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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)

 IKKB_HUMAN              Reviewed;         756 AA.
O14920; B4DZ30; B4E0U4; O75327;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
22-NOV-2017, entry version 199.
RecName: Full=Inhibitor of nuclear factor kappa-B kinase subunit beta;
Short=I-kappa-B-kinase beta;
Short=IKK-B;
Short=IKK-beta;
Short=IkBKB;
EC=2.7.11.10;
AltName: Full=I-kappa-B kinase 2;
Short=IKK2;
AltName: Full=Nuclear factor NF-kappa-B inhibitor kinase beta;
Short=NFKBIKB;
Name=IKBKB; Synonyms=IKKB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND MUTAGENESIS OF LYS-44;
SER-177 AND SER-181.
TISSUE=Cervix carcinoma;
PubMed=9346484; DOI=10.1126/science.278.5339.860;
Mercurio F., Zhu H., Murray B.W., Shevchenko A., Bennett B.L.,
Li J.W., Young D.B., Barbosa M., Mann M., Manning A., Rao A.;
"IKK-1 and IKK-2: cytokine-activated IkappaB kinases essential for NF-
kappaB activation.";
Science 278:860-866(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND MUTAGENESIS OF LYS-44.
PubMed=9346485; DOI=10.1126/science.278.5339.866;
Woronicz J.D., Gao X., Cao Z., Rothe M., Goeddel D.V.;
"IkappaB kinase-beta: NF-kappaB activation and complex formation with
IkappaB kinase-alpha and NIK.";
Science 278:866-869(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Heart;
PubMed=9813230; DOI=10.1016/S0378-1119(98)00462-4;
Hu M.C.-T., Wang Y.-P.;
"IkappaB kinase-alpha and -beta genes are coexpressed in adult and
embryonic tissues but localized to different human chromosomes.";
Gene 222:31-40(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND GENE MAPPING.
PubMed=9763654;
Shindo M., Nakano H., Sakon S., Yagita H., Mihara M., Okumura K.;
"Assignment of IkappaB kinase beta (IKBKB) to human chromosome band
8p12-->p11 by in situ hybridization.";
Cytogenet. Cell Genet. 82:32-33(1998).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
TISSUE=Testis, and Thymus;
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).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT TRP-554.
SeattleSNPs variation discovery resource;
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Lung;
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).
[9]
PROTEIN SEQUENCE OF 170-182 (ISOFORM 1), INACTIVATION BY YERSINIA YOPJ
(MICROBIAL INFECTION), ACETYLATION AT THR-180 (MICROBIAL INFECTION),
AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17116858; DOI=10.1073/pnas.0608995103;
Mittal R., Peak-Chew S.Y., McMahon H.T.;
"Acetylation of MEK2 and I kappa B kinase (IKK) activation loop
residues by YopJ inhibits signaling.";
Proc. Natl. Acad. Sci. U.S.A. 103:18574-18579(2006).
[10]
IKK PHOSPHORYLATION.
PubMed=9819420; DOI=10.1128/MCB.18.12.7336;
Nemoto S., DiDonato J.A., Lin A.;
"Coordinate regulation of IkappaB kinases by mitogen-activated protein
kinase kinase kinase 1 and NF-kappaB-inducing kinase.";
Mol. Cell. Biol. 18:7336-7343(1998).
[11]
IDENTIFICATION IN A COMPLEX WITH CHUK; NFKBIA; RELA; ELP1 AND MAP3K14.
PubMed=9751059; DOI=10.1038/26254;
Cohen L., Henzel W.J., Baeuerle P.A.;
"IKAP is a scaffold protein of the IkappaB kinase complex.";
Nature 395:292-296(1998).
[12]
INTERACTION WITH SQSTM1; PRKCZ AND PRKCI.
PubMed=10356400; DOI=10.1093/emboj/18.11.3044;
Sanz L., Sanchez P., Lallena M.-J., Diaz-Meco M.T., Moscat J.;
"The interaction of p62 with RIP links the atypical PKCs to NF-kappaB
activation.";
EMBO J. 18:3044-3053(1999).
[13]
PHOSPHORYLATION AT SER-177 AND SER-181.
PubMed=10022904; DOI=10.1128/MCB.19.3.2180;
Lallena M.J., Diaz-Meco M.T., Bren G., Paya C.V., Moscat J.;
"Activation of IkappaB kinase beta by protein kinase C isoforms.";
Mol. Cell. Biol. 19:2180-2188(1999).
[14]
PHOSPHORYLATION AT SER-177; SER-181; SER-670; SER-672; SER-675;
SER-682; SER-689; SER-692; SER-695; SER-697; SER-705; SER-733; SER-740
AND SER-750.
PubMed=10195894; DOI=10.1126/science.284.5412.309;
Delhase M., Hayakawa M., Chen Y., Karin M.;
"Positive and negative regulation of IkappaB kinase activity through
IKKbeta subunit phosphorylation.";
Science 284:309-313(1999).
[15]
INTERACTION WITH EIF2AK2.
PubMed=10848580; DOI=10.1128/MCB.20.13.4532-4542.2000;
Bonnet M.C., Weil R., Dam E., Hovanessian A.G., Meurs E.F.;
"PKR stimulates NF-kappaB irrespective of its kinase function by
interacting with the IkappaB kinase complex.";
Mol. Cell. Biol. 20:4532-4542(2000).
[16]
PHOSPHORYLATION AT SER-177 AND SER-181 BY TBK1, AND MUTAGENESIS OF
177-SER--SER-181.
PubMed=10783893; DOI=10.1038/35008109;
Tojima Y., Fujimoto A., Delhase M., Chen Y., Hatakeyama S.,
Nakayama K., Kaneko Y., Nimura Y., Motoyama N., Ikeda K., Karin M.,
Nakanishi M.;
"NAK is an IkappaB kinase-activating kinase.";
Nature 404:778-782(2000).
[17]
FUNCTION IN PHOSPHORYLATION OF NFKB1.
PubMed=11297557; DOI=10.1074/jbc.M101754200;
Salmeron A., Janzen J., Soneji Y., Bump N., Kamens J., Allen H.,
Ley S.C.;
"Direct phosphorylation of NF-kappa B1 p105 by the Ikappa B kinase
complex on serine 927 is essential for signal-induced p105
proteolysis.";
J. Biol. Chem. 276:22215-22222(2001).
[18]
INTERACTION WITH IKBKG AND TANK.
PubMed=12133833; DOI=10.1074/jbc.M205069200;
Chariot A., Leonardi A., Muller J., Bonif M., Brown K., Siebenlist U.;
"Association of the adaptor TANK with the I kappa B kinase (IKK)
regulator NEMO connects IKK complexes with IKK epsilon and TBK1
kinases.";
J. Biol. Chem. 277:37029-37036(2002).
[19]
IDENTIFICATION IN A COMPLEX WITH CREBBP; NCOA2; NCOA3; IKKA AND IKBKG.
PubMed=11971985; DOI=10.1128/MCB.22.10.3549-3561.2002;
Wu R.-C., Qin J., Hashimoto Y., Wong J., Xu J., Tsai S.Y., Tsai M.-J.,
O'Malley B.W.;
"Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) coactivator
activity by I kappa B kinase.";
Mol. Cell. Biol. 22:3549-3561(2002).
[20]
COMPOSITION OF THE IKK COMPLEX.
PubMed=12612076; DOI=10.1128/MCB.23.6.2029-2041.2003;
Tegethoff S., Behlke J., Scheidereit C.;
"Tetrameric oligomerization of IkappaB kinase gamma (IKKgamma) is
obligatory for IKK complex activity and NF-kappaB activation.";
Mol. Cell. Biol. 23:2029-2041(2003).
[21]
FUNCTION, AND INTERACTION WITH FOXO3.
PubMed=15084260; DOI=10.1016/S0092-8674(04)00302-2;
Hu M.C., Lee D.F., Xia W., Golfman L.S., Ou-Yang F., Yang J.Y.,
Zou Y., Bao S., Hanada N., Saso H., Kobayashi R., Hung M.C.;
"IkappaB kinase promotes tumorigenesis through inhibition of forkhead
FOXO3a.";
Cell 117:225-237(2004).
[22]
INTERACTION WITH TICAM1.
PubMed=14739303; DOI=10.1074/jbc.M311629200;
Han K.J., Su X., Xu L.-G., Bin L.H., Zhang J., Shu H.-B.;
"Mechanisms of the TRIF-induced interferon-stimulated response element
and NF-kappaB activation and apoptosis pathways.";
J. Biol. Chem. 279:15652-15661(2004).
[23]
INTERACTION WITH NALP2.
PubMed=15456791; DOI=10.1074/jbc.M406741200;
Bruey J.-M., Bruey-Sedano N., Newman R., Chandler S., Stehlik C.,
Reed J.C.;
"PAN1/NALP2/PYPAF2, an inducible inflammatory mediator that regulates
NF-kappaB and caspase-1 activation in macrophages.";
J. Biol. Chem. 279:51897-51907(2004).
[24]
INTERACTION WITH ARRB1 AND ARRB2.
PubMed=15173580; DOI=10.1073/pnas.0402851101;
Witherow D.S., Garrison T.R., Miller W.E., Lefkowitz R.J.;
"beta-Arrestin inhibits NF-kappaB activity by means of its interaction
with the NF-kappaB inhibitor IkappaBalpha.";
Proc. Natl. Acad. Sci. U.S.A. 101:8603-8607(2004).
[25]
S-NITROSYLATION AT CYS-179.
PubMed=15184672; DOI=10.1073/pnas.0400588101;
Reynaert N.L., Ckless K., Korn S.H., Vos N., Guala A.S., Wouters E.F.,
van der Vliet A., Janssen-Heininger Y.M.;
"Nitric oxide represses inhibitory kappaB kinase through S-
nitrosylation.";
Proc. Natl. Acad. Sci. U.S.A. 101:8945-8950(2004).
[26]
INTERACTION WITH NIBP.
PubMed=15951441; DOI=10.1074/jbc.M501670200;
Hu W.-H., Pendergast J.S., Mo X.-M., Brambilla R., Bracchi-Ricard V.,
Li F., Walters W.M., Blits B., He L., Schaal S.M., Bethea J.R.;
"NIBP, a novel NIK and IKK(beta)-binding protein that enhances NF-
(kappa)B activation.";
J. Biol. Chem. 280:29233-29241(2005).
[27]
PHOSPHORYLATION AT SER-181 BY PDPK1, AND INTERACTION WITH PDPK1.
PubMed=16207722; DOI=10.1074/jbc.M506235200;
Tanaka H., Fujita N., Tsuruo T.;
"3-Phosphoinositide-dependent protein kinase-1-mediated IkappaB kinase
beta (IkkB) phosphorylation activates NF-kappaB signaling.";
J. Biol. Chem. 280:40965-40973(2005).
[28]
UBIQUITINATION AT LYS-163.
PubMed=16267042; DOI=10.1074/jbc.M508656200;
Carter R.S., Pennington K.N., Arrate P., Oltz E.M., Ballard D.W.;
"Site-specific monoubiquitination of IkappaB kinase IKKbeta regulates
its phosphorylation and persistent activation.";
J. Biol. Chem. 280:43272-43279(2005).
[29]
INTERACTION WITH MAVS.
PubMed=16177806; DOI=10.1038/nature04193;
Meylan E., Curran J., Hofmann K., Moradpour D., Binder M.,
Bartenschlager R., Tschopp J.;
"Cardif is an adaptor protein in the RIG-I antiviral pathway and is
targeted by hepatitis C virus.";
Nature 437:1167-1172(2005).
[30]
HYDROXYLATION AT PRO-191, AND MUTAGENESIS OF PRO-191.
PubMed=17114296; DOI=10.1073/pnas.0602235103;
Cummins E.P., Berra E., Comerford K.M., Ginouves A., Fitzgerald K.T.,
Seeballuck F., Godson C., Nielsen J.E., Moynagh P., Pouyssegur J.,
Taylor C.T.;
"Prolyl hydroxylase-1 negatively regulates IkappaB kinase-beta, giving
insight into hypoxia-induced NFkappaB activity.";
Proc. Natl. Acad. Sci. U.S.A. 103:18154-18159(2006).
[31]
INTERACTION WITH YOPJ (MICROBIAL INFECTION), AND ACETYLATION
(MICROBIAL INFECTION).
PubMed=16728640; DOI=10.1126/science.1126867;
Mukherjee S., Keitany G., Li Y., Wang Y., Ball H.L., Goldsmith E.J.,
Orth K.;
"Yersinia YopJ acetylates and inhibits kinase activation by blocking
phosphorylation.";
Science 312:1211-1214(2006).
[32]
INTERACTION WITH ATM.
PubMed=16497931; DOI=10.1126/science.1121513;
Wu Z.H., Shi Y., Tibbetts R.S., Miyamoto S.;
"Molecular linkage between the kinase ATM and NF-kappaB signaling in
response to genotoxic stimuli.";
Science 311:1141-1146(2006).
[33]
IDENTIFICATION IN A MEMBRANE RAFT COMPLEX, AND SUBCELLULAR LOCATION.
PubMed=17287217; DOI=10.1074/jbc.M609157200;
Ohnuma K., Uchiyama M., Yamochi T., Nishibashi K., Hosono O.,
Takahashi N., Kina S., Tanaka H., Lin X., Dang N.H., Morimoto C.;
"Caveolin-1 triggers T-cell activation via CD26 in association with
CARMA1.";
J. Biol. Chem. 282:10117-10131(2007).
[34]
INTERACTION WITH FAF1.
PubMed=17684021; DOI=10.1074/jbc.C700106200;
Park M.Y., Moon J.H., Lee K.S., Choi H.I., Chung J., Hong H.J.,
Kim E.;
"FAF1 suppresses IkappaB kinase (IKK) activation by disrupting the IKK
complex assembly.";
J. Biol. Chem. 282:27572-27577(2007).
[35]
FUNCTION IN PHOSPHORYLATION OF BCL10.
PubMed=17213322; DOI=10.1073/pnas.0606982104;
Lobry C., Lopez T., Israel A., Weil R.;
"Negative feedback loop in T cell activation through IkappaB kinase-
induced phosphorylation and degradation of Bcl10.";
Proc. Natl. Acad. Sci. U.S.A. 104:908-913(2007).
[36]
REVIEW.
PubMed=10712233;
Jobin C., Sartor R.B.;
"The I kappa B/NF-kappa B system: a key determinant of mucosal
inflammation and protection.";
Am. J. Physiol. 278:C451-C462(2000).
[37]
REVIEW, AND DOMAIN.
PubMed=18626576; DOI=10.1007/s12026-008-8025-1;
Solt L.A., May M.J.;
"The IkappaB kinase complex: master regulator of NF-kappaB
signaling.";
Immunol. Res. 42:3-18(2008).
[38]
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).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672, AND 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).
[40]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[41]
INTERACTION WITH NAA10, AND FUNCTION IN PHOSPHORYLATION OF NAA10.
PubMed=19716809; DOI=10.1016/j.bbrc.2009.08.127;
Kuo H.P., Lee D.F., Xia W., Lai C.C., Li L.Y., Hung M.C.;
"Phosphorylation of ARD1 by IKKbeta contributes to its destabilization
and degradation.";
Biochem. Biophys. Res. Commun. 389:156-161(2009).
[42]
DEPHOSPHORYLATION AT SER-177 AND SER-181, AND INTERACTION WITH PPM1A
AND PPM1B.
PubMed=18930133; DOI=10.1016/j.cellsig.2008.09.012;
Sun W., Yu Y., Dotti G., Shen T., Tan X., Savoldo B., Pass A.K.,
Chu M., Zhang D., Lu X., Fu S., Lin X., Yang J.;
"PPM1A and PPM1B act as IKKbeta phosphatases to terminate TNFalpha-
induced IKKbeta-NF-kappaB activation.";
Cell. Signal. 21:95-102(2009).
[43]
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).
[44]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[45]
FUNCTION, AND INTERACTION WITH NLRC5.
PubMed=20434986; DOI=10.1016/j.cell.2010.03.040;
Cui J., Zhu L., Xia X., Wang H.Y., Legras X., Hong J., Ji J., Shen P.,
Zheng S., Chen Z.J., Wang R.F.;
"NLRC5 negatively regulates the NF-kappaB and type I interferon
signaling pathways.";
Cell 141:483-496(2010).
[46]
INTERACTION WITH TRIM21, MONOUBIQUITINATION, UBIQUITINATION
INACTIVATION BY YERSINIA YOPJ (MICROBIAL INFECTION), AND MUTAGENESIS
OF LYS-163; SER-177 AND SER-181.
PubMed=19675099; DOI=10.1093/jb/mvp127;
Wada K., Niida M., Tanaka M., Kamitani T.;
"Ro52-mediated monoubiquitination of IKK{beta} down-regulates
NF-{kappa}B signalling.";
J. Biochem. 146:821-832(2009).
[47]
FUNCTION IN PHOSPHORYLATION OF RELA.
PubMed=20410276; DOI=10.1128/JVI.00142-10;
Yoboua F., Martel A., Duval A., Mukawera E., Grandvaux N.;
"Respiratory syncytial virus-mediated NF-kappa B p65 phosphorylation
at serine 536 is dependent on RIG-I, TRAF6, and IKK beta.";
J. Virol. 84:7267-7277(2010).
[48]
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=20797629; DOI=10.1016/j.molcel.2010.07.030;
Tsuchiya Y., Asano T., Nakayama K., Kato T. Jr., Karin M., Kamata H.;
"Nuclear IKKbeta is an adaptor protein for IkappaBalpha ubiquitination
and degradation in UV-induced NF-kappaB activation.";
Mol. Cell 39:570-582(2010).
[49]
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).
[50]
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).
[51]
FUNCTION, AND PHOSPHORYLATION BY TBK1 AND IKBKE.
PubMed=21138416; DOI=10.1042/BJ20101701;
Clark K., Peggie M., Plater L., Sorcek R.J., Young E.R., Madwed J.B.,
Hough J., McIver E.G., Cohen P.;
"Novel cross-talk within the IKK family controls innate immunity.";
Biochem. J. 434:93-104(2011).
[52]
INTERACTION WITH ZNF268, AND SUBUNIT.
PubMed=23091055; DOI=10.1074/jbc.M112.399923;
Wang W., Guo M., Hu L., Cai J., Zeng Y., Luo J., Shu Z., Li W.,
Huang Z.;
"The zinc finger protein ZNF268 is overexpressed in human cervical
cancer and contributes to tumorigenesis via enhancing NF-kappaB
signaling.";
J. Biol. Chem. 287:42856-42866(2012).
[53]
INTERACTION WITH IKBKE.
PubMed=23453969; DOI=10.1016/j.celrep.2013.01.031;
Zhou A.Y., Shen R.R., Kim E., Lock Y.J., Xu M., Chen Z.J., Hahn W.C.;
"IKKepsilon-mediated tumorigenesis requires K63-linked
polyubiquitination by a cIAP1/cIAP2/TRAF2 E3 ubiquitin ligase
complex.";
Cell Rep. 3:724-733(2013).
[54]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672 AND SER-675, 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).
[55]
INTERACTION WITH AKAP13.
PubMed=23090968; DOI=10.1128/MCB.00887-12;
del Vescovo C.D., Cotecchia S., Diviani D.;
"A-kinase-anchoring protein-Lbc anchors IkappaB kinase beta to support
interleukin-6-mediated cardiomyocyte hypertrophy.";
Mol. Cell. Biol. 33:14-27(2013).
[56]
INVOLVEMENT IN IMD15.
PubMed=24369075; DOI=10.1056/NEJMoa1309199;
Pannicke U., Baumann B., Fuchs S., Henneke P., Rensing-Ehl A.,
Rizzi M., Janda A., Hese K., Schlesier M., Holzmann K., Borte S.,
Laux C., Rump E.M., Rosenberg A., Zelinski T., Schrezenmeier H.,
Wirth T., Ehl S., Schroeder M.L., Schwarz K.;
"Deficiency of innate and acquired immunity caused by an IKBKB
mutation.";
N. Engl. J. Med. 369:2504-2514(2013).
[57]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, AND 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).
[58]
INTERACTION WITH IFIT5.
PubMed=26334375; DOI=10.1016/j.cellsig.2015.08.018;
Zheng C., Zheng Z., Zhang Z., Meng J., Liu Y., Ke X., Hu Q., Wang H.;
"IFIT5 positively regulates NF-kappaB signaling through synergizing
the recruitment of IkappaB kinase (IKK) to TGF-beta-activated kinase 1
(TAK1).";
Cell. Signal. 27:2343-2354(2015).
[59]
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).
[60]
INTERACTION WITH LRRC14.
PubMed=27426725; DOI=10.1016/j.yexcr.2016.07.011;
Wu C., Yang Y., Ou J., Zhu L., Zhao W., Cui J.;
"LRRC14 attenuates Toll-like receptor-mediated NF-kappa-B signaling
through disruption of IKK complex.";
Exp. Cell Res. 347:65-73(2016).
[61]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 701-742.
PubMed=18462684; DOI=10.1016/j.str.2008.02.012;
Rushe M., Silvian L., Bixler S., Chen L.L., Cheung A., Bowes S.,
Cuervo H., Berkowitz S., Zheng T., Guckian K., Pellegrini M.,
Lugovskoy A.;
"Structure of a NEMO/IKK-associating domain reveals architecture of
the interaction site.";
Structure 16:798-808(2008).
[62]
VARIANT [LARGE SCALE ANALYSIS] SER-360.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[63]
VARIANTS [LARGE SCALE ANALYSIS] SER-360; ARG-369; GLN-526; THR-710 AND
LEU-734.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Serine kinase that plays an essential role in the NF-
kappa-B signaling pathway which is activated by multiple stimuli
such as inflammatory cytokines, bacterial or viral products, DNA
damages or other cellular stresses. Acts as part of the canonical
IKK complex in the conventional pathway of NF-kappa-B activation
and phosphorylates inhibitors of NF-kappa-B on 2 critical serine
residues. These modifications allow polyubiquitination of the
inhibitors and subsequent degradation by the proteasome. In turn,
free NF-kappa-B is translocated into the nucleus and activates the
transcription of hundreds of genes involved in immune response,
growth control, or protection against apoptosis. In addition to
the NF-kappa-B inhibitors, phosphorylates several other components
of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits
RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE.
IKK-related kinase phosphorylations may prevent the overproduction
of inflammatory mediators since they exert a negative regulation
on canonical IKKs. Phosphorylates FOXO3, mediating the TNF-
dependent inactivation of this pro-apoptotic transcription factor.
Also phosphorylates other substrates including NCOA3, BCL10 and
IRS1. Within the nucleus, acts as an adapter protein for NFKBIA
degradation in UV-induced NF-kappa-B activation.
{ECO:0000269|PubMed:11297557, ECO:0000269|PubMed:15084260,
ECO:0000269|PubMed:17213322, ECO:0000269|PubMed:19716809,
ECO:0000269|PubMed:20410276, ECO:0000269|PubMed:20434986,
ECO:0000269|PubMed:20797629, ECO:0000269|PubMed:21138416}.
-!- CATALYTIC ACTIVITY: ATP + [I-kappa-B protein] = ADP + [I-kappa-B
phosphoprotein].
-!- SUBUNIT: Component of the I-kappa-B-kinase (IKK) core complex
consisting of CHUK, IKBKB and IKBKG; probably four alpha/CHUK-
beta/IKBKB dimers are associated with four gamma/IKBKG subunits.
The IKK core complex seems to associate with regulatory or adapter
proteins to form a IKK-signalosome holo-complex (PubMed:12612076).
The IKK complex associates with TERF2IP/RAP1, leading to promote
IKK-mediated phosphorylation of RELA/p65 (By similarity). Part of
a complex composed of NCOA2, NCOA3, CHUK/IKKA, IKBKB, IKBKG and
CREBBP (PubMed:11971985). Part of a 70-90 kDa complex at least
consisting of CHUK/IKKA, IKBKB, NFKBIA, RELA, ELP1 and MAP3K14
(PubMed:9751059). Found in a membrane raft complex, at least
composed of BCL10, CARD11, DPP4 and IKBKB (PubMed:17287217).
Interacts with SQSTM1 through PRKCZ or PRKCI (PubMed:10356400).
Forms an NGF-induced complex with IKBKB, PRKCI and TRAF6 (By
similarity). May interact with MAVS/IPS1 (PubMed:16177806).
Interacts with NALP2 (PubMed:15456791). Interacts with TICAM1
(PubMed:14739303). Interacts with FAF1; the interaction disrupts
the IKK complex formation (PubMed:17684021). Interacts with ATM
(PubMed:16497931). Part of a ternary complex consisting of TANK,
IKBKB and IKBKG (PubMed:12133833). Interacts with NIBP; the
interaction is direct (PubMed:15951441). Interacts with ARRB1 and
ARRB2 (PubMed:15173580). Interacts with TRIM21 (PubMed:19675099).
Interacts with NLRC5; prevents IKBKB phosphorylation and kinase
activity (PubMed:20434986). Interacts with PDPK1
(PubMed:16207722). Interacts with EIF2AK2/PKR (PubMed:10848580).
The phosphorylated form interacts with PPM1A and PPM1B
(PubMed:18930133). Interacts with ZNF268 isoform 2; the
interaction is further increased in a TNF-alpha-dependent manner
(PubMed:23091055). Interacts with IKBKE (PubMed:23453969).
Interacts with NAA10, leading to NAA10 degradation
(PubMed:19716809). Interacts with FOXO3 (PubMed:15084260).
Interacts with AKAP13 (PubMed:23090968). Interacts with IFIT5; the
interaction synergizes the recruitment of IKK to MAP3K7 and
enhances IKK phosphorylation (PubMed:26334375). Interacts with
LRRC14; disrupts IKBKB-IKBKG interaction preventing I-kappa-B-
kinase (IKK) core complex formation and leading to a decrease of
IKBKB phosphorylation and NF-kappaB activation (PubMed:27426725).
{ECO:0000250|UniProtKB:O88351, ECO:0000250|UniProtKB:Q9QY78,
ECO:0000269|PubMed:10356400, ECO:0000269|PubMed:10848580,
ECO:0000269|PubMed:11971985, ECO:0000269|PubMed:12133833,
ECO:0000269|PubMed:12612076, ECO:0000269|PubMed:14739303,
ECO:0000269|PubMed:15084260, ECO:0000269|PubMed:15173580,
ECO:0000269|PubMed:15456791, ECO:0000269|PubMed:15951441,
ECO:0000269|PubMed:16177806, ECO:0000269|PubMed:16207722,
ECO:0000269|PubMed:16497931, ECO:0000269|PubMed:17287217,
ECO:0000269|PubMed:17684021, ECO:0000269|PubMed:18930133,
ECO:0000269|PubMed:19675099, ECO:0000269|PubMed:19716809,
ECO:0000269|PubMed:20434986, ECO:0000269|PubMed:23091055,
ECO:0000269|PubMed:23453969, ECO:0000269|PubMed:26334375,
ECO:0000269|PubMed:27426725, ECO:0000269|PubMed:9751059}.
-!- SUBUNIT: (Microbial infection) Interacts with Yersinia yopJ.
{ECO:0000269|PubMed:16728640}.
-!- INTERACTION:
Self; NbExp=8; IntAct=EBI-81266, EBI-81266;
O14965:AURKA; NbExp=2; IntAct=EBI-81266, EBI-448680;
Q16543:CDC37; NbExp=4; IntAct=EBI-81266, EBI-295634;
O15111:CHUK; NbExp=15; IntAct=EBI-81266, EBI-81249;
Q92793:CREBBP; NbExp=2; IntAct=EBI-81266, EBI-81215;
P08238:HSP90AB1; NbExp=2; IntAct=EBI-81266, EBI-352572;
Q9Y6K9:IKBKG; NbExp=33; IntAct=EBI-81266, EBI-81279;
Q14145:KEAP1; NbExp=6; IntAct=EBI-81266, EBI-751001;
P03230:LMP1 (xeno); NbExp=2; IntAct=EBI-81266, EBI-6973030;
Q99558:MAP3K14; NbExp=3; IntAct=EBI-81266, EBI-358011;
Q9Y6Q9:NCOA3; NbExp=3; IntAct=EBI-81266, EBI-81196;
P19838:NFKB1; NbExp=3; IntAct=EBI-81266, EBI-300010;
P25963:NFKBIA; NbExp=27; IntAct=EBI-81266, EBI-307386;
P67775:PPP2CA; NbExp=3; IntAct=EBI-81266, EBI-712311;
Q04206:RELA; NbExp=2; IntAct=EBI-81266, EBI-73886;
P23396:RPS3; NbExp=4; IntAct=EBI-81266, EBI-351193;
Q9UGK3:STAP2; NbExp=7; IntAct=EBI-81266, EBI-1553984;
P03409:tax (xeno); NbExp=3; IntAct=EBI-81266, EBI-5236464;
Q9UKE5:TNIK; NbExp=2; IntAct=EBI-81266, EBI-1051794;
P04637:TP53; NbExp=2; IntAct=EBI-81266, EBI-366083;
Q92574:TSC1; NbExp=3; IntAct=EBI-81266, EBI-1047085;
P24772:VACWR196 (xeno); NbExp=3; IntAct=EBI-81266, EBI-4291651;
Q5D1E7:Zc3h12a (xeno); NbExp=4; IntAct=EBI-81266, EBI-5326026;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20797629}.
Nucleus {ECO:0000269|PubMed:20797629}. Membrane raft
{ECO:0000269|PubMed:17287217}. Note=Colocalized with DPP4 in
membrane rafts. {ECO:0000269|PubMed:17287217}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=O14920-1; Sequence=Displayed;
Name=2;
IsoId=O14920-2; Sequence=VSP_041825;
Name=3;
IsoId=O14920-3; Sequence=VSP_041826, VSP_041827;
Name=4;
IsoId=O14920-4; Sequence=VSP_043408;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in heart, placenta, skeletal
muscle, kidney, pancreas, spleen, thymus, prostate, testis and
peripheral blood.
-!- DOMAIN: The kinase domain is located in the N-terminal region. The
leucine zipper is important to allow homo- and hetero-
dimerization. At the C-terminal region is located the region
responsible for the interaction with NEMO/IKBKG.
{ECO:0000269|PubMed:18626576}.
-!- PTM: Upon cytokine stimulation, phosphorylated on Ser-177 and Ser-
181 by MEKK1 and/or MAP3K14/NIK as well as TBK1 and PRKCZ; which
enhances activity. Once activated, autophosphorylates on the C-
terminal serine cluster; which decreases activity and prevents
prolonged activation of the inflammatory response. Phosphorylated
by the IKK-related kinases TBK1 and IKBKE, which is associated
with reduced CHUK/IKKA and IKBKB activity and NF-kappa-B-dependent
gene transcription. Dephosphorylated at Ser-177 and Ser-181 by
PPM1A and PPM1B. {ECO:0000269|PubMed:10022904,
ECO:0000269|PubMed:10195894, ECO:0000269|PubMed:10783893,
ECO:0000269|PubMed:16207722}.
-!- PTM: (Microbial infection) Acetylation of Thr-180 by Yersinia yopJ
prevents phosphorylation and activation, thus blocking the I-
kappa-B pathway. {ECO:0000269|PubMed:16728640,
ECO:0000269|PubMed:17116858}.
-!- PTM: Ubiquitinated. Monoubiquitination involves TRIM21 that leads
to inhibition of Tax-induced NF-kappa-B signaling. According to
PubMed:19675099, 'Ser-163' does not serve as a monoubiquitination
site. According to PubMed:16267042, ubiquitination on 'Ser-163'
modulates phosphorylation on C-terminal serine residues.
{ECO:0000269|PubMed:16267042, ECO:0000269|PubMed:19675099}.
-!- PTM: (Microbial infection) Monoubiquitination by TRIM21 is
disrupted by Yersinia yopJ. {ECO:0000269|PubMed:19675099}.
-!- PTM: Hydroxylated by PHD1/EGLN2, loss of hydroxylation under
hypoxic conditions results in activation of NF-kappa-B.
{ECO:0000269|PubMed:17114296}.
-!- DISEASE: Immunodeficiency 15 (IMD15) [MIM:615592]: An autosomal
recessive primary immunodeficiency disorder characterized by onset
in infancy of life-threatening bacterial, fungal, and viral
infections and failure to thrive. Laboratory studies show hypo- or
agammaglobulinemia with relatively normal numbers of B and T-
cells, and impaired differentiation and activation of immune
cells. {ECO:0000269|PubMed:24369075}. Note=The disease is caused
by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. I-kappa-B kinase subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00159}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/ikbkb/";
-----------------------------------------------------------------------
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EMBL; AF029684; AAC51860.1; -; mRNA.
EMBL; AF080158; AAD08997.1; -; mRNA.
EMBL; AF031416; AAC64675.1; -; mRNA.
EMBL; AK302723; BAG63942.1; -; mRNA.
EMBL; AK303528; BAG64556.1; -; mRNA.
EMBL; AK316418; BAH14789.1; -; mRNA.
EMBL; AY663108; AAT65965.1; -; Genomic_DNA.
EMBL; AC083973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC006231; AAH06231.1; -; mRNA.
CCDS; CCDS55228.1; -. [O14920-2]
CCDS; CCDS56535.1; -. [O14920-4]
CCDS; CCDS6128.1; -. [O14920-1]
RefSeq; NP_001177649.1; NM_001190720.2. [O14920-2]
RefSeq; NP_001229707.1; NM_001242778.1. [O14920-4]
RefSeq; NP_001547.1; NM_001556.2. [O14920-1]
UniGene; Hs.597664; -.
PDB; 3BRT; X-ray; 2.25 A; A/C=701-730.
PDB; 3BRV; X-ray; 2.20 A; A/C=701-745.
PDB; 4E3C; X-ray; 3.98 A; A/B/C/D/E/F=11-669.
PDB; 4KIK; X-ray; 2.83 A; A/B=2-664.
PDBsum; 3BRT; -.
PDBsum; 3BRV; -.
PDBsum; 4E3C; -.
PDBsum; 4KIK; -.
ProteinModelPortal; O14920; -.
SMR; O14920; -.
BioGrid; 109767; 141.
CORUM; O14920; -.
DIP; DIP-27527N; -.
ELM; O14920; -.
IntAct; O14920; 76.
MINT; MINT-107608; -.
STRING; 9606.ENSP00000430684; -.
BindingDB; O14920; -.
ChEMBL; CHEMBL1991; -.
DrugBank; DB06151; Acetylcysteine.
DrugBank; DB00945; Acetylsalicylic acid.
DrugBank; DB01169; Arsenic trioxide.
DrugBank; DB00995; Auranofin.
DrugBank; DB00244; Mesalazine.
DrugBank; DB05183; MLN0415.
DrugBank; DB00795; Sulfasalazine.
GuidetoPHARMACOLOGY; 2039; -.
iPTMnet; O14920; -.
PhosphoSitePlus; O14920; -.
BioMuta; IKBKB; -.
EPD; O14920; -.
MaxQB; O14920; -.
PaxDb; O14920; -.
PeptideAtlas; O14920; -.
PRIDE; O14920; -.
DNASU; 3551; -.
Ensembl; ENST00000416505; ENSP00000404920; ENSG00000104365. [O14920-4]
Ensembl; ENST00000519735; ENSP00000430483; ENSG00000104365. [O14920-3]
Ensembl; ENST00000520810; ENSP00000430684; ENSG00000104365. [O14920-1]
Ensembl; ENST00000520835; ENSP00000430868; ENSG00000104365. [O14920-2]
GeneID; 3551; -.
KEGG; hsa:3551; -.
UCSC; uc003xow.3; human. [O14920-1]
CTD; 3551; -.
DisGeNET; 3551; -.
EuPathDB; HostDB:ENSG00000104365.13; -.
GeneCards; IKBKB; -.
HGNC; HGNC:5960; IKBKB.
HPA; CAB004447; -.
HPA; HPA001249; -.
MalaCards; IKBKB; -.
MIM; 603258; gene.
MIM; 615592; phenotype.
neXtProt; NX_O14920; -.
OpenTargets; ENSG00000104365; -.
Orphanet; 397787; Severe combined immunodeficiency due to IKK2 deficiency.
PharmGKB; PA29776; -.
eggNOG; KOG4250; Eukaryota.
eggNOG; ENOG410XRMU; LUCA.
GeneTree; ENSGT00900000140902; -.
HOGENOM; HOG000038048; -.
HOVERGEN; HBG018241; -.
InParanoid; O14920; -.
KO; K07209; -.
OMA; WINEINI; -.
OrthoDB; EOG091G02VC; -.
PhylomeDB; O14920; -.
TreeFam; TF324269; -.
BRENDA; 2.7.11.10; 2681.
Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
Reactome; R-HSA-168927; TICAM1, RIP1-mediated IKK complex recruitment.
Reactome; R-HSA-1810476; RIP-mediated NFkB activation via ZBP1.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-209543; p75NTR recruits signalling complexes.
Reactome; R-HSA-209560; NF-kB is activated and signals survival.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-HSA-446652; Interleukin-1 family signaling.
Reactome; R-HSA-5357905; Regulation of TNFR1 signaling.
Reactome; R-HSA-5357956; TNFR1-induced NFkappaB signaling pathway.
Reactome; R-HSA-5602636; IKBKB deficiency causes SCID.
Reactome; R-HSA-5603027; IKBKG deficiency causes anhidrotic ectodermal dysplasia with immunodeficiency (EDA-ID) (via TLR).
Reactome; R-HSA-5603029; IkBA variant leads to EDA-ID.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation.
Reactome; R-HSA-933542; TRAF6 mediated NF-kB activation.
Reactome; R-HSA-933543; NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
Reactome; R-HSA-937039; IRAK1 recruits IKK complex.
Reactome; R-HSA-937041; IKK complex recruitment mediated by RIP1.
Reactome; R-HSA-975144; IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
SABIO-RK; O14920; -.
SignaLink; O14920; -.
SIGNOR; O14920; -.
ChiTaRS; IKBKB; human.
EvolutionaryTrace; O14920; -.
GeneWiki; IKK2; -.
GenomeRNAi; 3551; -.
PRO; PR:O14920; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000104365; -.
CleanEx; HS_IKBKB; -.
ExpressionAtlas; O14920; baseline and differential.
Genevisible; O14920; HS.
GO; GO:0035631; C:CD40 receptor complex; ISS:BHF-UCL.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISS:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0008385; C:IkappaB kinase complex; TAS:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008384; F:IkappaB kinase activity; TAS:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0097110; F:scaffold protein binding; IDA:MGI.
GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:UniProtKB.
GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:UniProtKB.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0006954; P:inflammatory response; TAS:UniProtKB.
GO; GO:0045087; P:innate immune response; TAS:UniProtKB.
GO; GO:0070498; P:interleukin-1-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
GO; GO:1903347; P:negative regulation of bicellular tight junction assembly; IMP:UniProtKB.
GO; GO:0035509; P:negative regulation of myosin-light-chain-phosphatase activity; IMP:UniProtKB.
GO; GO:0070423; P:nucleotide-binding oligomerization domain containing signaling pathway; TAS:Reactome.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; TAS:Reactome.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:1903140; P:regulation of establishment of endothelial barrier; IMP:UniProtKB.
GO; GO:0042325; P:regulation of phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0010803; P:regulation of tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
GO; GO:0009615; P:response to virus; TAS:UniProtKB.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0051403; P:stress-activated MAPK cascade; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IMP:UniProtKB.
InterPro; IPR022007; IKKbetaNEMObind.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR029071; Ubiquitin-like_domsf.
InterPro; IPR000626; Ubiquitin_dom.
Pfam; PF12179; IKKbetaNEMObind; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM01239; IKKbetaNEMObind; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF54236; SSF54236; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Complete proteome; Cytoplasm; Direct protein sequencing;
Hydroxylation; Isopeptide bond; Kinase; Membrane; Nucleotide-binding;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
S-nitrosylation; SCID; Serine/threonine-protein kinase; Transferase;
Ubl conjugation.
CHAIN 1 756 Inhibitor of nuclear factor kappa-B
kinase subunit beta.
/FTId=PRO_0000086013.
DOMAIN 15 300 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 21 29 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 458 479 Leucine-zipper.
REGION 737 742 NEMO-binding.
ACT_SITE 145 145 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 44 44 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 177 177 Phosphoserine; by TBK1 and PKC/PRKCZ.
{ECO:0000269|PubMed:10022904,
ECO:0000269|PubMed:10195894,
ECO:0000269|PubMed:10783893}.
MOD_RES 179 179 S-nitrosocysteine.
{ECO:0000269|PubMed:15184672}.
MOD_RES 180 180 O-acetylthreonine; by Yersinia yopJ.
{ECO:0000269|PubMed:17116858}.
MOD_RES 181 181 Phosphoserine; by TBK1, PKC/PRKCZ and
PDPK1. {ECO:0000269|PubMed:10022904,
ECO:0000269|PubMed:10195894,
ECO:0000269|PubMed:10783893,
ECO:0000269|PubMed:16207722}.
MOD_RES 191 191 Hydroxyproline.
{ECO:0000269|PubMed:17114296}.
MOD_RES 670 670 Phosphoserine; by autocatalysis.
{ECO:0000305|PubMed:10195894}.
MOD_RES 672 672 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:10195894}.
MOD_RES 675 675 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 675 675 Phosphoserine; by autocatalysis.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000305|PubMed:10195894}.
MOD_RES 682 682 Phosphoserine; by autocatalysis.
{ECO:0000305|PubMed:10195894}.
MOD_RES 689 689 Phosphoserine; by autocatalysis.
{ECO:0000305|PubMed:10195894}.
MOD_RES 692 692 Phosphoserine; by autocatalysis.
{ECO:0000305|PubMed:10195894}.
MOD_RES 695 695 Phosphoserine; by autocatalysis.
{ECO:0000305|PubMed:10195894}.
MOD_RES 697 697 Phosphoserine; by autocatalysis.
{ECO:0000305|PubMed:10195894}.
MOD_RES 705 705 Phosphoserine; by autocatalysis.
{ECO:0000305|PubMed:10195894}.
MOD_RES 733 733 Phosphoserine; by autocatalysis.
{ECO:0000305|PubMed:10195894}.
MOD_RES 740 740 Phosphoserine; by autocatalysis.
{ECO:0000305|PubMed:10195894}.
MOD_RES 750 750 Phosphoserine; by autocatalysis.
{ECO:0000305|PubMed:10195894}.
CROSSLNK 163 163 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:16267042}.
VAR_SEQ 1 66 MSWSPSLTTQTCGAWEMKERLGTGGFGNVIRWHNQETGEQI
AIKQCRQELSPRNRERWCLEIQIMR -> MSSDGTI (in
isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043408.
VAR_SEQ 1 34 MSWSPSLTTQTCGAWEMKERLGTGGFGNVIRWHN -> MFS
GGCHSPGFGRPSPAFPAPGSPPPAPRPCR (in isoform
2). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_041825.
VAR_SEQ 231 256 WHSKVRQKSEVDIVVSEDLNGTVKFS -> CVRMWPGTVAH
SCNPSTLGGRGRWIS (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_041826.
VAR_SEQ 257 756 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_041827.
VARIANT 360 360 A -> S (in breast cancer samples;
infiltrating ductal carcinoma; somatic
mutation). {ECO:0000269|PubMed:16959974,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_035626.
VARIANT 369 369 Q -> R (in dbSNP:rs56411242).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040567.
VARIANT 526 526 R -> Q (in dbSNP:rs2272736).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040568.
VARIANT 554 554 R -> W (in dbSNP:rs17875749).
{ECO:0000269|Ref.6}.
/FTId=VAR_021124.
VARIANT 710 710 A -> T (in dbSNP:rs34309584).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040569.
VARIANT 734 734 F -> L (in dbSNP:rs56301637).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040570.
VARIANT 736 736 A -> T (in dbSNP:rs17611716).
/FTId=VAR_051628.
MUTAGEN 44 44 K->A: Loss of kinase activity and no
effect on binding to NIK.
{ECO:0000269|PubMed:9346484,
ECO:0000269|PubMed:9346485}.
MUTAGEN 163 163 K->R: Monoubiquitinated; when associated
with E-177 and E-181.
{ECO:0000269|PubMed:19675099}.
MUTAGEN 177 181 SLCTS->ALCTA: COmplete loss of TBK1-
mediated phosphorylation.
{ECO:0000269|PubMed:10783893}.
MUTAGEN 177 177 S->A: Decrease of activity.
{ECO:0000269|PubMed:19675099,
ECO:0000269|PubMed:9346484}.
MUTAGEN 177 177 S->E: Full activation. Interaction with
TRIM21 is enhanced; when associated with
E-181. Monoubiquitinated; when associated
with R-163 and E-181. Strongly promoted
NF-kappa-B gene expression; when
associated with E-181.
{ECO:0000269|PubMed:19675099,
ECO:0000269|PubMed:9346484}.
MUTAGEN 181 181 S->A: Decrease of activity.
{ECO:0000269|PubMed:19675099,
ECO:0000269|PubMed:9346484}.
MUTAGEN 181 181 S->E: Full activation. Interaction with
TRIM21 is enhanced; when associated with
E-177. Monoubiquitinated; when associated
with R-163 and E-177. Strongly promoted
NF-kappa-B gene expression; when
associated with E-177.
{ECO:0000269|PubMed:19675099,
ECO:0000269|PubMed:9346484}.
MUTAGEN 191 191 P->A: Loss of hypoxic inducibility.
{ECO:0000269|PubMed:17114296}.
CONFLICT 259 259 L -> S (in Ref. 5; BAG63942/BAH14789).
{ECO:0000305}.
STRAND 15 22 {ECO:0000244|PDB:4KIK}.
STRAND 29 34 {ECO:0000244|PDB:4KIK}.
TURN 35 37 {ECO:0000244|PDB:4KIK}.
STRAND 40 44 {ECO:0000244|PDB:4KIK}.
HELIX 52 67 {ECO:0000244|PDB:4KIK}.
TURN 81 83 {ECO:0000244|PDB:4KIK}.
HELIX 84 86 {ECO:0000244|PDB:4KIK}.
STRAND 87 91 {ECO:0000244|PDB:4KIK}.
STRAND 94 97 {ECO:0000244|PDB:4KIK}.
HELIX 104 109 {ECO:0000244|PDB:4KIK}.
HELIX 111 113 {ECO:0000244|PDB:4KIK}.
HELIX 119 138 {ECO:0000244|PDB:4KIK}.
HELIX 148 150 {ECO:0000244|PDB:4KIK}.
STRAND 151 155 {ECO:0000244|PDB:4KIK}.
STRAND 157 164 {ECO:0000244|PDB:4KIK}.
HELIX 182 185 {ECO:0000244|PDB:4KIK}.
TURN 186 188 {ECO:0000244|PDB:4KIK}.
HELIX 191 195 {ECO:0000244|PDB:4KIK}.
HELIX 202 217 {ECO:0000244|PDB:4KIK}.
HELIX 228 235 {ECO:0000244|PDB:4KIK}.
STRAND 244 247 {ECO:0000244|PDB:4KIK}.
STRAND 253 258 {ECO:0000244|PDB:4KIK}.
HELIX 267 280 {ECO:0000244|PDB:4KIK}.
TURN 285 289 {ECO:0000244|PDB:4KIK}.
TURN 292 294 {ECO:0000244|PDB:4KIK}.
TURN 296 298 {ECO:0000244|PDB:4KIK}.
HELIX 299 307 {ECO:0000244|PDB:4KIK}.
STRAND 310 316 {ECO:0000244|PDB:4KIK}.
TURN 317 320 {ECO:0000244|PDB:4KIK}.
STRAND 321 327 {ECO:0000244|PDB:4KIK}.
HELIX 333 344 {ECO:0000244|PDB:4KIK}.
HELIX 348 350 {ECO:0000244|PDB:4KIK}.
STRAND 353 355 {ECO:0000244|PDB:4KIK}.
HELIX 367 370 {ECO:0000244|PDB:4KIK}.
TURN 382 385 {ECO:0000244|PDB:4KIK}.
STRAND 386 389 {ECO:0000244|PDB:4KIK}.
HELIX 408 415 {ECO:0000244|PDB:4KIK}.
HELIX 423 499 {ECO:0000244|PDB:4KIK}.
TURN 500 504 {ECO:0000244|PDB:4KIK}.
HELIX 509 520 {ECO:0000244|PDB:4KIK}.
HELIX 527 548 {ECO:0000244|PDB:4KIK}.
HELIX 559 575 {ECO:0000244|PDB:4KIK}.
HELIX 579 581 {ECO:0000244|PDB:4KIK}.
HELIX 588 661 {ECO:0000244|PDB:4KIK}.
HELIX 706 729 {ECO:0000244|PDB:3BRV}.
HELIX 734 736 {ECO:0000244|PDB:3BRV}.
HELIX 740 742 {ECO:0000244|PDB:3BRV}.
SEQUENCE 756 AA; 86564 MW; F9CADF671AE9E14E CRC64;
MSWSPSLTTQ TCGAWEMKER LGTGGFGNVI RWHNQETGEQ IAIKQCRQEL SPRNRERWCL
EIQIMRRLTH PNVVAARDVP EGMQNLAPND LPLLAMEYCQ GGDLRKYLNQ FENCCGLREG
AILTLLSDIA SALRYLHENR IIHRDLKPEN IVLQQGEQRL IHKIIDLGYA KELDQGSLCT
SFVGTLQYLA PELLEQQKYT VTVDYWSFGT LAFECITGFR PFLPNWQPVQ WHSKVRQKSE
VDIVVSEDLN GTVKFSSSLP YPNNLNSVLA ERLEKWLQLM LMWHPRQRGT DPTYGPNGCF
KALDDILNLK LVHILNMVTG TIHTYPVTED ESLQSLKARI QQDTGIPEED QELLQEAGLA
LIPDKPATQC ISDGKLNEGH TLDMDLVFLF DNSKITYETQ ISPRPQPESV SCILQEPKRN
LAFFQLRKVW GQVWHSIQTL KEDCNRLQQG QRAAMMNLLR NNSCLSKMKN SMASMSQQLK
AKLDFFKTSI QIDLEKYSEQ TEFGITSDKL LLAWREMEQA VELCGRENEV KLLVERMMAL
QTDIVDLQRS PMGRKQGGTL DDLEEQAREL YRRLREKPRD QRTEGDSQEM VRLLLQAIQS
FEKKVRVIYT QLSKTVVCKQ KALELLPKVE EVVSLMNEDE KTVVRLQEKR QKELWNLLKI
ACSKVRGPVS GSPDSMNASR LSQPGQLMSQ PSTASNSLPE PAKKSEELVA EAHNLCTLLE
NAIQDTVREQ DQSFTALDWS WLQTEEEEHS CLEQAS


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