CSNK2B: Difference between revisions

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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
{{Infobox protein family
| update_page = yes
| Symbol = CK_II_beta
| require_manual_inspection = no
| Name = Casein kinase II regulatory subunit
| update_protein_box = yes
| image = PDB 1rqf EBI.jpg
| update_summary = yes
| width =  
| update_citations = yes
| caption = structure of ck2 beta subunit crystallized in the presence of a p21waf1 peptide
}}
| Pfam = PF01214
 
| Pfam_clan =   
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
| InterPro = IPR000704
{{GNF_Protein_box
| SMART =  
| image = PBB_Protein_CSNK2B_image.jpg
| PROSITE = PDOC00845
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1jwh.
| MEROPS =  
| PDB = {{PDB2|1jwh}}, {{PDB2|1qf8}}, {{PDB2|1rqf}}
| SCOP = 1qf8
| Name = Casein kinase 2, beta polypeptide
| TCDB =  
| HGNCid = 2460
| OPM family =  
| Symbol = CSNK2B
| OPM protein =  
| AltSymbols =; CK2B; CK2N; CSK2B; G5A; MGC138222; MGC138224
| CAZy =  
| OMIM = 115441
| CDD =  
| ECnumber = 
| Homologene = 55572
| MGIid = 88548
| GeneAtlas_image1 = PBB_GE_CSNK2B_201390_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004682 |text = protein kinase CK2 activity}} {{GNF_GO|id=GO:0008605 |text = protein kinase CK2 regulator activity}} {{GNF_GO|id=GO:0016301 |text = kinase activity}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}}
| Component = {{GNF_GO|id=GO:0005956 |text = protein kinase CK2 complex}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0016055 |text = Wnt receptor signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1460
    | Hs_Ensembl = ENSG00000206300
    | Hs_RefseqProtein = NP_001311
    | Hs_RefseqmRNA = NM_001320
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = c6_COX
    | Hs_GenLoc_start = 31768327
    | Hs_GenLoc_end = 31775955
    | Hs_Uniprot = P67870
    | Mm_EntrezGene = 13001
    | Mm_Ensembl = ENSMUSG00000024387
    | Mm_RefseqmRNA = NM_009975
    | Mm_RefseqProtein = NP_034105
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 17
    | Mm_GenLoc_start = 34724251
    | Mm_GenLoc_end = 34729503
    | Mm_Uniprot = P67871
  }}
}}
}}
'''Casein kinase 2, beta polypeptide''', also known as '''CSNK2B''', is a human [[gene]].
'''Casein kinase II subunit beta''' is a [[protein]] that in humans is encoded by the ''CSNK2B'' [[gene]].<ref name="pmid2276748">{{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 | pmc =  | doi =10.1016/0888-7543(90)90266-W  }}</ref><ref name="pmid9503014">{{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 | pmc =  | doi = 10.1006/geno.1997.5145 }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =
| summary_text = 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 is composed of three subunits, alpha, alpha prime and beta, which form a tetrameric holoenzyme. The alpha and alpha prime subunits are catalytic, while the beta subunit serves regulatory functions. The enzyme localizes to the endoplasmic reticulum and the Golgi apparatus.<ref>{{cite web | title = Entrez Gene: CSNK2B casein kinase 2, beta polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1460| accessdate = }}</ref>
| summary_text = 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.<ref>{{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| accessdate = }}</ref>
}}
}}
Casein kinase, a ubiquitous, well-conserved [[protein kinase]] involved in [[cell (biology)|cell]] [[metabolism]] and [[Cellular differentiation|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.<ref name="pmid2666134">{{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| url = }}</ref><ref name="pmid1856204">{{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 | pmid = 1856204 | doi = | url = }}</ref> 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').<ref name="pmid7737972">{{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| url = }}</ref> The alpha-subunit is the [[biocatalysis|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 [[protein motif|motif]].<ref name="pmid7737972"/> The beta subunit is a [[Conservation (genetics)|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 (molecular)|binding]] a metal such as [[zinc]].<ref name="pmid8027080">{{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 | pmid = 8027080 | doi = | url = }}</ref> The [[mammalia]]n beta-subunit [[gene]] [[promotor (biology)|promoter]] shares common features with those of other [[mammalian]] protein kinases and is closely related to the [[promoter (biology)|promoter]] of the regulatory subunit of cAMP-dependent protein kinase.<ref name="pmid7737972"/>
==Interactions==
CSNK2B has been shown to [[Protein-protein interaction|interact]] with [[CD163]],<ref name=pmid11298324>{{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 |publisher= |location = Germany| issn = 0014-2980| pmid = 11298324 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1002/1521-4141(200104)31:4<999::AID-IMMU999>3.0.CO;2-R }}</ref> [[CSNK2A2]],<ref name=pmid14667819>{{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 |publisher= |location = United States| issn = 0888-7543| pmid = 14667819 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1016/S0888-7543(03)00235-0 }}</ref><ref name=pmid9571630>{{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 |publisher= |location = KOREA| issn = 1016-8478| pmid = 9571630 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref><ref name=pmid9188720>{{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 |publisher= |location = UNITED STATES| issn = 0006-2960| pmid = 9188720 |doi = 10.1021/bi962885q | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref><ref name=pmid10799509>{{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 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 10799509 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1074/jbc.275.19.14295 }}</ref> [[Casein kinase 2, alpha 1]],<ref name=pmid9571630/><ref name=pmid9188720/><ref name=pmid10799509/><ref name=pmid11710515>{{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 |publisher= |location = Korea (South)| issn = 1016-8478| pmid = 11710515 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref><ref name=pmid10094392>{{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 |publisher= |location = NETHERLANDS| issn = 0300-8177| pmid = 10094392 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1023/A:1006840613986 }}</ref> [[FGF1]],<ref name=pmid12145206>{{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 |publisher= |location = England| issn = 0261-4189| pmid = 12145206 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1093/emboj/cdf402 |pmc=126148 }}</ref> [[TRIB3]],<ref name=pmid18276110>{{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 |publisher= |location = England| issn = 0898-6568| pmid = 18276110 |doi = 10.1016/j.cellsig.2008.01.010 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> [[CDC34]],<ref name=pmid11546811>{{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 |publisher= |location = United States| issn = 0021-9258| pmid = 11546811 |doi = 10.1074/jbc.M106453200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> [[Ribosomal protein L5]],<ref name=pmid14667819/><ref name=pmid11710515/><ref name=pmid9042965>{{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 |publisher= |location = NETHERLANDS| issn = 0014-5793| pmid = 9042965 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1016/S0014-5793(97)00010-0 }}</ref><ref name=pmid8806611>{{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 |publisher= |location = UNITED STATES| issn = 0006-291X| pmid = 8806611 |doi = 10.1006/bbrc.1996.1330 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> [[BTF3]],<ref name=pmid10094400>{{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 |publisher= |location = NETHERLANDS| issn = 0300-8177| pmid = 10094400 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1023/A:1006806226764 }}</ref> [[BRCA1]],<ref name=pmid10403822>{{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 |publisher= |location = UNITED STATES| issn = 0006-291X| pmid = 10403822 |doi = 10.1006/bbrc.1999.0892 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> [[RNF7]],<ref name=pmid11710515/> [[P70-S6 Kinase 1]]<ref name=pmid16895915>{{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 |publisher= |location = United States| issn = 0021-9258| pmid = 16895915 |doi = 10.1074/jbc.M602618200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> and [[APC (gene)|APC]].<ref name=pmid11972058>{{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=[[PNAS|Proc. Natl. Acad. Sci. U.S.A.]] |volume=99 |issue=9 |pages=5959–64 |publisher= |location = United States| issn = 0027-8424| pmid = 11972058 |doi = 10.1073/pnas.092143199 | bibcode =2002PNAS...99.5959K | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |pmc=122884 }}</ref>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|CSNK2B}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading
| citations =  
| citations =
*{{cite journal  | author=Schubert U, Schneider T, Henklein P, ''et al.'' |title=Human-immunodeficiency-virus-type-1-encoded Vpu protein is phosphorylated by casein kinase II. |journal=Eur. J. Biochem. |volume=204 |issue= 2 |pages= 875-83 |year= 1992 |pmid= 1541298 |doi=  }}
*{{cite journal  | vauthors=Schubert U, Schneider T, Henklein P |title=Human-immunodeficiency-virus-type-1-encoded Vpu protein is phosphorylated by casein kinase II |journal=Eur. J. Biochem. |volume=204 |issue= 2 |pages= 875–83 |year= 1992 |pmid= 1541298 |doi=10.1111/j.1432-1033.1992.tb16707.x |display-authors=etal}}
*{{cite journal  | author=Teitz T, Eli D, Penner M, ''et al.'' |title=Expression of the cDNA for the beta subunit of human casein kinase II confers partial UV resistance on xeroderma pigmentosum cells. |journal=Mutat. Res. |volume=236 |issue= 1 |pages= 85-97 |year= 1990 |pmid= 1694965 |doi=  }}
*{{cite journal  | vauthors=Teitz T, Eli D, Penner M |title=Expression of the cDNA for the beta subunit of human casein kinase II confers partial UV resistance on xeroderma pigmentosum cells |journal=Mutat. Res. |volume=236 |issue= 1 |pages= 85–97 |year= 1990 |pmid= 1694965 |doi=  10.1016/0921-8777(90)90036-5|display-authors=etal}}
*{{cite journal  | author=Voss H, Wirkner U, Jakobi R, ''et al.'' |title=Structure of the gene encoding human casein kinase II subunit beta. |journal=J. Biol. Chem. |volume=266 |issue= 21 |pages= 13706-11 |year= 1991 |pmid= 1856204 |doi=  }}
*{{cite journal  | vauthors=Voss H, Wirkner U, Jakobi R |title=Structure of the gene encoding human casein kinase II subunit beta |journal=J. Biol. Chem. |volume=266 |issue= 21 |pages= 13706–11 |year= 1991 |pmid= 1856204 |doi=  |display-authors=etal}}
*{{cite journal  | author=Litchfield DW, Lozeman FJ, Cicirelli MF, ''et al.'' |title=Phosphorylation of the beta subunit of casein kinase II in human A431 cells. Identification of the autophosphorylation site and a site phosphorylated by p34cdc2. |journal=J. Biol. Chem. |volume=266 |issue= 30 |pages= 20380-9 |year= 1991 |pmid= 1939094 |doi=  }}
*{{cite journal  | vauthors=Litchfield DW, Lozeman FJ, Cicirelli MF |title=Phosphorylation of the beta subunit of casein kinase II in human A431 cells. Identification of the autophosphorylation site and a site phosphorylated by p34cdc2 |journal=J. Biol. Chem. |volume=266 |issue= 30 |pages= 20380–9 |year= 1991 |pmid= 1939094 |doi=  |display-authors=etal}}
*{{cite journal  | author=Yang-Feng TL, Teitz T, Cheung MC, ''et al.'' |title=Assignment of the human casein kinase II beta-subunit gene to 6p12----p21. |journal=Genomics |volume=8 |issue= 4 |pages= 741-2 |year= 1991 |pmid= 2276748 |doi= }}
*{{cite journal  | vauthors=Ackerman P, Glover CV, Osheroff N |title=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 |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 2 |pages= 821–5 |year= 1990 |pmid= 2300566 |doi=10.1073/pnas.87.2.821  | pmc=53358  |bibcode=1990PNAS...87..821A }}
*{{cite journal  | author=Ackerman P, Glover CV, Osheroff N |title=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. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 2 |pages= 821-5 |year= 1990 |pmid= 2300566 |doi= }}
*{{cite journal  | vauthors=Heller-Harrison RA, Meisner H, Czech MP |title=Cloning and characterization of a cDNA encoding the beta subunit of human casein kinase II |journal=Biochemistry |volume=28 |issue= 23 |pages= 9053–8 |year= 1990 |pmid= 2513884 |doi=10.1021/bi00449a014  }}
*{{cite journal  | author=Heller-Harrison RA, Meisner H, Czech MP |title=Cloning and characterization of a cDNA encoding the beta subunit of human casein kinase II. |journal=Biochemistry |volume=28 |issue= 23 |pages= 9053-8 |year= 1990 |pmid= 2513884 |doi=  }}
*{{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 |year= 1989 |pmid= 2666134 |doi=10.1111/j.1432-1033.1989.tb14917.x }}
*{{cite journal  | author=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 |year= 1989 |pmid= 2666134 |doi=  }}
*{{cite journal  | vauthors=Vincent MJ, Abdul Jabbar M |title=The human immunodeficiency virus type 1 Vpu protein: a potential regulator of proteolysis and protein transport in the mammalian secretory pathway |journal=Virology |volume=213 |issue= 2 |pages= 639–49 |year= 1996 |pmid= 7491787 |doi=10.1006/viro.1995.0035 }}
*{{cite journal  | author=Vincent MJ, Abdul Jabbar M |title=The human immunodeficiency virus type 1 Vpu protein: a potential regulator of proteolysis and protein transport in the mammalian secretory pathway. |journal=Virology |volume=213 |issue= 2 |pages= 639-49 |year= 1996 |pmid= 7491787 |doi= }}
*{{cite journal  | vauthors=Litchfield DW, Bosc DG, Slominski E |title=The protein kinase from mitotic human cells that phosphorylates Ser-209 on the casein kinase II beta-subunit is p34cdc2 |journal=Biochim. Biophys. Acta |volume=1269 |issue= 1 |pages= 69–78 |year= 1995 |pmid= 7578274 |doi=10.1016/0167-4889(95)00100-7  }}
*{{cite journal  | author=Litchfield DW, Bosc DG, Slominski E |title=The protein kinase from mitotic human cells that phosphorylates Ser-209 on the casein kinase II beta-subunit is p34cdc2. |journal=Biochim. Biophys. Acta |volume=1269 |issue= 1 |pages= 69-78 |year= 1995 |pmid= 7578274 |doi= }}
*{{cite journal  | vauthors=Jin YJ, Burakoff SJ |title=The 25-kDa FK506-binding protein is localized in the nucleus and associates with casein kinase II and nucleolin |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 16 |pages= 7769–73 |year= 1993 |pmid= 7689229 |doi=10.1073/pnas.90.16.7769  | pmc=47224  |bibcode=1993PNAS...90.7769J }}
*{{cite journal  | author=Jin YJ, Burakoff SJ |title=The 25-kDa FK506-binding protein is localized in the nucleus and associates with casein kinase II and nucleolin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 16 |pages= 7769-73 |year= 1993 |pmid= 7689229 |doi= }}
*{{cite journal  | vauthors=Gietz RD, Graham KC, Litchfield DW |title=Interactions between the subunits of casein kinase II |journal=J. Biol. Chem. |volume=270 |issue= 22 |pages= 13017–21 |year= 1995 |pmid= 7768894 |doi=10.1074/jbc.270.22.13017  }}
*{{cite journal  | author=Gietz RD, Graham KC, Litchfield DW |title=Interactions between the subunits of casein kinase II. |journal=J. Biol. Chem. |volume=270 |issue= 22 |pages= 13017-21 |year= 1995 |pmid= 7768894 |doi=  }}
*{{cite journal  | vauthors=Szebeni A, Herrera JE, Olson MO |title=Interaction of nucleolar protein B23 with peptides related to nuclear localization signals |journal=Biochemistry |volume=34 |issue= 25 |pages= 8037–42 |year= 1995 |pmid= 7794916 |doi=10.1021/bi00025a009 }}
*{{cite journal  | author=Szebeni A, Herrera JE, Olson MO |title=Interaction of nucleolar protein B23 with peptides related to nuclear localization signals. |journal=Biochemistry |volume=34 |issue= 25 |pages= 8037-42 |year= 1995 |pmid= 7794916 |doi=  }}
*{{cite journal  | vauthors=Arnold SF, Obourn JD, Jaffe H, Notides AC |title=Serine 167 is the major estradiol-induced phosphorylation site on the human estrogen receptor |journal=Mol. Endocrinol. |volume=8 |issue= 9 |pages= 1208–14 |year= 1995 |pmid= 7838153 |doi=10.1210/me.8.9.1208 }}
*{{cite journal  | author=Arnold SF, Obourn JD, Jaffe H, Notides AC |title=Serine 167 is the major estradiol-induced phosphorylation site on the human estrogen receptor. |journal=Mol. Endocrinol. |volume=8 |issue= 9 |pages= 1208-14 |year= 1995 |pmid= 7838153 |doi=  }}
*{{cite journal  | author=Pyerin W |title=Human casein kinase II: structures, genes, expression and requirement in cell growth stimulation |journal=Adv. Enzyme Regul. |volume=34 |issue= |pages= 225–46 |year= 1994 |pmid= 7942276 |doi=10.1016/0065-2571(94)90018-3 }}
*{{cite journal  | author=Pyerin W |title=Human casein kinase II: structures, genes, expression and requirement in cell growth stimulation. |journal=Adv. Enzyme Regul. |volume=34 |issue= |pages= 225-46 |year= 1994 |pmid= 7942276 |doi=  }}
*{{cite journal  | vauthors=el Benna J, Faust LP, Babior BM | author3-link=Bernard Babior |title=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 |journal=J. Biol. Chem. |volume=269 |issue= 38 |pages= 23431–6 |year= 1994 |pmid= 8089108 |doi=  }}
*{{cite journal  | author=el Benna J, Faust LP, [[Bernard Babior|Babior BM]] |title=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. |journal=J. Biol. Chem. |volume=269 |issue= 38 |pages= 23431-6 |year= 1994 |pmid= 8089108 |doi= }}
*{{cite journal  | vauthors=Schubert U, Henklein P, Boldyreff B |title=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 |journal=J. Mol. Biol. |volume=236 |issue= 1 |pages= 16–25 |year= 1994 |pmid= 8107101 |doi= 10.1006/jmbi.1994.1114 |display-authors=etal}}
*{{cite journal  | author=Schubert U, Henklein P, Boldyreff B, ''et al.'' |title=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. |journal=J. Mol. Biol. |volume=236 |issue= 1 |pages= 16-25 |year= 1994 |pmid= 8107101 |doi= 10.1006/jmbi.1994.1114 }}
*{{cite journal  | vauthors=Schubert U, Strebel K |title=Differential activities of the human immunodeficiency virus type 1-encoded Vpu protein are regulated by phosphorylation and occur in different cellular compartments |journal=J. Virol. |volume=68 |issue= 4 |pages= 2260–71 |year= 1994 |pmid= 8139011 |doi= | pmc=236702  }}
*{{cite journal  | author=Schubert U, Strebel K |title=Differential activities of the human immunodeficiency virus type 1-encoded Vpu protein are regulated by phosphorylation and occur in different cellular compartments. |journal=J. Virol. |volume=68 |issue= 4 |pages= 2260-71 |year= 1994 |pmid= 8139011 |doi=  }}
*{{cite journal  | vauthors=Tanasijevic MJ, Myers MG, Thoma RS |title=Phosphorylation of the insulin receptor substrate IRS-1 by casein kinase II |journal=J. Biol. Chem. |volume=268 |issue= 24 |pages= 18157–66 |year= 1993 |pmid= 8349691 |doi=  |display-authors=etal}}
*{{cite journal  | author=Tanasijevic MJ, Myers MG, Thoma RS, ''et al.'' |title=Phosphorylation of the insulin receptor substrate IRS-1 by casein kinase II. |journal=J. Biol. Chem. |volume=268 |issue= 24 |pages= 18157-66 |year= 1993 |pmid= 8349691 |doi=  }}
*{{cite journal  | vauthors=Friborg J, Ladha A, Göttlinger H |title=Functional analysis of the phosphorylation sites on the human immunodeficiency virus type 1 Vpu protein |journal=J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. |volume=8 |issue= 1 |pages= 10–22 |year= 1996 |pmid= 8548340 |doi= 10.1097/00042560-199501000-00004 |display-authors=etal}}
*{{cite journal  | author=Friborg J, Ladha A, Göttlinger H, ''et al.'' |title=Functional analysis of the phosphorylation sites on the human immunodeficiency virus type 1 Vpu protein. |journal=J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. |volume=8 |issue= 1 |pages= 10-22 |year= 1996 |pmid= 8548340 |doi=  }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=1460}}
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{{InterPro content|IPR000704}}


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Latest revision as of 01:25, 23 June 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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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. Bibcode:2002PNAS...99.5959K. 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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