigenesis (myc, jun, NF-kappaB). CK2 is also thought to influence Wnt signaling via beta-catenin phosphorylation and the PI 3-K signaling pathway via the phosphorylation of Akt.