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NF-kappa-B inhibitor alpha (I-kappa-B-alpha) (IkB-alpha) (IkappaBalpha) (Major histocompatibility complex enhancer-binding protein MAD3)

 IKBA_HUMAN              Reviewed;         317 AA.
P25963; B2R8L6;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
01-MAY-1992, sequence version 1.
12-SEP-2018, entry version 207.
RecName: Full=NF-kappa-B inhibitor alpha;
AltName: Full=I-kappa-B-alpha;
Short=IkB-alpha;
Short=IkappaBalpha;
AltName: Full=Major histocompatibility complex enhancer-binding protein MAD3;
Name=NFKBIA; Synonyms=IKBA, MAD3, NFKBI;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Monocyte;
PubMed=1829648; DOI=10.1016/0092-8674(91)90022-Q;
Haskill S., Beg A.A., Tompkins S.M., Morris J.S., Yurochko A.D.,
Sampson-Johannes A., Mondal K., Ralph P., Baldwin A.S. Jr.;
"Characterization of an immediate-early gene induced in adherent
monocytes that encodes I kappa B-like activity.";
Cell 65:1281-1289(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Lymph node;
PubMed=10637284; DOI=10.1084/jem.191.2.395;
Jungnickel B., Staratschek-Jox A., Braeuninger A., Spieker T.,
Wolf J., Diehl V., Hansmann M.-L., Rajewsky K., Kueppers R.;
"Clonal deleterious mutations in the IkappaB alpha gene in the
malignant cells in Hodgkin's lymphoma.";
J. Exp. Med. 191:395-402(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Liu B., Huang A.;
"Homo sapiens IkBa mRNA.";
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cerebellum;
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Kidney;
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).
[10]
INTERACTION WITH RELA.
PubMed=1493333; DOI=10.1091/mbc.3.12.1339;
Ganchi P.A., Sun S.C., Greene W.C., Ballard D.W.;
"I kappa B/MAD-3 masks the nuclear localization signal of NF-kappa B
p65 and requires the transactivation domain to inhibit NF-kappa B p65
DNA binding.";
Mol. Biol. Cell 3:1339-1352(1992).
[11]
UBIQUITINATION AT LYS-21 AND LYS-22, FUNCTION, AND MUTAGENESIS OF
LYS-21; LYS-22; LYS-38 AND LYS-47.
PubMed=7479976; DOI=10.1073/pnas.92.24.11259;
Scherer D.C., Brockman J.A., Chen Z., Maniatis T., Ballard D.W.;
"Signal-induced degradation of IkappaB alpha requires site-specific
ubiquitination.";
Proc. Natl. Acad. Sci. U.S.A. 92:11259-11263(1995).
[12]
PHOSPHORYLATION AT TYR-42, AND MUTAGENESIS OF TYR-42.
PubMed=8797825; DOI=10.1016/S0092-8674(00)80153-1;
Imbert V., Rupec R.A., Livolsi A., Pahl H.L., Traenckner E.B.-M.,
Mueller-Dieckmann C., Farahifar D., Rossi B., Auberger P.,
Baeuerle P.A., Peyron J.-F.;
"Tyrosine phosphorylation of IkappaB-alpha activates NF-kappaB without
proteolytic degradation of IkappaB-alpha.";
Cell 86:787-798(1996).
[13]
PHOSPHORYLATION AT SER-283; SER-288; SER-293 AND THR-291.
PubMed=8622692; DOI=10.1128/MCB.16.3.899;
McElhinny J.A., Trushin S.A., Bren G.D., Chester N., Paya C.V.;
"Casein kinase II phosphorylates I kappa B alpha at S-283, S-289, S-
293, and T-291 and is required for its degradation.";
Mol. Cell. Biol. 16:899-906(1996).
[14]
MUTAGENESIS OF LYS-21; LYS-22; ASP-31; SER-32; ASP-35; SER-36;
SER-234; SER-262 AND THR-263.
PubMed=8657102; DOI=10.1128/MCB.16.4.1295;
DiDonato J.A., Mercurio F., Rosette C., Wu-Li J., Suyang H., Ghosh S.,
Karin M.;
"Mapping of the inducible IkappaB phosphorylation sites that signal
its ubiquitination and degradation.";
Mol. Cell. Biol. 16:1295-1304(1996).
[15]
PHOSPHORYLATION AT THR-291; SER-283 AND THR-299.
PubMed=8657113; DOI=10.1128/MCB.16.4.1401;
Lin R., Beauparlant P., Makris C., Meloche S., Hiscott J.;
"Phosphorylation of IkappaBalpha in the C-terminal PEST domain by
casein kinase II affects intrinsic protein stability.";
Mol. Cell. Biol. 16:1401-1409(1996).
[16]
SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, AND MUTAGENESIS OF
115-LEU--ILE-120.
PubMed=9566872; DOI=10.1128/MCB.18.5.2524;
Sachdev S., Hoffmann A., Hannink M.;
"Nuclear localization of IkappaB alpha is mediated by the second
ankyrin repeat: the IkappaB alpha ankyrin repeats define a novel class
of cis-acting nuclear import sequences.";
Mol. Cell. Biol. 18:2524-2534(1998).
[17]
UBIQUITINATION BY THE SCF(FBXW11) COMPLEX.
PubMed=10437795; DOI=10.1016/S0014-5793(99)00895-9;
Vuillard L., Nicholson J., Hay R.T.;
"A complex containing betaTrCP recruits Cdc34 to catalyse
ubiquitination of IkappaBalpha.";
FEBS Lett. 455:311-314(1999).
[18]
PHOSPHORYLATION AT SER-32 AND SER-36, MUTAGENESIS OF SER-32 AND
SER-36, AND UBIQUITINATION BY UBE2D2 AND UBE2D3.
PubMed=10329681; DOI=10.1074/jbc.274.21.14823;
Gonen H., Bercovich B., Orian A., Carrano A., Takizawa C.,
Yamanaka K., Pagano M., Iwai K., Ciechanover A.;
"Identification of the ubiquitin carrier proteins, E2s, involved in
signal-induced conjugation and subsequent degradation of
IkappaBalpha.";
J. Biol. Chem. 274:14823-14830(1999).
[19]
INTERACTION WITH HEPATITIS B VIRUS/HBV PROTEIN X (MICROBIAL
INFECTION).
PubMed=10454581; DOI=10.1128/MCB.19.9.6345;
Weil R., Sirma H., Giannini C., Kremsdorf D., Bessia C., Dargemont C.,
Brechot C., Israel A.;
"Direct association and nuclear import of the hepatitis B virus X
protein with the NF-kappaB inhibitor IkappaBalpha.";
Mol. Cell. Biol. 19:6345-6354(1999).
[20]
PHOSPHORYLATION AT SER-32 AND SER-36.
PubMed=10882136; DOI=10.1016/S1097-2765(00)80445-1;
Peters R.T., Liao S.-M., Maniatis T.;
"IKK epsilon is part of a novel PMA-inducible IkappaB kinase
complex.";
Mol. Cell 5:513-522(2000).
[21]
PHOSPHORYLATION BY TBK1.
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).
[22]
INTERACTION WITH NKIRAS1 AND NKIRAS2.
PubMed=10657303; DOI=10.1126/science.287.5454.869;
Fenwick C., Na S.-Y., Voll R.E., Zhong H., Im S.-Y., Lee J.W.,
Ghosh S.;
"A subclass of Ras proteins that regulate the degradation of
IkappaB.";
Science 287:869-873(2000).
[23]
SUBCELLULAR LOCATION, NUCLEAR EXPORT SIGNAL, AND MUTAGENESIS OF
45-MET--ILE-52.
PubMed=10655476; DOI=10.1073/pnas.97.3.1014;
Huang T.T., Kudo N., Yoshida M., Miyamoto S.;
"A nuclear export signal in the N-terminal regulatory domain of
IkappaBalpha controls cytoplasmic localization of inactive NF-
kappaB/IkappaBalpha complexes.";
Proc. Natl. Acad. Sci. U.S.A. 97:1014-1019(2000).
[24]
SUMOYLATION AT LYS-21, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-21
AND LYS-22.
PubMed=11124955; DOI=10.1074/jbc.M009476200;
Rodriguez M.S., Dargemont C., Hay R.T.;
"SUMO-1 conjugation in vivo requires both a consensus modification
motif and nuclear targeting.";
J. Biol. Chem. 276:12654-12659(2001).
[25]
INTERACTION WITH PRKACA.
PubMed=20356841; DOI=10.1074/jbc.M109.077602;
Gambaryan S., Kobsar A., Rukoyatkina N., Herterich S., Geiger J.,
Smolenski A., Lohmann S.M., Walter U.;
"Thrombin and collagen induce a feedback inhibitory signaling pathway
in platelets involving dissociation of the catalytic subunit of
protein kinase A from an NFkappaB-IkappaB complex.";
J. Biol. Chem. 285:18352-18363(2010).
[26]
INTERACTION WITH PRMT2, AND SUBCELLULAR LOCATION.
PubMed=16648481; DOI=10.1128/MCB.26.10.3864-3874.2006;
Ganesh L., Yoshimoto T., Moorthy N.C., Akahata W., Boehm M.,
Nabel E.G., Nabel G.J.;
"Protein methyltransferase 2 inhibits NF-kappaB function and promotes
apoptosis.";
Mol. Cell. Biol. 26:3864-3874(2006).
[27]
INTERACTION WITH HIF1AN, HYDROXYLATION AT ASN-210 AND ASN-244, AND
MUTAGENESIS OF ASN-210 AND ASN-244.
PubMed=17003112; DOI=10.1073/pnas.0606877103;
Cockman M.E., Lancaster D.E., Stolze I.P., Hewitson K.S.,
McDonough M.A., Coleman M.L., Coles C.H., Yu X., Hay R.T., Ley S.C.,
Pugh C.W., Oldham N.J., Masson N., Schofield C.J., Ratcliffe P.J.;
"Posttranslational hydroxylation of ankyrin repeats in IkappaB
proteins by the hypoxia-inducible factor (HIF) asparaginyl
hydroxylase, factor inhibiting HIF (FIH).";
Proc. Natl. Acad. Sci. U.S.A. 103:14767-14772(2006).
[28]
INTERACTION WITH RWDD3, SUMOYLATION, AND MUTAGENESIS OF LYS-21 AND
LYS-22.
PubMed=17956732; DOI=10.1016/j.cell.2007.07.044;
Carbia-Nagashima A., Gerez J., Perez-Castro C., Paez-Pereda M.,
Silberstein S., Stalla G.K., Holsboer F., Arzt E.;
"RSUME, a small RWD-containing protein, enhances SUMO conjugation and
stabilizes HIF-1alpha during hypoxia.";
Cell 131:309-323(2007).
[29]
INTERACTION WITH MEFV.
PubMed=18577712; DOI=10.1182/blood-2008-01-134932;
Chae J.J., Wood G., Richard K., Jaffe H., Colburn N.T., Masters S.L.,
Gumucio D.L., Shoham N.G., Kastner D.L.;
"The familial Mediterranean fever protein, pyrin, is cleaved by
caspase-1 and activates NF-kappaB through its N-terminal fragment.";
Blood 112:1794-1803(2008).
[30]
UBIQUITINATION AT LYS-21 AND LYS-22.
PubMed=20347421; DOI=10.1016/j.molcel.2010.02.025;
Wu K., Kovacev J., Pan Z.Q.;
"Priming and extending: a UbcH5/Cdc34 E2 handoff mechanism for
polyubiquitination on a SCF substrate.";
Mol. Cell 37:784-796(2010).
[31]
DEUBIQUITINATION BY PORCINE REPRODUCTIVE AND RESPIRATORY SYNDROME
VIRUS NSP2 PROTEIN.
PubMed=20504922; DOI=10.1128/JVI.00217-10;
Sun Z., Chen Z., Lawson S.R., Fang Y.;
"The cysteine protease domain of porcine reproductive and respiratory
syndrome virus nonstructural protein 2 possesses deubiquitinating and
interferon antagonism functions.";
J. Virol. 84:7832-7846(2010).
[32]
INTERACTION WITH RWDD3.
PubMed=23469069; DOI=10.1371/journal.pone.0057795;
Gerez J., Fuertes M., Tedesco L., Silberstein S., Sevlever G.,
Paez-Pereda M., Holsboer F., Turjanski A.G., Arzt E.;
"In silico structural and functional characterization of the RSUME
splice variants.";
PLoS ONE 8:E57795-E57795(2013).
[33]
INTERACTION WITH DDRGK1.
PubMed=23675531; DOI=10.1371/journal.pone.0064231;
Xi P., Ding D., Zhou J., Wang M., Cong Y.S.;
"DDRGK1 regulates NF-kappaB activity by modulating IkappaBalpha
stability.";
PLoS ONE 8:E64231-E64231(2013).
[34]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 70-282.
PubMed=9865693; DOI=10.1016/S0092-8674(00)81698-0;
Jacobs M.D., Harrison S.C.;
"Structure of an IkappaBalpha/NF-kappaB complex.";
Cell 95:749-758(1998).
[35]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 73-302.
PubMed=9865694; DOI=10.1016/S0092-8674(00)81699-2;
Huxford T., Huang D.B., Malek S., Ghosh G.;
"The crystal structure of the IkappaBalpha/NF-kappaB complex reveals
mechanisms of NF-kappaB inactivation.";
Cell 95:759-770(1998).
[36]
VARIANT ADEDAID ILE-32.
PubMed=14523047; DOI=10.1172/JCI18714;
Courtois G., Smahi A., Reichenbach J., Doffinger R., Cancrini C.,
Bonnet M., Puel A., Chable-Bessia C., Yamaoka S., Feinberg J.,
Dupuis-Girod S., Bodemer C., Livadiotti S., Novelli F., Rossi P.,
Fischer A., Israel A., Munnich A., Le Deist F., Casanova J.L.;
"A hypermorphic IkappaBalpha mutation is associated with autosomal
dominant anhidrotic ectodermal dysplasia and T cell
immunodeficiency.";
J. Clin. Invest. 112:1108-1115(2003).
[37]
INVOLVEMENT IN ADEDAID.
PubMed=18412279; DOI=10.1002/humu.20740;
Lopez-Granados E., Keenan J.E., Kinney M.C., Leo H., Jain N., Ma C.A.,
Quinones R., Gelfand E.W., Jain A.;
"A novel mutation in NFKBIA/IKBA results in a degradation-resistant N-
truncated protein and is associated with ectodermal dysplasia with
immunodeficiency.";
Hum. Mutat. 29:861-868(2008).
-!- FUNCTION: Inhibits the activity of dimeric NF-kappa-B/REL
complexes by trapping REL dimers in the cytoplasm through masking
of their nuclear localization signals. On cellular stimulation by
immune and proinflammatory responses, becomes phosphorylated
promoting ubiquitination and degradation, enabling the dimeric
RELA to translocate to the nucleus and activate transcription.
{ECO:0000269|PubMed:7479976}.
-!- SUBUNIT: Interacts with RELA; the interaction requires the nuclear
import signal. Interacts with NKIRAS1 and NKIRAS2. Part of a 70-90
kDa complex at least consisting of CHUK, IKBKB, NFKBIA, RELA, ELP1
and MAP3K14. Interacts with isoform 1 and isoform 2 of RWDD3; the
interaction enhances sumoylation. Interacts (when phosphorylated
at the 2 serine residues in the destruction motif D-S-G-X(2,3,4)-
S) with BTRC. Associates with the SCF(BTRC) complex, composed of
SKP1, CUL1 and BTRC; the association is mediated via interaction
with BTRC. Part of a SCF(BTRC)-like complex lacking CUL1, which is
associated with RELA; RELA interacts directly with NFKBIA.
Interacts with PRMT2. Interacts with PRKACA in platelets; this
interaction is disrupted by thrombin and collagen. Interacts with
HIF1AN. Interacts with MEFV. Interacts with DDRGK1; positively
regulates NFKBIA phosphorylation and degradation.
{ECO:0000269|PubMed:10657303, ECO:0000269|PubMed:1493333,
ECO:0000269|PubMed:16648481, ECO:0000269|PubMed:17003112,
ECO:0000269|PubMed:17956732, ECO:0000269|PubMed:18577712,
ECO:0000269|PubMed:20356841, ECO:0000269|PubMed:23469069,
ECO:0000269|PubMed:23675531}.
-!- SUBUNIT: (Microbial infection) Interacts with HBV protein X.
{ECO:0000269|PubMed:10454581}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-307386, EBI-307386;
P14340:- (xeno); NbExp=2; IntAct=EBI-307386, EBI-465733;
Q9E7P0:- (xeno); NbExp=2; IntAct=EBI-307386, EBI-11361108;
O15111:CHUK; NbExp=14; IntAct=EBI-307386, EBI-81249;
Q60680-2:Chuk (xeno); NbExp=2; IntAct=EBI-307386, EBI-646264;
Q8N668:COMMD1; NbExp=3; IntAct=EBI-307386, EBI-1550112;
P35221:CTNNA1; NbExp=5; IntAct=EBI-307386, EBI-701918;
Q9UKB1:FBXW11; NbExp=2; IntAct=EBI-307386, EBI-355189;
P25098:GRK2; NbExp=2; IntAct=EBI-307386, EBI-3904795;
P34947:GRK5; NbExp=2; IntAct=EBI-307386, EBI-7149314;
Q9NWT6:HIF1AN; NbExp=5; IntAct=EBI-307386, EBI-745632;
O14920:IKBKB; NbExp=27; IntAct=EBI-307386, EBI-81266;
Q9Y6K9:IKBKG; NbExp=6; IntAct=EBI-307386, EBI-81279;
Q14511:NEDD9; NbExp=3; IntAct=EBI-307386, EBI-2108053;
P19838:NFKB1; NbExp=6; IntAct=EBI-307386, EBI-300010;
Q04864:REL; NbExp=2; IntAct=EBI-307386, EBI-307352;
Q04206:RELA; NbExp=24; IntAct=EBI-307386, EBI-73886;
P23396:RPS3; NbExp=6; IntAct=EBI-307386, EBI-351193;
P0CG48:UBC; NbExp=3; IntAct=EBI-307386, EBI-3390054;
Q9J0X9:UL54 (xeno); NbExp=3; IntAct=EBI-307386, EBI-7967856;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between
the nucleus and the cytoplasm by a nuclear localization signal
(NLS) and a CRM1-dependent nuclear export. {ECO:0000250}.
-!- INDUCTION: Induced in adherent monocytes.
-!- PTM: Phosphorylated; disables inhibition of NF-kappa-B DNA-binding
activity. Phosphorylation at positions 32 and 36 is prerequisite
to recognition by UBE2D3 leading to polyubiquitination and
subsequent degradation. {ECO:0000269|PubMed:10329681,
ECO:0000269|PubMed:10882136, ECO:0000269|PubMed:20504922}.
-!- PTM: Sumoylated; sumoylation requires the presence of the nuclear
import signal. Sumoylation blocks ubiquitination and proteasome-
mediated degradation of the protein thereby increasing the protein
stability. {ECO:0000269|PubMed:11124955,
ECO:0000269|PubMed:17956732, ECO:0000269|PubMed:20504922}.
-!- PTM: Monoubiquitinated at Lys-21 and/or Lys-22 by UBE2D3.
Ubiquitin chain elongation is then performed by CDC34 in
cooperation with the SCF(FBXW11) E3 ligase complex, building
ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin.
The resulting polyubiquitination leads to protein degradation.
Also ubiquitinated by SCF(BTRC) following stimulus-dependent
phosphorylation at Ser-32 and Ser-36.
{ECO:0000269|PubMed:10329681, ECO:0000269|PubMed:10882136,
ECO:0000269|PubMed:20347421, ECO:0000269|PubMed:20504922,
ECO:0000269|PubMed:7479976}.
-!- PTM: Deubiquitinated by porcine reproductive and respiratory
syndrome virus Nsp2 protein, which thereby interferes with NFKBIA
degradation and impairs subsequent NF-kappa-B activation.
-!- DISEASE: Ectodermal dysplasia, anhidrotic, with T-cell
immunodeficiency autosomal dominant (ADEDAID) [MIM:612132]: A form
of ectoderma dysplasia, a heterogeneous group of disorders due to
abnormal development of two or more ectodermal structures. This
form of ectodermal dysplasia is associated with decreased
production of pro-inflammatory cytokines and certain interferons,
rendering patients susceptible to infection.
{ECO:0000269|PubMed:14523047, ECO:0000269|PubMed:18412279}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the NF-kappa-B inhibitor family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NFKBIAbase; Note=NFKBIA mutation db;
URL="http://structure.bmc.lu.se/idbase/NFKBIAbase/";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/nfkbia/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M69043; AAA16489.1; -; mRNA.
EMBL; AJ249294; CAB65556.2; -; Genomic_DNA.
EMBL; AJ249295; CAB65556.2; JOINED; Genomic_DNA.
EMBL; AJ249283; CAB65556.2; JOINED; Genomic_DNA.
EMBL; AJ249284; CAB65556.2; JOINED; Genomic_DNA.
EMBL; AJ249285; CAB65556.2; JOINED; Genomic_DNA.
EMBL; AJ249286; CAB65556.2; JOINED; Genomic_DNA.
EMBL; AY033600; AAK51149.1; -; mRNA.
EMBL; BT007091; AAP35754.1; -; mRNA.
EMBL; AY496422; AAR29599.1; -; Genomic_DNA.
EMBL; AK313421; BAG36213.1; -; mRNA.
EMBL; AL133163; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471078; EAW65875.1; -; Genomic_DNA.
EMBL; BC002601; AAH02601.1; -; mRNA.
EMBL; BC004983; AAH04983.1; -; mRNA.
CCDS; CCDS9656.1; -.
PIR; A39935; A39935.
RefSeq; NP_065390.1; NM_020529.2.
UniGene; Hs.81328; -.
PDB; 1IKN; X-ray; 2.30 A; D=67-302.
PDB; 1NFI; X-ray; 2.70 A; E/F=70-282.
PDBsum; 1IKN; -.
PDBsum; 1NFI; -.
DisProt; DP00468; -.
ProteinModelPortal; P25963; -.
SMR; P25963; -.
BioGrid; 110859; 147.
CORUM; P25963; -.
DIP; DIP-139N; -.
ELM; P25963; -.
IntAct; P25963; 69.
MINT; P25963; -.
STRING; 9606.ENSP00000216797; -.
BindingDB; P25963; -.
ChEMBL; CHEMBL2898; -.
DrugBank; DB00945; Acetylsalicylic acid.
iPTMnet; P25963; -.
PhosphoSitePlus; P25963; -.
BioMuta; NFKBIA; -.
DMDM; 126682; -.
EPD; P25963; -.
MaxQB; P25963; -.
PaxDb; P25963; -.
PeptideAtlas; P25963; -.
PRIDE; P25963; -.
ProteomicsDB; 54304; -.
DNASU; 4792; -.
Ensembl; ENST00000216797; ENSP00000216797; ENSG00000100906.
GeneID; 4792; -.
KEGG; hsa:4792; -.
UCSC; uc001wtf.5; human.
CTD; 4792; -.
DisGeNET; 4792; -.
EuPathDB; HostDB:ENSG00000100906.10; -.
GeneCards; NFKBIA; -.
HGNC; HGNC:7797; NFKBIA.
HPA; CAB003815; -.
HPA; HPA029207; -.
MalaCards; NFKBIA; -.
MIM; 164008; gene.
MIM; 612132; phenotype.
neXtProt; NX_P25963; -.
OpenTargets; ENSG00000100906; -.
Orphanet; 251579; Giant cell glioblastoma.
Orphanet; 251576; Gliosarcoma.
Orphanet; 98813; Hypohidrotic ectodermal dysplasia with immunodeficiency.
PharmGKB; PA31601; -.
eggNOG; KOG0504; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00550000074527; -.
HOGENOM; HOG000059576; -.
HOVERGEN; HBG018875; -.
InParanoid; P25963; -.
KO; K04734; -.
OMA; GHNCLHL; -.
OrthoDB; EOG091G0CSV; -.
PhylomeDB; P25963; -.
TreeFam; TF320166; -.
Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
Reactome; R-HSA-1810476; RIP-mediated NFkB activation via ZBP1.
Reactome; R-HSA-202424; Downstream TCR signaling.
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-4755510; SUMOylation of immune response proteins.
Reactome; R-HSA-5603029; IkBA variant leads to EDA-ID.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-9020702; Interleukin-1 signaling.
Reactome; R-HSA-933542; TRAF6 mediated NF-kB activation.
SABIO-RK; P25963; -.
SignaLink; P25963; -.
SIGNOR; P25963; -.
ChiTaRS; NFKBIA; human.
EvolutionaryTrace; P25963; -.
GeneWiki; I%CE%BAB%CE%B1; -.
GenomeRNAi; 4792; -.
PMAP-CutDB; P25963; -.
PRO; PR:P25963; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000100906; Expressed in 237 organ(s), highest expression level in vena cava.
CleanEx; HS_NFKBIA; -.
ExpressionAtlas; P25963; baseline and differential.
Genevisible; P25963; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0033256; C:I-kappaB/NF-kappaB complex; TAS:BHF-UCL.
GO; GO:0005622; C:intracellular; IDA:CAFA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0031072; F:heat shock protein binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0051059; F:NF-kappaB binding; IDA:MGI.
GO; GO:0008139; F:nuclear localization sequence binding; IPI:UniProtKB.
GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
GO; GO:0008134; F:transcription factor binding; TAS:ProtInc.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
GO; GO:0070417; P:cellular response to cold; NAS:BHF-UCL.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:0007253; P:cytoplasmic sequestering of NF-kappaB; IMP:BHF-UCL.
GO; GO:0042994; P:cytoplasmic sequestering of transcription factor; IDA:UniProtKB.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IDA:CAFA.
GO; GO:0070498; P:interleukin-1-mediated signaling pathway; TAS:Reactome.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IEA:Ensembl.
GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
GO; GO:0043392; P:negative regulation of DNA binding; NAS:UniProtKB.
GO; GO:0010888; P:negative regulation of lipid storage; IMP:BHF-UCL.
GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IMP:BHF-UCL.
GO; GO:0045638; P:negative regulation of myeloid cell differentiation; IEA:Ensembl.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:MGI.
GO; GO:0045746; P:negative regulation of Notch signaling pathway; IEA:Ensembl.
GO; GO:0070427; P:nucleotide-binding oligomerization domain containing 1 signaling pathway; IEA:Ensembl.
GO; GO:0070431; P:nucleotide-binding oligomerization domain containing 2 signaling pathway; IEA:Ensembl.
GO; GO:0032270; P:positive regulation of cellular protein metabolic process; IMP:BHF-UCL.
GO; GO:0010875; P:positive regulation of cholesterol efflux; IMP:BHF-UCL.
GO; GO:0050729; P:positive regulation of inflammatory response; IDA:CAFA.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0000060; P:protein import into nucleus, translocation; IEA:Ensembl.
GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl.
GO; GO:1901222; P:regulation of NIK/NF-kappaB signaling; NAS:UniProtKB.
GO; GO:0043330; P:response to exogenous dsRNA; IEA:Ensembl.
GO; GO:0032495; P:response to muramyl dipeptide; IEA:Ensembl.
GO; GO:0035994; P:response to muscle stretch; IEA:Ensembl.
GO; GO:0034142; P:toll-like receptor 4 signaling pathway; IEA:Ensembl.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IDA:CAFA.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd00204; ANK; 1.
Gene3D; 1.25.40.20; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
Pfam; PF00023; Ank; 1.
Pfam; PF12796; Ank_2; 1.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 5.
SUPFAM; SSF48403; SSF48403; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 3.
1: Evidence at protein level;
3D-structure; ANK repeat; Complete proteome; Cytoplasm;
Disease mutation; Ectodermal dysplasia; Host-virus interaction;
Hydroxylation; Isopeptide bond; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Ubl conjugation.
CHAIN 1 317 NF-kappa-B inhibitor alpha.
/FTId=PRO_0000066999.
REPEAT 73 103 ANK 1.
REPEAT 110 139 ANK 2.
REPEAT 143 172 ANK 3.
REPEAT 182 211 ANK 4.
REPEAT 216 245 ANK 5.
MOTIF 30 36 Destruction motif.
MOTIF 45 54 Nuclear export signal.
MOTIF 110 120 Nuclear import signal.
MOD_RES 32 32 Phosphoserine; by IKKA and IKKE.
{ECO:0000269|PubMed:10329681,
ECO:0000269|PubMed:10882136}.
MOD_RES 36 36 Phosphoserine; by IKKA, IKKB, IKKE and
TBK1. {ECO:0000269|PubMed:10329681,
ECO:0000269|PubMed:10882136}.
MOD_RES 42 42 Phosphotyrosine; by Tyr-kinases.
{ECO:0000269|PubMed:8797825}.
MOD_RES 210 210 (3S)-3-hydroxyasparagine; by HIF1AN;
partial. {ECO:0000269|PubMed:17003112}.
MOD_RES 244 244 (3S)-3-hydroxyasparagine; by HIF1AN;
partial. {ECO:0000269|PubMed:17003112}.
MOD_RES 283 283 Phosphoserine; by CK2.
{ECO:0000269|PubMed:8622692,
ECO:0000269|PubMed:8657113}.
MOD_RES 288 288 Phosphoserine; by CK2.
{ECO:0000269|PubMed:8622692}.
MOD_RES 291 291 Phosphothreonine; by CK2.
{ECO:0000269|PubMed:8622692,
ECO:0000269|PubMed:8657113}.
MOD_RES 293 293 Phosphoserine; by CK2.
{ECO:0000269|PubMed:8622692}.
MOD_RES 299 299 Phosphothreonine; by CK2.
{ECO:0000269|PubMed:8657113}.
CROSSLNK 21 21 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO or
ubiquitin); alternate.
{ECO:0000269|PubMed:20347421,
ECO:0000269|PubMed:7479976}.
CROSSLNK 21 21 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:Q9Z1E3}.
CROSSLNK 22 22 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:20347421,
ECO:0000269|PubMed:7479976}.
VARIANT 32 32 S -> I (in ADEDAID; dbSNP:rs28933100).
{ECO:0000269|PubMed:14523047}.
/FTId=VAR_034871.
MUTAGEN 21 21 K->R: Little change in Tax-stimulated
transactivation. No sumoylation. Greatly
reduced Tax- or cytokine-stimulated
transactivation and decrease in
ubiquitination and degradation; when
associated with R-22.
{ECO:0000269|PubMed:11124955,
ECO:0000269|PubMed:17956732,
ECO:0000269|PubMed:7479976,
ECO:0000269|PubMed:8657102}.
MUTAGEN 22 22 K->R: Little change in Tax-stimulated
transactivation. No sumoylation. Greatly
reduced Tax- or cytokine-stimulated
transactivation and decrease in
ubiquitination and degradation; when
associated with R-21.
{ECO:0000269|PubMed:11124955,
ECO:0000269|PubMed:17956732,
ECO:0000269|PubMed:7479976,
ECO:0000269|PubMed:8657102}.
MUTAGEN 31 31 D->A: Loss of phosphorylation; when
associated with A-35.
{ECO:0000269|PubMed:8657102}.
MUTAGEN 32 32 S->A: Loss of phosphorylation,
ubiquitination and degradation; when
associated with A-36.
{ECO:0000269|PubMed:10329681,
ECO:0000269|PubMed:8657102}.
MUTAGEN 32 32 S->T: Decrease in phosphorylation and
degradation; when associated with T-36.
{ECO:0000269|PubMed:10329681,
ECO:0000269|PubMed:8657102}.
MUTAGEN 35 35 D->A: Loss in phosphorylation; when
associated with A-31.
{ECO:0000269|PubMed:8657102}.
MUTAGEN 35 35 D->G: No change neither in
phosphorylation, nor on degradation.
{ECO:0000269|PubMed:8657102}.
MUTAGEN 36 36 S->A: Loss of phosphorylation,
ubiquitination, and degradation; when
associated with A-32.
{ECO:0000269|PubMed:10329681,
ECO:0000269|PubMed:8657102}.
MUTAGEN 36 36 S->T: Decrease in phosphorylation and
degradation; when associated with T-32.
{ECO:0000269|PubMed:10329681,
ECO:0000269|PubMed:8657102}.
MUTAGEN 38 38 K->R: No change in Tax-stimulated
transactivation. No change in Tax-
stimulated transactivation; when
associated with R-47.
{ECO:0000269|PubMed:7479976}.
MUTAGEN 42 42 Y->F: No phosphorylation.
{ECO:0000269|PubMed:8797825}.
MUTAGEN 45 52 MVKELQEI->AAKEAQEA: No nuclear export.
{ECO:0000269|PubMed:10655476}.
MUTAGEN 47 47 K->R: Little change in Tax-stimulated
transactivation. No change in Tax-
stimulated transactivation; when
associated with R-38.
{ECO:0000269|PubMed:7479976}.
MUTAGEN 115 120 LHLAVI->AHAAVA: Greatly reduced nuclear
localization. Great reduction in its
ability to inhibit DNA binding of RELA.
{ECO:0000269|PubMed:9566872}.
MUTAGEN 210 210 N->A: Almost abolished ability to inhibit
NF-kappa-B DNA-binding activity; when
associated with A-244.
{ECO:0000269|PubMed:17003112}.
MUTAGEN 234 234 S->A: No inducible ubiquitination nor
protein degradation.
{ECO:0000269|PubMed:8657102}.
MUTAGEN 244 244 N->A: Almost abolished ability to inhibit
NF-kappa-B DNA-binding activity; when
associated with A-210.
{ECO:0000269|PubMed:17003112}.
MUTAGEN 262 262 S->A: No inducible ubiquitination nor
protein degradation.
{ECO:0000269|PubMed:8657102}.
MUTAGEN 263 263 T->A: No inducible ubiquitination nor
protein degradation.
{ECO:0000269|PubMed:8657102}.
TURN 72 74 {ECO:0000244|PDB:1NFI}.
HELIX 79 83 {ECO:0000244|PDB:1IKN}.
STRAND 87 91 {ECO:0000244|PDB:1IKN}.
HELIX 101 104 {ECO:0000244|PDB:1NFI}.
HELIX 114 120 {ECO:0000244|PDB:1IKN}.
HELIX 124 128 {ECO:0000244|PDB:1IKN}.
HELIX 147 154 {ECO:0000244|PDB:1IKN}.
HELIX 157 165 {ECO:0000244|PDB:1IKN}.
TURN 167 170 {ECO:0000244|PDB:1IKN}.
STRAND 171 173 {ECO:0000244|PDB:1IKN}.
HELIX 175 177 {ECO:0000244|PDB:1IKN}.
HELIX 186 192 {ECO:0000244|PDB:1IKN}.
HELIX 196 205 {ECO:0000244|PDB:1IKN}.
TURN 214 216 {ECO:0000244|PDB:1IKN}.
HELIX 220 226 {ECO:0000244|PDB:1IKN}.
HELIX 230 237 {ECO:0000244|PDB:1IKN}.
TURN 238 240 {ECO:0000244|PDB:1IKN}.
HELIX 253 256 {ECO:0000244|PDB:1IKN}.
HELIX 263 270 {ECO:0000244|PDB:1IKN}.
HELIX 275 277 {ECO:0000244|PDB:1IKN}.
TURN 285 287 {ECO:0000244|PDB:1IKN}.
SEQUENCE 317 AA; 35609 MW; 088B313226786395 CRC64;
MFQAAERPQE WAMEGPRDGL KKERLLDDRH DSGLDSMKDE EYEQMVKELQ EIRLEPQEVP
RGSEPWKQQL TEDGDSFLHL AIIHEEKALT MEVIRQVKGD LAFLNFQNNL QQTPLHLAVI
TNQPEIAEAL LGAGCDPELR DFRGNTPLHL ACEQGCLASV GVLTQSCTTP HLHSILKATN
YNGHTCLHLA SIHGYLGIVE LLVSLGADVN AQEPCNGRTA LHLAVDLQNP DLVSLLLKCG
ADVNRVTYQG YSPYQLTWGR PSTRIQQQLG QLTLENLQML PESEDEESYD TESEFTEFTE
DELPYDDCVF GGQRLTL


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