CSNK2B

Last updated
CSNK2B
Protein CSNK2B PDB 1jwh.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases CSNK2B , CK2B, CK2N, CSK2B, G5A, casein kinase 2 beta, Ckb2, Ckb1, POBINDS
External IDs OMIM: 115441 MGI: 88548 HomoloGene: 55572 GeneCards: CSNK2B
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001320
NM_001282385

NM_009975
NM_001303445
NM_001303446
NM_001303476

RefSeq (protein)

NP_001269314
NP_001311

NP_001290374
NP_001290375
NP_001290405
NP_034105

Location (UCSC) Chr 6: 31.67 – 31.67 Mb Chr 17: 35.34 – 35.34 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse
Casein kinase II regulatory subunit
PDB 1rqf EBI.jpg
structure of ck2 beta subunit crystallized in the presence of a p21waf1 peptide
Identifiers
SymbolCK_II_beta
Pfam PF01214
InterPro IPR000704
PROSITE PDOC00845
SCOP2 1qf8 / SCOPe / SUPFAM
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

Casein kinase II subunit beta is a protein that in humans is encoded by the CSNK2B gene. [5] [6] It is 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. [7]

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. [8] [9] 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'). [10] 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. [10] 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. [11] 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. [10]

Interactions

CSNK2B has been shown to interact with CD163, [12] CSNK2A2, [13] [14] [15] [16] Casein kinase 2, alpha 1, [14] [15] [16] [17] [18] FGF1, [19] TRIB3, [20] CDC34, [21] Ribosomal protein L5, [13] [17] [22] [23] BTF3, [24] BRCA1, [25] RNF7, [17] P70-S6 Kinase 1 [26] and APC. [27]

Related Research Articles

<span class="mw-page-title-main">Phosphorylase kinase</span>

Phosphorylase kinase (PhK) is a serine/threonine-specific protein kinase which activates glycogen phosphorylase to release glucose-1-phosphate from glycogen. PhK phosphorylates glycogen phosphorylase at two serine residues, triggering a conformational shift which favors the more active glycogen phosphorylase “a” form over the less active glycogen phosphorylase b.

<span class="mw-page-title-main">Casein kinase 2, alpha 1</span> Protein and coding gene in humans

Casein kinase II subunit alpha is an enzyme that in humans is encoded by the CSNK2A1 gene.

<span class="mw-page-title-main">CSNK2A2</span> Protein-coding gene in the species Homo sapiens

Casein kinase II subunit alpha' is an enzyme that in humans is encoded by the CSNK2A2 gene.

<span class="mw-page-title-main">ATF1</span> Protein-coding gene in humans

Cyclic AMP-dependent transcription factor ATF-1 is a protein that in humans is encoded by the ATF1 gene.

<span class="mw-page-title-main">60S ribosomal protein L5</span> Protein found in humans

60S ribosomal protein L5 is a protein that in humans is encoded by the RPL5 gene.

<span class="mw-page-title-main">CAMK4</span> Protein-coding gene in the species Homo sapiens

Calcium/calmodulin-dependent protein kinase type IV is an enzyme that in humans is encoded by the CAMK4 gene.

<span class="mw-page-title-main">NFYB</span> Protein-coding gene in the species Homo sapiens

Nuclear transcription factor Y subunit beta is a protein that in humans is encoded by the NFYB gene.

<span class="mw-page-title-main">CAMK2G</span> Protein-coding gene in the species Homo sapiens

Calcium/calmodulin-dependent protein kinase type II gamma chain is an enzyme that in humans is encoded by the CAMK2G gene.

<span class="mw-page-title-main">Protein kinase D1</span> Protein-coding gene in the species Homo sapiens

Serine/threonine-protein kinase D1 is an enzyme that in humans is encoded by the PRKD1 gene.

<span class="mw-page-title-main">PRKAA2</span> Protein-coding gene in the species Homo sapiens

5'-AMP-activated protein kinase catalytic subunit alpha-2 is an enzyme that in humans is encoded by the PRKAA2 gene.

<span class="mw-page-title-main">Protein kinase, AMP-activated, alpha 1</span> Protein-coding gene in the species Homo sapiens

5'-AMP-activated protein kinase catalytic subunit alpha-1 is an enzyme that in humans is encoded by the PRKAA1 gene.

<span class="mw-page-title-main">AKAP5</span> Protein-coding gene in the species Homo sapiens

A-kinase anchor protein 5 is a protein that in humans is encoded by the AKAP5 gene.

<span class="mw-page-title-main">GRK6</span> Protein-coding gene in the species Homo sapiens

This gene encodes a member of the G protein-coupled receptor kinase subfamily of the Ser/Thr protein kinase family, and is most highly similar to GRK4 and GRK5. The protein phosphorylates the activated forms of G protein-coupled receptors to regulate their signaling.

<span class="mw-page-title-main">PRKACB</span> Protein-coding gene in the species Homo sapiens

cAMP-dependent protein kinase catalytic subunit beta is an enzyme that in humans is encoded by the PRKACB gene.

<span class="mw-page-title-main">CDC2L1</span> Protein-coding gene in the species Homo sapiens

PITSLRE serine/threonine-protein kinase CDC2L1 is an enzyme that in humans is encoded by the CDC2L1 gene.

<span class="mw-page-title-main">PHKG1</span> Protein-coding gene in the species Homo sapiens

Phosphorylase b kinase gamma catalytic chain, skeletal muscle isoform is an enzyme that in humans is encoded by the PHKG1 gene.

<span class="mw-page-title-main">Phosducin</span> Protein-coding gene in the species Homo sapiens

Phosducin, also known as PDC, is a human protein and gene. It belongs to the phosducin family of proteins.

<span class="mw-page-title-main">RNF7</span> Protein-coding gene in the species Homo sapiens

RING-box protein 2 is a protein that in humans is encoded by the RNF7 gene.

<span class="mw-page-title-main">PRKAR1B</span> Protein-coding gene in the species Homo sapiens

cAMP-dependent protein kinase type I-beta regulatory subunit is an enzyme that in humans is encoded by the PRKAR1B gene.

<span class="mw-page-title-main">PKIA</span> Protein-coding gene in the species Homo sapiens

cAMP-dependent protein kinase inhibitor alpha is a protein that in humans is encoded by the PKIA gene.

References

  1. 1 2 3 ENSG00000204435, ENSG00000232960, ENSG00000206406, ENSG00000224774, ENSG00000230700, ENSG00000224398 GRCh38: Ensembl release 89: ENSG00000228875, ENSG00000204435, ENSG00000232960, ENSG00000206406, ENSG00000224774, ENSG00000230700, ENSG00000224398 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000024387 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. 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.
  6. 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.
  7. "Entrez Gene: CSNK2B casein kinase 2, beta polypeptide".
  8. 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.
  9. 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. doi: 10.1016/S0021-9258(18)92756-0 . PMID   1856204.
  10. 1 2 3 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.
  11. 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. doi: 10.1016/S0021-9258(17)32434-1 . PMID   8027080.
  12. 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.
  13. 1 2 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.
  14. 1 2 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.
  15. 1 2 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.
  16. 1 2 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.
  17. 1 2 3 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.
  18. 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. S2CID   257329.
  19. 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.
  20. 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.
  21. 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.
  22. 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. S2CID   84557809.
  23. 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.
  24. 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. S2CID   1057554.
  25. 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.
  26. 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.
  27. 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. Bibcode:2002PNAS...99.5959K. doi: 10.1073/pnas.092143199 . ISSN   0027-8424. PMC   122884 . PMID   11972058.

Further reading

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