The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

Csnk2a1  -  casein kinase 2, alpha 1 polypeptide

Rattus norvegicus

Synonyms: CK II alpha, Casein kinase II subunit alpha
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Csnk2a1

  • The enhanced responses of ODC and of CK-II to DMH proceeded the actual polyp and tumor formation [1].

High impact information on Csnk2a1

  • Molecular characterization revealed a 10-fold repeated motif of highly conserved acidic serine clusters that contain an abundance of phosphorylation consensus sites for casein kinase II (CK II) [2].
  • Using this antibody, we showed that p53 is phosphorylated at the CK II site upon UV treatment of early passage rat embryo fibroblasts and RKO cells [3].
  • These results indicate that phosphorylation at the CK II site is one of the post-translational mechanisms through which p53 is activated in response to UV radiation and that different mechanisms activate p53 after DNA damage by gamma radiation [3].
  • CK-II activity was also selectively and rapidly augmented in another form of LTP produced by bath application of tetraethylammonium; this LTP (called LTPk) is Ca2+ dependent but N-methyl-D-aspartate independent [4].
  • The stimulated protein kinase activity, which was blocked by a selective antagonist of N-methyl-D-aspartate receptors, exhibited specific properties of CK-II, including phosphorylation of the specific substrates of CK-II, marked inhibition by a low heparin concentration, and the use of GTP as a phosphate donor [4].

Biological context of Csnk2a1


Anatomical context of Csnk2a1

  • We now report that casein kinase II (CK-II), which is present in high concentration in the hippocampus, is also activated in the CA1 region during LTP [4].
  • Based on the pattern of phosphorylation of the wildtype and two variant forms of eIF2B epsilon using casein kinase (CK)-I, CK-II, or GSK-3 as well as that observed with skeletal muscle extracts, we conclude that the predominant eIF2B epsilon kinase in psoas muscle is GSK-3 [7].

Associations of Csnk2a1 with chemical compounds

  • Protein phosphatase-1 (PP-1) and -2A (PP-2A), two regulatory subunits of PP-1, the glycogen-binding subunit G and inhibitor-2 (I-2), kinase FA, and casein kinase II (CK-II) were investigated in skeletal muscle of diabetic rats 2 days after streptozotocin injection [8].
  • The activity gradient of CK-II was markedly altered in DMH-treated cell populations: brisk activity of the kinase was observed in the upper crypt zone, the preserve of the mature, non-dividing colonocyte [1].
  • Phosphorylation of casein or synthetic oligopeptides by CK-II was not affected by Ca2+, diolein, or phosphatidylserine [5].
  • Since CK II is central in all these events, which are specifically affected by ethanol, the role of nuclear CK II is investigated in the present study [9].
  • The polycations spermine and spermidine, bioactive molecules formed in the ODC-controlled polyamine pathway, were shown to markedly activate colonic CK-II [1].

Other interactions of Csnk2a1

  • The activities of the growth-related enzymes ornithine decarboxylase (ODC) and casein kinase II (CK-II) were assayed along the colon crypt axis in a precise temporal sequence following administration of 1,2-dimethylhydrazine (DMH) to male rats [1].
  • In activated cells, cPGES phosphorylation occurred in parallel with increased cPGES enzymic activity and PGE2 production from exogenous and endogenous arachidonic acid, and these processes were facilitated by Hsp90 (heat-shock protein 90), a molecular chaperone that formed a tertiary complex with cPGES and CK-II [10].

Analytical, diagnostic and therapeutic context of Csnk2a1

  • CK-II activity increased within 2 min after a train of high-frequency electrical stimulations and reached a maximum (2-fold increase) 5 min later before returning to baseline value [4].


  1. Growth-related enzyme activities in crypt compartments during rat colon carcinogenesis. Lamprecht, S.A., Schwartz, B., Avigdor, A., Guberman, R. Anticancer Res. (1990) [Pubmed]
  2. Nopp140 shuttles on tracks between nucleolus and cytoplasm. Meier, U.T., Blobel, G. Cell (1992) [Pubmed]
  3. Functional activation of p53 via phosphorylation following DNA damage by UV but not gamma radiation. Kapoor, M., Lozano, G. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  4. Rapid activation of hippocampal casein kinase II during long-term potentiation. Charriaut-Marlangue, C., Otani, S., Creuzet, C., Ben-Ari, Y., Loeb, J. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  5. Phosphorylation of type II (beta) protein kinase C by casein kinase II. Tominaga, M., Kitagawa, Y., Tanaka, S., Kishimoto, A. J. Biochem. (1991) [Pubmed]
  6. Action of 3 tyrphostin derivatives on casein kinase II from rat liver. Kang, T.B., Huang, C., Liang, N.C. Zhongguo yao li xue bao = Acta pharmacologica Sinica. (1997) [Pubmed]
  7. Glycogen synthase kinase-3 is the predominant insulin-regulated eukaryotic initiation factor 2B kinase in skeletal muscle. Jefferson, L.S., Fabian, J.R., Kimball, S.R. Int. J. Biochem. Cell Biol. (1999) [Pubmed]
  8. Protein phosphatase-1 and -2A, kinase FA, and casein kinase II in skeletal muscle of streptozotocin diabetic rats. Metallo, A., Villa-Moruzzi, E. Arch. Biochem. Biophys. (1991) [Pubmed]
  9. Effect of ethanol on nuclear casein kinase II activity in brain. Haviryaji, K.S., Vemuri, M.C. Neurochem. Res. (1997) [Pubmed]
  10. Regulation of cytosolic prostaglandin E synthase by phosphorylation. Kobayashi, T., Nakatani, Y., Tanioka, T., Tsujimoto, M., Nakajo, S., Nakaya, K., Murakami, M., Kudo, I. Biochem. J. (2004) [Pubmed]
WikiGenes - Universities