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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.
28-MAR-2018, entry version 161.
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]
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).
[17]
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 LRDD.
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).
{ECO:0000250|UniProtKB:Q9Y6K9, ECO:0000269|PubMed:12133833,
ECO:0000269|PubMed:16684768, ECO:0000269|PubMed:19303852,
ECO:0000269|PubMed:20622870}.
-!- INTERACTION:
Q60680:Chuk; NbExp=6; IntAct=EBI-998011, EBI-646245;
O88351:Ikbkb; NbExp=7; IntAct=EBI-998011, EBI-447960;
Q924T7:Rnf31; NbExp=7; IntAct=EBI-998011, EBI-647680;
P0CG48:UBC (xeno); NbExp=3; IntAct=EBI-998011, EBI-3390054;
P62991:Ubc; NbExp=3; IntAct=EBI-998011, EBI-413074;
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-kappaB 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; CAM45971.1; -; 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.
UniGene; Mm.12967; -.
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; -.
ProteinModelPortal; O88522; -.
SMR; O88522; -.
BioGrid; 200602; 45.
CORUM; O88522; -.
DIP; DIP-29811N; -.
IntAct; O88522; 20.
MINT; O88522; -.
STRING; 10090.ENSMUSP00000004330; -.
iPTMnet; O88522; -.
PhosphoSitePlus; O88522; -.
EPD; O88522; -.
MaxQB; O88522; -.
PaxDb; O88522; -.
PRIDE; O88522; -.
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; HOG000293233; -.
HOVERGEN; HBG000417; -.
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-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.
EvolutionaryTrace; O88522; -.
PRO; PR:O88522; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000004221; -.
CleanEx; MM_IKBKG; -.
ExpressionAtlas; O88522; baseline and differential.
Genevisible; O88522; MM.
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:0005622; C:intracellular; ISO:MGI.
GO; GO:0072686; C:mitotic spindle; ISO:MGI.
GO; GO:0005634; C:nucleus; 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: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: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:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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; Complete proteome; 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 NF-kappa-B essential modulator.
/FTId=PRO_0000096783.
ZN_FING 382 412 CCHC NOA-type. {ECO:0000255|PROSITE-
ProRule:PRU01142}.
REGION 44 111 Interaction with CHUK/IKBKB.
{ECO:0000250}.
REGION 150 250 Interaction with TANK.
{ECO:0000269|PubMed:12133833}.
REGION 242 343 Ubiquitin-binding (UBD).
REGION 246 358 Self-association. {ECO:0000250}.
REGION 249 412 Required for interaction with TNFAIP3.
{ECO:0000250}.
REGION 250 339 Linear polyubiquitin-binding, does not
bind to 'Lys-63'-linked polyubiquitin.
REGION 315 336 Leucine-zipper. {ECO:0000255}.
REGION 375 412 Interaction with CYLD. {ECO:0000250}.
COILED 49 345 {ECO:0000255}.
MOD_RES 31 31 Phosphoserine; by IKKB.
{ECO:0000250|UniProtKB:Q9Y6K9}.
MOD_RES 43 43 Phosphoserine; by IKKB.
{ECO:0000250|UniProtKB:Q9Y6K9}.
MOD_RES 68 68 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y6K9}.
MOD_RES 85 85 Phosphoserine; by ATM.
{ECO:0000250|UniProtKB:Q9Y6K9}.
MOD_RES 369 369 Phosphoserine; by IKKB.
{ECO:0000269|PubMed:11971901}.
MOD_RES 380 380 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
DISULFID 54 54 Interchain. {ECO:0000250}.
DISULFID 340 340 Interchain. {ECO:0000250}.
CROSSLNK 111 111 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q9Y6K9}.
CROSSLNK 139 139 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q9Y6K9}.
CROSSLNK 143 143 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q9Y6K9}.
CROSSLNK 226 226 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q9Y6K9}.
CROSSLNK 246 246 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q9Y6K9}.
CROSSLNK 270 270 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 270 270 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:Q9Y6K9}.
CROSSLNK 276 276 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q9Y6K9}.
CROSSLNK 278 278 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:17728323}.
CROSSLNK 285 285 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q9Y6K9}.
CROSSLNK 295 295 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q9Y6K9}.
CROSSLNK 302 302 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 302 302 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:Q9Y6K9}.
CROSSLNK 314 314 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:17728323}.
CROSSLNK 318 318 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:17728323}.
CROSSLNK 319 319 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:17728323}.
CROSSLNK 392 392 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:17728323}.
MUTAGEN 278 278 K->R: Slight decrease in TRAF6-induced
polyubiquitination.
{ECO:0000269|PubMed:17728323}.
MUTAGEN 293 293 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.
{ECO:0000269|PubMed:19303852}.
MUTAGEN 301 301 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.
{ECO:0000269|PubMed:19303852}.
MUTAGEN 302 302 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.
{ECO:0000269|PubMed:19303852}.
MUTAGEN 305 305 F->A: Abolishes linear polyubiquitin-
binding, impairs 'Lys-63'-linked
polyubiquitin-binding and impairs of NF-
kappa-B activation.
{ECO:0000269|PubMed:19303852}.
MUTAGEN 309 309 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.
{ECO:0000269|PubMed:19303852}.
MUTAGEN 312 312 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.
{ECO:0000269|PubMed:19303852}.
MUTAGEN 313 313 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.
{ECO:0000269|PubMed:19303852}.
MUTAGEN 314 314 K->R: Slight decrease in TRAF6-induced
polyubiquitination. Important decrease in
TRAF6-induced polyubiquitination; when
associated with R-318 and R-319.
{ECO:0000269|PubMed:17728323}.
MUTAGEN 316 316 V->P: Loss of interaction with TRAF6 and
TRAF6-induced polyubiquitination.
{ECO:0000269|PubMed:17728323}.
MUTAGEN 317 317 E->A: Abolishes linear polyubiquitin-
binding; when associated with A-313 and
A-320. {ECO:0000269|PubMed:19303852}.
MUTAGEN 318 318 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.
{ECO:0000269|PubMed:17728323}.
MUTAGEN 319 319 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.
{ECO:0000269|PubMed:17728323}.
MUTAGEN 320 320 E->A: Abolishes linear polyubiquitin-
binding; when associated with A-313 and
A-317. {ECO:0000269|PubMed:19303852}.
MUTAGEN 369 369 S->A: Decreases phosphorylation and
increases NF-kappa-B activity.
{ECO:0000269|PubMed:11971901}.
MUTAGEN 375 375 S->A: Decreases phosphorylation and
increases NF-kappa-B activity.
{ECO:0000269|PubMed:11971901}.
MUTAGEN 392 392 K->R: 40% decrease in IL1-induced NF-
kappa-B activation.
{ECO:0000269|PubMed:17728323}.
CONFLICT 13 13 M -> T (in Ref. 1; AAC40153).
{ECO:0000305}.
HELIX 253 289 {ECO:0000244|PDB:4OWF}.
HELIX 291 333 {ECO:0000244|PDB:4OWF}.
HELIX 337 340 {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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