CSNK2B

{{Infobox protein family

| Symbol = CK_II_beta

| Name = Casein kinase II regulatory subunit

| image = PDB 1rqf EBI.jpg

| width =

| caption = structure of ck2 beta subunit crystallized in the presence of a p21waf1 peptide

| Pfam = PF01214

| Pfam_clan =

| InterPro = IPR000704

| SMART =

| PROSITE = PDOC00845

| MEROPS =

| SCOP = 1qf8

| TCDB =

| OPM family =

| OPM protein =

| CAZy =

| CDD =

}}

Casein kinase II subunit beta is a protein that in humans is encoded by the CSNK2B gene.{{cite journal | vauthors = Yang-Feng TL, Teitz T, Cheung MC, Kan YW, Canaani D | title = Assignment of the human casein kinase II beta-subunit gene to 6p12----p21 | journal = Genomics | volume = 8 | issue = 4 | pages = 741–2 | date=March 1991| pmid = 2276748 | doi =10.1016/0888-7543(90)90266-W | doi-access = free }}{{cite journal | vauthors = 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 | title = Fine mapping of the autosomal recessive polycystic kidney disease locus (PKHD1) and the genes MUT, RDS, CSNK2 beta, and GSTA1 at 6p21.1-p12 | journal = Genomics | volume = 48 | issue = 1 | pages = 40–5 | date=April 1998| pmid = 9503014 | doi = 10.1006/geno.1997.5145 | doi-access = free }} 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.{{cite web | title = Entrez Gene: CSNK2B casein kinase 2, beta polypeptide| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1460}}

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.{{cite journal | vauthors = Jakobi R, Voss H, Pyerin W | title = Human phosvitin/casein kinase type II. Molecular cloning and sequencing of full-length cDNA encoding subunit beta | journal = Eur. J. Biochem. | volume = 183 | issue = 1 | pages = 227–33 |date=July 1989 | pmid = 2666134 | doi = 10.1111/j.1432-1033.1989.tb14917.x| doi-access = free }}{{cite journal | vauthors = Voss H, Wirkner U, Jakobi R, Hewitt NA, Schwager C, Zimmermann J, Ansorge W, Pyerin W | title = Structure of the gene encoding human casein kinase II subunit beta | journal = J. Biol. Chem. | volume = 266 | issue = 21 | pages = 13706–11 |date=July 1991 | doi = 10.1016/S0021-9258(18)92756-0 | pmid = 1856204 | doi-access = free }} 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').{{cite journal | vauthors = Bidwai AP, Reed JC, Glover CV | title = 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 | journal = J. Biol. Chem. | volume = 270 | issue = 18 | pages = 10395–404 |date=May 1995 | pmid = 7737972 | doi = 10.1074/jbc.270.18.10395| doi-access =free }} 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. 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.{{cite journal | vauthors = Reed JC, Bidwai AP, Glover CV | title = Cloning and disruption of CKB2, the gene encoding the 32-kDa regulatory beta'-subunit of Saccharomyces cerevisiae casein kinase II | journal = J. Biol. Chem. | volume = 269 | issue = 27 | pages = 18192–200 |date=July 1994 | doi = 10.1016/S0021-9258(17)32434-1 | pmid = 8027080 | doi-access = free }} 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.

Interactions

CSNK2B has been shown to interact with CD163,{{cite journal |last=Ritter |first=M |author2=Buechler C |author3=Kapinsky M |author4=Schmitz G |date=April 2001|title=Interaction of CD163 with the regulatory subunit of casein kinase II (CKII) and dependence of CD163 signaling on CKII and protein kinase C |journal=Eur. J. Immunol. |volume=31 |issue=4 |pages=999–1009 |location = Germany| issn = 0014-2980| pmid = 11298324 |doi=10.1002/1521-4141(200104)31:4<999::AID-IMMU999>3.0.CO;2-R |doi-access=free }} CSNK2A2,{{cite journal |last=Lehner |first=Ben |author2=Semple Jennifer I |author3=Brown Stephanie E |author4=Counsell Damian |author5=Campbell R Duncan |author6=Sanderson Christopher M |date=January 2004|title=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 |journal=Genomics |volume=83 |issue=1 |pages=153–67 |location = United States| issn = 0888-7543| pmid = 14667819 |doi=10.1016/S0888-7543(03)00235-0 }}{{cite journal |last=Kim |first=M S |author2=Lee Y T |author3=Kim J M |author4=Cha J Y |author5=Bae Y S |date=February 1998|title=Characterization of protein interaction among subunits of protein kinase CKII in vivo and in vitro |journal=Mol. Cells |volume=8 |issue=1 |pages=43–8 |location = KOREA|doi=10.1016/S1016-8478(23)13390-5 | issn = 1016-8478| pmid = 9571630 |doi-access=free }}{{cite journal |last=Marin |first=O |author2=Meggio F |author3=Sarno S |author4=Pinna L A |date=June 1997|title=Physical dissection of the structural elements responsible for regulatory properties and intersubunit interactions of protein kinase CK2 beta-subunit |journal=Biochemistry |volume=36 |issue=23 |pages=7192–8 |location = UNITED STATES| issn = 0006-2960| pmid = 9188720 |doi = 10.1021/bi962885q }}{{cite journal |last=Bosc |first=D G |author2=Graham K C |author3=Saulnier R B |author4=Zhang C |author5=Prober D |author6=Gietz R D |author7=Litchfield D W |date=May 2000|title=Identification and characterization of CKIP-1, a novel pleckstrin homology domain-containing protein that interacts with protein kinase CK2 |journal=J. Biol. Chem. |volume=275 |issue=19 |pages=14295–306 |location = UNITED STATES| issn = 0021-9258| pmid = 10799509 |doi=10.1074/jbc.275.19.14295 |doi-access=free }} Casein kinase 2, alpha 1,{{cite journal |last=Ahn |first=B H |author2=Kim T H |author3=Bae Y S |date=October 2001|title=Mapping of the interaction domain of the protein kinase CKII beta subunit with target proteins |journal=Mol. Cells |volume=12 |issue=2 |pages=158–63 |location = Korea (South)|doi=10.1016/S1016-8478(23)17077-4 | issn = 1016-8478| pmid = 11710515 |doi-access=free }}{{cite journal |last=Kusk |first=M |author2=Ahmed R |author3=Thomsen B |author4=Bendixen C |author5=Issinger O G |author6=Boldyreff B |date=January 1999|title=Interactions of protein kinase CK2beta subunit within the holoenzyme and with other proteins |journal=Mol. Cell. Biochem. |volume=191 |issue=1–2 |pages=51–8 |location = NETHERLANDS| issn = 0300-8177| pmid = 10094392 |doi=10.1023/A:1006840613986 |s2cid=257329 }} FGF1,{{cite journal |last=Skjerpen |first=Camilla Skiple |author2=Nilsen Trine |author3=Wesche Jørgen |author4=Olsnes Sjur |date=August 2002|title=Binding of FGF-1 variants to protein kinase CK2 correlates with mitogenicity |journal=EMBO J. |volume=21 |issue=15 |pages=4058–69 |location = England| issn = 0261-4189| pmid = 12145206 |doi=10.1093/emboj/cdf402 |pmc=126148 }} TRIB3,{{cite journal |last=Zhou |first=Ying |author2=Li Lu |author3=Liu Qiongming |author4=Xing Guichun |author5=Kuai Xuezhang |author6=Sun Jing |author7=Yin Xiushan |author8=Wang Jian |author9=Zhang Lingqiang |author10=He Fuchu |date=May 2008|title=E3 ubiquitin ligase SIAH1 mediates ubiquitination and degradation of TRB3 |journal=Cell. Signal. |volume=20 |issue=5 |pages=942–8 |location = England| issn = 0898-6568| pmid = 18276110 |doi = 10.1016/j.cellsig.2008.01.010 }} CDC34,{{cite journal |last=Block |first=K |author2=Boyer T G |author3=Yew P R |date=November 2001|title=Phosphorylation of the human ubiquitin-conjugating enzyme, CDC34, by casein kinase 2 |journal=J. Biol. Chem. |volume=276 |issue=44 |pages=41049–58 |location = United States| issn = 0021-9258| pmid = 11546811 |doi = 10.1074/jbc.M106453200 |doi-access=free }} Ribosomal protein L5,{{cite journal |last=Boldyreff |first=B |author2=Issinger O G |date=February 1997|title=A-Raf kinase is a new interacting partner of protein kinase CK2 beta subunit |journal=FEBS Lett. |volume=403 |issue=2 |pages=197–9 |location = NETHERLANDS| issn = 0014-5793| pmid = 9042965 |doi=10.1016/S0014-5793(97)00010-0 |s2cid=84557809 |doi-access= }}{{cite journal |last=Kim |first=J M |author2=Cha J Y |author3=Marshak D R |author4=Bae Y S |date=September 1996|title=Interaction of the beta subunit of casein kinase II with the ribosomal protein L5 |journal=Biochem. Biophys. Res. Commun. |volume=226 |issue=1 |pages=180–6 |location = UNITED STATES| issn = 0006-291X| pmid = 8806611 |doi = 10.1006/bbrc.1996.1330 |doi-access=free }} BTF3,{{cite journal |last=Grein |first=S |author2=Pyerin W |date=January 1999|title=BTF3 is a potential new substrate of protein kinase CK2 |journal=Mol. Cell. Biochem. |volume=191 |issue=1–2 |pages=121–8 |location = NETHERLANDS| issn = 0300-8177| pmid = 10094400 |doi=10.1023/A:1006806226764 |s2cid=1057554 }} BRCA1,{{cite journal |last=O'Brien |first=K A |author2=Lemke S J |author3=Cocke K S |author4=Rao R N |author5=Beckmann R P |date=July 1999|title=Casein kinase 2 binds to and phosphorylates BRCA1 |journal=Biochem. Biophys. Res. Commun. |volume=260 |issue=3 |pages=658–64 |location = UNITED STATES| issn = 0006-291X| pmid = 10403822 |doi = 10.1006/bbrc.1999.0892 }} RNF7, P70-S6 Kinase 1{{cite journal |last=Panasyuk |first=Ganna |author2=Nemazanyy Ivan |author3=Zhyvoloup Alexander |author4=Bretner Maria |author5=Litchfield David W |author6=Filonenko Valeriy |author7=Gout Ivan T |date=October 2006|title=Nuclear export of S6K1 II is regulated by protein kinase CK2 phosphorylation at Ser-17 |journal=J. Biol. Chem. |volume=281 |issue=42 |pages=31188–201 |location = United States| issn = 0021-9258| pmid = 16895915 |doi = 10.1074/jbc.M602618200 |doi-access= free}} and APC.{{cite journal |last=Homma |first=Miwako Kato |author2=Li Dongxia |author3=Krebs Edwin G |author4=Yuasa Yasuhito |author5=Homma Yoshimi |date=April 2002|title=Association and regulation of casein kinase 2 activity by adenomatous polyposis coli protein |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue=9 |pages=5959–64 |location = United States| issn = 0027-8424| pmid = 11972058 |doi = 10.1073/pnas.092143199 | bibcode =2002PNAS...99.5959K |pmc=122884 |doi-access=free }}

References

External links

{{UCSC gene info|CSNK2B}}
[https://www.ebi.ac.uk/pdbe/pdbe-kb/proteins/P67870 PDBe-KB] provides an overview of all the structure information available in the PDB for Human Casein kinase II subunit beta (CSNK2B)

CSNK2B

Interactions

References

External links

Further reading