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Csnk2b  -  casein kinase 2, beta polypeptide

Mus musculus

Synonyms: CK II beta, Casein kinase II subunit beta, Ck2n, Phosvitin
 
 
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High impact information on Csnk2b

  • These are the cAMP-dependent protein kinase type I and II isozymes and a "histone kinase" and a "phosvitin kinase"; neither of the latter two is regulated by cyclic nucleotides [1].
  • The mouse protein kinase CK2 beta subunit gene (Csnk2b) is composed of seven exons contained within 7874 bp [2].
  • We have selected an anti-Torpedo acetylcholine receptor monoclonal antibody which binds specifically to phosvitin; this binding is inhibited by acetylcholine receptor [3].
  • Partially purified protein kinase has a Km for ATP of approximately 30 microMs, whereas the Km for GTP is approximately 300 microMs and the substrate preference is phosvitin greater than casein much greater than histone greater than protamine [4].
  • In this study, we evaluated the effect of egg yolk phosvitin on UV-light-induced oxidative stress [5].
 

Biological context of Csnk2b

 

Anatomical context of Csnk2b

  • Using phosphoprotein staining we have shown that the 72 kDa polypeptide is the larger phosvitin so far described in a vertebrate egg yolk [7].
 

Associations of Csnk2b with chemical compounds

 

Analytical, diagnostic and therapeutic context of Csnk2b

  • Genomic DNA was extracted from peripheral blood and PCR was performed to amplify Csnk2a2 and Csnk2b genes before sequencing [9].

References

  1. Protein phosphotransferase activities and cyclic nucleotide action in proliferating lymphocytes. Masaracchia, R.A., Walsh, D.A. Cancer Res. (1976) [Pubmed]
  2. Structure of the gene encoding the murine protein kinase CK2 beta subunit. Boldyreff, B., Issinger, O.G. Genomics (1995) [Pubmed]
  3. An anti-acetylcholine receptor monoclonal antibody cross-reacts with phosvitin. Pizzighella, S., Gordon, A.S., Souroujon, M.C., Mochly-Rosen, D., Sharp, A., Fuchs, S. FEBS Lett. (1983) [Pubmed]
  4. A plasmodium protein kinase that is developmentally regulated, stimulated by spermine, and inhibited by quercetin. Wiser, M.F., Eaton, J.W., Sheppard, J.R. J. Cell. Biochem. (1983) [Pubmed]
  5. Protective effect of egg yolk phosvitin against ultraviolet- light-induced lipid peroxidation in the presence of iron ions. Ishikawa, S., Ohtsuki, S., Tomita, K., Arihara, K., Itoh, M. Biological trace element research. (2005) [Pubmed]
  6. Protein kinase activity on the cell surface of a macrophage-like cell line, J774.1 cells. Amano, F., Kitagawa, T., Akamatsu, Y. Biochim. Biophys. Acta (1984) [Pubmed]
  7. Vitellogenin and yolk protein processing in Bothrops jararaca (Wied), a tropical venomous snake. Janeiro-Cinquini, T.R., Ribolla, P.E., Capurro, M.d.e. .L., Winter, C.E. Comp. Biochem. Physiol. B, Biochem. Mol. Biol. (1999) [Pubmed]
  8. Phosphorylation of endogenous membrane proteins by endogenous protein kinase at the outer surface of Ehrlich cells. Agren, G., Ronquist, G. Ups. J. Med. Sci. (1976) [Pubmed]
  9. Search for mutations involved in human globozoospermia. Pirrello, O., Machev, N., Schimdt, F., Terriou, P., Ménézo, Y., Viville, S. Hum. Reprod. (2005) [Pubmed]
 
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