Summary: Casein kinase II regulatory subunit
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CSNK2B Edit Wikipedia article
| Casein kinase II regulatory subunit | |||||||||
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structure of ck2 beta subunit crystallized in the presence of a p21waf1 peptide
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| Identifiers | |||||||||
| Symbol | CK_II_beta | ||||||||
| Pfam | PF01214 | ||||||||
| InterPro | IPR000704 | ||||||||
| PROSITE | PDOC00845 | ||||||||
| SCOP | 1qf8 | ||||||||
| SUPERFAMILY | 1qf8 | ||||||||
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Casein kinase II subunit beta is a protein that in humans is encoded by the CSNK2B gene.[5][6]
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.[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]
References
- ^ a b c ENSG00000204435, ENSG00000232960, ENSG00000206406, ENSG00000224774, ENSG00000230700, ENSG00000224398 GRCh38: Ensembl release 89: ENSG00000228875, ENSG00000204435, ENSG00000232960, ENSG00000206406, ENSG00000224774, ENSG00000230700, ENSG00000224398 - Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000024387 - Ensembl, May 2017
- ^ "Human PubMed Reference:".
- ^ "Mouse PubMed Reference:".
- ^ 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. PMID 2276748. doi:10.1016/0888-7543(90)90266-W.
- ^ 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. PMID 9503014. doi:10.1006/geno.1997.5145.
- ^ "Entrez Gene: CSNK2B casein kinase 2, beta polypeptide".
- ^ 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. PMID 2666134. doi:10.1111/j.1432-1033.1989.tb14917.x.
- ^ 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.
- ^ a b c 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. PMID 7737972. doi:10.1074/jbc.270.18.10395.
- ^ 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.
- ^ 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. ISSN 0014-2980. PMID 11298324. doi:10.1002/1521-4141(200104)31:4<999::AID-IMMU999>3.0.CO;2-R.
- ^ a b 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. ISSN 0888-7543. PMID 14667819. doi:10.1016/S0888-7543(03)00235-0.
- ^ a b 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.
- ^ a b 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. ISSN 0006-2960. PMID 9188720. doi:10.1021/bi962885q.
- ^ a b 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. ISSN 0021-9258. PMID 10799509. doi:10.1074/jbc.275.19.14295.
- ^ a b c 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.
- ^ 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. ISSN 0300-8177. PMID 10094392. doi:10.1023/A:1006840613986.
- ^ 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. ISSN 0261-4189. PMC 126148
. PMID 12145206. doi:10.1093/emboj/cdf402. - ^ 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. ISSN 0898-6568. PMID 18276110. doi:10.1016/j.cellsig.2008.01.010.
- ^ 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. ISSN 0021-9258. PMID 11546811. doi:10.1074/jbc.M106453200.
- ^ 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. ISSN 0014-5793. PMID 9042965. doi:10.1016/S0014-5793(97)00010-0.
- ^ 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. ISSN 0006-291X. PMID 8806611. doi:10.1006/bbrc.1996.1330.
- ^ 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. ISSN 0300-8177. PMID 10094400. doi:10.1023/A:1006806226764.
- ^ 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. ISSN 0006-291X. PMID 10403822. doi:10.1006/bbrc.1999.0892.
- ^ 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. ISSN 0021-9258. PMID 16895915. doi:10.1074/jbc.M602618200.
- ^ 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. ISSN 0027-8424. PMC 122884 . PMID 11972058. doi:10.1073/pnas.092143199.
External links
- Human CSNK2B genome location and CSNK2B gene details page in the UCSC Genome Browser.
Further reading
- Schubert U, Schneider T, Henklein P, et al. (1992). "Human-immunodeficiency-virus-type-1-encoded Vpu protein is phosphorylated by casein kinase II". Eur. J. Biochem. 204 (2): 875–83. PMID 1541298. doi:10.1111/j.1432-1033.1992.tb16707.x.
- Teitz T, Eli D, Penner M, et al. (1990). "Expression of the cDNA for the beta subunit of human casein kinase II confers partial UV resistance on xeroderma pigmentosum cells". Mutat. Res. 236 (1): 85–97. PMID 1694965. doi:10.1016/0921-8777(90)90036-5.
- Voss H, Wirkner U, Jakobi R, et al. (1991). "Structure of the gene encoding human casein kinase II subunit beta". J. Biol. Chem. 266 (21): 13706–11. PMID 1856204.
- Litchfield DW, Lozeman FJ, Cicirelli MF, et al. (1991). "Phosphorylation of the beta subunit of casein kinase II in human A431 cells. Identification of the autophosphorylation site and a site phosphorylated by p34cdc2". J. Biol. Chem. 266 (30): 20380–9. PMID 1939094.
- Ackerman P, Glover CV, Osheroff N (1990). "Stimulation of casein kinase II by epidermal growth factor: relationship between the physiological activity of the kinase and the phosphorylation state of its beta subunit". Proc. Natl. Acad. Sci. U.S.A. 87 (2): 821–5. PMC 53358 . PMID 2300566. doi:10.1073/pnas.87.2.821.
- Heller-Harrison RA, Meisner H, Czech MP (1990). "Cloning and characterization of a cDNA encoding the beta subunit of human casein kinase II". Biochemistry. 28 (23): 9053–8. PMID 2513884. doi:10.1021/bi00449a014.
- Jakobi R, Voss H, Pyerin W (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. PMID 2666134. doi:10.1111/j.1432-1033.1989.tb14917.x.
- Vincent MJ, Abdul Jabbar M (1996). "The human immunodeficiency virus type 1 Vpu protein: a potential regulator of proteolysis and protein transport in the mammalian secretory pathway". Virology. 213 (2): 639–49. PMID 7491787. doi:10.1006/viro.1995.0035.
- Litchfield DW, Bosc DG, Slominski E (1995). "The protein kinase from mitotic human cells that phosphorylates Ser-209 on the casein kinase II beta-subunit is p34cdc2". Biochim. Biophys. Acta. 1269 (1): 69–78. PMID 7578274. doi:10.1016/0167-4889(95)00100-7.
- Jin YJ, Burakoff SJ (1993). "The 25-kDa FK506-binding protein is localized in the nucleus and associates with casein kinase II and nucleolin". Proc. Natl. Acad. Sci. U.S.A. 90 (16): 7769–73. PMC 47224 . PMID 7689229. doi:10.1073/pnas.90.16.7769.
- Gietz RD, Graham KC, Litchfield DW (1995). "Interactions between the subunits of casein kinase II". J. Biol. Chem. 270 (22): 13017–21. PMID 7768894. doi:10.1074/jbc.270.22.13017.
- Szebeni A, Herrera JE, Olson MO (1995). "Interaction of nucleolar protein B23 with peptides related to nuclear localization signals". Biochemistry. 34 (25): 8037–42. PMID 7794916. doi:10.1021/bi00025a009.
- Arnold SF, Obourn JD, Jaffe H, Notides AC (1995). "Serine 167 is the major estradiol-induced phosphorylation site on the human estrogen receptor". Mol. Endocrinol. 8 (9): 1208–14. PMID 7838153. doi:10.1210/me.8.9.1208.
- Pyerin W (1994). "Human casein kinase II: structures, genes, expression and requirement in cell growth stimulation". Adv. Enzyme Regul. 34: 225–46. PMID 7942276. doi:10.1016/0065-2571(94)90018-3.
- el Benna J, Faust LP, Babior BM (1994). "The phosphorylation of the respiratory burst oxidase component p47phox during neutrophil activation. Phosphorylation of sites recognized by protein kinase C and by proline-directed kinases". J. Biol. Chem. 269 (38): 23431–6. PMID 8089108.
- Schubert U, Henklein P, Boldyreff B, et al. (1994). "The human immunodeficiency virus type 1 encoded Vpu protein is phosphorylated by casein kinase-2 (CK-2) at positions Ser52 and Ser56 within a predicted alpha-helix-turn-alpha-helix-motif". J. Mol. Biol. 236 (1): 16–25. PMID 8107101. doi:10.1006/jmbi.1994.1114.
- Schubert U, Strebel K (1994). "Differential activities of the human immunodeficiency virus type 1-encoded Vpu protein are regulated by phosphorylation and occur in different cellular compartments". J. Virol. 68 (4): 2260–71. PMC 236702 . PMID 8139011.
- Tanasijevic MJ, Myers MG, Thoma RS, et al. (1993). "Phosphorylation of the insulin receptor substrate IRS-1 by casein kinase II". J. Biol. Chem. 268 (24): 18157–66. PMID 8349691.
- Friborg J, Ladha A, Göttlinger H, et al. (1996). "Functional analysis of the phosphorylation sites on the human immunodeficiency virus type 1 Vpu protein". J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. 8 (1): 10–22. PMID 8548340. doi:10.1097/00042560-199501000-00004.
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This article incorporates text from the public domain Pfam and InterPro IPR000704
This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Casein kinase II regulatory subunit Provide feedback
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External database links
| PROSITE: | PDOC00845 |
| SCOP: | 1qf8 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR000704
Casein kinase, a ubiquitous well-conserved protein kinase involved in cell metabolism and differentiation, is characterised by its preference for Ser or Thr in acidic stretches of amino acids. The enzyme is a tetramer of 2 alpha- and 2 beta-subunits [PUBMED:2666134, PUBMED:1856204]. 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') [PUBMED:7737972].
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 [PUBMED:7737972]. The beta subunit contains, in its central section, a cysteine-rich motif, CX(n)C, that could be involved in binding a metal such as zinc [PUBMED:8027080]. 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 [PUBMED:7737972].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Cellular component | protein kinase CK2 complex (GO:0005956) |
| Molecular function | protein kinase regulator activity (GO:0019887) |
Domain organisation
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Alignments
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Full (1807) |
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| RP15 (473) |
RP35 (983) |
RP55 (1360) |
RP75 (1716) |
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| Seed (191) |
Full (1807) |
Representative proteomes | UniProt (2678) |
NCBI (2935) |
Meta (13) |
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|---|---|---|---|---|---|---|---|---|---|
| RP15 (473) |
RP35 (983) |
RP55 (1360) |
RP75 (1716) |
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| Raw Stockholm | |||||||||
| Gzipped | |||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
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Curation and family details
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Curation
| Seed source: | Prosite |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Finn RD, Bateman A |
| Number in seed: | 191 |
| Number in full: | 1807 |
| Average length of the domain: | 186.10 aa |
| Average identity of full alignment: | 47 % |
| Average coverage of the sequence by the domain: | 66.57 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 183 | ||||||||||||
| Family (HMM) version: | 17 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Interactions
Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the CK_II_beta domain has been found. There are 40 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
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