Full text data of CSNK2B
CSNK2B
(CK2N, G5A)
[Confidence: low (only semi-automatic identification from reviews)]
Casein kinase II subunit beta; CK II beta (Phosvitin; Protein G5a)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Casein kinase II subunit beta; CK II beta (Phosvitin; Protein G5a)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P67870
ID CSK2B_HUMAN Reviewed; 215 AA.
AC P67870; B0UXA9; P07312; P13862; Q4VX47;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-OCT-2004, sequence version 1.
DT 22-JAN-2014, entry version 115.
DE RecName: Full=Casein kinase II subunit beta;
DE Short=CK II beta;
DE AltName: Full=Phosvitin;
DE AltName: Full=Protein G5a;
GN Name=CSNK2B; Synonyms=CK2N, G5A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2666134; DOI=10.1111/j.1432-1033.1989.tb14917.x;
RA Jakobi R., Voss H., Pyerin W.;
RT "Human phosvitin/casein kinase type II. Molecular cloning and
RT sequencing of full-length cDNA encoding subunit beta.";
RL Eur. J. Biochem. 183:227-233(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1694965; DOI=10.1016/0921-8777(90)90036-5;
RA Teitz T., Eli D., Penner M., Bakhanashvili M., Naiman T., Timme T.L.,
RA Wood C.M., Moses R.E., Canaani D.;
RT "Expression of the cDNA for the beta subunit of human casein kinase II
RT confers partial UV resistance on xeroderma pigmentosum cells.";
RL Mutat. Res. 236:85-97(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2513884; DOI=10.1021/bi00449a014;
RA Heller-Harrison R.A., Meisner H., Czech M.P.;
RT "Cloning and characterization of a cDNA encoding the beta subunit of
RT human casein kinase II.";
RL Biochemistry 28:9053-9058(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1856204;
RA Voss A., Wirkner U., Jacobi R., Hewitt N., Schwager C., Zimmermann J.,
RA Ansorge W., Pyerin W.;
RT "Structure of the gene encoding human casein kinase II subunit beta.";
RL J. Biol. Chem. 266:13706-13711(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12102635; DOI=10.1021/bi025791r;
RA Singh L.S., Kalafatis M.;
RT "Sequencing of full-length cDNA encoding the alpha and beta subunits
RT of human casein kinase II from human platelets and megakaryocytic
RT cells. Expression of the casein kinase IIalpha intronless gene in a
RT megakaryocytic cell line.";
RL Biochemistry 41:8935-8940(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
RA Campbell R.D., Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Shiina S., Tamiya G., Oka A., Inoko H.;
RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G;);
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [14]
RP PHOSPHORYLATION.
RX PubMed=2300566; DOI=10.1073/pnas.87.2.821;
RA Ackerman P., Glover C.V., Osheroff N.;
RT "Stimulation of casein kinase II by epidermal growth factor:
RT relationship between the physiological activity of the kinase and the
RT phosphorylation state of its beta subunit.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:821-825(1990).
RN [15]
RP INTERACTION WITH CD163.
RX PubMed=11298324;
RX DOI=10.1002/1521-4141(200104)31:4<999::AID-IMMU999>3.0.CO;2-R;
RA Ritter M., Buechler C., Kapinsky M., Schmitz G.;
RT "Interaction of CD163 with the regulatory subunit of casein kinase II
RT (CKII) and dependence of CD163 signaling on CKII and protein kinase
RT C.";
RL Eur. J. Immunol. 31:999-1009(2001).
RN [16]
RP FUNCTION, AND INTERACTION WITH SSRP1 AND SUPT16H.
RX PubMed=11239457; DOI=10.1016/S1097-2765(01)00176-9;
RA Keller D.M., Zeng X., Wang Y., Zhang Q.H., Kapoor M., Shu H.,
RA Goodman R., Lozano G., Zhao Y., Lu H.;
RT "A DNA damage-induced p53 serine 392 kinase complex contains CK2,
RT hSpt16, and SSRP1.";
RL Mol. Cell 7:283-292(2001).
RN [17]
RP INTERACTION WITH FGF1.
RX PubMed=11964394; DOI=10.1074/jbc.M112193200;
RA Skjerpen C.S., Wesche J., Olsnes S.;
RT "Identification of ribosome-binding protein p34 as an intracellular
RT protein that binds acidic fibroblast growth factor.";
RL J. Biol. Chem. 277:23864-23871(2002).
RN [18]
RP INTERACTION WITH SSRP1 AND SUPT16H.
RX PubMed=12393879; DOI=10.1074/jbc.M209820200;
RA Keller D.M., Lu H.;
RT "p53 serine 392 phosphorylation increases after UV through induction
RT of the assembly of the CK2.hSPT16.SSRP1 complex.";
RL J. Biol. Chem. 277:50206-50213(2002).
RN [19]
RP FUNCTION IN PHOSPHORYLATION OF MUSK, AND INTERACTION WITH MUSK.
RX PubMed=16818610; DOI=10.1101/gad.375206;
RA Cheusova T., Khan M.A., Schubert S.W., Gavin A.C., Buchou T.,
RA Jacob G., Sticht H., Allende J., Boldyreff B., Brenner H.R.,
RA Hashemolhosseini S.;
RT "Casein kinase 2-dependent serine phosphorylation of MuSK regulates
RT acetylcholine receptor aggregation at the neuromuscular junction.";
RL Genes Dev. 20:1800-1816(2006).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, AND MASS
RP SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-212, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 1-182, SUBUNIT, AND
RP ZINC-BINDING SITES.
RX PubMed=10357806; DOI=10.1093/emboj/18.11.2930;
RA Chantalat L., Leroy D., Filhol O., Nueda A., Benitez M.J.,
RA Chambaz E.M., Cochet C., Dideberg O.;
RT "Crystal structure of the human protein kinase CK2 regulatory subunit
RT reveals its zinc finger-mediated dimerization.";
RL EMBO J. 18:2930-2940(1999).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH CSNK2A1,
RP ZINC-BINDING SITES, SUBUNIT, AND PHOSPHORYLATION AT SER-2 AND SER-3.
RX PubMed=11574463; DOI=10.1093/emboj/20.19.5320;
RA Niefind K., Guerra B., Ermakowa I., Issinger O.G.;
RT "Crystal structure of human protein kinase CK2: insights into basic
RT properties of the CK2 holoenzyme.";
RL EMBO J. 20:5320-5331(2001).
CC -!- FUNCTION: Participates in Wnt signaling (By similarity). Plays a
CC complex role in regulating the basal catalytic activity of the
CC alpha subunit.
CC -!- SUBUNIT: Tetramer composed of an alpha subunit, an alpha' subunit
CC and two beta subunits. The beta subunit dimerization is mediated
CC by zinc ions. Interacts with TCTEX1D3 (By similarity). Interacts
CC with CD163. Also component of a CK2-SPT16-SSRP1 complex composed
CC of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, the complex
CC associating following UV irradiation. Interacts with MUSK;
CC mediates phosphorylation of MUSK by CK2. Interacts with FGF1; this
CC interaction is increased in the presence of FIBP, suggesting a
CC possible cooperative interaction between CSNKB and FIBP in binding
CC to FGF1.
CC -!- INTERACTION:
CC Self; NbExp=7; IntAct=EBI-348169, EBI-348169;
CC O00555:CACNA1A; NbExp=2; IntAct=EBI-348169, EBI-766279;
CC O00257-3:CBX4; NbExp=2; IntAct=EBI-348169, EBI-4392727;
CC Q9JK25:Clip1 (xeno); NbExp=2; IntAct=EBI-348169, EBI-908338;
CC O08785:Clock (xeno); NbExp=2; IntAct=EBI-348169, EBI-79859;
CC P68400:CSNK2A1; NbExp=13; IntAct=EBI-348169, EBI-347804;
CC P19784:CSNK2A2; NbExp=6; IntAct=EBI-348169, EBI-347451;
CC Q6VY07:PACS1; NbExp=3; IntAct=EBI-348169, EBI-2555014;
CC Q96EB6:SIRT1; NbExp=5; IntAct=EBI-348169, EBI-1802965;
CC -!- PTM: Phosphorylated by alpha subunit.
CC -!- SIMILARITY: Belongs to the casein kinase 2 subunit beta family.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI18393.2; Type=Erroneous initiation;
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DR EMBL; X16937; CAA34811.1; -; mRNA.
DR EMBL; X16312; CAA34379.1; -; mRNA.
DR EMBL; M30448; AAA52123.1; -; mRNA.
DR EMBL; X57152; CAA40442.1; -; Genomic_DNA.
DR EMBL; AY113186; AAM50092.1; -; mRNA.
DR EMBL; CR541699; CAG46500.1; -; mRNA.
DR EMBL; AF129756; AAD18081.1; -; Genomic_DNA.
DR EMBL; BA000025; BAB63386.1; -; Genomic_DNA.
DR EMBL; DQ314868; ABC40727.1; -; Genomic_DNA.
DR EMBL; AK311860; BAG34801.1; -; mRNA.
DR EMBL; AL662899; CAI96141.1; -; Genomic_DNA.
DR EMBL; AL662899; CAI18393.2; ALT_INIT; Genomic_DNA.
DR EMBL; AL670886; CAI17800.1; -; Genomic_DNA.
DR EMBL; AL805934; CAI18523.1; -; Genomic_DNA.
DR EMBL; BX511262; CAM45825.1; -; Genomic_DNA.
DR EMBL; CR753842; CAQ06572.1; -; Genomic_DNA.
DR EMBL; CR354443; CAQ07002.1; -; Genomic_DNA.
DR EMBL; CR759761; CAQ10879.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03473.1; -; Genomic_DNA.
DR EMBL; BC112017; AAI12018.1; -; mRNA.
DR EMBL; BC112019; AAI12020.1; -; mRNA.
DR PIR; A39459; A39459.
DR RefSeq; NP_001269314.1; NM_001282385.1.
DR RefSeq; NP_001311.3; NM_001320.6.
DR UniGene; Hs.73527; -.
DR PDB; 1DS5; X-ray; 3.16 A; E/F/G/H=181-203.
DR PDB; 1JWH; X-ray; 3.10 A; C/D=1-215.
DR PDB; 1QF8; X-ray; 1.74 A; A/B=1-182.
DR PDB; 3EED; X-ray; 2.80 A; A/B=1-193.
DR PDB; 4DGL; X-ray; 3.00 A; A/B=1-215.
DR PDB; 4MD7; X-ray; 3.10 A; A/B/C/D=1-215.
DR PDB; 4MD8; X-ray; 3.30 A; A/B/C/D=1-215.
DR PDB; 4MD9; X-ray; 3.50 A; A/B/C/D/I/J/N/O=1-215.
DR PDBsum; 1DS5; -.
DR PDBsum; 1JWH; -.
DR PDBsum; 1QF8; -.
DR PDBsum; 3EED; -.
DR PDBsum; 4DGL; -.
DR PDBsum; 4MD7; -.
DR PDBsum; 4MD8; -.
DR PDBsum; 4MD9; -.
DR ProteinModelPortal; P67870; -.
DR SMR; P67870; 7-207.
DR DIP; DIP-131N; -.
DR IntAct; P67870; 174.
DR MINT; MINT-88683; -.
DR STRING; 9606.ENSP00000365025; -.
DR BindingDB; P67870; -.
DR ChEMBL; CHEMBL2358; -.
DR DMDM; 54037520; -.
DR PaxDb; P67870; -.
DR PRIDE; P67870; -.
DR DNASU; 1460; -.
DR Ensembl; ENST00000375865; ENSP00000365025; ENSG00000204435.
DR Ensembl; ENST00000375866; ENSP00000365026; ENSG00000204435.
DR Ensembl; ENST00000375882; ENSP00000365042; ENSG00000204435.
DR Ensembl; ENST00000383427; ENSP00000372919; ENSG00000206406.
DR Ensembl; ENST00000383433; ENSP00000372925; ENSG00000206406.
DR Ensembl; ENST00000400110; ENSP00000382980; ENSG00000206406.
DR Ensembl; ENST00000412802; ENSP00000413469; ENSG00000224774.
DR Ensembl; ENST00000418230; ENSP00000411322; ENSG00000228875.
DR Ensembl; ENST00000422567; ENSP00000407018; ENSG00000224398.
DR Ensembl; ENST00000429633; ENSP00000409510; ENSG00000230700.
DR Ensembl; ENST00000431476; ENSP00000394855; ENSG00000224398.
DR Ensembl; ENST00000436169; ENSP00000412520; ENSG00000224398.
DR Ensembl; ENST00000443673; ENSP00000400188; ENSG00000230700.
DR Ensembl; ENST00000448596; ENSP00000391038; ENSG00000232960.
DR Ensembl; ENST00000451917; ENSP00000415303; ENSG00000224774.
DR Ensembl; ENST00000452985; ENSP00000415237; ENSG00000228875.
DR Ensembl; ENST00000453234; ENSP00000395275; ENSG00000224774.
DR Ensembl; ENST00000454382; ENSP00000390900; ENSG00000232960.
DR Ensembl; ENST00000454511; ENSP00000393756; ENSG00000232960.
DR Ensembl; ENST00000455161; ENSP00000407379; ENSG00000230700.
DR Ensembl; ENST00000458330; ENSP00000410802; ENSG00000228875.
DR GeneID; 1460; -.
DR KEGG; hsa:1460; -.
DR UCSC; uc003nvr.1; human.
DR CTD; 1460; -.
DR GeneCards; GC06P031633; -.
DR GeneCards; GC06Pj31620; -.
DR GeneCards; GC06Pk31615; -.
DR GeneCards; GC06Pl31672; -.
DR GeneCards; GC06Pm31709; -.
DR GeneCards; GC06Pn31623; -.
DR GeneCards; GC06Po31622; -.
DR HGNC; HGNC:2460; CSNK2B.
DR HPA; CAB004349; -.
DR HPA; CAB013087; -.
DR HPA; CAB016059; -.
DR HPA; HPA005944; -.
DR MIM; 115441; gene.
DR neXtProt; NX_P67870; -.
DR PharmGKB; PA26960; -.
DR eggNOG; COG5041; -.
DR HOGENOM; HOG000039270; -.
DR HOVERGEN; HBG051131; -.
DR InParanoid; P67870; -.
DR KO; K03115; -.
DR PhylomeDB; P67870; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR SignaLink; P67870; -.
DR EvolutionaryTrace; P67870; -.
DR GeneWiki; CSNK2B; -.
DR GenomeRNAi; 1460; -.
DR NextBio; 6001; -.
DR PRO; PR:P67870; -.
DR ArrayExpress; P67870; -.
DR Bgee; P67870; -.
DR CleanEx; HS_CSNK2B; -.
DR Genevestigator; P67870; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005956; C:protein kinase CK2 complex; NAS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019887; F:protein kinase regulator activity; NAS:UniProtKB.
DR GO; GO:0033211; P:adiponectin-mediated signaling pathway; IDA:BHF-UCL.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR GO; GO:0043623; P:cellular protein complex assembly; NAS:BHF-UCL.
DR GO; GO:0061154; P:endothelial tube morphogenesis; IMP:BHF-UCL.
DR GO; GO:0000278; P:mitotic cell cycle; TAS:Reactome.
DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IDA:BHF-UCL.
DR GO; GO:0008285; P:negative regulation of cell proliferation; TAS:BHF-UCL.
DR GO; GO:0032927; P:positive regulation of activin receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
DR GO; GO:0051101; P:regulation of DNA binding; NAS:BHF-UCL.
DR GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1820.10; -; 1.
DR Gene3D; 2.20.25.20; -; 1.
DR InterPro; IPR016149; Casein_kin_II_reg-sub_a-hlx.
DR InterPro; IPR016150; Casein_kin_II_reg-sub_b-sht.
DR InterPro; IPR000704; Casein_kinase_II_reg-sub.
DR PANTHER; PTHR11740; PTHR11740; 1.
DR Pfam; PF01214; CK_II_beta; 1.
DR PRINTS; PR00472; CASNKINASEII.
DR SMART; SM01085; CK_II_beta; 1.
DR SUPFAM; SSF57798; SSF57798; 1.
DR PROSITE; PS01101; CK2_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Metal-binding;
KW Phosphoprotein; Reference proteome; Wnt signaling pathway; Zinc.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 215 Casein kinase II subunit beta.
FT /FTId=PRO_0000068236.
FT REGION 188 193 Interaction with alpha subunit (By
FT similarity).
FT COMPBIAS 55 64 Asp/Glu-rich (acidic).
FT METAL 109 109 Zinc.
FT METAL 114 114 Zinc.
FT METAL 137 137 Zinc.
FT METAL 140 140 Zinc.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 2 2 Phosphoserine; by autocatalysis.
FT MOD_RES 3 3 Phosphoserine; by autocatalysis.
FT MOD_RES 209 209 Phosphoserine.
FT MOD_RES 212 212 N6-acetyllysine.
FT CONFLICT 194 194 P -> A (in Ref. 3; AAA52123).
FT HELIX 9 15
FT TURN 17 20
FT HELIX 27 31
FT HELIX 33 36
FT HELIX 39 41
FT STRAND 43 45
FT HELIX 46 53
FT HELIX 67 87
FT HELIX 91 102
FT TURN 103 106
FT HELIX 112 114
FT STRAND 120 122
FT STRAND 134 136
FT TURN 138 140
FT STRAND 142 144
FT HELIX 149 151
FT HELIX 156 158
FT TURN 159 162
FT HELIX 163 170
FT HELIX 172 174
FT STRAND 190 192
FT HELIX 195 198
FT TURN 199 201
FT HELIX 202 205
SQ SEQUENCE 215 AA; 24942 MW; E465B1E699B0E0EC CRC64;
MSSSEEVSWI SWFCGLRGNE FFCEVDEDYI QDKFNLTGLN EQVPHYRQAL DMILDLEPDE
ELEDNPNQSD LIEQAAEMLY GLIHARYILT NRGIAQMLEK YQQGDFGYCP RVYCENQPML
PIGLSDIPGE AMVKLYCPKC MDVYTPKSSR HHHTDGAYFG TGFPHMLFMV HPEYRPKRPA
NQFVPRLYGF KIHPMAYQLQ LQAASNFKSP VKTIR
//
ID CSK2B_HUMAN Reviewed; 215 AA.
AC P67870; B0UXA9; P07312; P13862; Q4VX47;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-OCT-2004, sequence version 1.
DT 22-JAN-2014, entry version 115.
DE RecName: Full=Casein kinase II subunit beta;
DE Short=CK II beta;
DE AltName: Full=Phosvitin;
DE AltName: Full=Protein G5a;
GN Name=CSNK2B; Synonyms=CK2N, G5A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2666134; DOI=10.1111/j.1432-1033.1989.tb14917.x;
RA Jakobi R., Voss H., Pyerin W.;
RT "Human phosvitin/casein kinase type II. Molecular cloning and
RT sequencing of full-length cDNA encoding subunit beta.";
RL Eur. J. Biochem. 183:227-233(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1694965; DOI=10.1016/0921-8777(90)90036-5;
RA Teitz T., Eli D., Penner M., Bakhanashvili M., Naiman T., Timme T.L.,
RA Wood C.M., Moses R.E., Canaani D.;
RT "Expression of the cDNA for the beta subunit of human casein kinase II
RT confers partial UV resistance on xeroderma pigmentosum cells.";
RL Mutat. Res. 236:85-97(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2513884; DOI=10.1021/bi00449a014;
RA Heller-Harrison R.A., Meisner H., Czech M.P.;
RT "Cloning and characterization of a cDNA encoding the beta subunit of
RT human casein kinase II.";
RL Biochemistry 28:9053-9058(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1856204;
RA Voss A., Wirkner U., Jacobi R., Hewitt N., Schwager C., Zimmermann J.,
RA Ansorge W., Pyerin W.;
RT "Structure of the gene encoding human casein kinase II subunit beta.";
RL J. Biol. Chem. 266:13706-13711(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12102635; DOI=10.1021/bi025791r;
RA Singh L.S., Kalafatis M.;
RT "Sequencing of full-length cDNA encoding the alpha and beta subunits
RT of human casein kinase II from human platelets and megakaryocytic
RT cells. Expression of the casein kinase IIalpha intronless gene in a
RT megakaryocytic cell line.";
RL Biochemistry 41:8935-8940(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
RA Campbell R.D., Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Shiina S., Tamiya G., Oka A., Inoko H.;
RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G;);
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [14]
RP PHOSPHORYLATION.
RX PubMed=2300566; DOI=10.1073/pnas.87.2.821;
RA Ackerman P., Glover C.V., Osheroff N.;
RT "Stimulation of casein kinase II by epidermal growth factor:
RT relationship between the physiological activity of the kinase and the
RT phosphorylation state of its beta subunit.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:821-825(1990).
RN [15]
RP INTERACTION WITH CD163.
RX PubMed=11298324;
RX DOI=10.1002/1521-4141(200104)31:4<999::AID-IMMU999>3.0.CO;2-R;
RA Ritter M., Buechler C., Kapinsky M., Schmitz G.;
RT "Interaction of CD163 with the regulatory subunit of casein kinase II
RT (CKII) and dependence of CD163 signaling on CKII and protein kinase
RT C.";
RL Eur. J. Immunol. 31:999-1009(2001).
RN [16]
RP FUNCTION, AND INTERACTION WITH SSRP1 AND SUPT16H.
RX PubMed=11239457; DOI=10.1016/S1097-2765(01)00176-9;
RA Keller D.M., Zeng X., Wang Y., Zhang Q.H., Kapoor M., Shu H.,
RA Goodman R., Lozano G., Zhao Y., Lu H.;
RT "A DNA damage-induced p53 serine 392 kinase complex contains CK2,
RT hSpt16, and SSRP1.";
RL Mol. Cell 7:283-292(2001).
RN [17]
RP INTERACTION WITH FGF1.
RX PubMed=11964394; DOI=10.1074/jbc.M112193200;
RA Skjerpen C.S., Wesche J., Olsnes S.;
RT "Identification of ribosome-binding protein p34 as an intracellular
RT protein that binds acidic fibroblast growth factor.";
RL J. Biol. Chem. 277:23864-23871(2002).
RN [18]
RP INTERACTION WITH SSRP1 AND SUPT16H.
RX PubMed=12393879; DOI=10.1074/jbc.M209820200;
RA Keller D.M., Lu H.;
RT "p53 serine 392 phosphorylation increases after UV through induction
RT of the assembly of the CK2.hSPT16.SSRP1 complex.";
RL J. Biol. Chem. 277:50206-50213(2002).
RN [19]
RP FUNCTION IN PHOSPHORYLATION OF MUSK, AND INTERACTION WITH MUSK.
RX PubMed=16818610; DOI=10.1101/gad.375206;
RA Cheusova T., Khan M.A., Schubert S.W., Gavin A.C., Buchou T.,
RA Jacob G., Sticht H., Allende J., Boldyreff B., Brenner H.R.,
RA Hashemolhosseini S.;
RT "Casein kinase 2-dependent serine phosphorylation of MuSK regulates
RT acetylcholine receptor aggregation at the neuromuscular junction.";
RL Genes Dev. 20:1800-1816(2006).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, AND MASS
RP SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-212, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 1-182, SUBUNIT, AND
RP ZINC-BINDING SITES.
RX PubMed=10357806; DOI=10.1093/emboj/18.11.2930;
RA Chantalat L., Leroy D., Filhol O., Nueda A., Benitez M.J.,
RA Chambaz E.M., Cochet C., Dideberg O.;
RT "Crystal structure of the human protein kinase CK2 regulatory subunit
RT reveals its zinc finger-mediated dimerization.";
RL EMBO J. 18:2930-2940(1999).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH CSNK2A1,
RP ZINC-BINDING SITES, SUBUNIT, AND PHOSPHORYLATION AT SER-2 AND SER-3.
RX PubMed=11574463; DOI=10.1093/emboj/20.19.5320;
RA Niefind K., Guerra B., Ermakowa I., Issinger O.G.;
RT "Crystal structure of human protein kinase CK2: insights into basic
RT properties of the CK2 holoenzyme.";
RL EMBO J. 20:5320-5331(2001).
CC -!- FUNCTION: Participates in Wnt signaling (By similarity). Plays a
CC complex role in regulating the basal catalytic activity of the
CC alpha subunit.
CC -!- SUBUNIT: Tetramer composed of an alpha subunit, an alpha' subunit
CC and two beta subunits. The beta subunit dimerization is mediated
CC by zinc ions. Interacts with TCTEX1D3 (By similarity). Interacts
CC with CD163. Also component of a CK2-SPT16-SSRP1 complex composed
CC of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, the complex
CC associating following UV irradiation. Interacts with MUSK;
CC mediates phosphorylation of MUSK by CK2. Interacts with FGF1; this
CC interaction is increased in the presence of FIBP, suggesting a
CC possible cooperative interaction between CSNKB and FIBP in binding
CC to FGF1.
CC -!- INTERACTION:
CC Self; NbExp=7; IntAct=EBI-348169, EBI-348169;
CC O00555:CACNA1A; NbExp=2; IntAct=EBI-348169, EBI-766279;
CC O00257-3:CBX4; NbExp=2; IntAct=EBI-348169, EBI-4392727;
CC Q9JK25:Clip1 (xeno); NbExp=2; IntAct=EBI-348169, EBI-908338;
CC O08785:Clock (xeno); NbExp=2; IntAct=EBI-348169, EBI-79859;
CC P68400:CSNK2A1; NbExp=13; IntAct=EBI-348169, EBI-347804;
CC P19784:CSNK2A2; NbExp=6; IntAct=EBI-348169, EBI-347451;
CC Q6VY07:PACS1; NbExp=3; IntAct=EBI-348169, EBI-2555014;
CC Q96EB6:SIRT1; NbExp=5; IntAct=EBI-348169, EBI-1802965;
CC -!- PTM: Phosphorylated by alpha subunit.
CC -!- SIMILARITY: Belongs to the casein kinase 2 subunit beta family.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI18393.2; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; X16937; CAA34811.1; -; mRNA.
DR EMBL; X16312; CAA34379.1; -; mRNA.
DR EMBL; M30448; AAA52123.1; -; mRNA.
DR EMBL; X57152; CAA40442.1; -; Genomic_DNA.
DR EMBL; AY113186; AAM50092.1; -; mRNA.
DR EMBL; CR541699; CAG46500.1; -; mRNA.
DR EMBL; AF129756; AAD18081.1; -; Genomic_DNA.
DR EMBL; BA000025; BAB63386.1; -; Genomic_DNA.
DR EMBL; DQ314868; ABC40727.1; -; Genomic_DNA.
DR EMBL; AK311860; BAG34801.1; -; mRNA.
DR EMBL; AL662899; CAI96141.1; -; Genomic_DNA.
DR EMBL; AL662899; CAI18393.2; ALT_INIT; Genomic_DNA.
DR EMBL; AL670886; CAI17800.1; -; Genomic_DNA.
DR EMBL; AL805934; CAI18523.1; -; Genomic_DNA.
DR EMBL; BX511262; CAM45825.1; -; Genomic_DNA.
DR EMBL; CR753842; CAQ06572.1; -; Genomic_DNA.
DR EMBL; CR354443; CAQ07002.1; -; Genomic_DNA.
DR EMBL; CR759761; CAQ10879.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03473.1; -; Genomic_DNA.
DR EMBL; BC112017; AAI12018.1; -; mRNA.
DR EMBL; BC112019; AAI12020.1; -; mRNA.
DR PIR; A39459; A39459.
DR RefSeq; NP_001269314.1; NM_001282385.1.
DR RefSeq; NP_001311.3; NM_001320.6.
DR UniGene; Hs.73527; -.
DR PDB; 1DS5; X-ray; 3.16 A; E/F/G/H=181-203.
DR PDB; 1JWH; X-ray; 3.10 A; C/D=1-215.
DR PDB; 1QF8; X-ray; 1.74 A; A/B=1-182.
DR PDB; 3EED; X-ray; 2.80 A; A/B=1-193.
DR PDB; 4DGL; X-ray; 3.00 A; A/B=1-215.
DR PDB; 4MD7; X-ray; 3.10 A; A/B/C/D=1-215.
DR PDB; 4MD8; X-ray; 3.30 A; A/B/C/D=1-215.
DR PDB; 4MD9; X-ray; 3.50 A; A/B/C/D/I/J/N/O=1-215.
DR PDBsum; 1DS5; -.
DR PDBsum; 1JWH; -.
DR PDBsum; 1QF8; -.
DR PDBsum; 3EED; -.
DR PDBsum; 4DGL; -.
DR PDBsum; 4MD7; -.
DR PDBsum; 4MD8; -.
DR PDBsum; 4MD9; -.
DR ProteinModelPortal; P67870; -.
DR SMR; P67870; 7-207.
DR DIP; DIP-131N; -.
DR IntAct; P67870; 174.
DR MINT; MINT-88683; -.
DR STRING; 9606.ENSP00000365025; -.
DR BindingDB; P67870; -.
DR ChEMBL; CHEMBL2358; -.
DR DMDM; 54037520; -.
DR PaxDb; P67870; -.
DR PRIDE; P67870; -.
DR DNASU; 1460; -.
DR Ensembl; ENST00000375865; ENSP00000365025; ENSG00000204435.
DR Ensembl; ENST00000375866; ENSP00000365026; ENSG00000204435.
DR Ensembl; ENST00000375882; ENSP00000365042; ENSG00000204435.
DR Ensembl; ENST00000383427; ENSP00000372919; ENSG00000206406.
DR Ensembl; ENST00000383433; ENSP00000372925; ENSG00000206406.
DR Ensembl; ENST00000400110; ENSP00000382980; ENSG00000206406.
DR Ensembl; ENST00000412802; ENSP00000413469; ENSG00000224774.
DR Ensembl; ENST00000418230; ENSP00000411322; ENSG00000228875.
DR Ensembl; ENST00000422567; ENSP00000407018; ENSG00000224398.
DR Ensembl; ENST00000429633; ENSP00000409510; ENSG00000230700.
DR Ensembl; ENST00000431476; ENSP00000394855; ENSG00000224398.
DR Ensembl; ENST00000436169; ENSP00000412520; ENSG00000224398.
DR Ensembl; ENST00000443673; ENSP00000400188; ENSG00000230700.
DR Ensembl; ENST00000448596; ENSP00000391038; ENSG00000232960.
DR Ensembl; ENST00000451917; ENSP00000415303; ENSG00000224774.
DR Ensembl; ENST00000452985; ENSP00000415237; ENSG00000228875.
DR Ensembl; ENST00000453234; ENSP00000395275; ENSG00000224774.
DR Ensembl; ENST00000454382; ENSP00000390900; ENSG00000232960.
DR Ensembl; ENST00000454511; ENSP00000393756; ENSG00000232960.
DR Ensembl; ENST00000455161; ENSP00000407379; ENSG00000230700.
DR Ensembl; ENST00000458330; ENSP00000410802; ENSG00000228875.
DR GeneID; 1460; -.
DR KEGG; hsa:1460; -.
DR UCSC; uc003nvr.1; human.
DR CTD; 1460; -.
DR GeneCards; GC06P031633; -.
DR GeneCards; GC06Pj31620; -.
DR GeneCards; GC06Pk31615; -.
DR GeneCards; GC06Pl31672; -.
DR GeneCards; GC06Pm31709; -.
DR GeneCards; GC06Pn31623; -.
DR GeneCards; GC06Po31622; -.
DR HGNC; HGNC:2460; CSNK2B.
DR HPA; CAB004349; -.
DR HPA; CAB013087; -.
DR HPA; CAB016059; -.
DR HPA; HPA005944; -.
DR MIM; 115441; gene.
DR neXtProt; NX_P67870; -.
DR PharmGKB; PA26960; -.
DR eggNOG; COG5041; -.
DR HOGENOM; HOG000039270; -.
DR HOVERGEN; HBG051131; -.
DR InParanoid; P67870; -.
DR KO; K03115; -.
DR PhylomeDB; P67870; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR SignaLink; P67870; -.
DR EvolutionaryTrace; P67870; -.
DR GeneWiki; CSNK2B; -.
DR GenomeRNAi; 1460; -.
DR NextBio; 6001; -.
DR PRO; PR:P67870; -.
DR ArrayExpress; P67870; -.
DR Bgee; P67870; -.
DR CleanEx; HS_CSNK2B; -.
DR Genevestigator; P67870; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005956; C:protein kinase CK2 complex; NAS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019887; F:protein kinase regulator activity; NAS:UniProtKB.
DR GO; GO:0033211; P:adiponectin-mediated signaling pathway; IDA:BHF-UCL.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR GO; GO:0043623; P:cellular protein complex assembly; NAS:BHF-UCL.
DR GO; GO:0061154; P:endothelial tube morphogenesis; IMP:BHF-UCL.
DR GO; GO:0000278; P:mitotic cell cycle; TAS:Reactome.
DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IDA:BHF-UCL.
DR GO; GO:0008285; P:negative regulation of cell proliferation; TAS:BHF-UCL.
DR GO; GO:0032927; P:positive regulation of activin receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
DR GO; GO:0051101; P:regulation of DNA binding; NAS:BHF-UCL.
DR GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1820.10; -; 1.
DR Gene3D; 2.20.25.20; -; 1.
DR InterPro; IPR016149; Casein_kin_II_reg-sub_a-hlx.
DR InterPro; IPR016150; Casein_kin_II_reg-sub_b-sht.
DR InterPro; IPR000704; Casein_kinase_II_reg-sub.
DR PANTHER; PTHR11740; PTHR11740; 1.
DR Pfam; PF01214; CK_II_beta; 1.
DR PRINTS; PR00472; CASNKINASEII.
DR SMART; SM01085; CK_II_beta; 1.
DR SUPFAM; SSF57798; SSF57798; 1.
DR PROSITE; PS01101; CK2_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Metal-binding;
KW Phosphoprotein; Reference proteome; Wnt signaling pathway; Zinc.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 215 Casein kinase II subunit beta.
FT /FTId=PRO_0000068236.
FT REGION 188 193 Interaction with alpha subunit (By
FT similarity).
FT COMPBIAS 55 64 Asp/Glu-rich (acidic).
FT METAL 109 109 Zinc.
FT METAL 114 114 Zinc.
FT METAL 137 137 Zinc.
FT METAL 140 140 Zinc.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 2 2 Phosphoserine; by autocatalysis.
FT MOD_RES 3 3 Phosphoserine; by autocatalysis.
FT MOD_RES 209 209 Phosphoserine.
FT MOD_RES 212 212 N6-acetyllysine.
FT CONFLICT 194 194 P -> A (in Ref. 3; AAA52123).
FT HELIX 9 15
FT TURN 17 20
FT HELIX 27 31
FT HELIX 33 36
FT HELIX 39 41
FT STRAND 43 45
FT HELIX 46 53
FT HELIX 67 87
FT HELIX 91 102
FT TURN 103 106
FT HELIX 112 114
FT STRAND 120 122
FT STRAND 134 136
FT TURN 138 140
FT STRAND 142 144
FT HELIX 149 151
FT HELIX 156 158
FT TURN 159 162
FT HELIX 163 170
FT HELIX 172 174
FT STRAND 190 192
FT HELIX 195 198
FT TURN 199 201
FT HELIX 202 205
SQ SEQUENCE 215 AA; 24942 MW; E465B1E699B0E0EC CRC64;
MSSSEEVSWI SWFCGLRGNE FFCEVDEDYI QDKFNLTGLN EQVPHYRQAL DMILDLEPDE
ELEDNPNQSD LIEQAAEMLY GLIHARYILT NRGIAQMLEK YQQGDFGYCP RVYCENQPML
PIGLSDIPGE AMVKLYCPKC MDVYTPKSSR HHHTDGAYFG TGFPHMLFMV HPEYRPKRPA
NQFVPRLYGF KIHPMAYQLQ LQAASNFKSP VKTIR
//
MIM
115441
*RECORD*
*FIELD* NO
115441
*FIELD* TI
*115441 CASEIN KINASE II, BETA; CSNK2B
;;CASEIN KINASE II, BETA SUBUNIT; CK2B;;
PHOSVITIN
read more*FIELD* TX
CLONING
Phosvitin/casein kinase type II (CK2) is a ubiquitous, highly conserved
enzyme consisting of subunits alpha (115440), alpha-prime (115442), and
beta. It is a ubiquitous messenger-independent serine/threonine kinase,
localized in both the cytoplasm and the nucleus. Jakobi et al. (1989)
prepared subunit beta from human placenta and determined the amino acid
sequence of a protease digestion peptide. The deduced nucleotide
sequence was used for the synthesis of a mixture of 20-mers as a
hybridization probe to screen a lambda-gt10 HeLa cell cDNA library for
clones encoding the beta subunit. The beta subunit presumably serves
regulatory functions. Heller-Harrison et al. (1989) found evidence of a
single gene. They described a cDNA of 2.57 kb containing 96 bp of
5-prime untranslated sequence, 645 bp of open reading frame, and 1,832
bp of 3-prime untranslated sequence.
GENE STRUCTURE
Voss et al. (1991) analyzed the structure of the gene encoding human
casein kinase II subunit beta and Boldyreff and Issinger (1995)
determined the structure of the mouse counterpart. The latter is
composed of 7 exons contained within 7,874 bp. The lengths of the mouse
coding exons correspond exactly to the lengths of the exons in the human
CK2B gene. Both genes contain a first untranslated exon. Despite common
features, a striking difference concerned the human CK2A subunit binding
domain at position -170 to -239 of the human gene. This domain has no
counterpart in the mouse gene.
MAPPING
By hybridization to spot-blotting filters of flow-sorted human
chromosomes followed by in situ hybridization, Yang-Feng et al. (1990)
mapped the CSNK2B gene to 6p21.1.
Albertella et al. (1996) characterized the genes in the central 1,100-kb
class III region of the major histocompatibility complex. One of the
genes found in this region was identified as CSNK2B. This would suggest
that CSNK2B is located in the 6p21.3 region rather than the 6p21.1
region.
GENE FUNCTION
Sarno et al. (2000) reported that a C-terminally truncated form of
CK2-beta lacking residues 170 to 215 could not stably associate with the
catalytic CK2 subunits. This CK2-beta mutant retained its central
homodimerization domain and still existed as a dimer. However, the
mutant was defective in a number of other properties mediated by
elements still present in its N-terminal half, notably downregulation of
catalytic activity, autophosphorylation, and responsiveness to
polycationic effectors. All these functions were restored by
simultaneous addition of a synthetic peptide reproducing the CK2-beta
deleted region, which was able to associate with the catalytic subunits
and to stimulate catalytic activity. This peptide includes a segment
that shares similarity with a region of cyclin A (see 604036) involved
in activation of CDK2 (116953), and Sarno et al. (2000) found that a
peptide reproducing this sequence (residues 181 to 203) interacted with
the CK2-alpha subunit and stimulated its catalytic activity. This
smaller peptide also partially restored the ability of truncated
CK2-beta to autophosphorylate. Sarno et al. (2000) concluded that
residues 181 to 203 are essential for the regulatory properties of
CK2-beta.
Phosphorylation of the human p53 protein (191170) at ser392 is
responsive to ultraviolet (UV) but not gamma irradiation. Keller et al.
(2001) identified and purified a mammalian UV-activated protein kinase
complex that phosphorylates ser392 in vitro. This kinase complex
contains CK2 and the chromatin transcriptional elongation factor FACT, a
heterodimer of SPT16 (605012) and SSRP1 (604328). In vitro studies
showed that FACT alters the specificity of CK2 in the complex such that
it selectively phosphorylates p53 over other substrates, including
casein. In addition, phosphorylation by the kinase complex was found to
enhance p53 activity. These results provided a potential mechanism for
p53 activation by UV irradiation.
Doray et al. (2002) demonstrated that the Golgi-localized,
gamma-ear-containing adenosine diphosphate ribosylation factor-binding
proteins (GGA1, 606004 and GGA3, 606006) and the coat protein adaptor
protein-1 (AP-1) complex (see AP1G2, 603534) colocalize in
clathrin-coated buds of the trans-Golgi networks of mouse L cells and
human HeLa cells. Binding studies revealed a direct interaction between
the hinge domains of the GGAs and the gamma-ear domain of AP-1. Further,
AP-1 contained bound casein kinase-2 that phosphorylated GGA1 and GGA3,
thereby causing autoinhibition. Doray et al. (2002) demonstrated that
this autoinhibition could induce the directed transfer of mannose
6-phosphate receptors (see 154540) from the GGAs to AP-1. Mannose
6-phosphate receptors that were defective in binding to GGAs were poorly
incorporated into adaptor protein complex containing clathrin coated
vesicles. Thus, Doray et al. (2002) concluded that GGAs and the AP-1
complex interact to package mannose 6-phosphate receptors into
AP-1-containing coated vesicles.
Rodriguez et al. (2008) stated that, in addition to cytoplasm, nuclei,
and other organelles, CK2 localizes to the external side of the cell
membrane, where it acts as an ectokinase and phosphorylates
extracellular proteins and external domains of proteins. By mutation
analysis, they showed that an N-terminal region of Xenopus Ck2-beta
containing 2 phenylalanines and an acidic cluster was necessary but not
sufficient to allow Ck2-alpha to function as an ectokinase in
transfected HEK293 cells.
*FIELD* RF
1. Albertella, M. R.; Jones, H.; Thomson, W.; Olavesen, M. G.; Campbell,
R. D.: Localization of eight additional genes in the human major
histocompatibility complex, including the gene encoding the casein
kinase II beta subunit (CSNK2B). Genomics 36: 240-251, 1996.
2. Boldyreff, B.; Issinger, O.-G.: Structure of the gene encoding
the murine protein kinase CK2-beta subunit. Genomics 29: 253-256,
1995.
3. Doray, B.; Ghosh, P.; Griffith, J.; Geuze, H. J.; Kornfeld, S.
: Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi
network. Science 297: 1700-1703, 2002.
4. Heller-Harrison, R. A.; Meisner, H.; Czech, M. P.: Cloning and
characterization of a cDNA encoding the beta subunit of human casein
kinase II. Biochemistry 28: 9053-9058, 1989.
5. Jakobi, R.; Voss, H.; Pyerin, W.: Human phosvitin/casein kinase
type II: molecular cloning and sequencing of full-length cDNA encoding
subunit beta. Europ. J. Biochem. 183: 227-233, 1989.
6. Keller, D. M.; Zeng, X.; Wang, Y.; Zhang, Q. H.; Kapoor, M.; Shu,
H.; Goodman, R.; Lozano, G.; Zhao, Y.; Lu, H.: A DNA damage-induced
p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1. Molec.
Cell 7: 283-292, 2001.
7. Rodriguez, F. A.; Contreras, C.; Bolanos-Garcia, V.; Allende, J.
E.: Protein kinase CK2 as an ectokinase: the role of the regulatory
CK2-beta subunit. Proc. Nat. Acad. Sci. 105: 5693-5698, 2008.
8. Sarno, S.; Marin, O.; Boschetti, M.; Pagano, M. A.; Meggio, F.;
Pinna, L. A.: Cooperative modulation of protein kinase CK2 by separate
domains of its regulatory beta-subunit. Biochemistry 39: 12324-12329,
2000.
9. Voss, H.; Wirkner, U.; Jacoki, R.; Hewitt, N. A.; Schwager, C.;
Zimmermann, J.; Ansorge, W.; Pyerin, W.: Structure of the gene encoding
human casein kinase II subunit beta. J. Biol. Chem. 266: 13706-13711,
1991.
10. Yang-Feng, T. L.; Teitz, T.; Cheung, M. C.; Kan, Y. W.; Canaani,
D.: Assignment of the human casein kinase II beta-subunit gene to
6p12-p21. Genomics 8: 741-742, 1990.
*FIELD* CN
Matthew B. Gross - updated: 06/11/2008
Patricia A. Hartz - updated: 6/6/2008
Ada Hamosh - updated: 10/23/2002
Stylianos E. Antonarakis - updated: 3/12/2001
*FIELD* CD
Victor A. McKusick: 11/22/1989
*FIELD* ED
mgross: 06/11/2008
terry: 6/6/2008
mgross: 9/18/2003
alopez: 10/23/2002
mgross: 3/12/2001
psherman: 10/22/1999
mark: 1/19/1998
mark: 10/9/1996
terry: 10/9/1996
terry: 10/30/1995
mark: 10/2/1995
supermim: 3/16/1992
carol: 1/2/1991
carol: 12/14/1990
carol: 10/26/1990
*RECORD*
*FIELD* NO
115441
*FIELD* TI
*115441 CASEIN KINASE II, BETA; CSNK2B
;;CASEIN KINASE II, BETA SUBUNIT; CK2B;;
PHOSVITIN
read more*FIELD* TX
CLONING
Phosvitin/casein kinase type II (CK2) is a ubiquitous, highly conserved
enzyme consisting of subunits alpha (115440), alpha-prime (115442), and
beta. It is a ubiquitous messenger-independent serine/threonine kinase,
localized in both the cytoplasm and the nucleus. Jakobi et al. (1989)
prepared subunit beta from human placenta and determined the amino acid
sequence of a protease digestion peptide. The deduced nucleotide
sequence was used for the synthesis of a mixture of 20-mers as a
hybridization probe to screen a lambda-gt10 HeLa cell cDNA library for
clones encoding the beta subunit. The beta subunit presumably serves
regulatory functions. Heller-Harrison et al. (1989) found evidence of a
single gene. They described a cDNA of 2.57 kb containing 96 bp of
5-prime untranslated sequence, 645 bp of open reading frame, and 1,832
bp of 3-prime untranslated sequence.
GENE STRUCTURE
Voss et al. (1991) analyzed the structure of the gene encoding human
casein kinase II subunit beta and Boldyreff and Issinger (1995)
determined the structure of the mouse counterpart. The latter is
composed of 7 exons contained within 7,874 bp. The lengths of the mouse
coding exons correspond exactly to the lengths of the exons in the human
CK2B gene. Both genes contain a first untranslated exon. Despite common
features, a striking difference concerned the human CK2A subunit binding
domain at position -170 to -239 of the human gene. This domain has no
counterpart in the mouse gene.
MAPPING
By hybridization to spot-blotting filters of flow-sorted human
chromosomes followed by in situ hybridization, Yang-Feng et al. (1990)
mapped the CSNK2B gene to 6p21.1.
Albertella et al. (1996) characterized the genes in the central 1,100-kb
class III region of the major histocompatibility complex. One of the
genes found in this region was identified as CSNK2B. This would suggest
that CSNK2B is located in the 6p21.3 region rather than the 6p21.1
region.
GENE FUNCTION
Sarno et al. (2000) reported that a C-terminally truncated form of
CK2-beta lacking residues 170 to 215 could not stably associate with the
catalytic CK2 subunits. This CK2-beta mutant retained its central
homodimerization domain and still existed as a dimer. However, the
mutant was defective in a number of other properties mediated by
elements still present in its N-terminal half, notably downregulation of
catalytic activity, autophosphorylation, and responsiveness to
polycationic effectors. All these functions were restored by
simultaneous addition of a synthetic peptide reproducing the CK2-beta
deleted region, which was able to associate with the catalytic subunits
and to stimulate catalytic activity. This peptide includes a segment
that shares similarity with a region of cyclin A (see 604036) involved
in activation of CDK2 (116953), and Sarno et al. (2000) found that a
peptide reproducing this sequence (residues 181 to 203) interacted with
the CK2-alpha subunit and stimulated its catalytic activity. This
smaller peptide also partially restored the ability of truncated
CK2-beta to autophosphorylate. Sarno et al. (2000) concluded that
residues 181 to 203 are essential for the regulatory properties of
CK2-beta.
Phosphorylation of the human p53 protein (191170) at ser392 is
responsive to ultraviolet (UV) but not gamma irradiation. Keller et al.
(2001) identified and purified a mammalian UV-activated protein kinase
complex that phosphorylates ser392 in vitro. This kinase complex
contains CK2 and the chromatin transcriptional elongation factor FACT, a
heterodimer of SPT16 (605012) and SSRP1 (604328). In vitro studies
showed that FACT alters the specificity of CK2 in the complex such that
it selectively phosphorylates p53 over other substrates, including
casein. In addition, phosphorylation by the kinase complex was found to
enhance p53 activity. These results provided a potential mechanism for
p53 activation by UV irradiation.
Doray et al. (2002) demonstrated that the Golgi-localized,
gamma-ear-containing adenosine diphosphate ribosylation factor-binding
proteins (GGA1, 606004 and GGA3, 606006) and the coat protein adaptor
protein-1 (AP-1) complex (see AP1G2, 603534) colocalize in
clathrin-coated buds of the trans-Golgi networks of mouse L cells and
human HeLa cells. Binding studies revealed a direct interaction between
the hinge domains of the GGAs and the gamma-ear domain of AP-1. Further,
AP-1 contained bound casein kinase-2 that phosphorylated GGA1 and GGA3,
thereby causing autoinhibition. Doray et al. (2002) demonstrated that
this autoinhibition could induce the directed transfer of mannose
6-phosphate receptors (see 154540) from the GGAs to AP-1. Mannose
6-phosphate receptors that were defective in binding to GGAs were poorly
incorporated into adaptor protein complex containing clathrin coated
vesicles. Thus, Doray et al. (2002) concluded that GGAs and the AP-1
complex interact to package mannose 6-phosphate receptors into
AP-1-containing coated vesicles.
Rodriguez et al. (2008) stated that, in addition to cytoplasm, nuclei,
and other organelles, CK2 localizes to the external side of the cell
membrane, where it acts as an ectokinase and phosphorylates
extracellular proteins and external domains of proteins. By mutation
analysis, they showed that an N-terminal region of Xenopus Ck2-beta
containing 2 phenylalanines and an acidic cluster was necessary but not
sufficient to allow Ck2-alpha to function as an ectokinase in
transfected HEK293 cells.
*FIELD* RF
1. Albertella, M. R.; Jones, H.; Thomson, W.; Olavesen, M. G.; Campbell,
R. D.: Localization of eight additional genes in the human major
histocompatibility complex, including the gene encoding the casein
kinase II beta subunit (CSNK2B). Genomics 36: 240-251, 1996.
2. Boldyreff, B.; Issinger, O.-G.: Structure of the gene encoding
the murine protein kinase CK2-beta subunit. Genomics 29: 253-256,
1995.
3. Doray, B.; Ghosh, P.; Griffith, J.; Geuze, H. J.; Kornfeld, S.
: Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi
network. Science 297: 1700-1703, 2002.
4. Heller-Harrison, R. A.; Meisner, H.; Czech, M. P.: Cloning and
characterization of a cDNA encoding the beta subunit of human casein
kinase II. Biochemistry 28: 9053-9058, 1989.
5. Jakobi, R.; Voss, H.; Pyerin, W.: Human phosvitin/casein kinase
type II: molecular cloning and sequencing of full-length cDNA encoding
subunit beta. Europ. J. Biochem. 183: 227-233, 1989.
6. Keller, D. M.; Zeng, X.; Wang, Y.; Zhang, Q. H.; Kapoor, M.; Shu,
H.; Goodman, R.; Lozano, G.; Zhao, Y.; Lu, H.: A DNA damage-induced
p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1. Molec.
Cell 7: 283-292, 2001.
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*FIELD* CN
Matthew B. Gross - updated: 06/11/2008
Patricia A. Hartz - updated: 6/6/2008
Ada Hamosh - updated: 10/23/2002
Stylianos E. Antonarakis - updated: 3/12/2001
*FIELD* CD
Victor A. McKusick: 11/22/1989
*FIELD* ED
mgross: 06/11/2008
terry: 6/6/2008
mgross: 9/18/2003
alopez: 10/23/2002
mgross: 3/12/2001
psherman: 10/22/1999
mark: 1/19/1998
mark: 10/9/1996
terry: 10/9/1996
terry: 10/30/1995
mark: 10/2/1995
supermim: 3/16/1992
carol: 1/2/1991
carol: 12/14/1990
carol: 10/26/1990