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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.
22-APR-2020, entry version 219.
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 EDAID2 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 EDAID2.
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:
P25963; P14340; Xeno; NbExp=2; IntAct=EBI-307386, EBI-465733;
P25963; P25963; NbExp=2; IntAct=EBI-307386, EBI-307386;
P25963; PRO_0000037965 [P14340]; Xeno; NbExp=2; IntAct=EBI-307386, EBI-9825968;
P25963; PRO_0000038062 [P21530]; Xeno; NbExp=4; IntAct=EBI-307386, EBI-12558622;
P25963; Q9E7P0; Xeno; NbExp=2; IntAct=EBI-307386, EBI-11361108;
P25963; O15111: CHUK; NbExp=15; IntAct=EBI-307386, EBI-81249;
P25963; Q60680-2: Chuk; Xeno; NbExp=2; IntAct=EBI-307386, EBI-646264;
P25963; Q8N668: COMMD1; NbExp=3; IntAct=EBI-307386, EBI-1550112;
P25963; P35221: CTNNA1; NbExp=5; IntAct=EBI-307386, EBI-701918;
P25963; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-307386, EBI-744099;
P25963; Q9UKB1: FBXW11; NbExp=2; IntAct=EBI-307386, EBI-355189;
P25963; P25098: GRK2; NbExp=2; IntAct=EBI-307386, EBI-3904795;
P25963; P34947: GRK5; NbExp=2; IntAct=EBI-307386, EBI-7149314;
P25963; Q9NWT6: HIF1AN; NbExp=6; IntAct=EBI-307386, EBI-745632;
P25963; O14920: IKBKB; NbExp=27; IntAct=EBI-307386, EBI-81266;
P25963; Q9Y6K9: IKBKG; NbExp=6; IntAct=EBI-307386, EBI-81279;
P25963; Q14511: NEDD9; NbExp=3; IntAct=EBI-307386, EBI-2108053;
P25963; Q14511-2: NEDD9; NbExp=3; IntAct=EBI-307386, EBI-11746523;
P25963; P19838: NFKB1; NbExp=6; IntAct=EBI-307386, EBI-300010;
P25963; Q00653: NFKB2; NbExp=2; IntAct=EBI-307386, EBI-307326;
P25963; Q96HA1-2: POM121; NbExp=3; IntAct=EBI-307386, EBI-11956563;
P25963; O43242: PSMD3; NbExp=3; IntAct=EBI-307386, EBI-357622;
P25963; Q04864: REL; NbExp=3; IntAct=EBI-307386, EBI-307352;
P25963; Q04206: RELA; NbExp=24; IntAct=EBI-307386, EBI-73886;
P25963; Q04206-2: RELA; NbExp=2; IntAct=EBI-307386, EBI-289947;
P25963; P23396: RPS3; NbExp=6; IntAct=EBI-307386, EBI-351193;
P25963; P56279: TCL1A; NbExp=3; IntAct=EBI-307386, EBI-749995;
P25963; P0CG48: UBC; NbExp=3; IntAct=EBI-307386, EBI-3390054;
P25963; 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 and immunodeficiency 2 (EDAID2)
[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. EDAID2
inheritance is autosomal dominant. {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/";
---------------------------------------------------------------------------
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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.
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; -.
SMR; P25963; -.
BioGrid; 110859; 154.
CORUM; P25963; -.
DIP; DIP-139N; -.
ELM; P25963; -.
IntAct; P25963; 93.
MINT; P25963; -.
STRING; 9606.ENSP00000216797; -.
ChEMBL; CHEMBL2898; -.
DrugBank; DB00945; Acetylsalicylic acid.
DrugBank; DB06543; Astaxanthin.
DrugBank; DB05983; Bardoxolone methyl.
iPTMnet; P25963; -.
MetOSite; P25963; -.
PhosphoSitePlus; P25963; -.
BioMuta; NFKBIA; -.
DMDM; 126682; -.
EPD; P25963; -.
jPOST; P25963; -.
MassIVE; P25963; -.
MaxQB; P25963; -.
PaxDb; P25963; -.
PeptideAtlas; P25963; -.
PRIDE; P25963; -.
ProteomicsDB; 54304; -.
Antibodypedia; 3541; 1763 antibodies.
DNASU; 4792; -.
Ensembl; ENST00000216797; ENSP00000216797; ENSG00000100906.
GeneID; 4792; -.
KEGG; hsa:4792; -.
UCSC; uc001wtf.5; human.
CTD; 4792; -.
DisGeNET; 4792; -.
GeneCards; NFKBIA; -.
HGNC; HGNC:7797; NFKBIA.
HPA; ENSG00000100906; Tissue enhanced (bone).
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.
Orphanet; 150; Nasopharyngeal carcinoma.
PharmGKB; PA31601; -.
eggNOG; KOG0504; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00940000162733; -.
InParanoid; P25963; -.
KO; K04734; -.
OMA; NCQRHLT; -.
OrthoDB; 1341288at2759; -.
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; -.
Pharos; P25963; Tchem.
PRO; PR:P25963; -.
Proteomes; UP000005640; Chromosome 14.
RNAct; P25963; protein.
Bgee; ENSG00000100906; Expressed in vena cava and 236 other tissues.
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: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: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: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: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: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:0006606; P:protein import into nucleus; IEA:Ensembl.
GO; GO:0042127; P:regulation of cell population 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.
DisProt; DP00468; -.
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; Cytoplasm; Disease mutation;
Ectodermal dysplasia; Host-virus interaction; Hydroxylation;
Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
Ubl conjugation.
CHAIN 1..317
/note="NF-kappa-B inhibitor alpha"
/id="PRO_0000066999"
REPEAT 73..103
/note="ANK 1"
REPEAT 110..139
/note="ANK 2"
REPEAT 143..172
/note="ANK 3"
REPEAT 182..211
/note="ANK 4"
REPEAT 216..245
/note="ANK 5"
MOTIF 30..36
/note="Destruction motif"
MOTIF 45..54
/note="Nuclear export signal"
MOTIF 110..120
/note="Nuclear import signal"
MOD_RES 32
/note="Phosphoserine; by IKKA and IKKE"
/evidence="ECO:0000269|PubMed:10329681,
ECO:0000269|PubMed:10882136"
MOD_RES 36
/note="Phosphoserine; by IKKA, IKKB, IKKE and TBK1"
/evidence="ECO:0000269|PubMed:10329681,
ECO:0000269|PubMed:10882136"
MOD_RES 42
/note="Phosphotyrosine; by Tyr-kinases"
/evidence="ECO:0000269|PubMed:8797825"
MOD_RES 210
/note="(3S)-3-hydroxyasparagine; by HIF1AN; partial"
/evidence="ECO:0000269|PubMed:17003112"
MOD_RES 244
/note="(3S)-3-hydroxyasparagine; by HIF1AN; partial"
/evidence="ECO:0000269|PubMed:17003112"
MOD_RES 283
/note="Phosphoserine; by CK2"
/evidence="ECO:0000269|PubMed:8622692,
ECO:0000269|PubMed:8657113"
MOD_RES 288
/note="Phosphoserine; by CK2"
/evidence="ECO:0000269|PubMed:8622692"
MOD_RES 291
/note="Phosphothreonine; by CK2"
/evidence="ECO:0000269|PubMed:8622692,
ECO:0000269|PubMed:8657113"
MOD_RES 293
/note="Phosphoserine; by CK2"
/evidence="ECO:0000269|PubMed:8622692"
MOD_RES 299
/note="Phosphothreonine; by CK2"
/evidence="ECO:0000269|PubMed:8657113"
CROSSLNK 21
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO or ubiquitin); alternate"
/evidence="ECO:0000269|PubMed:20347421,
ECO:0000269|PubMed:7479976"
CROSSLNK 21
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin); alternate"
/evidence="ECO:0000250|UniProtKB:Q9Z1E3"
CROSSLNK 22
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000269|PubMed:20347421,
ECO:0000269|PubMed:7479976"
VARIANT 32
/note="S -> I (in EDAID2; dbSNP:rs28933100)"
/evidence="ECO:0000269|PubMed:14523047"
/id="VAR_034871"
MUTAGEN 21
/note="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."
/evidence="ECO:0000269|PubMed:11124955,
ECO:0000269|PubMed:17956732, ECO:0000269|PubMed:7479976,
ECO:0000269|PubMed:8657102"
MUTAGEN 22
/note="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."
/evidence="ECO:0000269|PubMed:11124955,
ECO:0000269|PubMed:17956732, ECO:0000269|PubMed:7479976,
ECO:0000269|PubMed:8657102"
MUTAGEN 31
/note="D->A: Loss of phosphorylation; when associated with
A-35."
/evidence="ECO:0000269|PubMed:8657102"
MUTAGEN 32
/note="S->A: Loss of phosphorylation, ubiquitination and
degradation; when associated with A-36."
/evidence="ECO:0000269|PubMed:10329681,
ECO:0000269|PubMed:8657102"
MUTAGEN 32
/note="S->T: Decrease in phosphorylation and degradation;
when associated with T-36."
/evidence="ECO:0000269|PubMed:10329681,
ECO:0000269|PubMed:8657102"
MUTAGEN 35
/note="D->A: Loss in phosphorylation; when associated with
A-31."
/evidence="ECO:0000269|PubMed:8657102"
MUTAGEN 35
/note="D->G: No change neither in phosphorylation, nor on
degradation."
/evidence="ECO:0000269|PubMed:8657102"
MUTAGEN 36
/note="S->A: Loss of phosphorylation, ubiquitination, and
degradation; when associated with A-32."
/evidence="ECO:0000269|PubMed:10329681,
ECO:0000269|PubMed:8657102"
MUTAGEN 36
/note="S->T: Decrease in phosphorylation and degradation;
when associated with T-32."
/evidence="ECO:0000269|PubMed:10329681,
ECO:0000269|PubMed:8657102"
MUTAGEN 38
/note="K->R: No change in Tax-stimulated transactivation.
No change in Tax-stimulated transactivation; when
associated with R-47."
/evidence="ECO:0000269|PubMed:7479976"
MUTAGEN 42
/note="Y->F: No phosphorylation."
/evidence="ECO:0000269|PubMed:8797825"
MUTAGEN 45..52
/note="MVKELQEI->AAKEAQEA: No nuclear export."
/evidence="ECO:0000269|PubMed:10655476"
MUTAGEN 47
/note="K->R: Little change in Tax-stimulated
transactivation. No change in Tax-stimulated
transactivation; when associated with R-38."
/evidence="ECO:0000269|PubMed:7479976"
MUTAGEN 115..120
/note="LHLAVI->AHAAVA: Greatly reduced nuclear
localization. Great reduction in its ability to inhibit DNA
binding of RELA."
/evidence="ECO:0000269|PubMed:9566872"
MUTAGEN 210
/note="N->A: Almost abolished ability to inhibit NF-kappa-B
DNA-binding activity; when associated with A-244."
/evidence="ECO:0000269|PubMed:17003112"
MUTAGEN 234
/note="S->A: No inducible ubiquitination nor protein
degradation."
/evidence="ECO:0000269|PubMed:8657102"
MUTAGEN 244
/note="N->A: Almost abolished ability to inhibit NF-kappa-B
DNA-binding activity; when associated with A-210."
/evidence="ECO:0000269|PubMed:17003112"
MUTAGEN 262
/note="S->A: No inducible ubiquitination nor protein
degradation."
/evidence="ECO:0000269|PubMed:8657102"
MUTAGEN 263
/note="T->A: No inducible ubiquitination nor protein
degradation."
/evidence="ECO:0000269|PubMed:8657102"
TURN 72..74
/evidence="ECO:0000244|PDB:1NFI"
HELIX 79..83
/evidence="ECO:0000244|PDB:1IKN"
STRAND 87..91
/evidence="ECO:0000244|PDB:1IKN"
HELIX 101..104
/evidence="ECO:0000244|PDB:1NFI"
HELIX 114..120
/evidence="ECO:0000244|PDB:1IKN"
HELIX 124..128
/evidence="ECO:0000244|PDB:1IKN"
HELIX 147..154
/evidence="ECO:0000244|PDB:1IKN"
HELIX 157..165
/evidence="ECO:0000244|PDB:1IKN"
TURN 167..170
/evidence="ECO:0000244|PDB:1IKN"
STRAND 171..173
/evidence="ECO:0000244|PDB:1IKN"
HELIX 175..177
/evidence="ECO:0000244|PDB:1IKN"
HELIX 186..192
/evidence="ECO:0000244|PDB:1IKN"
HELIX 196..205
/evidence="ECO:0000244|PDB:1IKN"
TURN 214..216
/evidence="ECO:0000244|PDB:1IKN"
HELIX 220..226
/evidence="ECO:0000244|PDB:1IKN"
HELIX 230..237
/evidence="ECO:0000244|PDB:1IKN"
TURN 238..240
/evidence="ECO:0000244|PDB:1IKN"
HELIX 253..256
/evidence="ECO:0000244|PDB:1IKN"
HELIX 263..270
/evidence="ECO:0000244|PDB:1IKN"
HELIX 275..277
/evidence="ECO:0000244|PDB:1IKN"
TURN 285..287
/evidence="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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U1848r CLIA kit IkappaBalpha,I-kappa-B-alpha,Ikba,IkB-alpha,NF-kappa-B inhibitor alpha,Nfkbia,Rat,Rattus norvegicus,RL_IF-1 96T
U1848r CLIA IkappaBalpha,I-kappa-B-alpha,Ikba,IkB-alpha,NF-kappa-B inhibitor alpha,Nfkbia,Rat,Rattus norvegicus,RL_IF-1 96T
U1848m CLIA IkappaBalpha,I-kappa-B-alpha,Ikba,IkB-alpha,Mouse,Mus musculus,NF-kappa-B inhibitor alpha,Nfkbia 96T
E1848m ELISA IkappaBalpha,I-kappa-B-alpha,Ikba,IkB-alpha,Mouse,Mus musculus,NF-kappa-B inhibitor alpha,Nfkbia 96T
E1848m ELISA kit IkappaBalpha,I-kappa-B-alpha,Ikba,IkB-alpha,Mouse,Mus musculus,NF-kappa-B inhibitor alpha,Nfkbia 96T
U1848m CLIA kit IkappaBalpha,I-kappa-B-alpha,Ikba,IkB-alpha,Mouse,Mus musculus,NF-kappa-B inhibitor alpha,Nfkbia 96T
E1848p ELISA kit ECI-6,IkappaBalpha,I-kappa-B-alpha,IKBA,IkB-alpha,NF-kappa-B inhibitor alpha,NFKBIA,Pig,Sus scrofa 96T
U1848p CLIA ECI-6,IkappaBalpha,I-kappa-B-alpha,IKBA,IkB-alpha,NF-kappa-B inhibitor alpha,NFKBIA,Pig,Sus scrofa 96T
U1848p CLIA kit ECI-6,IkappaBalpha,I-kappa-B-alpha,IKBA,IkB-alpha,NF-kappa-B inhibitor alpha,NFKBIA,Pig,Sus scrofa 96T
Pathways :
WP262: EBV LMP1 signaling
WP1224: EBV LMP1 signaling
WP1209: EBV LMP1 signaling
WP1571: EBV LMP1 signaling
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP210: Cytoplasmic Ribosomal Proteins
WP2199: Seed Development
WP1340: Ovarian Infertility Genes
WP537: Translation Factors
WP1003: Ovarian Infertility Genes
WP1618: alpha-Linolenic acid metabolism
WP263: Ovarian Infertility Genes
WP296: TCA Cycle - biocyc
WP1434: Osteopontin Signaling
WP231: TNF alpha Signaling Pathway
WP566: canonical wnt - zebrafish
WP1655: Geraniol degradation
WP2100: AhR pathway
WP402: ERK1 - ERK2 MAPK cascade
WP773: Ovarian Infertility Genes
WP244: Alpha 6 Beta 4 signaling pathway
WP811: TNF-alpha NF-kB Signaling Pathway
WP1225: estrogen signalling
WP457: TNF-alpha NF-kB Signaling Pathway

Related Genes :
[NFKBIA IKBA MAD3 NFKBI] NF-kappa-B inhibitor alpha (I-kappa-B-alpha) (IkB-alpha) (IkappaBalpha) (Major histocompatibility complex enhancer-binding protein MAD3)
[Nfkbia Ikba] NF-kappa-B inhibitor alpha (I-kappa-B-alpha) (IkB-alpha) (IkappaBalpha)
[Nfkbia Ikba] NF-kappa-B inhibitor alpha (I-kappa-B-alpha) (IkB-alpha) (IkappaBalpha) (RL/IF-1)
[NFKBIA IKBA] NF-kappa-B inhibitor alpha (ECI-6) (I-kappa-B-alpha) (IkB-alpha) (IkappaBalpha)
[IKBKG NEMO] NF-kappa-B essential modulator (NEMO) (IkB kinase-associated protein 1) (IKKAP1) (Inhibitor of nuclear factor kappa-B kinase subunit gamma) (I-kappa-B kinase subunit gamma) (IKK-gamma) (IKKG) (IkB kinase subunit gamma) (NF-kappa-B essential modifier)
[CHUK IKKA TCF16] 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)
[IKBKG FIP3 NEMO] NF-kappa-B essential modulator (NEMO) (FIP-3) (IkB kinase-associated protein 1) (IKKAP1) (Inhibitor of nuclear factor kappa-B kinase subunit gamma) (I-kappa-B kinase subunit gamma) (IKK-gamma) (IKKG) (IkB kinase subunit gamma) (NF-kappa-B essential modifier)
[CHUK IKKA] Inhibitor of nuclear factor kappa-B kinase subunit alpha (I-kappa-B kinase alpha) (IKK-A) (IKK-alpha) (IkBKA) (EC 2.7.11.10) (I-kappa-B kinase 1) (IKK1) (Nuclear factor NF-kappa-B inhibitor kinase alpha) (NFKBIKA)
[RELA NFKB3] Transcription factor p65 (Nuclear factor NF-kappa-B p65 subunit) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3)
[NFKB1] Nuclear factor NF-kappa-B p105 subunit (DNA-binding factor KBF1) (EBP-1) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1) [Cleaved into: Nuclear factor NF-kappa-B p50 subunit]
[Nfkb1] Nuclear factor NF-kappa-B p105 subunit (DNA-binding factor KBF1) (EBP-1) (NF-kappa-B1 p84/NF-kappa-B1 p98) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1) [Cleaved into: Nuclear factor NF-kappa-B p50 subunit]
[Ikbkg Nemo] NF-kappa-B essential modulator (NEMO) (IkB kinase-associated protein 1) (IKKAP1) (mFIP-3) (Inhibitor of nuclear factor kappa-B kinase subunit gamma) (I-kappa-B kinase subunit gamma) (IKK-gamma) (IKKG) (IkB kinase subunit gamma) (NF-kappa-B essential modifier)
[NFKB2 LYT10] Nuclear factor NF-kappa-B p100 subunit (DNA-binding factor KBF2) (H2TF1) (Lymphocyte translocation chromosome 10 protein) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 2) (Oncogene Lyt-10) (Lyt10) [Cleaved into: Nuclear factor NF-kappa-B p52 subunit]
[IKBKG] NF-kappa-B essential modulator (NEMO) (FIP-3) (IkB kinase-associated protein 1) (IKKAP1) (Inhibitor of nuclear factor kappa-B kinase subunit gamma) (I-kappa-B kinase subunit gamma) (IKK-gamma) (IKKG) (IkB kinase subunit gamma) (NF-kappa-B essential modifier)
[Ikbkg Nemo] NF-kappa-B essential modulator (NEMO) (IkB kinase-associated protein 1) (IKKAP1) (Inhibitor of nuclear factor kappa-B kinase subunit gamma) (I-kappa-B kinase subunit gamma) (IKK-gamma) (IKKG) (IkB kinase subunit gamma) (NF-kappa-B essential modifier)
[Chuk Ikka] 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)
[chuk ikk1 zgc:56539] 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)
[NFKBIB IKBB TRIP9] NF-kappa-B inhibitor beta (NF-kappa-BIB) (I-kappa-B-beta) (IkB-B) (IkB-beta) (IkappaBbeta) (Thyroid receptor-interacting protein 9) (TR-interacting protein 9) (TRIP-9)
[IKBKB IKKB] Inhibitor of nuclear factor kappa-B kinase subunit beta (I-kappa-B-kinase beta) (IKK-B) (IKK-beta) (IkBKB) (EC 2.7.11.10) (I-kappa-B kinase 2) (IKK2) (Nuclear factor NF-kappa-B inhibitor kinase beta) (NFKBIKB)
[Nfkb2] Nuclear factor NF-kappa-B p100 subunit (DNA-binding factor KBF2) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 2) [Cleaved into: Nuclear factor NF-kappa-B p52 subunit]
[Nfkb1] Nuclear factor NF-kappa-B p105 subunit (DNA-binding factor KBF1) (EBP-1) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1) [Cleaved into: Nuclear factor NF-kappa-B p50 subunit] (Fragment)
[Ikbkb Ikkb] Inhibitor of nuclear factor kappa-B kinase subunit beta (I-kappa-B-kinase beta) (IKK-B) (IKK-beta) (IkBKB) (EC 2.7.11.10) (I-kappa-B kinase 2) (IKK2) (Nuclear factor NF-kappa-B inhibitor kinase beta) (NFKBIKB)
[Rela Nfkb3] Transcription factor p65 (Nuclear factor NF-kappa-B p65 subunit) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3)
[TONSL IKBR NFKBIL2] Tonsoku-like protein (Inhibitor of kappa B-related protein) (I-kappa-B-related protein) (IkappaBR) (NF-kappa-B inhibitor-like protein 2) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor-like 2)
[Nfkbid Ikbns] NF-kappa-B inhibitor delta (I-kappa-B-delta) (IkB-delta) (IkappaBdelta) (IkappaBNS)
[NFKB1] Nuclear factor NF-kappa-B p105 subunit (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1) [Cleaved into: Nuclear factor NF-kappa-B p50 subunit]
[IKBKB] 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)
[TCF3 BHLHB21 E2A ITF1] Transcription factor E2-alpha (Class B basic helix-loop-helix protein 21) (bHLHb21) (Immunoglobulin enhancer-binding factor E12/E47) (Immunoglobulin transcription factor 1) (Kappa-E2-binding factor) (Transcription factor 3) (TCF-3) (Transcription factor ITF-1)
[Ikbkb Ikkb] Inhibitor of nuclear factor kappa-B kinase subunit beta (I-kappa-B-kinase beta) (IKK-B) (IKK-beta) (IkBKB) (EC 2.7.11.10) (I-kappa-B kinase 2) (IKK2) (Nuclear factor NF-kappa-B inhibitor kinase beta) (NFKBIKB)
[Tnip1 Abin Naf1] TNFAIP3-interacting protein 1 (A20-binding inhibitor of NF-kappa-B activation 1) (ABIN) (ABIN-1) (Nef-associated factor 1) (Naf1) (Virion-associated nuclear shuttling protein) (VAN) (mVAN)

Bibliography :
[7937093] Three NF-kappa B sites in the I kappa B-alpha promoter are required for induction of gene expression by TNF alpha.