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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)

 NEMO_MOUSE              Reviewed;         412 AA.
O88522; Q924H4;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
17-JUN-2020, entry version 176.
RecName: Full=NF-kappa-B essential modulator;
Short=NEMO;
AltName: Full=IkB kinase-associated protein 1;
Short=IKKAP1;
Short=mFIP-3;
AltName: Full=Inhibitor of nuclear factor kappa-B kinase subunit gamma;
Short=I-kappa-B kinase subunit gamma;
Short=IKK-gamma;
Short=IKKG;
Short=IkB kinase subunit gamma;
AltName: Full=NF-kappa-B essential modifier;
Name=Ikbkg; Synonyms=Nemo;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=T-cell;
PubMed=9657155; DOI=10.1016/s0092-8674(00)81466-x;
Yamaoka S., Courtois G., Bessia C., Whiteside S.T., Weil R., Agou F.,
Kirk H.E., Kay R.J., Israel A.;
"Complementation cloning of NEMO, a component of the I-kappaB kinase
complex essential for NF-kappaB activation.";
Cell 93:1231-1240(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11410370; DOI=10.1016/s0378-1119(01)00492-9;
Galgoczy P., Rosenthal A., Platzer M.;
"Human-mouse comparative sequence analysis of the NEMO gene reveals an
alternative promoter within the neighboring G6PD gene.";
Gene 271:93-98(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Liver;
Perelygin A.A., Perelygina L.M.;
"Ikbkg gene modulates the herpes virus susceptibility in mice.";
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NOD;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of the
mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 85-412, AND PROTEIN SEQUENCE OF 144-159.
TISSUE=Cervix carcinoma;
PubMed=9891086; DOI=10.1128/mcb.19.2.1526;
Mercurio F., Murray B.W., Shevchenko A., Bennett B.L., Young D.B., Li J.W.,
Pascual G., Motiwala A., Zhu H., Mann M., Manning A.M.;
"IkappaB kinase (IKK)-associated protein 1, a common component of the
heterogeneous IKK complex.";
Mol. Cell. Biol. 19:1526-1538(1999).
[8]
FUNCTION.
PubMed=9927690; DOI=10.1073/pnas.96.3.1042;
Li Y., Kang J., Friedman J., Tarassishin L., Ye J., Kovalenko A.,
Wallach D., Horwitz M.S.;
"Identification of a cell protein (FIP-3) as a modulator of NF-kappaB
activity and as a target of an adenovirus inhibitor of tumor necrosis
factor alpha-induced apoptosis.";
Proc. Natl. Acad. Sci. U.S.A. 96:1042-1047(1999).
[9]
IKK COMPLEX.
PubMed=11080499; DOI=10.1074/jbc.m008353200;
Li X.-H., Fang X., Gaynor R.B.;
"Role of ikkgamma/nemo in assembly of the IkappaB kinase complex.";
J. Biol. Chem. 276:4494-4500(2001).
[10]
PHOSPHORYLATION AT SER-369, AND MUTAGENESIS OF SER-369 AND SER-375.
PubMed=11971901; DOI=10.1074/jbc.m201393200;
Prajapati S., Gaynor R.B.;
"Regulation of Ikappa B kinase (IKK)gamma /NEMO function by IKKbeta
-mediated phosphorylation.";
J. Biol. Chem. 277:24331-24339(2002).
[11]
INTERACTION WITH TANK AND IKBKB.
PubMed=12133833; DOI=10.1074/jbc.m205069200;
Chariot A., Leonardi A., Muller J., Bonif M., Brown K., Siebenlist U.;
"Association of the adaptor TANK with the I kappa B kinase (IKK) regulator
NEMO connects IKK complexes with IKK epsilon and TBK1 kinases.";
J. Biol. Chem. 277:37029-37036(2002).
[12]
INTERACTION WITH TNIP1 AND TNFAIP3.
PubMed=16684768; DOI=10.1074/jbc.m601502200;
Mauro C., Pacifico F., Lavorgna A., Mellone S., Iannetti A., Acquaviva R.,
Formisano S., Vito P., Leonardi A.;
"ABIN-1 binds to NEMO/IKKgamma and co-operates with A20 in inhibiting NF-
kappaB.";
J. Biol. Chem. 281:18482-18488(2006).
[13]
UBIQUITINATION AT LYS-278; LYS-314; LYS-318; LYS-319 AND LYS-392, AND
MUTAGENESIS OF LYS-278; LYS-314; VAL-316; LYS-318; LYS-319 AND LYS-392.
PubMed=17728323; DOI=10.1093/hmg/ddm237;
Sebban-Benin H., Pescatore A., Fusco F., Pascuale V., Gautheron J.,
Yamaoka S., Moncla A., Ursini M.V., Courtois G.;
"Identification of TRAF6-dependent NEMO polyubiquitination sites through
analysis of a new NEMO mutation causing incontinentia pigmenti.";
Hum. Mol. Genet. 16:2805-2815(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
[15]
INTERACTION WITH TERF2IP.
PubMed=20622870; DOI=10.1038/ncb2080;
Teo H., Ghosh S., Luesch H., Ghosh A., Wong E.T., Malik N., Orth A.,
de Jesus P., Perry A.S., Oliver J.D., Tran N.L., Speiser L.J., Wong M.,
Saez E., Schultz P., Chanda S.K., Verma I.M., Tergaonkar V.;
"Telomere-independent Rap1 is an IKK adaptor and regulates NF-kappaB-
dependent gene expression.";
Nat. Cell Biol. 12:758-767(2010).
[16]
INTERACTION WITH RIPK1.
PubMed=31519886; DOI=10.1038/s41467-019-11839-w;
Zhang X., Zhang H., Xu C., Li X., Li M., Wu X., Pu W., Zhou B., Wang H.,
Li D., Ding Q., Ying H., Wang H., Zhang H.;
"Ubiquitination of RIPK1 suppresses programmed cell death by regulating
RIPK1 kinase activation during embryogenesis.";
Nat. Commun. 10:4158-4158(2019).
[17]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 250-343 IN COMPLEX WITH UBIQUITIN,
UBIQUITIN-BINDING, AND MUTAGENESIS OF VAL-293; TYR-301; LYS-302; PHE-305;
ARG-309; ARG-312; GLU-313; GLU-313; GLU-317 AND GLU-320.
PubMed=19303852; DOI=10.1016/j.cell.2009.03.007;
Rahighi S., Ikeda F., Kawasaki M., Akutsu M., Suzuki N., Kato R.,
Kensche T., Uejima T., Bloor S., Komander D., Randow F., Wakatsuki S.,
Dikic I.;
"Specific recognition of linear ubiquitin chains by NEMO is important for
NF-kappaB activation.";
Cell 136:1098-1109(2009).
[18]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 251-337, UBIQUITIN-BINDING, AND
OLIGOMETRIZATION.
PubMed=19854204; DOI=10.1016/j.jmb.2009.10.018;
Grubisha O., Kaminska M., Duquerroy S., Fontan E., Cordier F., Haouz A.,
Raynal B., Chiaravalli J., Delepierre M., Israel A., Veron M., Agou F.;
"DARPin-assisted crystallography of the CC2-LZ domain of NEMO reveals a
coupling between dimerization and ubiquitin binding.";
J. Mol. Biol. 395:89-104(2010).
-!- FUNCTION: Regulatory subunit of the IKK core complex which
phosphorylates inhibitors of NF-kappa-B thus leading to the
dissociation of the inhibitor/NF-kappa-B complex and ultimately the
degradation of the inhibitor. Its binding to scaffolding polyubiquitin
seems to play a role in IKK activation by multiple signaling receptor
pathways. Also considered to be a mediator for TAX activation of NF-
kappa-B. Could be implicated in NF-kappa-B-mediated protection from
cytokine toxicity. Involved in TLR3- and IFIH1-mediated antiviral
innate response; this function requires 'Lys-27'-linked
polyubiquitination. {ECO:0000269|PubMed:9927690}.
-!- SUBUNIT: Homodimer; disulfide-linked. 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. The IKK
complex associates with TERF2IP/RAP1, leading to promote IKK-mediated
phosphorylation of RELA/p65. Part of a complex composed of NCOA2,
NCOA3, CHUK/IKKA, IKBKB, IKBKG and CREBBP. Interacts with COPS3, CYLD,
NALP2, TRPC4AP and PIDD1. Interacts with ATM; the complex is exported
from the nucleus. Interacts with TRAF6. Interacts with IKBKE. Interacts
with TANK; the interaction is enhanced by TBK1 and IKBKE. Part of a
ternary complex consisting of TANK, IKBKB and IKBKG. Interacts with
ZFAND5. Interacts with RIPK2. Interacts with TNIP1 and TNFAIP3; TNIP1
facilitates the TNFAIP3-mediated de-ubiquitination of IKBKG. Interacts
with TNFAIP3; the interaction is induced by TNF stimulation and by
polyubiquitin. Interacts with NLRP10. Interacts with TANK; this
interaction increases in response to DNA damage (By similarity).
Interacts with USP10; this interaction increases in response to DNA
damage (By similarity). Interacts with ZC3H12A; this interaction
increases in response to DNA damage (By similarity). Interacts with
TRIM29; this interaction induces IKBKG/NEMO ubiquitination and
proteolytic degradation (By similarity). Interacts with TRIM13; this
interaction leads to IKBKG/NEMO ubiquitination (By similarity).
Interacts with ARFIP2 (By similarity). Interacts with RIPK1
(PubMed:31519886). {ECO:0000250|UniProtKB:Q9Y6K9,
ECO:0000269|PubMed:12133833, ECO:0000269|PubMed:16684768,
ECO:0000269|PubMed:19303852, ECO:0000269|PubMed:20622870,
ECO:0000269|PubMed:31519886}.
-!- INTERACTION:
O88522; Q60680: Chuk; NbExp=6; IntAct=EBI-998011, EBI-646245;
O88522; O88351: Ikbkb; NbExp=7; IntAct=EBI-998011, EBI-447960;
O88522; Q924T7: Rnf31; NbExp=7; IntAct=EBI-998011, EBI-647680;
O88522; P62991: Ubc; NbExp=3; IntAct=EBI-998011, EBI-413074;
O88522; P0CG48: UBC; Xeno; NbExp=3; IntAct=EBI-998011, EBI-3390054;
O88522; P24772: VACWR196; Xeno; NbExp=2; IntAct=EBI-998011, EBI-4291651;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
-!- DOMAIN: The leucine-zipper domain and the CCHC NOA-type zinc-finger are
essential for polyubiquitin binding and for the activation of IRF3.
{ECO:0000250}.
-!- PTM: Phosphorylation at Ser-68 attenuates aminoterminal
homodimerization. {ECO:0000250}.
-!- PTM: Polyubiquitinated on Lys-278 through 'Lys-63'; the ubiquitination
is mediated by NOD2 and RIPK2 and probably plays a role in signaling by
facilitating interactions with ubiquitin domain-containing proteins and
activates the NF-kappa-B pathway. Polyubiquitinated on Lys-392 through
'Lys-63'; the ubiquitination is mediated by BCL10, MALT1 and TRAF6 and
probably plays a role in signaling by facilitating interactions with
ubiquitin domain-containing proteins and activates the NF-kappa-B
pathway. Monoubiquitinated on Lys-270 and Lys-302; promotes nuclear
export. Polyubiquitinated through 'Lys-27' by TRIM23; involved in
antiviral innate and inflammatory responses. Linear polyubiquitinated
on Lys-111, Lys-143, Lys-226, Lys-246, Lys-270, Lys-278, Lys-285, Lys-
295, Lys-302 and Lys-319; the head-to-tail polyubiquitination is
mediated by the LUBAC complex and plays a key role in NF-kappa-B
activation. Deubiquitinated by USP10 in a TANK-dependent and
-independent manner, leading to the negative regulation of NF-kappa-B
signaling upon DNA damage (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:Q9Y6K9}.
-!- PTM: Sumoylated on Lys-270 and Lys-302 with SUMO1; the modification
results in phosphorylation of Ser-85 by ATM leading to a replacement of
the sumoylation by mono-ubiquitination on these residues.
{ECO:0000250}.
-!- PTM: Neddylated by TRIM40, resulting in stabilization of NFKBIA and
down-regulation of NF-kappa-B activity. {ECO:0000250}.
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EMBL; AF069542; AAC40153.1; -; mRNA.
EMBL; AF326207; AAK69186.1; -; Genomic_DNA.
EMBL; AF513109; AAP47160.1; -; mRNA.
EMBL; AK154095; BAE32372.1; -; mRNA.
EMBL; AL669976; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466650; EDL29810.1; -; Genomic_DNA.
CCDS; CCDS41023.1; -.
RefSeq; NP_001154895.1; NM_001161423.1.
RefSeq; NP_034677.2; NM_010547.2.
RefSeq; XP_006527913.1; XM_006527850.2.
RefSeq; XP_006527914.1; XM_006527851.2.
RefSeq; XP_006527915.1; XM_006527852.2.
RefSeq; XP_011245829.1; XM_011247527.2.
PDB; 2V4H; X-ray; 2.90 A; A/B=251-337.
PDB; 2ZVN; X-ray; 3.00 A; B/D/F/H=253-337.
PDB; 2ZVO; X-ray; 2.90 A; B/D=250-339.
PDB; 3F89; X-ray; 2.80 A; A/B=250-339.
PDB; 3JSV; X-ray; 2.70 A; C/D=250-343.
PDB; 4OWF; X-ray; 2.00 A; A/B=250-339.
PDBsum; 2V4H; -.
PDBsum; 2ZVN; -.
PDBsum; 2ZVO; -.
PDBsum; 3F89; -.
PDBsum; 3JSV; -.
PDBsum; 4OWF; -.
SMR; O88522; -.
BioGRID; 200602; 47.
ComplexPortal; CPX-3270; IkappaB kinase complex.
CORUM; O88522; -.
DIP; DIP-29811N; -.
IntAct; O88522; 20.
MINT; O88522; -.
STRING; 10090.ENSMUSP00000109762; -.
iPTMnet; O88522; -.
PhosphoSitePlus; O88522; -.
EPD; O88522; -.
jPOST; O88522; -.
MaxQB; O88522; -.
PaxDb; O88522; -.
PRIDE; O88522; -.
Antibodypedia; 73338; 1206 antibodies.
Ensembl; ENSMUST00000114127; ENSMUSP00000109762; ENSMUSG00000004221.
Ensembl; ENSMUST00000114128; ENSMUSP00000109763; ENSMUSG00000004221.
Ensembl; ENSMUST00000114133; ENSMUSP00000109768; ENSMUSG00000004221.
Ensembl; ENSMUST00000164101; ENSMUSP00000126770; ENSMUSG00000004221.
GeneID; 16151; -.
KEGG; mmu:16151; -.
UCSC; uc009toz.2; mouse.
CTD; 8517; -.
MGI; MGI:1338074; Ikbkg.
eggNOG; ENOG410IJBJ; Eukaryota.
eggNOG; ENOG410Y1FG; LUCA.
GeneTree; ENSGT00530000063808; -.
HOGENOM; CLU_034097_0_0_1; -.
InParanoid; O88522; -.
KO; K07210; -.
TreeFam; TF326608; -.
Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
Reactome; R-MMU-168638; NOD1/2 Signaling Pathway.
Reactome; R-MMU-1810476; RIP-mediated NFkB activation via ZBP1.
Reactome; R-MMU-202424; Downstream TCR signaling.
Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
Reactome; R-MMU-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-MMU-450302; activated TAK1 mediates p38 MAPK activation.
Reactome; R-MMU-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
Reactome; R-MMU-4755510; SUMOylation of immune response proteins.
Reactome; R-MMU-5357905; Regulation of TNFR1 signaling.
Reactome; R-MMU-5357956; TNFR1-induced NFkappaB signaling pathway.
Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-MMU-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation.
Reactome; R-MMU-5689880; Ub-specific processing proteases.
Reactome; R-MMU-5689896; Ovarian tumor domain proteases.
Reactome; R-MMU-9020702; Interleukin-1 signaling.
Reactome; R-MMU-933542; TRAF6 mediated NF-kB activation.
Reactome; R-MMU-937039; IRAK1 recruits IKK complex.
Reactome; R-MMU-937041; IKK complex recruitment mediated by RIP1.
Reactome; R-MMU-975144; IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
BioGRID-ORCS; 16151; 7 hits in 17 CRISPR screens.
ChiTaRS; Ikbkg; mouse.
EvolutionaryTrace; O88522; -.
PRO; PR:O88522; -.
Proteomes; UP000000589; Chromosome X.
RNAct; O88522; protein.
Bgee; ENSMUSG00000004221; Expressed in blood and 288 other tissues.
ExpressionAtlas; O88522; baseline and differential.
Genevisible; O88522; MM.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0008385; C:IkappaB kinase complex; ISO:MGI.
GO; GO:0072686; C:mitotic spindle; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0000922; C:spindle pole; ISO:MGI.
GO; GO:0000151; C:ubiquitin ligase complex; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IDA:MGI.
GO; GO:1990450; F:linear polyubiquitin binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042975; F:peroxisome proliferator activated receptor binding; ISO:MGI.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:1990459; F:transferrin receptor binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; IDA:MGI.
GO; GO:0043276; P:anoikis; IMP:ParkinsonsUK-UCL.
GO; GO:0001782; P:B cell homeostasis; IMP:MGI.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0051650; P:establishment of vesicle localization; ISO:MGI.
GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IMP:ParkinsonsUK-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IGI:ParkinsonsUK-UCL.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
GO; GO:0016239; P:positive regulation of macroautophagy; IMP:ParkinsonsUK-UCL.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
InterPro; IPR032419; CC2-LZ_dom.
InterPro; IPR021063; NEMO_N.
InterPro; IPR034735; NEMO_ZF.
Pfam; PF16516; CC2-LZ; 1.
Pfam; PF11577; NEMO; 1.
PROSITE; PS51801; ZF_CCHC_NOA; 1.
1: Evidence at protein level;
3D-structure; Coiled coil; Cytoplasm; Direct protein sequencing;
Disulfide bond; DNA damage; Isopeptide bond; Metal-binding; Nucleus;
Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1..412
/note="NF-kappa-B essential modulator"
/id="PRO_0000096783"
ZN_FING 382..412
/note="CCHC NOA-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01142"
REGION 44..111
/note="Interaction with CHUK/IKBKB"
/evidence="ECO:0000250"
REGION 150..250
/note="Interaction with TANK"
/evidence="ECO:0000269|PubMed:12133833"
REGION 242..343
/note="Ubiquitin-binding (UBD)"
REGION 246..358
/note="Self-association"
/evidence="ECO:0000250"
REGION 249..412
/note="Required for interaction with TNFAIP3"
/evidence="ECO:0000250"
REGION 250..339
/note="Linear polyubiquitin-binding, does not bind to 'Lys-
63'-linked polyubiquitin"
REGION 315..336
/note="Leucine-zipper"
/evidence="ECO:0000255"
REGION 375..412
/note="Interaction with CYLD"
/evidence="ECO:0000250"
COILED 49..345
/evidence="ECO:0000255"
MOD_RES 31
/note="Phosphoserine; by IKKB"
/evidence="ECO:0000250|UniProtKB:Q9Y6K9"
MOD_RES 43
/note="Phosphoserine; by IKKB"
/evidence="ECO:0000250|UniProtKB:Q9Y6K9"
MOD_RES 68
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q9Y6K9"
MOD_RES 85
/note="Phosphoserine; by ATM"
/evidence="ECO:0000250|UniProtKB:Q9Y6K9"
MOD_RES 369
/note="Phosphoserine; by IKKB"
/evidence="ECO:0000269|PubMed:11971901"
MOD_RES 380
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:21183079"
DISULFID 54
/note="Interchain"
/evidence="ECO:0000250"
DISULFID 340
/note="Interchain"
/evidence="ECO:0000250"
CROSSLNK 111
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000250|UniProtKB:Q9Y6K9"
CROSSLNK 139
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000250|UniProtKB:Q9Y6K9"
CROSSLNK 143
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000250|UniProtKB:Q9Y6K9"
CROSSLNK 226
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000250|UniProtKB:Q9Y6K9"
CROSSLNK 246
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000250|UniProtKB:Q9Y6K9"
CROSSLNK 270
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO); alternate"
/evidence="ECO:0000250"
CROSSLNK 270
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin); alternate"
/evidence="ECO:0000250|UniProtKB:Q9Y6K9"
CROSSLNK 276
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000250|UniProtKB:Q9Y6K9"
CROSSLNK 278
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000269|PubMed:17728323"
CROSSLNK 285
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000250|UniProtKB:Q9Y6K9"
CROSSLNK 295
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000250|UniProtKB:Q9Y6K9"
CROSSLNK 302
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO); alternate"
/evidence="ECO:0000250"
CROSSLNK 302
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin); alternate"
/evidence="ECO:0000250|UniProtKB:Q9Y6K9"
CROSSLNK 314
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000269|PubMed:17728323"
CROSSLNK 318
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000269|PubMed:17728323"
CROSSLNK 319
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000269|PubMed:17728323"
CROSSLNK 392
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000269|PubMed:17728323"
MUTAGEN 278
/note="K->R: Slight decrease in TRAF6-induced
polyubiquitination."
/evidence="ECO:0000269|PubMed:17728323"
MUTAGEN 293
/note="V->A: Abolishes linear polyubiquitin-binding,
impairs 'Lys-63'-linked polyubiquitin-binding and impairs
NF-kappa-B activation; when associated with A-301 and A-
302."
/evidence="ECO:0000269|PubMed:19303852"
MUTAGEN 301
/note="Y->A: Abolishes linear polyubiquitin-binding,
impairs 'Lys-63'-linked polyubiquitin-binding and impairs
NF-kappa-B activation; when associated with A-293 and A-
302."
/evidence="ECO:0000269|PubMed:19303852"
MUTAGEN 302
/note="K->A: Abolishes linear polyubiquitin-binding,
impairs 'Lys-63'-linked polyubiquitin-binding and impairs
NF-kappa-B activation; when associated with A-293 and A-
301."
/evidence="ECO:0000269|PubMed:19303852"
MUTAGEN 305
/note="F->A: Abolishes linear polyubiquitin-binding,
impairs 'Lys-63'-linked polyubiquitin-binding and impairs
of NF-kappa-B activation."
/evidence="ECO:0000269|PubMed:19303852"
MUTAGEN 309
/note="R->A: Abolishes linear polyubiquitin-binding, no
effect on 'Lys-63'-linked polyubiquitin-binding and impairs
NF-kappa-B activation; when associated with A-312 and A-
313."
/evidence="ECO:0000269|PubMed:19303852"
MUTAGEN 312
/note="R->A: Abolishes linear polyubiquitin-binding, no
effect on 'Lys-63'-linked polyubiquitin-binding and impairs
NF-kappa-B activation; when associated with A-309 and A-
313."
/evidence="ECO:0000269|PubMed:19303852"
MUTAGEN 313
/note="E->A: Impairs linear polyubiquitin-binding.
Abolishes linear polyubiquitin-binding, no effect on 'Lys-
63'-linked polyubiquitin-binding and impairs NF-kappa-B
activation; when associated with A-309 and A-312. Abolishes
linear polyubiquitin-binding; when associated with A-317
and A-320."
/evidence="ECO:0000269|PubMed:19303852"
MUTAGEN 314
/note="K->R: Slight decrease in TRAF6-induced
polyubiquitination. Important decrease in TRAF6-induced
polyubiquitination; when associated with R-318 and R-319."
/evidence="ECO:0000269|PubMed:17728323"
MUTAGEN 316
/note="V->P: Loss of interaction with TRAF6 and TRAF6-
induced polyubiquitination."
/evidence="ECO:0000269|PubMed:17728323"
MUTAGEN 317
/note="E->A: Abolishes linear polyubiquitin-binding; when
associated with A-313 and A-320."
/evidence="ECO:0000269|PubMed:19303852"
MUTAGEN 318
/note="K->R: Slight decrease in TRAF6-induced
polyubiquitination. Decrease in TRAF6-induced
polyubiquitination; when associated with R-319. Important
decrease in TRAF6-induced polyubiquitination; when
associated with R-314 and R-319."
/evidence="ECO:0000269|PubMed:17728323"
MUTAGEN 319
/note="K->R: Slight decrease in TRAF6-induced
polyubiquitination. Decrease in TRAF6-induced
polyubiquitination; when associated with R-318. Important
decrease in TRAF6-induced polyubiquitination; when
associated with R-314 and R-318."
/evidence="ECO:0000269|PubMed:17728323"
MUTAGEN 320
/note="E->A: Abolishes linear polyubiquitin-binding; when
associated with A-313 and A-317."
/evidence="ECO:0000269|PubMed:19303852"
MUTAGEN 369
/note="S->A: Decreases phosphorylation and increases NF-
kappa-B activity."
/evidence="ECO:0000269|PubMed:11971901"
MUTAGEN 375
/note="S->A: Decreases phosphorylation and increases NF-
kappa-B activity."
/evidence="ECO:0000269|PubMed:11971901"
MUTAGEN 392
/note="K->R: 40% decrease in IL1-induced NF-kappa-B
activation."
/evidence="ECO:0000269|PubMed:17728323"
CONFLICT 13
/note="M -> T (in Ref. 1; AAC40153)"
/evidence="ECO:0000305"
HELIX 253..289
/evidence="ECO:0000244|PDB:4OWF"
HELIX 291..333
/evidence="ECO:0000244|PDB:4OWF"
HELIX 337..340
/evidence="ECO:0000244|PDB:3JSV"
SEQUENCE 412 AA; 47972 MW; 66C693C857A2D5E6 CRC64;
MNKHPWKNQL SEMVQPSGGP AEDQDMLGEE SSLGKPAMLH LPSEQGTPET LQRCLEENQE
LRDAIRQSNQ MLRERCEELL HFQVSQREEK EFLMCKFQEA RKLVERLSLE KLDLRSQREQ
ALKELEQLKK CQQQMAEDKA SVKAQVTSLL GELQESQSRL EAATKDRQAL EGRIRAVSEQ
VRQLESEREV LQQQHSVQVD QLRMQNQSVE AALRMERQAA SEEKRKLAQL QAAYHQLFQD
YDSHIKSSKG MQLEDLRQQL QQAEEALVAK QELIDKLKEE AEQHKIVMET VPVLKAQADI
YKADFQAERH AREKLVEKKE YLQEQLEQLQ REFNKLKVGC HESARIEDMR KRHVETPQPP
LLPAPAHHSF HLALSNQRRS PPEEPPDFCC PKCQYQAPDM DTLQIHVMEC IE


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E1953h ELISA kit Homo sapiens,Human,I-kappa-B kinase 2,I-kappa-B-kinase beta,IkBKB,IKBKB,IKK2,IKKB,IKK-B,IKK-beta,Inhibitor of nuclear factor kappa-B kinase subunit beta,NFKBIKB,Nuclear factor NF-kappa-B in 96T
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Pathways :
WP758: EBV LMP1 signaling
WP2292: Chemokine signaling pathway
WP1224: EBV LMP1 signaling
WP32: Translation Factors
WP866: EBV LMP1 signaling
WP262: EBV LMP1 signaling
WP2152: BDNF
WP1493: Carbon assimilation C4 pathway
WP1654: gamma-Hexachlorocyclohexane degradation
WP2199: Seed Development
WP1571: EBV LMP1 signaling
WP1694: Pyrimidine metabolism
WP1278: EBV LMP1 signaling
WP1701: Starch and sucrose metabolism
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP542: Electron Transport Chain
WP1644: DNA replication
WP1722: Th1/Th2
WP253: Glycolysis
WP868: estrogen signalling
WP1844: MAP kinase cascade
WP1567: Glycolysis and Gluconeogenesis
WP1693: Purine metabolism
WP1243: EBV LMP1 signaling
WP1328: EBV LMP1 signaling

Related Genes :
[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)
[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)
[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)
[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)
[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)
[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)
[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)
[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 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)
[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)
[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)
[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)
[IKBKE IKKE IKKI KIAA0151] Inhibitor of nuclear factor kappa-B kinase subunit epsilon (I-kappa-B kinase epsilon) (IKK-E) (IKK-epsilon) (IkBKE) (EC 2.7.11.10) (Inducible I kappa-B kinase) (IKK-i)
[Ikbke Ikke Ikki] Inhibitor of nuclear factor kappa-B kinase subunit epsilon (I-kappa-B kinase epsilon) (IKK-E) (IKK-epsilon) (IkBKE) (EC 2.7.11.10) (Inducible I kappa-B kinase) (IKK-i)
[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]
[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]
[NFKBIA IKBA MAD3 NFKBI] NF-kappa-B inhibitor alpha (I-kappa-B-alpha) (IkB-alpha) (IkappaBalpha) (Major histocompatibility complex enhancer-binding protein MAD3)
[TBK1 NAK] Serine/threonine-protein kinase TBK1 (EC 2.7.11.1) (NF-kappa-B-activating kinase) (T2K) (TANK-binding kinase 1)
[Rel CG11992] Nuclear factor NF-kappa-B p110 subunit (Rel-p110) (Relish protein) [Cleaved into: Nuclear factor NF-kappa-B p68 subunit (Rel-p68); Nuclear factor NF-kappa-B p49 subunit (Rel-p49)]
[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]
[RELA NFKB3] Transcription factor p65 (Nuclear factor NF-kappa-B p65 subunit) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3)
[Nfkbia Ikba] NF-kappa-B inhibitor alpha (I-kappa-B-alpha) (IkB-alpha) (IkappaBalpha) (RL/IF-1)
[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)
[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]
[Nfkbia Ikba] NF-kappa-B inhibitor alpha (I-kappa-B-alpha) (IkB-alpha) (IkappaBalpha)
[NFKBIA IKBA] NF-kappa-B inhibitor alpha (ECI-6) (I-kappa-B-alpha) (IkB-alpha) (IkappaBalpha)
[TRAF3IP2 C6orf2 C6orf4 C6orf5 C6orf6] Adapter protein CIKS (Connection to IKK and SAPK/JNK) (Nuclear factor NF-kappa-B activator 1) (ACT1) (TRAF3-interacting protein 2)
[Rela Nfkb3] Transcription factor p65 (Nuclear factor NF-kappa-B p65 subunit) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3)
[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)

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