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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.
13-FEB-2019, entry version 166.
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;
Q9WTL8:Arntl (xeno); NbExp=4; IntAct=EBI-348169, EBI-644534;
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;
P97784:Cry1 (xeno); NbExp=2; IntAct=EBI-348169, EBI-1266607;
P68400:CSNK2A1; NbExp=26; IntAct=EBI-348169, EBI-347804;
P19784:CSNK2A2; NbExp=10; IntAct=EBI-348169, EBI-347451;
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;
-!- 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}.
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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; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL670886; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL805934; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX511262; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR354443; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR753842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR759761; -; NOT_ANNOTATED_CDS; 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; 333.
CORUM; P67870; -.
DIP; DIP-131N; -.
IntAct; P67870; 219.
MINT; P67870; -.
STRING; 9606.ENSP00000365025; -.
BindingDB; P67870; -.
ChEMBL; CHEMBL2358; -.
MoonDB; P67870; Predicted.
iPTMnet; P67870; -.
PhosphoSitePlus; P67870; -.
BioMuta; CSNK2B; -.
DMDM; 54037520; -.
EPD; P67870; -.
jPOST; P67870; -.
MaxQB; P67870; -.
PaxDb; P67870; -.
PeptideAtlas; P67870; -.
PRIDE; P67870; -.
ProteomicsDB; 57524; -.
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; -.
EuPathDB; HostDB:ENSG00000204435.13; -.
GeneCards; CSNK2B; -.
HGNC; HGNC:2460; CSNK2B.
HPA; CAB004349; -.
HPA; CAB013087; -.
HPA; CAB016059; -.
HPA; HPA005944; -.
MalaCards; CSNK2B; -.
MIM; 115441; gene.
neXtProt; NX_P67870; -.
OpenTargets; ENSG00000204435; -.
Orphanet; 178469; Autosomal dominant non-syndromic intellectual disability.
PharmGKB; PA26960; -.
eggNOG; KOG3092; Eukaryota.
eggNOG; COG5041; LUCA.
GeneTree; ENSGT00390000003781; -.
HOGENOM; HOG000039270; -.
HOVERGEN; HBG051131; -.
InParanoid; P67870; -.
KO; K03115; -.
OrthoDB; 1335521at2759; -.
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.
Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
SignaLink; P67870; -.
SIGNOR; P67870; -.
ChiTaRS; CSNK2B; human.
EvolutionaryTrace; P67870; -.
GeneWiki; CSNK2B; -.
GenomeRNAi; 1460; -.
PRO; PR:P67870; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000204435; Expressed in 86 organ(s), highest expression level in right testis.
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; HDA: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; IBA:GO_Central.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:CAFA.
GO; GO:0043021; F:ribonucleoprotein complex binding; IBA:GO_Central.
GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL.
GO; GO:0008134; F:transcription factor binding; IPI:BHF-UCL.
GO; GO:0033211; P:adiponectin-activated signaling pathway; IDA:BHF-UCL.
GO; GO:0034622; P:cellular protein-containing complex assembly; NAS:BHF-UCL.
GO; GO:0061154; P:endothelial tube morphogenesis; IMP:BHF-UCL.
GO; GO:0097421; P:liver regeneration; IBA:GO_Central.
GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IDA:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:BHF-UCL.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:CAFA.
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: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; IBA:GO_Central.
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_N.
InterPro; IPR035991; Casein_kinase_II_beta_like.
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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Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP1566: Citrate cycle (TCA cycle)
WP1614: 1- and 2-Methylnaphthalene degradation
WP1655: Geraniol degradation
WP210: Cytoplasmic Ribosomal Proteins
WP2218: sGC
WP32: Translation Factors
WP1045: TGF-beta Receptor Signaling Pathway
WP1048: TGF Beta Signaling Pathway
WP105: Fatty Acid Beta Oxidation 2
WP1058: Senescence and Autophagy
WP1061: Fatty Acid Beta Oxidation
WP1106: Keap1-Nrf2
WP1107: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP113: TGF Beta Signaling Pathway
WP1161: TGF-beta Receptor Signaling Pathway
WP1164: TGF Beta Signaling Pathway
WP1177: Fatty Acid Beta Oxidation
WP1207: Fatty Acid Beta Oxidation
WP1224: EBV LMP1 signaling
WP1225: estrogen signalling
WP1226: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1237: Fatty Acid Beta Oxidation
WP126: Fatty Acid Beta Oxidation 1
WP1269: Fatty Acid Beta Oxidation
WP1307: Fatty Acid Beta Oxidation

Related Genes :
[CKB2 YOR039W OR26.32] Casein kinase II subunit beta' (CK II beta')
[CSNK2A1 CK2A1] Casein kinase II subunit alpha (CK II alpha) (EC 2.7.11.1)
[CSNK2A2 CK2A2] Casein kinase II subunit alpha' (CK II alpha') (EC 2.7.11.1)
[snrp-200 Y46G5A.4] Putative U5 small nuclear ribonucleoprotein 200 kDa helicase (EC 3.6.4.13)
[Csnk2a1] Casein kinase II subunit alpha (CK II alpha) (EC 2.7.11.1)
[Csnk2a1 Ckiia] Casein kinase II subunit alpha (CK II alpha) (EC 2.7.11.1)
[CSNK2A3 CSNK2A1P] Casein kinase II subunit alpha 3 (CK II alpha 3) (EC 2.7.11.1) (Casein kinase II alpha 1 polypeptide pseudogene)
[Csnk2a2] Casein kinase II subunit alpha' (CK II alpha') (EC 2.7.11.1)
[cka1 orb5 SPAC23C11.11] Casein kinase II subunit alpha (CK II subunit alpha) (EC 2.7.11.1)
[dprE1 MSMEG_6382 MSMEI_6214 LJ00_31545] Decaprenylphosphoryl-beta-D-ribose oxidase (EC 1.1.98.3) (Decaprenylphospho-beta-D-ribofuranose 2-dehydrogenase) (Decaprenylphosphoryl-beta-D-ribofuranose 2'-epimerase subunit DprE1) (Decaprenyl-phosphoribose 2'-epimerase subunit 1) (Decaprenylphosphoryl-beta-D-ribofuranose 2'-oxidase) (Decaprenylphosphoryl-beta-D-ribose 2-epimerase flavoprotein subunit) (FAD-dependent decaprenylphosphoryl-beta-D-ribofuranose 2-oxidase)
[CSNK2A1 CK2A1] Casein kinase II subunit alpha (CK II alpha) (EC 2.7.11.1)
[Rack1 Gnb2-rs1 Gnb2l1] Receptor of activated protein C kinase 1 (12-3) (Guanine nucleotide-binding protein subunit beta-2-like 1) (Receptor for activated C kinase) (Receptor of activated protein kinase C 1) (p205) [Cleaved into: Receptor of activated protein C kinase 1, N-terminally processed (Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed)]
[CSNK1D HCKID] Casein kinase I isoform delta (CKI-delta) (CKId) (EC 2.7.11.1) (Tau-protein kinase CSNK1D) (EC 2.7.11.26)
[PIK3R2] Phosphatidylinositol 3-kinase regulatory subunit beta (PI3-kinase regulatory subunit beta) (PI3K regulatory subunit beta) (PtdIns-3-kinase regulatory subunit beta) (Phosphatidylinositol 3-kinase 85 kDa regulatory subunit beta) (PI3-kinase subunit p85-beta) (PtdIns-3-kinase regulatory subunit p85-beta)
[RACK1 GNB2L1 HLC7 PIG21] Receptor of activated protein C kinase 1 (Cell proliferation-inducing gene 21 protein) (Guanine nucleotide-binding protein subunit beta-2-like 1) (Guanine nucleotide-binding protein subunit beta-like protein 12.3) (Human lung cancer oncogene 7 protein) (HLC-7) (Receptor for activated C kinase) (Small ribosomal subunit protein RACK1) [Cleaved into: Receptor of activated protein C kinase 1, N-terminally processed (Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed)]
[Pik3r2] Phosphatidylinositol 3-kinase regulatory subunit beta (PI3-kinase regulatory subunit beta) (PI3K regulatory subunit beta) (PtdIns-3-kinase regulatory subunit beta) (Phosphatidylinositol 3-kinase 85 kDa regulatory subunit beta) (PI3-kinase subunit p85-beta) (PtdIns-3-kinase regulatory subunit p85-beta)
[Cbfb Pebp2b Pebpb2] Core-binding factor subunit beta (CBF-beta) (Polyomavirus enhancer-binding protein 2 beta subunit) (PEA2-beta) (PEBP2-beta) (SL3-3 enhancer factor 1 subunit beta) (SL3/AKV core-binding factor beta subunit)
[B4GALT1 GGTB2] Beta-1,4-galactosyltransferase 1 (Beta-1,4-GalTase 1) (Beta4Gal-T1) (b4Gal-T1) (EC 2.4.1.-) (Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase) (Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase) (EC 2.4.1.38) (Lactose synthase A protein) (EC 2.4.1.22) (N-acetyllactosamine synthase) (EC 2.4.1.90) (Nal synthase) (UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 1) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 1) [Cleaved into: Processed beta-1,4-galactosyltransferase 1]
[IKBKB IKKB] Inhibitor of nuclear factor kappa-B kinase subunit beta (I-kappa-B-kinase beta) (IKK-B) (IKK-beta) (IkBKB) (EC 2.7.11.10) (I-kappa-B kinase 2) (IKK2) (Nuclear factor NF-kappa-B inhibitor kinase beta) (NFKBIKB)
[PIK3CB PIK3C1] Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform (PI3-kinase subunit beta) (PI3K-beta) (PI3Kbeta) (PtdIns-3-kinase subunit beta) (EC 2.7.1.153) (Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit beta) (PtdIns-3-kinase subunit p110-beta) (p110beta)
[Pik3cb] Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform (PI3-kinase subunit beta) (PI3K-beta) (PI3Kbeta) (PtdIns-3-kinase subunit beta) (EC 2.7.1.153) (Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit beta) (PtdIns-3-kinase subunit p110-beta) (p110beta)
[B4GALT1 GALT GGTB2] Beta-1,4-galactosyltransferase 1 (Beta-1,4-GalTase 1) (Beta4Gal-T1) (b4Gal-T1) (EC 2.4.1.-) (Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase) (Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase) (EC 2.4.1.38) (Lactose synthase A protein) (EC 2.4.1.22) (N-acetyllactosamine synthase) (EC 2.4.1.90) (Nal synthase) (UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 1) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 1) [Cleaved into: Processed beta-1,4-galactosyltransferase 1]
[B4galt1 Ggtb Ggtb2] Beta-1,4-galactosyltransferase 1 (Beta-1,4-GalTase 1) (Beta4Gal-T1) (b4Gal-T1) (EC 2.4.1.-) (Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase) (Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase) (EC 2.4.1.38) (Lactose synthase A protein) (EC 2.4.1.22) (N-acetyllactosamine synthase) (EC 2.4.1.90) (Nal synthase) (UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 1) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 1) [Cleaved into: Processed beta-1,4-galactosyltransferase 1]
[PLEKHO1 CKIP1 OC120 HQ0024c] Pleckstrin homology domain-containing family O member 1 (PH domain-containing family O member 1) (C-Jun-binding protein) (JBP) (Casein kinase 2-interacting protein 1) (CK2-interacting protein 1) (CKIP-1) (Osteoclast maturation-associated gene 120 protein)
[CAMK2B CAM2 CAMK2 CAMKB] Calcium/calmodulin-dependent protein kinase type II subunit beta (CaM kinase II subunit beta) (CaMK-II subunit beta) (EC 2.7.11.17)
[Csnk1d Hckid] Casein kinase I isoform delta (CKI-delta) (CKId) (EC 2.7.11.1) (Tau-protein kinase CSNK1D) (EC 2.7.11.26)
[Ikbkb Ikkb] Inhibitor of nuclear factor kappa-B kinase subunit beta (I-kappa-B-kinase beta) (IKK-B) (IKK-beta) (IkBKB) (EC 2.7.11.10) (I-kappa-B kinase 2) (IKK2) (Nuclear factor NF-kappa-B inhibitor kinase beta) (NFKBIKB)
[FAM20C DMP4] Extracellular serine/threonine protein kinase FAM20C (EC 2.7.11.1) (Dentin matrix protein 4) (DMP-4) (Golgi casein kinase) (Golgi-enriched fraction casein kinase) (GEF-CK)
[Csnk1d Hckid] Casein kinase I isoform delta (CKI-delta) (EC 2.7.11.1) (Tau-protein kinase CSNK1D) (EC 2.7.11.26)
[B3GNT2 B3gnt1 Beta3gnt] N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2 (EC 2.4.1.149) (Beta-1,3-N-acetylglucosaminyltransferase 1) (BGnT-1) (Beta-1,3-Gn-T1) (Beta3Gn-T1) (Beta-1,3-galactosyltransferase 7) (Beta-1,3-GalTase 7) (Beta3Gal-T7) (Beta3GalT7) (b3Gal-T7) (Beta-3-Gx-T7) (UDP-Gal:beta-GlcNAc beta-1,3-galactosyltransferase 7) (UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2) (BGnT-2) (Beta-1,3-Gn-T2) (Beta-1,3-N-acetylglucosaminyltransferase 2) (Beta3Gn-T2) (UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase 7)

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