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Gene Review

CSNK2B  -  casein kinase 2, beta polypeptide

Homo sapiens

Synonyms: CK II beta, CK2B, CK2N, CSK2B, Casein kinase II subunit beta, ...
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Disease relevance of CSNK2B

  • The greatest rates of phosphorylation were obtained with acidic phosphoprotein substrates such as casein or phosvitin, although potential physiological substrates for this activity included specific virion polypeptides of frog virus [1].
  • Furthermore, when immature core subparticles which are enriched in Pr65gag are prepared from virions by Sepharose 6B exclusion column chromatography, about 50% of the kinase activity (as assayed with the exogenous substrate phosvitin) remains associated with the cores [2].
  • We have found that in the presence of ATP and Mg2+, exogenously added substrates such as phosvitin and poly(Glu4-Tyr) are phosphorylated by intact K562 erythroleukemia, HL60 promyelocytic leukemia, and U937 histiocytic leukemia human cells [3].
  • The enzyme, which uses both ATP and GTP as phosphoryl donors, catalyzes the phosphorylation of casein, phosvitin and E. coli RNA polymerase, but not of histone proteins [4].
  • Establishment of human glioblastoma multiforme cell line, G5A [5].

High impact information on CSNK2B

  • Fibrous apatite has been grown by the enzymatic hydrolysis of calcium beta-glycerophosphate on reconstituted calfskin collagen tapes which had been modified by the addition of a phosphoprotein, phosvitin, in the presence of a cross-linking agent, dimethylsuberimidate [6].
  • The enzyme did not nucleotidylylate common casein kinase II substrates (casein, phosvitin) and the reaction was inhibited by heparin [7].
  • The best available substrate for polypeptide-dependent protein kinase was beta-casein, and little or no phosphorylation was observed with alpha-casein, kappa-casein, phosvitin, alpha-lactalbumin, alpha-lactoglobulin, and histone [8].
  • Cultured cells of different origin (rat liver, mouse cerebellum, and human lung) exhibited phosvitin-induced protein kinase release from intact cells [9].
  • Chromatin-associated protein kinases active towards phosvitin, lysine-rich histone, and endogenous nonhistone proteins were characterized in human prostatic nuclei [10].

Biological context of CSNK2B


Anatomical context of CSNK2B


Associations of CSNK2B with chemical compounds


Physical interactions of CSNK2B


Enzymatic interactions of CSNK2B

  • One abundant ecto-PK component is believed to be a protein kinase CKII since it phosphorylates phosvitin and casein, is sensitive to heparin at low concentrations, and can use both ATP and GTP as cosubstrate [20].
  • Tightly adsorbed fractions possessed high troponin T kinase and phosvitin kinase activities and phosphorylated only serine-1 of troponin T. The results suggest that standard preparations of phosphorylase kinase are contaminated by troponin T kinase, which can phosphorylate serine-1 of troponin T [25].

Other interactions of CSNK2B

  • Partial cDNA and complete exonic genomic sequencing of one of the new genes has identified it as the casein kinase II beta subunit (CSNK2B) [11].
  • Thus, a three-component band fitting is used to characterize the Raman amide I band of alpha-synuclein, phosvitin, alpha-casein, beta-casein, and the non-A beta component (NAC) of Alzheimer's plaque [26].
  • There are three phosphopeptides in the yolk: phosvitin (PV, 37.4 kDa) and phosvettes 1 (PVT1, 27.7 kDa) and 2 (PVT2, 26.1 kDa) [27].
  • The amount of histatin 5 adsorbed was also found to increase as a function of the amount of phosvitin and statherin used to pre-coat HA up to a maximum level that was two- to four-fold greater than that observed on untreated HA [28].
  • The A-431 membrane preparation also was capable of phosphorylating exogenous proteins, such as histone, phosvitin, and ribonuclease, by a process which was stimulated by EGF [29].

Analytical, diagnostic and therapeutic context of CSNK2B


  1. Purification and properties of a virion protein kinase. Silberstein, H., August, J.T. J. Biol. Chem. (1976) [Pubmed]
  2. Separation of a murine leukaemia virus protein kinase activity from its Pr65gag polyprotein substrate after DNA--cellulose chromatography. Yoshinaka, Y., Shames, R., Luftig, R.B. J. Gen. Virol. (1983) [Pubmed]
  3. Shedding of tyrosine and serine/threonine ecto-protein kinases from human leukemic cells. Paas, Y., Fishelson, Z. Arch. Biochem. Biophys. (1995) [Pubmed]
  4. Isolation and partial characterization of a protein kinase NII from wheat germ chromatin. Angiolillo, A., Panara, F., Piccinini, G., Gianfranceschi, G.L. Mol. Biol. Rep. (1991) [Pubmed]
  5. Establishment of human glioblastoma multiforme cell line, G5A. Nakamura, T., Seki, S., Matsubara, O., Kasuga, T. Bull. Tokyo Med. Dent. Univ. (1984) [Pubmed]
  6. Fibrous apatite grown on modified collagen. Banks, E., Nakajima, S., Shapiro, L.C., Tilevitz, O., Alonzo, J.R., Chianelli, R.R. Science (1977) [Pubmed]
  7. Casein kinase II specifically nucleotidylylates in vitro the amino acid sequence of the protein encoded by the alpha 22 gene of herpes simplex virus 1. Mitchell, C., Blaho, J.A., Roizman, B. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  8. New protein kinase from plasma membrane of Ehrlich ascites tumor cells activated by natural polypeptides. Racker, E., Abdel-Ghany, M., Sherrill, K., Riegler, C., Blair, E.A. Proc. Natl. Acad. Sci. U.S.A. (1984) [Pubmed]
  9. Substrate-effected release of surface-located protein kinase from intact cells. Kübler, D., Pyerin, W., Burow, E., Kinzel, V. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
  10. Chromatin-associated protein kinases in human normal and benign hyperplastic prostate. Rayan, A., Goueli, S.A., Lange, P., Ahmed, K. Cancer Res. (1985) [Pubmed]
  11. Localization of eight additional genes in the human major histocompatibility complex, including the gene encoding the casein kinase II beta subunit (CSNK2B). Albertella, M.R., Jones, H., Thomson, W., Olavesen, M.G., Campbell, R.D. Genomics (1996) [Pubmed]
  12. Assignment of the casein kinase II gene family to cattle chromosomes. Gao, Q., Li, L., Womack, J.E. Anim. Genet. (1997) [Pubmed]
  13. Recombinant human casein kinase II. A study with the complete set of subunits (alpha, alpha' and beta), site-directed autophosphorylation mutants and a bicistronically expressed holoenzyme. Bodenbach, L., Fauss, J., Robitzki, A., Krehan, A., Lorenz, P., Lozeman, F.J., Pyerin, W. Eur. J. Biochem. (1994) [Pubmed]
  14. Analysis of a novel DNA-binding protein kinase CKII-like enzyme of Chironomus cells. Stigare, J., Buddelmeijer, N., Pigon, A., Egyházi, E. Cell. Mol. Biol. Res. (1994) [Pubmed]
  15. Structural studies of phosvitin in solution and in the solid state. Renugopalakrishnan, V., Horowitz, P.M., Glimcher, M.J. J. Biol. Chem. (1985) [Pubmed]
  16. Isolation of a calcium-binding phosphoprotein from the oocytes and hemolymph of the blood-sucking insect Rhodnius prolixus. Silva-Neto, M.A., Atella, G.C., Fialho, E., Paes, M.C., Zingali, R.B., Petretski, J.H., Alves, E.W., Masuda, H. J. Biol. Chem. (1996) [Pubmed]
  17. Concurrent inductions of avian hepatic lipogenesis, plasma lipids, and plasma apolipoprotein B by estrogen. Dashti, N., Kelley, J.L., Thayer, R.H., Ontko, J.A. J. Lipid Res. (1983) [Pubmed]
  18. Selective repression of RNA polymerase II by microinjected phosvitin. Egyházi, E., Pigon, A. Chromosoma (1986) [Pubmed]
  19. Tissue sources of protein kinase activities in human seminal fluid: studies of normal, oligozoospermic, and vasectomized men. Wilson, M.J., Kaye, K.W. Fertil. Steril. (1983) [Pubmed]
  20. Evidence for CKI and CKII at the cell surface. Walter, J., Kinzel, V., Kübler, D. Cell. Mol. Biol. Res. (1994) [Pubmed]
  21. Affinity properties of phosvitin: interaction of phosvitin with serine hydroxymethyl transferase. Lakhey, H.V., Rao, A.G., Prakash, V., Krishnaswamy, P.R., Savithri, H.S., Rao, N.A., Ramadoss, C.S. Indian J. Biochem. Biophys. (1999) [Pubmed]
  22. Inhibitory effect of 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole on a protein kinase. Zandomeni, R., Weinmann, R. J. Biol. Chem. (1984) [Pubmed]
  23. Studies on an endogenous substrate of wheat germ protein kinase. Yan, T.F., Tao, M. J. Biol. Chem. (1982) [Pubmed]
  24. Egg yolk phosvitin inhibits hydroxyl radical formation from the fenton reaction. Ishikawa, S., Yano, Y., Arihara, K., Itoh, M. Biosci. Biotechnol. Biochem. (2004) [Pubmed]
  25. Phosphorylase kinase phosphorylation of skeletal-muscle troponin T. Risnik, V.V., Dobrovolskii, A.B., Gusev, N.B., Severin, S.E. Biochem. J. (1980) [Pubmed]
  26. Raman spectroscopic characterization of secondary structure in natively unfolded proteins: alpha-synuclein. Maiti, N.C., Apetri, M.M., Zagorski, M.G., Carey, P.R., Anderson, V.E. J. Am. Chem. Soc. (2004) [Pubmed]
  27. Yolk proteins and their plasmatic precursor in the tetraploid Odontophrynus americanus (Amphibia, Anura). Winter, C.E., Floeter-Winter, L.M., Affonso, M.H., Ioshimoto, L.M., Beçak, W. Comp. Biochem. Physiol., B (1985) [Pubmed]
  28. Multi-component adsorption model for pellicle formation: the influence of salivary proteins and non-salivary phospho proteins on the binding of histatin 5 onto hydroxyapatite. Yin, A., Margolis, H.C., Yao, Y., Grogan, J., Oppenheim, F.G. Arch. Oral Biol. (2006) [Pubmed]
  29. Rapid enhancement of protein phosphorylation in A-431 cell membrane preparations by epidermal growth factor. Carpenter, G., King, L., Cohen, S. J. Biol. Chem. (1979) [Pubmed]
  30. Human phosvitin/casein kinase type II. Molecular cloning and sequencing of full-length cDNA encoding subunit beta. Jakobi, R., Voss, H., Pyerin, W. Eur. J. Biochem. (1989) [Pubmed]
  31. System for quantitation of gene expression in single cells by computerized microimaging: application to c-fos expression after microinjection of anti-casein kinase II antibody. Pepperkok, R., Herr, S., Lorenz, P., Pyerin, W., Ansorge, W. Exp. Cell Res. (1993) [Pubmed]
  32. Determination of the dissociation constant of phosvitin-anti-phosphoserine interaction by affinity capillary electrophoresis. Lin, S., Hsiao, I.Y., Hsu, S.M. Anal. Biochem. (1997) [Pubmed]
  33. Preventive effect of egg yolk phosvitin on heat-insolubilization of egg white protein and its application to heat-induced egg white gel. Matsudomi, N., Ito, K., Yoshika, Y. Biosci. Biotechnol. Biochem. (2006) [Pubmed]
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