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Gene Review

CSNK2A1  -  casein kinase 2, alpha 1 polypeptide

Homo sapiens

Synonyms: CK II alpha, CK2A1, CKII, CSNK2A3, Casein kinase II subunit alpha
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Disease relevance of CSNK2A1


High impact information on CSNK2A1

  • Both Myc-Max and Mad-Max heterocomplexes are favored over Max homodimers, and, unlike Max homodimers, the DNA binding activity of the heterodimers is unaffected by CKII phosphorylation [6].
  • Microinjection of CKII suppresses induction of AP-1 by either phorbol ester or an inhibitory peptide [7].
  • The potential role of CKII as either a regulatory or constitutive modifier of SRF in vivo will be discussed [8].
  • It appears that the ability of insulin to activate CKII in skeletal muscle is not impaired in insulin-resistant Pima Indians, and that the biochemical lesion responsible for insulin resistance occurs either downstream from CKII or in a different pathway of insulin action [9].
  • The role of both CKII and PP2A in controlling multiple sorting steps in the TGN/endosomal system indicates that the distribution of itinerant membrane proteins may be acutely regulated via signal transduction pathways [10].

Chemical compound and disease context of CSNK2A1

  • Though structurally unrelated to chrysin, an HIV-1 inhibitory benzothiophene also bound selectively to CKII [11].
  • Cotransfection experiment also demonstrated that packaging of HDV genomic RNA was not affected by the kinase inhibitor DRB or H7 and mutation at the putative CKII phosphorylation sites (serine-2, serine-123, or both), and the putative PKC site (serine-210) of HDAg did not elicit any significant effect on the HDV virion assembly [12].

Biological context of CSNK2A1


Anatomical context of CSNK2A1


Associations of CSNK2A1 with chemical compounds


Physical interactions of CSNK2A1


Enzymatic interactions of CSNK2A1

  • Here we report that casein kinase II (CKII) phosphorylates synphilin-1 and that the beta subunit of this enzyme complex binds to synphilin-1 [18].
  • Two-dimensional phosphopeptide mapping of the sites phosphorylated by PKA, PKC, and CKII in vitro demonstrates that these enzymes are capable of phosphorylating IRF2 at multiple distinct sites [28].
  • These results suggest that two serine residues of the acidic central region of the N-myc protein are phosphorylated by CKII in vivo as well as in vitro [29].
  • Serine 32 and serine 36 of IkappaBalpha are directly phosphorylated by protein kinase CKII in vitro [30].
  • Sequence analysis revealed that purified CKII and the kinase activity within cell extracts phosphorylated I kappa B alpha at its C terminus at S-283, S-288, S-293, and T-291 [3].

Regulatory relationships of CSNK2A1


Other interactions of CSNK2A1

  • Additionally, both CKII alpha and beta subunits are present within cytoplasmic inclusions in cells that overexpress synphilin-1 [18].
  • Strikingly, ERK1 failed to phosphorylate Spi-1, in vitro, whereas JNK1, like CK II, phosphorylated Spi-B and Spi-1 [32].
  • It was also similar to a recombinant alpha 2 beta 2 holoenzyme whose expression had been attained in E. coli with a bicistronic construct containing the coding regions of CKII beta and CKII alpha in a tandem arrangement [1].
  • We demonstrate that CKII associates with and phosphorylates the C-terminal region of CD5, a conserved domain known to be relevant for the generation of second lipid messengers, and thereby enables at least one component of its signaling function [33].
  • Strong phosphorylation by CKII was detected with the fused protein of wild-type N-myc [29].

Analytical, diagnostic and therapeutic context of CSNK2A1

  • Both Ser2 and Ser3 were identified as the autophosphorylation sites; replacement of one of these with Ala by oligonucleotide-mediated site-directed mutagenesis influenced only the extent of CKII beta autophosphorylation, replacement of both resulted in a loss of autophosphorylation [1].
  • Immunoprecipitation studies demonstrated that CKII and I kappa B alpha physically associate in vivo [3].
  • Western blot analysis demonstrates that casein kinase II (CKII), a ubiquitous serine/threonine kinase enriched in brain, is present in these immunoprecipitates [19].
  • To examine the subunit structure of EF-1 and phosphorylation by protein kinase CKII, recombinant beta, gamma, and delta subunits from rabbit were expressed in E. coli and the subunits were reconstituted into partial and complete complexes and analyzed by gel filtration [34].
  • We now show that during normal growth of primary cell cultures and HeLa cells CKII activity is increased concomitant with cellular growth and that the activity declines when confluency is reached [35].


  1. 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]
  2. Casein kinase II phosphorylation increases the rate of serum response factor-binding site exchange. Marais, R.M., Hsuan, J.J., McGuigan, C., Wynne, J., Treisman, R. EMBO J. (1992) [Pubmed]
  3. Casein kinase II phosphorylates I kappa B alpha at S-283, S-289, S-293, and T-291 and is required for its degradation. McElhinny, J.A., Trushin, S.A., Bren, G.D., Chester, N., Paya, C.V. Mol. Cell. Biol. (1996) [Pubmed]
  4. Casein kinase II alpha subunit and C1-inhibitor are independent predictors of outcome in patients with squamous cell carcinoma of the lung. O-charoenrat, P., Rusch, V., Talbot, S.G., Sarkaria, I., Viale, A., Socci, N., Ngai, I., Rao, P., Singh, B. Clin. Cancer Res. (2004) [Pubmed]
  5. The MYCN protein of human neuroblastoma cells is phosphorylated by casein kinase II in the central region and at serine 367. Hamann, U., Wenzel, A., Frank, R., Schwab, M. Oncogene (1991) [Pubmed]
  6. Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity. Ayer, D.E., Kretzner, L., Eisenman, R.N. Cell (1993) [Pubmed]
  7. Casein kinase II is a negative regulator of c-Jun DNA binding and AP-1 activity. Lin, A., Frost, J., Deng, T., Smeal, T., al-Alawi, N., Kikkawa, U., Hunter, T., Brenner, D., Karin, M. Cell (1992) [Pubmed]
  8. Casein kinase II enhances the DNA binding activity of serum response factor. Manak, J.R., de Bisschop, N., Kris, R.M., Prywes, R. Genes Dev. (1990) [Pubmed]
  9. Activation of skeletal muscle casein kinase II by insulin is not diminished in subjects with insulin resistance. Maeda, R., Raz, I., Zurlo, F., Sommercorn, J. J. Clin. Invest. (1991) [Pubmed]
  10. Regulation of endosome sorting by a specific PP2A isoform. Molloy, S.S., Thomas, L., Kamibayashi, C., Mumby, M.C., Thomas, G. J. Cell Biol. (1998) [Pubmed]
  11. Casein kinase II is a selective target of HIV-1 transcriptional inhibitors. Critchfield, J.W., Coligan, J.E., Folks, T.M., Butera, S.T. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  12. Assembly of hepatitis delta virus particles: package of multimeric hepatitis delta virus genomic RNA and role of phosphorylation. Yeh, T.S., Lee, Y.H. Virology (1998) [Pubmed]
  13. Genomic organization and promoter identification of the human protein kinase CK2 catalytic subunit alpha (CSNK2A1). Wirkner, U., Voss, H., Ansorge, W., Pyerin, W. Genomics (1998) [Pubmed]
  14. Phosphorylation of vitronectin by casein kinase II. Identification of the sites and their promotion of cell adhesion and spreading. Seger, D., Gechtman, Z., Shaltiel, S. J. Biol. Chem. (1998) [Pubmed]
  15. Phosphorylation of threonine 10 on CKBBP1/SAG/ROC2/Rbx2 by protein kinase CKII promotes the degradation of IkappaBalpha and p27Kip1. Kim, Y.S., Lee, J.Y., Son, M.Y., Park, W., Bae, Y.S. J. Biol. Chem. (2003) [Pubmed]
  16. Phosphorylation of the DNA repair protein APE/REF-1 by CKII affects redox regulation of AP-1. Fritz, G., Kaina, B. Oncogene (1999) [Pubmed]
  17. The human gene (CSNK2A1) coding for the casein kinase II subunit alpha is located on chromosome 20 and contains tandemly arranged Alu repeats. Wirkner, U., Voss, H., Lichter, P., Ansorge, W., Pyerin, W. Genomics (1994) [Pubmed]
  18. Casein kinase II-mediated phosphorylation regulates alpha-synuclein/synphilin-1 interaction and inclusion body formation. Lee, G., Tanaka, M., Park, K., Lee, S.S., Kim, Y.M., Junn, E., Lee, S.H., Mouradian, M.M. J. Biol. Chem. (2004) [Pubmed]
  19. Casein kinase II phosphorylates the neural cell adhesion molecule L1. Wong, E.V., Schaefer, A.W., Landreth, G., Lemmon, V. J. Neurochem. (1996) [Pubmed]
  20. Human-immunodeficiency-virus-type-1-encoded Vpu protein is phosphorylated by casein kinase II. Schubert, U., Schneider, T., Henklein, P., Hoffmann, K., Berthold, E., Hauser, H., Pauli, G., Porstmann, T. Eur. J. Biochem. (1992) [Pubmed]
  21. The DNA-binding and transcriptional activities of MAZ, a myc-associated zinc finger protein, are regulated by casein kinase II. Tsutsui, H., Geltinger, C., Murata, T., Itakura, K., Wada, T., Handa, H., Yokoyama, K.K. Biochem. Biophys. Res. Commun. (1999) [Pubmed]
  22. Identification and partial characterization of factor Va heavy chain kinase from human platelets. Kalafatis, M. J. Biol. Chem. (1998) [Pubmed]
  23. Casein kinase II interacts with the bZIP domains of several transcription factors. Yamaguchi, Y., Wada, T., Suzuki, F., Takagi, T., Hasegawa, J., Handa, H. Nucleic Acids Res. (1998) [Pubmed]
  24. Molecular dissection of nucleolin's role in growth and cell proliferation: new insights. Srivastava, M., Pollard, H.B. FASEB J. (1999) [Pubmed]
  25. The highly basic ribosomal protein L41 interacts with the beta subunit of protein kinase CKII and stimulates phosphorylation of DNA topoisomerase IIalpha by CKII. Lee, J.H., Kim, J.M., Kim, M.S., Lee, Y.T., Marshak, D.R., Bae, Y.S. Biochem. Biophys. Res. Commun. (1997) [Pubmed]
  26. Interaction between casein kinase II and the 90-kDa stress protein, HSP90. Miyata, Y., Yahara, I. Biochemistry (1995) [Pubmed]
  27. Copurification of casein kinase II with transcription factor ATF/E4TF3. Wada, T., Takagi, T., Yamaguchi, Y., Kawase, H., Hiramoto, M., Ferdous, A., Takayama, M., Lee, K.A., Hurst, H.C., Handa, H. Nucleic Acids Res. (1996) [Pubmed]
  28. Phosphorylation of the oncogenic transcription factor interferon regulatory factor 2 (IRF2) in vitro and in vivo. Birnbaum, M.J., van Zundert, B., Vaughan, P.S., Whitmarsh, A.J., van Wijnen, A.J., Davis, R.J., Stein, G.S., Stein, J.L. J. Cell. Biochem. (1997) [Pubmed]
  29. Specific phosphorylation of the acidic central region of the N-myc protein by casein kinase II. Hagiwara, T., Nakaya, K., Nakamura, Y., Nakajima, H., Nishimura, S., Taya, Y. Eur. J. Biochem. (1992) [Pubmed]
  30. Serine 32 and serine 36 of IkappaBalpha are directly phosphorylated by protein kinase CKII in vitro. Taylor, J.A., Bren, G.D., Pennington, K.N., Trushin, S.A., Asin, S., Paya, C.V. J. Mol. Biol. (1999) [Pubmed]
  31. Purification and characterization of echinoderm casein kinase II. Regulation by protein kinase C. Sanghera, J.S., Charlton, L.A., Paddon, H.B., Pelech, S.L. Biochem. J. (1992) [Pubmed]
  32. Differential phosphorylations of Spi-B and Spi-1 transcription factors. Mao, C., Ray-Gallet, D., Tavitian, A., Moreau-Gachelin, F. Oncogene (1996) [Pubmed]
  33. Human CD5 signaling and constitutive phosphorylation of C-terminal serine residues by casein kinase II. Calvo, J., Vildà, J.M., Places, L., Simarro, M., Padilla, O., Andreu, D., Campbell, K.S., Aussel, C., Lozano, F. J. Immunol. (1998) [Pubmed]
  34. A structural model for elongation factor 1 (EF-1) and phosphorylation by protein kinase CKII. Sheu, G.T., Traugh, J.A. Mol. Cell. Biochem. (1999) [Pubmed]
  35. Growth-dependent modulation of casein kinase II and its substrate nucleolin in primary human cell cultures and HeLa cells. Schneider, H.R., Issinger, O.G. Biochim. Biophys. Acta (1989) [Pubmed]
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