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Casein kinase II subunit beta (CK II beta) (Phosvitin) (Protein G5a)

 CSK2B_HUMAN             Reviewed;         215 AA.
P67870; B0UXA9; P07312; P13862; Q4VX47;
11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 1.
30-AUG-2017, entry version 152.
RecName: Full=Casein kinase II subunit beta;
Short=CK II beta;
AltName: Full=Phosvitin;
AltName: Full=Protein G5a;
Name=CSNK2B; Synonyms=CK2N, G5A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2666134; DOI=10.1111/j.1432-1033.1989.tb14917.x;
Jakobi R., Voss H., Pyerin W.;
"Human phosvitin/casein kinase type II. Molecular cloning and
sequencing of full-length cDNA encoding subunit beta.";
Eur. J. Biochem. 183:227-233(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1694965; DOI=10.1016/0921-8777(90)90036-5;
Teitz T., Eli D., Penner M., Bakhanashvili M., Naiman T., Timme T.L.,
Wood C.M., Moses R.E., Canaani D.;
"Expression of the cDNA for the beta subunit of human casein kinase II
confers partial UV resistance on xeroderma pigmentosum cells.";
Mutat. Res. 236:85-97(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2513884; DOI=10.1021/bi00449a014;
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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1856204;
Voss A., Wirkner U., Jacobi R., Hewitt N., 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).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=12102635; DOI=10.1021/bi025791r;
Singh L.S., Kalafatis M.;
"Sequencing of full-length cDNA encoding the alpha and beta subunits
of human casein kinase II from human platelets and megakaryocytic
cells. Expression of the casein kinase IIalpha intronless gene in a
megakaryocytic cell line.";
Biochemistry 41:8935-8940(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14656967; DOI=10.1101/gr.1736803;
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
Campbell R.D., Hood L.;
"Analysis of the gene-dense major histocompatibility complex class III
region and its comparison to mouse.";
Genome Res. 13:2621-2636(2003).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Shiina S., Tamiya G., Oka A., Inoko H.;
"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[14]
PHOSPHORYLATION.
PubMed=2300566; DOI=10.1073/pnas.87.2.821;
Ackerman P., Glover C.V., Osheroff N.;
"Stimulation of casein kinase II by epidermal growth factor:
relationship between the physiological activity of the kinase and the
phosphorylation state of its beta subunit.";
Proc. Natl. Acad. Sci. U.S.A. 87:821-825(1990).
[15]
INTERACTION WITH CD163.
PubMed=11298324;
DOI=10.1002/1521-4141(200104)31:4<999::AID-IMMU999>3.0.CO;2-R;
Ritter M., Buechler C., Kapinsky M., Schmitz G.;
"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. 31:999-1009(2001).
[16]
FUNCTION, AND INTERACTION WITH SSRP1 AND SUPT16H.
PubMed=11239457; DOI=10.1016/S1097-2765(01)00176-9;
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.";
Mol. Cell 7:283-292(2001).
[17]
INTERACTION WITH FGF1.
PubMed=11964394; DOI=10.1074/jbc.M112193200;
Skjerpen C.S., Wesche J., Olsnes S.;
"Identification of ribosome-binding protein p34 as an intracellular
protein that binds acidic fibroblast growth factor.";
J. Biol. Chem. 277:23864-23871(2002).
[18]
INTERACTION WITH SSRP1 AND SUPT16H.
PubMed=12393879; DOI=10.1074/jbc.M209820200;
Keller D.M., Lu H.;
"p53 serine 392 phosphorylation increases after UV through induction
of the assembly of the CK2.hSPT16.SSRP1 complex.";
J. Biol. Chem. 277:50206-50213(2002).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[20]
FUNCTION IN PHOSPHORYLATION OF MUSK, AND INTERACTION WITH MUSK.
PubMed=16818610; DOI=10.1101/gad.375206;
Cheusova T., Khan M.A., Schubert S.W., Gavin A.C., Buchou T.,
Jacob G., Sticht H., Allende J., Boldyreff B., Brenner H.R.,
Hashemolhosseini S.;
"Casein kinase 2-dependent serine phosphorylation of MuSK regulates
acetylcholine receptor aggregation at the neuromuscular junction.";
Genes Dev. 20:1800-1816(2006).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-69 AND SER-209,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[23]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-209, CLEAVAGE OF INITIATOR METHIONINE [LARGE
SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[24]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-212, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[25]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-209, CLEAVAGE OF INITIATOR METHIONINE [LARGE
SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[27]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-209, CLEAVAGE OF INITIATOR METHIONINE [LARGE
SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-37 AND SER-209, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[30]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-212, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[32]
X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 1-182, SUBUNIT, AND
ZINC-BINDING SITES.
PubMed=10357806; DOI=10.1093/emboj/18.11.2930;
Chantalat L., Leroy D., Filhol O., Nueda A., Benitez M.J.,
Chambaz E.M., Cochet C., Dideberg O.;
"Crystal structure of the human protein kinase CK2 regulatory subunit
reveals its zinc finger-mediated dimerization.";
EMBO J. 18:2930-2940(1999).
[33]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH CSNK2A1,
ZINC-BINDING SITES, SUBUNIT, AND PHOSPHORYLATION AT SER-2 AND SER-3.
PubMed=11574463; DOI=10.1093/emboj/20.19.5320;
Niefind K., Guerra B., Ermakowa I., Issinger O.G.;
"Crystal structure of human protein kinase CK2: insights into basic
properties of the CK2 holoenzyme.";
EMBO J. 20:5320-5331(2001).
-!- FUNCTION: Participates in Wnt signaling (By similarity). Plays a
complex role in regulating the basal catalytic activity of the
alpha subunit. {ECO:0000250, ECO:0000269|PubMed:11239457,
ECO:0000269|PubMed:16818610}.
-!- SUBUNIT: Tetramer composed of an alpha subunit, an alpha' subunit
and two beta subunits. The beta subunit dimerization is mediated
by zinc ions. Interacts with TCTEX1D3 (By similarity). Interacts
with CD163. Also component of a CK2-SPT16-SSRP1 complex composed
of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, the complex
associating following UV irradiation. Interacts with MUSK;
mediates phosphorylation of MUSK by CK2. Interacts with FGF1; this
interaction is increased in the presence of FIBP, suggesting a
possible cooperative interaction between CSNKB and FIBP in binding
to FGF1. {ECO:0000250, ECO:0000269|PubMed:10357806,
ECO:0000269|PubMed:11239457, ECO:0000269|PubMed:11298324,
ECO:0000269|PubMed:11574463, ECO:0000269|PubMed:11964394,
ECO:0000269|PubMed:12393879, ECO:0000269|PubMed:16818610}.
-!- INTERACTION:
Self; NbExp=7; IntAct=EBI-348169, EBI-348169;
O00555:CACNA1A; NbExp=2; IntAct=EBI-348169, EBI-766279;
O00257-3:CBX4; NbExp=2; IntAct=EBI-348169, EBI-4392727;
Q9JK25:Clip1 (xeno); NbExp=2; IntAct=EBI-348169, EBI-908338;
O08785:Clock (xeno); NbExp=2; IntAct=EBI-348169, EBI-79859;
P68400:CSNK2A1; NbExp=19; IntAct=EBI-348169, EBI-347804;
P19784:CSNK2A2; NbExp=10; IntAct=EBI-348169, EBI-347451;
P09067:HOXB5; NbExp=4; IntAct=EBI-348169, EBI-3893317;
Q9C086:INO80B; NbExp=4; IntAct=EBI-348169, EBI-715611;
Q6VY07:PACS1; NbExp=3; IntAct=EBI-348169, EBI-2555014;
Q99496:RNF2; NbExp=2; IntAct=EBI-348169, EBI-722416;
Q96EB6:SIRT1; NbExp=5; IntAct=EBI-348169, EBI-1802965;
Q9NZC7-5:WWOX; NbExp=4; IntAct=EBI-348169, EBI-12040603;
Q86VK4-3:ZNF410; NbExp=4; IntAct=EBI-348169, EBI-11741890;
-!- PTM: Phosphorylated by alpha subunit.
{ECO:0000269|PubMed:11574463, ECO:0000269|PubMed:2300566}.
-!- SIMILARITY: Belongs to the casein kinase 2 subunit beta family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAI18393.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; X16937; CAA34811.1; -; mRNA.
EMBL; X16312; CAA34379.1; -; mRNA.
EMBL; M30448; AAA52123.1; -; mRNA.
EMBL; X57152; CAA40442.1; -; Genomic_DNA.
EMBL; AY113186; AAM50092.1; -; mRNA.
EMBL; CR541699; CAG46500.1; -; mRNA.
EMBL; AF129756; AAD18081.1; -; Genomic_DNA.
EMBL; BA000025; BAB63386.1; -; Genomic_DNA.
EMBL; DQ314868; ABC40727.1; -; Genomic_DNA.
EMBL; AK311860; BAG34801.1; -; mRNA.
EMBL; AL662899; CAI96141.1; -; Genomic_DNA.
EMBL; AL662899; CAI18393.2; ALT_INIT; Genomic_DNA.
EMBL; AL670886; CAI17800.1; -; Genomic_DNA.
EMBL; AL805934; CAI18523.1; -; Genomic_DNA.
EMBL; BX511262; CAM45825.1; -; Genomic_DNA.
EMBL; CR753842; CAQ06572.1; -; Genomic_DNA.
EMBL; CR354443; CAQ07002.1; -; Genomic_DNA.
EMBL; CR759761; CAQ10879.1; -; Genomic_DNA.
EMBL; CH471081; EAX03473.1; -; Genomic_DNA.
EMBL; BC112017; AAI12018.1; -; mRNA.
EMBL; BC112019; AAI12020.1; -; mRNA.
CCDS; CCDS4712.1; -.
PIR; A39459; A39459.
RefSeq; NP_001269314.1; NM_001282385.1.
RefSeq; NP_001311.3; NM_001320.6.
UniGene; Hs.73527; -.
PDB; 1DS5; X-ray; 3.16 A; E/F/G/H=181-203.
PDB; 1JWH; X-ray; 3.10 A; C/D=1-215.
PDB; 1QF8; X-ray; 1.74 A; A/B=1-182.
PDB; 3EED; X-ray; 2.80 A; A/B=1-193.
PDB; 4DGL; X-ray; 3.00 A; A/B=1-215.
PDB; 4MD7; X-ray; 3.10 A; A/B/C/D=1-215.
PDB; 4MD8; X-ray; 3.30 A; A/B/C/D=1-215.
PDB; 4MD9; X-ray; 3.50 A; A/B/C/D/I/J/N/O=1-215.
PDB; 4NH1; X-ray; 3.30 A; C/D=1-215.
PDBsum; 1DS5; -.
PDBsum; 1JWH; -.
PDBsum; 1QF8; -.
PDBsum; 3EED; -.
PDBsum; 4DGL; -.
PDBsum; 4MD7; -.
PDBsum; 4MD8; -.
PDBsum; 4MD9; -.
PDBsum; 4NH1; -.
ProteinModelPortal; P67870; -.
SMR; P67870; -.
BioGrid; 107843; 320.
DIP; DIP-131N; -.
IntAct; P67870; 208.
MINT; MINT-88683; -.
STRING; 9606.ENSP00000365025; -.
BindingDB; P67870; -.
ChEMBL; CHEMBL2358; -.
iPTMnet; P67870; -.
PhosphoSitePlus; P67870; -.
DMDM; 54037520; -.
EPD; P67870; -.
MaxQB; P67870; -.
PaxDb; P67870; -.
PeptideAtlas; P67870; -.
PRIDE; P67870; -.
DNASU; 1460; -.
Ensembl; ENST00000375865; ENSP00000365025; ENSG00000204435.
Ensembl; ENST00000375866; ENSP00000365026; ENSG00000204435.
Ensembl; ENST00000375882; ENSP00000365042; ENSG00000204435.
Ensembl; ENST00000383427; ENSP00000372919; ENSG00000206406.
Ensembl; ENST00000383433; ENSP00000372925; ENSG00000206406.
Ensembl; ENST00000400110; ENSP00000382980; ENSG00000206406.
Ensembl; ENST00000412802; ENSP00000413469; ENSG00000224774.
Ensembl; ENST00000418230; ENSP00000411322; ENSG00000228875.
Ensembl; ENST00000422567; ENSP00000407018; ENSG00000224398.
Ensembl; ENST00000429633; ENSP00000409510; ENSG00000230700.
Ensembl; ENST00000431476; ENSP00000394855; ENSG00000224398.
Ensembl; ENST00000436169; ENSP00000412520; ENSG00000224398.
Ensembl; ENST00000443673; ENSP00000400188; ENSG00000230700.
Ensembl; ENST00000448596; ENSP00000391038; ENSG00000232960.
Ensembl; ENST00000451917; ENSP00000415303; ENSG00000224774.
Ensembl; ENST00000452985; ENSP00000415237; ENSG00000228875.
Ensembl; ENST00000453234; ENSP00000395275; ENSG00000224774.
Ensembl; ENST00000454382; ENSP00000390900; ENSG00000232960.
Ensembl; ENST00000454511; ENSP00000393756; ENSG00000232960.
Ensembl; ENST00000455161; ENSP00000407379; ENSG00000230700.
Ensembl; ENST00000458330; ENSP00000410802; ENSG00000228875.
GeneID; 1460; -.
KEGG; hsa:1460; -.
UCSC; uc003nvr.3; human.
CTD; 1460; -.
DisGeNET; 1460; -.
GeneCards; CSNK2B; -.
HGNC; HGNC:2460; CSNK2B.
HPA; CAB004349; -.
HPA; CAB013087; -.
HPA; CAB016059; -.
HPA; HPA005944; -.
MIM; 115441; gene.
neXtProt; NX_P67870; -.
OpenTargets; ENSG00000204435; -.
PharmGKB; PA26960; -.
eggNOG; KOG3092; Eukaryota.
eggNOG; COG5041; LUCA.
GeneTree; ENSGT00390000003781; -.
HOGENOM; HOG000039270; -.
HOVERGEN; HBG051131; -.
InParanoid; P67870; -.
KO; K03115; -.
PhylomeDB; P67870; -.
TreeFam; TF314462; -.
Reactome; R-HSA-1483191; Synthesis of PC.
Reactome; R-HSA-201688; WNT mediated activation of DVL.
Reactome; R-HSA-2514853; Condensation of Prometaphase Chromosomes.
Reactome; R-HSA-445144; Signal transduction by L1.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-HSA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
Reactome; R-HSA-8934903; Receptor Mediated Mitophagy.
SignaLink; P67870; -.
SIGNOR; P67870; -.
EvolutionaryTrace; P67870; -.
GeneWiki; CSNK2B; -.
GenomeRNAi; 1460; -.
PRO; PR:P67870; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000204435; -.
CleanEx; HS_CSNK2B; -.
ExpressionAtlas; P67870; baseline and differential.
Genevisible; P67870; HS.
GO; GO:0000785; C:chromatin; IEA:Ensembl.
GO; GO:0005929; C:cilium; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0016363; C:nuclear matrix; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0005956; C:protein kinase CK2 complex; IDA:CAFA.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0019887; F:protein kinase regulator activity; NAS:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:CAFA.
GO; GO:0005102; F:receptor binding; IPI:BHF-UCL.
GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:Ensembl.
GO; GO:0008134; F:transcription factor binding; IPI:BHF-UCL.
GO; GO:0033211; P:adiponectin-activated signaling pathway; IDA:BHF-UCL.
GO; GO:0043623; P:cellular protein complex assembly; NAS:BHF-UCL.
GO; GO:0061154; P:endothelial tube morphogenesis; IMP:BHF-UCL.
GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
GO; GO:0016236; P:macroautophagy; TAS:Reactome.
GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IDA:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell proliferation; TAS:BHF-UCL.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:CAFA.
GO; GO:0006656; P:phosphatidylcholine biosynthetic process; TAS:Reactome.
GO; GO:0032927; P:positive regulation of activin receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
GO; GO:0006457; P:protein folding; TAS:Reactome.
GO; GO:0051101; P:regulation of DNA binding; NAS:BHF-UCL.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
Gene3D; 1.10.1820.10; -; 1.
InterPro; IPR016149; Casein_kin_II_reg-sub_a-hlx.
InterPro; IPR000704; Casein_kinase_II_reg-sub.
PANTHER; PTHR11740; PTHR11740; 1.
Pfam; PF01214; CK_II_beta; 1.
PRINTS; PR00472; CASNKINASEII.
SMART; SM01085; CK_II_beta; 1.
SUPFAM; SSF57798; SSF57798; 1.
PROSITE; PS01101; CK2_BETA; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Isopeptide bond;
Metal-binding; Phosphoprotein; Reference proteome; Ubl conjugation;
Wnt signaling pathway; Zinc.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
CHAIN 2 215 Casein kinase II subunit beta.
/FTId=PRO_0000068236.
REGION 188 193 Interaction with alpha subunit.
{ECO:0000250}.
COMPBIAS 55 64 Asp/Glu-rich (acidic).
METAL 109 109 Zinc.
METAL 114 114 Zinc.
METAL 137 137 Zinc.
METAL 140 140 Zinc.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 2 2 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:11574463}.
MOD_RES 3 3 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:11574463}.
MOD_RES 8 8 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 37 37 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 69 69 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 209 209 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 212 212 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
CROSSLNK 212 212 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25755297}.
CONFLICT 194 194 P -> A (in Ref. 3; AAA52123).
{ECO:0000305}.
HELIX 9 15 {ECO:0000244|PDB:1QF8}.
TURN 17 20 {ECO:0000244|PDB:1JWH}.
HELIX 27 31 {ECO:0000244|PDB:1QF8}.
HELIX 33 36 {ECO:0000244|PDB:1QF8}.
HELIX 39 41 {ECO:0000244|PDB:1QF8}.
STRAND 43 45 {ECO:0000244|PDB:4DGL}.
HELIX 46 53 {ECO:0000244|PDB:1QF8}.
STRAND 59 61 {ECO:0000244|PDB:4NH1}.
HELIX 67 87 {ECO:0000244|PDB:1QF8}.
HELIX 91 102 {ECO:0000244|PDB:1QF8}.
TURN 103 106 {ECO:0000244|PDB:1QF8}.
HELIX 112 114 {ECO:0000244|PDB:1QF8}.
STRAND 120 122 {ECO:0000244|PDB:1QF8}.
STRAND 134 136 {ECO:0000244|PDB:1QF8}.
TURN 138 140 {ECO:0000244|PDB:1QF8}.
STRAND 142 144 {ECO:0000244|PDB:3EED}.
HELIX 149 151 {ECO:0000244|PDB:1QF8}.
STRAND 152 155 {ECO:0000244|PDB:4MD7}.
HELIX 156 158 {ECO:0000244|PDB:1QF8}.
TURN 159 162 {ECO:0000244|PDB:4DGL}.
HELIX 163 170 {ECO:0000244|PDB:1QF8}.
HELIX 172 174 {ECO:0000244|PDB:1QF8}.
STRAND 187 189 {ECO:0000244|PDB:4MD9}.
STRAND 190 192 {ECO:0000244|PDB:4DGL}.
HELIX 195 198 {ECO:0000244|PDB:4DGL}.
TURN 199 201 {ECO:0000244|PDB:4DGL}.
HELIX 202 205 {ECO:0000244|PDB:4DGL}.
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


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