CSNK2B

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
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Ensembl

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UniProt

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Casein kinase II regulatory subunit
File:PDB 1rqf EBI.jpg
structure of ck2 beta subunit crystallized in the presence of a p21waf1 peptide
Identifiers
SymbolCK_II_beta
PfamPF01214
InterProIPR000704
PROSITEPDOC00845
SCOP1qf8
SUPERFAMILY1qf8

Casein kinase II subunit beta is a protein that in humans is encoded by the CSNK2B gene.[1][2]

This gene encodes the beta subunit of casein kinase II, a ubiquitous protein kinase which regulates metabolic pathways, signal transduction, transcription, translation, and replication. The enzyme localizes to the endoplasmic reticulum and the Golgi apparatus.[3]

Casein kinase, a ubiquitous, well-conserved protein kinase involved in cell metabolism and differentiation, is characterised by its preference for Serine or Threonine in acidic stretches of amino acids. The enzyme is a tetramer of 2 alpha- and 2 beta-subunits.[4][5] However, some species (e.g., mammals) possess 2 related forms of the alpha-subunit (alpha and alpha'), while others (e.g., fungi) possess 2 related beta-subunits (beta and beta').[6] The alpha-subunit is the catalytic unit and contains regions characteristic of serine/threonine protein kinases. The beta-subunit is believed to be regulatory, possessing an N-terminal auto-phosphorylation site, an internal acidic domain, and a potential metal-binding motif.[6] The beta subunit is a highly conserved protein of about 25kDa that contains, in its central section, a cysteine-rich motif, CX(n)C, that could be involved in binding a metal such as zinc.[7] The mammalian beta-subunit gene promoter shares common features with those of other mammalian protein kinases and is closely related to the promoter of the regulatory subunit of cAMP-dependent protein kinase.[6]

Interactions

CSNK2B has been shown to interact with CD163,[8] CSNK2A2,[9][10][11][12] Casein kinase 2, alpha 1,[10][11][12][13][14] FGF1,[15] TRIB3,[16] CDC34,[17] Ribosomal protein L5,[9][13][18][19] BTF3,[20] BRCA1,[21] RNF7,[13] P70-S6 Kinase 1[22] and APC.[23]

References

  1. ↑ Yang-Feng TL, Teitz T, Cheung MC, Kan YW, Canaani D (March 1991). "Assignment of the human casein kinase II beta-subunit gene to 6p12----p21". Genomics. 8 (4): 741–2. doi:10.1016/0888-7543(90)90266-W. PMID 2276748.
  2. ↑ Mucher G, Becker J, Knapp M, Buttner R, Moser M, Rudnik-Schoneborn S, Somlo S, Germino G, Onuchic L, Avner E, Guay-Woodford L, Zerres K (April 1998). "Fine mapping of the autosomal recessive polycystic kidney disease locus (PKHD1) and the genes MUT, RDS, CSNK2 beta, and GSTA1 at 6p21.1-p12". Genomics. 48 (1): 40–5. doi:10.1006/geno.1997.5145. PMID 9503014.
  3. ↑ "Entrez Gene: CSNK2B casein kinase 2, beta polypeptide".
  4. ↑ Jakobi R, Voss H, Pyerin W (July 1989). "Human phosvitin/casein kinase type II. Molecular cloning and sequencing of full-length cDNA encoding subunit beta". Eur. J. Biochem. 183 (1): 227–33. doi:10.1111/j.1432-1033.1989.tb14917.x. PMID 2666134.
  5. ↑ Voss H, Wirkner U, Jakobi R, Hewitt NA, Schwager C, Zimmermann J, Ansorge W, Pyerin W (July 1991). "Structure of the gene encoding human casein kinase II subunit beta". J. Biol. Chem. 266 (21): 13706–11. PMID 1856204.
  6. ↑ 6.0 6.1 6.2 Bidwai AP, Reed JC, Glover CV (May 1995). "Cloning and disruption of CKB1, the gene encoding the 38-kDa beta subunit of Saccharomyces cerevisiae casein kinase II (CKII). Deletion of CKII regulatory subunits elicits a salt-sensitive phenotype". J. Biol. Chem. 270 (18): 10395–404. doi:10.1074/jbc.270.18.10395. PMID 7737972.
  7. ↑ Reed JC, Bidwai AP, Glover CV (July 1994). "Cloning and disruption of CKB2, the gene encoding the 32-kDa regulatory beta'-subunit of Saccharomyces cerevisiae casein kinase II". J. Biol. Chem. 269 (27): 18192–200. PMID 8027080.
  8. ↑ Ritter, M; Buechler C; Kapinsky M; Schmitz G (April 2001). "Interaction of CD163 with the regulatory subunit of casein kinase II (CKII) and dependence of CD163 signaling on CKII and protein kinase C". Eur. J. Immunol. Germany. 31 (4): 999–1009. doi:10.1002/1521-4141(200104)31:4<999::AID-IMMU999>3.0.CO;2-R. ISSN 0014-2980. PMID 11298324.
  9. ↑ 9.0 9.1 Lehner, Ben; Semple Jennifer I; Brown Stephanie E; Counsell Damian; Campbell R Duncan; Sanderson Christopher M (January 2004). "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region". Genomics. United States. 83 (1): 153–67. doi:10.1016/S0888-7543(03)00235-0. ISSN 0888-7543. PMID 14667819.
  10. ↑ 10.0 10.1 Kim, M S; Lee Y T; Kim J M; Cha J Y; Bae Y S (February 1998). "Characterization of protein interaction among subunits of protein kinase CKII in vivo and in vitro". Mol. Cells. KOREA. 8 (1): 43–8. ISSN 1016-8478. PMID 9571630.
  11. ↑ 11.0 11.1 Marin, O; Meggio F; Sarno S; Pinna L A (June 1997). "Physical dissection of the structural elements responsible for regulatory properties and intersubunit interactions of protein kinase CK2 beta-subunit". Biochemistry. UNITED STATES. 36 (23): 7192–8. doi:10.1021/bi962885q. ISSN 0006-2960. PMID 9188720.
  12. ↑ 12.0 12.1 Bosc, D G; Graham K C; Saulnier R B; Zhang C; Prober D; Gietz R D; Litchfield D W (May 2000). "Identification and characterization of CKIP-1, a novel pleckstrin homology domain-containing protein that interacts with protein kinase CK2". J. Biol. Chem. UNITED STATES. 275 (19): 14295–306. doi:10.1074/jbc.275.19.14295. ISSN 0021-9258. PMID 10799509.
  13. ↑ 13.0 13.1 13.2 Ahn, B H; Kim T H; Bae Y S (October 2001). "Mapping of the interaction domain of the protein kinase CKII beta subunit with target proteins". Mol. Cells. Korea (South). 12 (2): 158–63. ISSN 1016-8478. PMID 11710515.
  14. ↑ Kusk, M; Ahmed R; Thomsen B; Bendixen C; Issinger O G; Boldyreff B (January 1999). "Interactions of protein kinase CK2beta subunit within the holoenzyme and with other proteins". Mol. Cell. Biochem. NETHERLANDS. 191 (1–2): 51–8. doi:10.1023/A:1006840613986. ISSN 0300-8177. PMID 10094392.
  15. ↑ Skjerpen, Camilla Skiple; Nilsen Trine; Wesche Jørgen; Olsnes Sjur (August 2002). "Binding of FGF-1 variants to protein kinase CK2 correlates with mitogenicity". EMBO J. England. 21 (15): 4058–69. doi:10.1093/emboj/cdf402. ISSN 0261-4189. PMC 126148. PMID 12145206.
  16. ↑ Zhou, Ying; Li Lu; Liu Qiongming; Xing Guichun; Kuai Xuezhang; Sun Jing; Yin Xiushan; Wang Jian; Zhang Lingqiang; He Fuchu (May 2008). "E3 ubiquitin ligase SIAH1 mediates ubiquitination and degradation of TRB3". Cell. Signal. England. 20 (5): 942–8. doi:10.1016/j.cellsig.2008.01.010. ISSN 0898-6568. PMID 18276110.
  17. ↑ Block, K; Boyer T G; Yew P R (November 2001). "Phosphorylation of the human ubiquitin-conjugating enzyme, CDC34, by casein kinase 2". J. Biol. Chem. United States. 276 (44): 41049–58. doi:10.1074/jbc.M106453200. ISSN 0021-9258. PMID 11546811.
  18. ↑ Boldyreff, B; Issinger O G (February 1997). "A-Raf kinase is a new interacting partner of protein kinase CK2 beta subunit". FEBS Lett. NETHERLANDS. 403 (2): 197–9. doi:10.1016/S0014-5793(97)00010-0. ISSN 0014-5793. PMID 9042965.
  19. ↑ Kim, J M; Cha J Y; Marshak D R; Bae Y S (September 1996). "Interaction of the beta subunit of casein kinase II with the ribosomal protein L5". Biochem. Biophys. Res. Commun. UNITED STATES. 226 (1): 180–6. doi:10.1006/bbrc.1996.1330. ISSN 0006-291X. PMID 8806611.
  20. ↑ Grein, S; Pyerin W (January 1999). "BTF3 is a potential new substrate of protein kinase CK2". Mol. Cell. Biochem. NETHERLANDS. 191 (1–2): 121–8. doi:10.1023/A:1006806226764. ISSN 0300-8177. PMID 10094400.
  21. ↑ O'Brien, K A; Lemke S J; Cocke K S; Rao R N; Beckmann R P (July 1999). "Casein kinase 2 binds to and phosphorylates BRCA1". Biochem. Biophys. Res. Commun. UNITED STATES. 260 (3): 658–64. doi:10.1006/bbrc.1999.0892. ISSN 0006-291X. PMID 10403822.
  22. ↑ Panasyuk, Ganna; Nemazanyy Ivan; Zhyvoloup Alexander; Bretner Maria; Litchfield David W; Filonenko Valeriy; Gout Ivan T (October 2006). "Nuclear export of S6K1 II is regulated by protein kinase CK2 phosphorylation at Ser-17". J. Biol. Chem. United States. 281 (42): 31188–201. doi:10.1074/jbc.M602618200. ISSN 0021-9258. PMID 16895915.
  23. ↑ Homma, Miwako Kato; Li Dongxia; Krebs Edwin G; Yuasa Yasuhito; Homma Yoshimi (April 2002). "Association and regulation of casein kinase 2 activity by adenomatous polyposis coli protein". Proc. Natl. Acad. Sci. U.S.A. United States. 99 (9): 5959–64. doi:10.1073/pnas.092143199. ISSN 0027-8424. PMC 122884. PMID 11972058.

External links

Further reading


This article incorporates text from the public domain Pfam and InterPro: IPR000704
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