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Inhibitor of nuclear factor kappa-B kinase subunit alpha (I-kappa-B kinase alpha) (IKK-A) (IKK-alpha) (IkBKA) (IkappaB kinase) (EC 2.7.11.10) (Conserved helix-loop-helix ubiquitous kinase) (I-kappa-B kinase 1) (IKK1) (Nuclear factor NF-kappa-B inhibitor kinase alpha) (NFKBIKA) (Transcription factor 16) (TCF-16)

 IKKA_HUMAN              Reviewed;         745 AA.
O15111; O14666; Q13132; Q5W0I4; Q92467;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 2.
30-AUG-2017, entry version 194.
RecName: Full=Inhibitor of nuclear factor kappa-B kinase subunit alpha;
Short=I-kappa-B kinase alpha;
Short=IKK-A;
Short=IKK-alpha;
Short=IkBKA;
Short=IkappaB kinase;
EC=2.7.11.10;
AltName: Full=Conserved helix-loop-helix ubiquitous kinase;
AltName: Full=I-kappa-B kinase 1;
Short=IKK1;
AltName: Full=Nuclear factor NF-kappa-B inhibitor kinase alpha;
Short=NFKBIKA;
AltName: Full=Transcription factor 16;
Short=TCF-16;
Name=CHUK; Synonyms=IKKA, TCF16;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF LYS-44, AND VARIANT
ILE-268.
TISSUE=T-cell;
PubMed=9244310; DOI=10.1016/S0092-8674(00)80344-X;
Regnier C.H., Song H.Y., Gao X., Goeddel D.V., Cao Z., Rothe M.;
"Identification and characterization of an IkappaB kinase.";
Cell 90:373-383(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND VARIANT
ILE-268.
PubMed=9252186; DOI=10.1038/41493;
DiDonato J.A., Hayakawa M., Rothwarf D.M., Zandi E., Karin M.;
"A cytokine-responsive IkappaB kinase that activates the transcription
factor NF-kappaB.";
Nature 388:548-554(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND MUTAGENESIS
OF LYS-44 AND SER-176.
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ILE-268.
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).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-268.
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 32-745, AND VARIANT ILE-268.
TISSUE=Cervix carcinoma;
PubMed=8777433;
Connelly M.A., Marcu K.B.;
"CHUK, a new member of the helix-loop-helix and leucine zipper
families of interacting proteins, contains a serine-threonine kinase
catalytic domain.";
Cell. Mol. Biol. Res. 41:537-549(1995).
[8]
PROTEIN SEQUENCE OF 169-181, INACTIVATION BY YERSINIA YOPJ (MICROBIAL
INFECTION), ACETYLATION AT THR-179 (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).
[9]
IDENTIFICATION IN A COMPLEX WITH IKBKB; NFKBIA; RELA; IKBKAP 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).
[10]
PHOSPHORYLATION AT SER-176, AND MUTAGENESIS OF SER-176; THR-179 AND
SER-180.
PubMed=9520446; DOI=10.1073/pnas.95.7.3792;
Ling L., Cao Z., Goeddel D.V.;
"NF-kappaB-inducing kinase activates IKK-alpha by phosphorylation of
Ser-176.";
Proc. Natl. Acad. Sci. U.S.A. 95:3792-3797(1998).
[11]
PHOSPHORYLATION AT THR-23, AND MUTAGENESIS OF THR-23.
PubMed=10485710; DOI=10.1038/43466;
Ozes O.N., Mayo L.D., Gustin J.A., Pfeffer S.R., Pfeffer L.M.,
Donner D.B.;
"NF-kappaB activation by tumour necrosis factor requires the Akt
serine-threonine kinase.";
Nature 401:82-85(1999).
[12]
INTERACTION WITH IKBKB.
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).
[13]
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).
[14]
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).
[15]
SUBUNIT OF A COMPLEX CONTAINING CREBBP; NCOA2; NCOA3; IKBKB 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).
[16]
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).
[17]
SUBCELLULAR LOCATION, AND FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
PubMed=12789342; DOI=10.1038/nature01576;
Yamamoto Y., Verma U.N., Prajapati S., Kwak Y.T., Gaynor R.B.;
"Histone H3 phosphorylation by IKK-alpha is critical for cytokine-
induced gene expression.";
Nature 423:655-659(2003).
[18]
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).
[19]
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).
[20]
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).
[21]
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).
[22]
INTERACTION WITH PIAS1.
PubMed=17540171; DOI=10.1016/j.cell.2007.03.056;
Liu B., Yang Y., Chernishof V., Loo R.R., Jang H., Tahk S., Yang R.,
Mink S., Shultz D., Bellone C.J., Loo J.A., Shuai K.;
"Proinflammatory stimuli induce IKKalpha-mediated phosphorylation of
PIAS1 to restrict inflammation and immunity.";
Cell 129:903-914(2007).
[23]
FUNCTION IN PHOSPHORYLATION OF CREBBP.
PubMed=17434128; DOI=10.1016/j.molcel.2007.02.019;
Huang W.C., Ju T.K., Hung M.C., Chen C.C.;
"Phosphorylation of CBP by IKKalpha promotes cell growth by switching
the binding preference of CBP from p53 to NF-kappaB.";
Mol. Cell 26:75-87(2007).
[24]
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).
[25]
PHOSPHORYLATION AT THR-23 AND SER-180 BY SGK1.
PubMed=19088076; DOI=10.1074/jbc.M805055200;
Tai D.J., Su C.C., Ma Y.L., Lee E.H.;
"SGK1 phosphorylation of IkappaB Kinase alpha and p300 Up-regulates
NF-kappaB activity and increases N-Methyl-D-aspartate receptor NR2A
and NR2B expression.";
J. Biol. Chem. 284:4073-4089(2009).
[26]
INTERACTION WITH TRAF2.
PubMed=19150425; DOI=10.1016/j.molcel.2008.11.023;
Li S., Wang L., Dorf M.E.;
"PKC phosphorylation of TRAF2 mediates IKKalpha/beta recruitment and
K63-linked polyubiquitination.";
Mol. Cell 33:30-42(2009).
[27]
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).
[28]
INVOLVEMENT IN COCOS.
PubMed=20961246; DOI=10.1056/NEJMoa0911698;
Lahtela J., Nousiainen H.O., Stefanovic V., Tallila J., Viskari H.,
Karikoski R., Gentile M., Saloranta C., Varilo T., Salonen R.,
Kestila M.;
"Mutant CHUK and severe fetal encasement malformation.";
N. Engl. J. Med. 363:1631-1637(2010).
[29]
FUNCTION IN MAP3K14 PHOSPHORYLATION.
PubMed=20501937; DOI=10.1126/scisignal.2000778;
Razani B., Zarnegar B., Ytterberg A.J., Shiba T., Dempsey P.W.,
Ware C.F., Loo J.A., Cheng G.;
"Negative feedback in noncanonical NF-kappaB signaling modulates NIK
stability through IKKalpha-mediated phosphorylation.";
Sci. Signal. 3:RA41-RA41(2010).
[30]
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).
[31]
FUNCTION IN PHOSPHORYLATION OF TAX1BP1.
PubMed=21765415; DOI=10.1038/ni.2066;
Shembade N., Pujari R., Harhaj N.S., Abbott D.W., Harhaj E.W.;
"The kinase IKKalpha inhibits activation of the transcription factor
NF-kappaB by phosphorylating the regulatory molecule TAX1BP1.";
Nat. Immunol. 12:834-843(2011).
[32]
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).
[33]
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).
[34]
VARIANTS [LARGE SCALE ANALYSIS] CYS-126; ALA-155 AND ILE-268.
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).
[35]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 732-745.
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).
-!- 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 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. Negatively regulates the pathway
by phosphorylating the scaffold protein TAXBP1 and thus promoting
the assembly of the A20/TNFAIP3 ubiquitin-editing complex
(composed of A20/TNFAIP3, TAX1BP1, and the E3 ligases ITCH and
RNF11). Therefore, CHUK plays a key role in the negative feedback
of NF-kappa-B canonical signaling to limit inflammatory gene
activation. As part of the non-canonical pathway of NF-kappa-B
activation, the MAP3K14-activated CHUK/IKKA homodimer
phosphorylates NFKB2/p100 associated with RelB, inducing its
proteolytic processing to NFKB2/p52 and the formation of NF-kappa-
B RelB-p52 complexes. In turn, these complexes regulate genes
encoding molecules involved in B-cell survival and lymphoid
organogenesis. Participates also in the negative feedback of the
non-canonical NF-kappa-B signaling pathway by phosphorylating and
destabilizing MAP3K14/NIK. Within the nucleus, phosphorylates
CREBBP and consequently increases both its transcriptional and
histone acetyltransferase activities. Modulates chromatin
accessibility at NF-kappa-B-responsive promoters by
phosphorylating histones H3 at 'Ser-10' that are subsequently
acetylated at 'Lys-14' by CREBBP. Additionally, phosphorylates the
CREBBP-interacting protein NCOA3. Also phosphorylates FOXO3 and
may regulate this pro-apoptotic transcription factor
(PubMed:15084260). {ECO:0000269|PubMed:12789342,
ECO:0000269|PubMed:15084260, ECO:0000269|PubMed:17434128,
ECO:0000269|PubMed:20434986, ECO:0000269|PubMed:20501937,
ECO:0000269|PubMed:21765415}.
-!- CATALYTIC ACTIVITY: ATP + [I-kappa-B protein] = ADP + [I-kappa-B
phosphoprotein].
-!- ENZYME REGULATION: Activated when phosphorylated and inactivated
when dephosphorylated.
-!- 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:10195894,
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, IKBKAP and MAP3K14 (PubMed:9751059). Directly interacts with
TRPC4AP (By similarity). May interact with TRAF2
(PubMed:19150425). Interacts with NALP2 (PubMed:15456791). May
interact with MAVS/IPS1 (PubMed:16177806). Interacts with ARRB1
and ARRB2 (PubMed:15173580). Interacts with NLRC5; prevents CHUK
phosphorylation and kinase activity (PubMed:20434986). Interacts
with PIAS1; this interaction induces PIAS1 phosphorylation
(PubMed:17540171). Interacts with ZNF268 isoform 2; the
interaction is further increased in a TNF-alpha-dependent manner
(PubMed:23091055). Interacts with FOXO3 (PubMed:15084260).
Interacts with IFIT5; the interaction synergizes the recruitment
of IKK to MAP3K7 and enhances IKK phosphorylation
(PubMed:26334375). {ECO:0000250|UniProtKB:Q60680,
ECO:0000269|PubMed:10195894, ECO:0000269|PubMed:11971985,
ECO:0000269|PubMed:12612076, ECO:0000269|PubMed:15084260,
ECO:0000269|PubMed:15173580, ECO:0000269|PubMed:15456791,
ECO:0000269|PubMed:16177806, ECO:0000269|PubMed:17540171,
ECO:0000269|PubMed:19150425, ECO:0000269|PubMed:20434986,
ECO:0000269|PubMed:23091055, ECO:0000269|PubMed:26334375,
ECO:0000269|PubMed:9751059}.
-!- INTERACTION:
P32121:ARRB2; NbExp=3; IntAct=EBI-81249, EBI-714559;
Q16543:CDC37; NbExp=4; IntAct=EBI-81249, EBI-295634;
P46527:CDKN1B; NbExp=4; IntAct=EBI-81249, EBI-519280;
P03129:E7 (xeno); NbExp=2; IntAct=EBI-81249, EBI-866453;
Q07857:E7 (xeno); NbExp=2; IntAct=EBI-81249, EBI-9690349;
Q6TY28:E7 (xeno); NbExp=2; IntAct=EBI-81249, EBI-9690312;
Q6TY35:E7 (xeno); NbExp=2; IntAct=EBI-81249, EBI-9690239;
Q80901:E7 (xeno); NbExp=2; IntAct=EBI-81249, EBI-9690278;
Q8B5B5:E7 (xeno); NbExp=2; IntAct=EBI-81249, EBI-9690330;
Q13451:FKBP5; NbExp=2; IntAct=EBI-81249, EBI-306914;
P07900:HSP90AA1; NbExp=3; IntAct=EBI-81249, EBI-296047;
O14920:IKBKB; NbExp=15; IntAct=EBI-81249, EBI-81266;
Q9Y6K9:IKBKG; NbExp=21; IntAct=EBI-81249, EBI-81279;
Q92985:IRF7; NbExp=4; IntAct=EBI-81249, EBI-968267;
Q99558:MAP3K14; NbExp=6; IntAct=EBI-81249, EBI-358011;
Q5TCX8:MAP3K21; NbExp=2; IntAct=EBI-81249, EBI-1057380;
P01106:MYC; NbExp=3; IntAct=EBI-81249, EBI-447544;
P19838:NFKB1; NbExp=3; IntAct=EBI-81249, EBI-300010;
P25963:NFKBIA; NbExp=14; IntAct=EBI-81249, EBI-307386;
Q77M19:P (xeno); NbExp=2; IntAct=EBI-81249, EBI-6149376;
Q04206:RELA; NbExp=2; IntAct=EBI-81249, EBI-73886;
Q86VP1:TAX1BP1; NbExp=2; IntAct=EBI-81249, EBI-529518;
P24772:VACWR196 (xeno); NbExp=3; IntAct=EBI-81249, EBI-4291651;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12789342}.
Nucleus {ECO:0000269|PubMed:12789342}. Note=Shuttles between the
cytoplasm and the nucleus.
-!- TISSUE SPECIFICITY: Widely expressed.
-!- 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: Phosphorylated by MAP3K14/NIK, AKT and to a lesser extent by
MEKK1, and dephosphorylated by PP2A. Autophosphorylated.
-!- PTM: (Microbial infection) Acetylation of Thr-179 by Yersinia yopJ
prevents phosphorylation and activation, thus blocking the I-
kappa-B signaling pathway. {ECO:0000269|PubMed:17116858}.
-!- DISEASE: Cocoon syndrome (COCOS) [MIM:613630]: A lethal syndrome
characterized by multiple fetal malformations including defective
face and seemingly absent limbs, which are bound to the trunk and
encased under the skin. {ECO:0000269|PubMed:20961246}. 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/chuk/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF012890; AAC51662.1; -; mRNA.
EMBL; AF009225; AAC51671.1; -; mRNA.
EMBL; AF080157; AAD08996.1; -; mRNA.
EMBL; AY652653; AAT49098.1; -; Genomic_DNA.
EMBL; AL138921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; U22512; AAC50713.1; -; mRNA.
CCDS; CCDS7488.1; -.
RefSeq; NP_001269.3; NM_001278.4.
UniGene; Hs.198998; -.
PDB; 3BRT; X-ray; 2.25 A; A/C=732-745.
PDB; 5EBZ; X-ray; 4.50 A; A/B/C/D/E/F/G/H/I/J/K/L=10-660.
PDB; 5TQW; EM; 5.60 A; A/B=10-660.
PDB; 5TQX; EM; 5.40 A; A/B=10-660.
PDB; 5TQY; EM; 5.20 A; A/B=10-660.
PDBsum; 3BRT; -.
PDBsum; 5EBZ; -.
PDBsum; 5TQW; -.
PDBsum; 5TQX; -.
PDBsum; 5TQY; -.
ProteinModelPortal; O15111; -.
SMR; O15111; -.
BioGrid; 107569; 135.
DIP; DIP-27526N; -.
ELM; O15111; -.
IntAct; O15111; 60.
MINT; MINT-88648; -.
STRING; 9606.ENSP00000359424; -.
BindingDB; O15111; -.
ChEMBL; CHEMBL3476; -.
DrugBank; DB06151; Acetylcysteine.
DrugBank; DB00233; Aminosalicylic Acid.
DrugBank; DB00244; Mesalazine.
DrugBank; DB00795; Sulfasalazine.
GuidetoPHARMACOLOGY; 1989; -.
iPTMnet; O15111; -.
PhosphoSitePlus; O15111; -.
BioMuta; CHUK; -.
EPD; O15111; -.
MaxQB; O15111; -.
PaxDb; O15111; -.
PeptideAtlas; O15111; -.
PRIDE; O15111; -.
Ensembl; ENST00000370397; ENSP00000359424; ENSG00000213341.
GeneID; 1147; -.
KEGG; hsa:1147; -.
UCSC; uc001kqp.4; human.
CTD; 1147; -.
DisGeNET; 1147; -.
GeneCards; CHUK; -.
H-InvDB; HIX0201495; -.
HGNC; HGNC:1974; CHUK.
HPA; CAB004240; -.
HPA; CAB018564; -.
HPA; HPA001402; -.
MalaCards; CHUK; -.
MIM; 600664; gene.
MIM; 613630; phenotype.
neXtProt; NX_O15111; -.
OpenTargets; ENSG00000213341; -.
PharmGKB; PA26510; -.
eggNOG; KOG4250; Eukaryota.
eggNOG; ENOG410XRMU; LUCA.
GeneTree; ENSGT00880000137876; -.
HOGENOM; HOG000038048; -.
HOVERGEN; HBG018241; -.
InParanoid; O15111; -.
KO; K04467; -.
OMA; FVLMDHI; -.
OrthoDB; EOG091G02VC; -.
PhylomeDB; O15111; -.
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-1810476; RIP-mediated NFkB activation via ZBP1.
Reactome; R-HSA-198323; AKT phosphorylates targets in the cytosol.
Reactome; R-HSA-202424; Downstream TCR signaling.
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 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-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5674400; Constitutive Signaling by AKT1 E17K in Cancer.
Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB 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; O15111; -.
SignaLink; O15111; -.
SIGNOR; O15111; -.
ChiTaRS; CHUK; human.
EvolutionaryTrace; O15111; -.
GeneWiki; CHUK; -.
GenomeRNAi; 1147; -.
PRO; PR:O15111; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000213341; -.
CleanEx; HS_CHUK; -.
Genevisible; O15111; HS.
GO; GO:0035631; C:CD40 receptor complex; ISS:BHF-UCL.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
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:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0097110; F:scaffold protein binding; IDA:MGI.
GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0071276; P:cellular response to cadmium ion; IMP:CAFA.
GO; GO:0034614; P:cellular response to reactive oxygen species; IMP:CAFA.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:UniProtKB.
GO; GO:0098586; P:cellular response to virus; IMP:CAFA.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IMP:CAFA.
GO; GO:0007252; P:I-kappaB phosphorylation; TAS:ProtInc.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0006954; P:inflammatory response; TAS:UniProtKB.
GO; GO:0045087; P:innate immune response; TAS:UniProtKB.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
GO; GO:0038061; P:NIK/NF-kappaB signaling; IMP:CAFA.
GO; GO:0070423; P:nucleotide-binding oligomerization domain containing signaling pathway; TAS:Reactome.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; TAS:Reactome.
GO; GO:1902741; P:positive regulation of interferon-alpha secretion; IMP:CAFA.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; TAS:UniProtKB.
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; IMP:CAFA.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0010803; P:regulation of tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
GO; GO:0010034; P:response to acetate; IEA:Ensembl.
GO; GO:0043200; P:response to amino acid; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0033194; P:response to hydroperoxide; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
GO; GO:0009615; P:response to virus; TAS:UniProtKB.
GO; GO:0007266; P:Rho protein signal transduction; IEA:Ensembl.
GO; GO:0003009; P:skeletal muscle contraction; IEA:Ensembl.
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:0051146; P:striated muscle cell differentiation; IEA:Ensembl.
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; IBA:GO_Central.
InterPro; IPR022007; IKKbetaNEMObind.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF12179; IKKbetaNEMObind; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM01239; IKKbetaNEMObind; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Complete proteome; Cytoplasm;
Direct protein sequencing; Kinase; Nucleotide-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 745 Inhibitor of nuclear factor kappa-B
kinase subunit alpha.
/FTId=PRO_0000086011.
DOMAIN 15 302 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 21 29 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 455 476 Leucine-zipper.
REGION 738 743 NEMO-binding.
ACT_SITE 144 144 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 44 44 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 23 23 Phosphothreonine; by PKB/AKT1 and SGK1.
{ECO:0000269|PubMed:10485710,
ECO:0000269|PubMed:19088076}.
MOD_RES 176 176 Phosphoserine; by MAP3K14.
{ECO:0000269|PubMed:9520446}.
MOD_RES 179 179 O-acetylthreonine; by Yersinia yopJ.
{ECO:0000269|PubMed:17116858}.
MOD_RES 180 180 Phosphoserine; by SGK1.
{ECO:0000269|PubMed:19088076}.
VARIANT 126 126 S -> C (in dbSNP:rs34427437).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040565.
VARIANT 155 155 V -> A (in dbSNP:rs2230803).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040566.
VARIANT 268 268 V -> I (in dbSNP:rs2230804).
{ECO:0000269|PubMed:15164054,
ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:8777433,
ECO:0000269|PubMed:9244310,
ECO:0000269|PubMed:9252186,
ECO:0000269|PubMed:9813230}.
/FTId=VAR_021359.
MUTAGEN 23 23 T->A: Loss of phosphorylation and
decrease of kinase activity.
{ECO:0000269|PubMed:10485710}.
MUTAGEN 44 44 K->A: Loss of kinase activity.
{ECO:0000269|PubMed:9244310,
ECO:0000269|PubMed:9346484}.
MUTAGEN 44 44 K->M: Loss of autophosphorylation.
{ECO:0000269|PubMed:9244310,
ECO:0000269|PubMed:9346484}.
MUTAGEN 176 176 S->A: Loss of phosphorylation and of
activity. {ECO:0000269|PubMed:9346484,
ECO:0000269|PubMed:9520446}.
MUTAGEN 176 176 S->E: Full activation.
{ECO:0000269|PubMed:9346484,
ECO:0000269|PubMed:9520446}.
MUTAGEN 179 179 T->A: No change in phosphorylation.
{ECO:0000269|PubMed:9520446}.
MUTAGEN 180 180 S->A: No change in phosphorylation.
{ECO:0000269|PubMed:9520446}.
CONFLICT 543 543 E -> G (in Ref. 2; AAC51671).
{ECO:0000305}.
CONFLICT 604 604 L -> R (in Ref. 7; AAC50713).
{ECO:0000305}.
CONFLICT 679 680 TS -> AY (in Ref. 7; AAC50713).
{ECO:0000305}.
CONFLICT 684 684 P -> A (in Ref. 3; no nucleotide entry
and 7; AAC50713). {ECO:0000305}.
CONFLICT 686 687 TS -> DL (in Ref. 7; AAC50713).
{ECO:0000305}.
HELIX 735 737 {ECO:0000244|PDB:3BRT}.
HELIX 741 743 {ECO:0000244|PDB:3BRT}.
SEQUENCE 745 AA; 84640 MW; 4EA55C6FFC66FA16 CRC64;
MERPPGLRPG AGGPWEMRER LGTGGFGNVC LYQHRELDLK IAIKSCRLEL STKNRERWCH
EIQIMKKLNH ANVVKACDVP EELNILIHDV PLLAMEYCSG GDLRKLLNKP ENCCGLKESQ
ILSLLSDIGS GIRYLHENKI IHRDLKPENI VLQDVGGKII HKIIDLGYAK DVDQGSLCTS
FVGTLQYLAP ELFENKPYTA TVDYWSFGTM VFECIAGYRP FLHHLQPFTW HEKIKKKDPK
CIFACEEMSG EVRFSSHLPQ PNSLCSLVVE PMENWLQLML NWDPQQRGGP VDLTLKQPRC
FVLMDHILNL KIVHILNMTS AKIISFLLPP DESLHSLQSR IERETGINTG SQELLSETGI
SLDPRKPASQ CVLDGVRGCD SYMVYLFDKS KTVYEGPFAS RSLSDCVNYI VQDSKIQLPI
IQLRKVWAEA VHYVSGLKED YSRLFQGQRA AMLSLLRYNA NLTKMKNTLI SASQQLKAKL
EFFHKSIQLD LERYSEQMTY GISSEKMLKA WKEMEEKAIH YAEVGVIGYL EDQIMSLHAE
IMELQKSPYG RRQGDLMESL EQRAIDLYKQ LKHRPSDHSY SDSTEMVKII VHTVQSQDRV
LKELFGHLSK LLGCKQKIID LLPKVEVALS NIKEADNTVM FMQGKRQKEI WHLLKIACTQ
SSARSLVGSS LEGAVTPQTS AWLPPTSAEH DHSLSCVVTP QDGETSAQMI EENLNCLGHL
STIIHEANEE QGNSMMNLDW SWLTE


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