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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)

 NEMO_HUMAN              Reviewed;         419 AA.
Q9Y6K9; Q7LBY6; Q7Z7F1;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
30-MAY-2000, sequence version 2.
22-NOV-2017, entry version 198.
RecName: Full=NF-kappa-B essential modulator;
Short=NEMO;
AltName: Full=FIP-3;
AltName: Full=IkB kinase-associated protein 1;
Short=IKKAP1;
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=FIP3, NEMO;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Mammary cancer;
PubMed=10087442; DOI=10.1007/BF02256442;
Jin D.-Y., Jeang K.-T.;
"Isolation of full-length cDNA and chromosomal localization of human
NF-kappaB modulator NEMO to Xq28.";
J. Biomed. Sci. 6:115-120(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Cervix carcinoma;
PubMed=9751060; DOI=10.1038/26261;
Rothwarf D.M., Zandi E., Natoli G., Karin M.;
"IKK-gamma is an essential regulatory subunit of the IkappaB kinase
complex.";
Nature 395:297-300(1998).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT IP VAL-407.
PubMed=10839543; DOI=10.1038/35013114;
Smahi A., Courtois G., Vabres P., Yamaoka S., Heuertz S., Munnich A.,
Israel A., Heiss N.S., Klauck S.M., Kioschis P., Wiemann S.,
Poustka A., Esposito T., Bardaro T., Gianfrancesco F., Ciccodicola A.,
D'Urso M., Woffendin H., Jakins T., Donnai D., Stewart H.,
Kenwrick S.J., Aradhya S., Yamagata T., Levy M., Lewis R.A.,
Nelson D.L.;
"Genomic rearrangement in NEMO impairs NF-kappaB activation and is a
cause of incontinentia pigmenti.";
Nature 405:466-472(2000).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Astrocytoma;
PubMed=10944468; DOI=10.1006/bbrc.2000.3282;
Ye Z., Connor J.R.;
"cDNA cloning by amplification of circularized first strand cDNAs
reveals non-IRE-regulated iron-responsive mRNAs.";
Biochem. Biophys. Res. Commun. 275:223-227(2000).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Perelygin A.A., Perelygina L.M.;
"Ikbkg gene modulates the herpes virus susceptibility in mice.";
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung, Placenta, and Skin;
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).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 51-419 (ISOFORM 1), 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).
[12]
INTERACTION WITH HTLV-1 TAX-1.
PubMed=10364167; DOI=10.1074/jbc.274.25.17402;
Jin D.-Y., Giordano V., Kibler K.V., Nakano H., Jeang K.-T.;
"Role of adapter function in oncoprotein-mediated activation of NF-
kappaB: human T-cell leukemia virus type I Tax interacts directly with
IkappaB kinase gamma.";
J. Biol. Chem. 274:17402-17405(1999).
[13]
INTERACTION WITH HTLV-1 TAX-1.
PubMed=11064457; DOI=10.1038/sj.onc.1203894;
Xiao G., Sun S.C.;
"Activation of IKKalpha and IKKbeta through their fusion with HTLV-I
tax protein.";
Oncogene 19:5198-5203(2000).
[14]
INTERACTION WITH TNFAIP3.
PubMed=11389905; DOI=10.1016/S0014-5793(01)02504-2;
Klinkenberg M., Van Huffel S., Heyninck K., Beyaert R.;
"Functional redundancy of the zinc fingers of A20 for inhibition of
NF-kappaB activation and protein-protein interactions.";
FEBS Lett. 498:93-97(2001).
[15]
INTERACTION WITH COPS3.
PubMed=11418127; DOI=10.1016/S0014-5793(01)02535-2;
Hong X., Xu L.-G., Li X., Zhai Z., Shu H.-B.;
"CSN3 interacts with IKKgamma and inhibits TNF- but not IL-1-induced
NF-kappaB activation.";
FEBS Lett. 499:133-136(2001).
[16]
SUBUNIT OF THE 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).
[17]
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).
[18]
SUBUNIT OF A COMPLEX CONTAINING CREBBP; NCOA2; NCOA3; IKKA AND IKKB.
PubMed=11971985; DOI=10.1128/MCB.22.10.3549-3561.2002;
Wu R.-C., Qin J., Hashimoto Y., Wong J., Xu J., Tsai S.Y., Tsai M.-J.,
O'Malley B.W.;
"Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) coactivator
activity by I kappa B kinase.";
Mol. Cell. Biol. 22:3549-3561(2002).
[19]
SUMOYLATION AT LYS-277 AND LYS-309, UBIQUITINATION AT LYS-277 AND
LYS-309, MUTAGENESIS OF LYS-277 AND LYS-309, SUBCELLULAR LOCATION, AND
CHARACTERIZATION OF VARIANT EDAID ARG-417.
PubMed=14651848; DOI=10.1016/S0092-8674(03)00895-X;
Huang T.T., Wuerzberger-Davis S.M., Wu Z.H., Miyamoto S.;
"Sequential modification of NEMO/IKKgamma by SUMO-1 and ubiquitin
mediates NF-kappaB activation by genotoxic stress.";
Cell 115:565-576(2003).
[20]
PHOSPHORYLATION AT SER-31; SER-43 AND SER-376.
PubMed=12657630; DOI=10.1074/jbc.M301705200;
Carter R.S., Pennington K.N., Ungurait B.J., Ballard D.W.;
"In vivo identification of inducible phosphoacceptors in the
IKKgamma/NEMO subunit of human IkappaB kinase.";
J. Biol. Chem. 278:19642-19648(2003).
[21]
SELF-ASSOCIATION, AND COMPOSITION OF THE IKK COMPLEX.
PubMed=12612076; DOI=10.1128/MCB.23.6.2029-2041.2003;
Tegethoff S., Behlke J., Scheidereit C.;
"Tetrameric oligomerization of IkappaB kinase gamma (IKKgamma) is
obligatory for IKK complex activity and NF-kappaB activation.";
Mol. Cell. Biol. 23:2029-2041(2003).
[22]
INTERACTION WITH CYLD.
PubMed=12917691; DOI=10.1038/nature01802;
Kovalenko A., Chable-Bessia C., Cantarella G., Israeel A., Wallach D.,
Courtois G.;
"The tumour suppressor CYLD negatively regulates NF-kappaB signalling
by deubiquitination.";
Nature 424:801-805(2003).
[23]
UBIQUITINATION AT LYS-285, AND MUTAGENESIS OF LYS-115; LYS-224;
LYS-285 AND LYS-399.
PubMed=15620648; DOI=10.1016/j.cub.2004.12.032;
Abbott D.W., Wilkins A., Asara J.M., Cantley L.C.;
"The Crohn's disease protein, NOD2, requires RIP2 in order to induce
ubiquitinylation of a novel site on NEMO.";
Curr. Biol. 14:2217-2227(2004).
[24]
INTERACTION WITH ZFAND5.
PubMed=14754897; DOI=10.1074/jbc.M309491200;
Huang J., Teng L., Li L., Liu T., Li L., Chen D., Xu L.-G., Zhai Z.,
Shu H.-B.;
"ZNF216 is an A20-like and IkappaB kinase gamma-interacting inhibitor
of NFkappaB activation.";
J. Biol. Chem. 279:16847-16853(2004).
[25]
INTERACTION WITH NALP2.
PubMed=15456791; DOI=10.1074/jbc.M406741200;
Bruey J.-M., Bruey-Sedano N., Newman R., Chandler S., Stehlik C.,
Reed J.C.;
"PAN1/NALP2/PYPAF2, an inducible inflammatory mediator that regulates
NF-kappaB and caspase-1 activation in macrophages.";
J. Biol. Chem. 279:51897-51907(2004).
[26]
UBIQUITINATION.
PubMed=15125833; DOI=10.1016/S1097-2765(04)00236-9;
Sun L., Deng L., Ea C.-K., Xia Z.-P., Chen Z.J.;
"The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by
BCL10 and MALT1 in T lymphocytes.";
Mol. Cell 14:289-301(2004).
[27]
FUNCTION, UBIQUITINATION AT LYS-399, AND MUTAGENESIS OF LYS-399.
PubMed=14695475; DOI=10.1038/nature02273;
Zhou H., Wertz I., O'Rourke K., Ultsch M., Seshagiri S., Eby M.,
Xiao W., Dixit V.M.;
"Bcl10 activates the NF-kappaB pathway through ubiquitination of
NEMO.";
Nature 427:167-171(2004).
[28]
INTERACTION WITH LRDD.
PubMed=16360037; DOI=10.1016/j.cell.2005.09.036;
Janssens S., Tinel A., Lippens S., Tschopp J.;
"PIDD mediates NF-kappaB activation in response to DNA damage.";
Cell 123:1079-1092(2005).
[29]
UBIQUITIN-BINDING, MUTAGENESIS OF LEU-329, AND CHARACTERIZATION OF
VARIANT EDAID ASN-311.
PubMed=16547522; DOI=10.1038/ncb1384;
Wu C.J., Conze D.B., Li T., Srinivasula S.M., Ashwell J.D.;
"Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in
NF-kappaB activation.";
Nat. Cell Biol. 8:398-406(2006).
[30]
ERRATUM.
Wu C.J., Conze D.B., Li T., Srinivasula S.M., Ashwell J.D.;
Nat. Cell Biol. 8:424-424(2006).
[31]
INTERACTION WITH ATM, PHOSPHORYLATION AT SER-85, AND MUTAGENESIS OF
SER-85.
PubMed=16497931; DOI=10.1126/science.1121513;
Wu Z.H., Shi Y., Tibbetts R.S., Miyamoto S.;
"Molecular linkage between the kinase ATM and NF-kappaB signaling in
response to genotoxic stimuli.";
Science 311:1141-1146(2006).
[32]
UBIQUITINATION.
PubMed=17135271; DOI=10.1074/jbc.M609503200;
Lamothe B., Besse A., Campos A.D., Webster W.K., Wu H., Darnay B.G.;
"Site-specific Lys-63-linked tumor necrosis factor receptor-associated
factor 6 auto-ubiquitination is a critical determinant of I kappa B
kinase activation.";
J. Biol. Chem. 282:4102-4112(2007).
[33]
SUBUNIT, AND DISULFIDE BONDS.
PubMed=18164680; DOI=10.1016/j.bbrc.2007.12.123;
Herscovitch M., Comb W., Ennis T., Coleman K., Yong S., Armstead B.,
Kalaitzidis D., Chandani S., Gilmore T.D.;
"Intermolecular disulfide bond formation in the NEMO dimer requires
Cys54 and Cys347.";
Biochem. Biophys. Res. Commun. 367:103-108(2008).
[34]
INTERACTION WITH RIPK2.
PubMed=18079694; DOI=10.1038/sj.emboj.7601962;
Hasegawa M., Fujimoto Y., Lucas P.C., Nakano H., Fukase K., Nunez G.,
Inohara N.;
"A critical role of RICK/RIP2 polyubiquitination in Nod-induced NF-
kappaB activation.";
EMBO J. 27:373-383(2008).
[35]
INTERACTION WITH IKBKB, PHOSPHORYLATION AT SER-68, AND MUTAGENESIS OF
SER-68.
PubMed=17977820; DOI=10.1074/jbc.M708856200;
Palkowitsch L., Leidner J., Ghosh S., Marienfeld R.B.;
"Phosphorylation of serine 68 in the IkappaB kinase (IKK)-binding
domain of NEMO interferes with the structure of the IKK complex and
tumor necrosis factor-alpha-induced NF-kappaB activity.";
J. Biol. Chem. 283:76-86(2008).
[36]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[37]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[38]
UBIQUITIN-BINDING, MUTAGENESIS OF VAL-414 AND MET-415, AND
CHARACTERIZATION OF VARIANT IP VAL-407.
PubMed=19033441; DOI=10.1074/jbc.M806655200;
Cordier F., Grubisha O., Traincard F., Veron M., Delepierre M.,
Agou F.;
"The zinc finger of NEMO is a functional ubiquitin-binding domain.";
J. Biol. Chem. 284:2902-2907(2009).
[39]
FUNCTION, AND DOMAIN LEUCINE-ZIPPER AND C2HC-TYPE ZINC-FINGER.
PubMed=19854139; DOI=10.1016/j.molcel.2009.09.037;
Zeng W., Xu M., Liu S., Sun L., Chen Z.J.;
"Key role of Ubc5 and lysine-63 polyubiquitination in viral activation
of IRF3.";
Mol. Cell 36:315-325(2009).
[40]
UBIQUITINATION AT LYS-285 AND LYS-309.
PubMed=19136968; DOI=10.1038/ncb1821;
Tokunaga F., Sakata S., Saeki Y., Satomi Y., Kirisako T., Kamei K.,
Nakagawa T., Kato M., Murata S., Yamaoka S., Yamamoto M., Akira S.,
Takao T., Tanaka K., Iwai K.;
"Involvement of linear polyubiquitylation of NEMO in NF-kappaB
activation.";
Nat. Cell Biol. 11:123-132(2009).
[41]
MUTAGENESIS OF GLU-296; PHE-312; LEU-329 AND LEU-336, AND
CHARACTERIZATION OF VARIANTS IMD33 ALA-315 AND PRO-323.
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).
[42]
INTERACTION WITH SHIGELLA FLEXNERI IPAH9.8, AND UBIQUITINATION AT
LYS-309 AND LYS-321.
PubMed=20010814; DOI=10.1038/ncb2006;
Ashida H., Kim M., Schmidt-Supprian M., Ma A., Ogawa M., Sasakawa C.;
"A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKgamma to
dampen the host NF-kappaB-mediated inflammatory response.";
Nat. Cell Biol. 12:66-73(2010).
[43]
FUNCTION, AND UBIQUITINATION.
PubMed=20724660; DOI=10.1073/pnas.1004621107;
Arimoto K., Funami K., Saeki Y., Tanaka K., Okawa K., Takeuchi O.,
Akira S., Murakami Y., Shimotohno K.;
"Polyubiquitin conjugation to NEMO by tripartite motif protein 23
(TRIM23) is critical in antiviral defense.";
Proc. Natl. Acad. Sci. U.S.A. 107:15856-15861(2010).
[44]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[45]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[46]
NEDDYLATION BY TRIM40.
PubMed=21474709; DOI=10.1093/carcin/bgr068;
Noguchi K., Okumura F., Takahashi N., Kataoka A., Kamiyama T.,
Todo S., Hatakeyama S.;
"TRIM40 promotes neddylation of IKKgamma and is downregulated in
gastrointestinal cancers.";
Carcinogenesis 32:995-1004(2011).
[47]
UBIQUITIN-BINDING, AND CHARACTERIZATION OF VARIANT EDAID ASN-311.
PubMed=21606507; DOI=10.1084/jem.20102177;
Nanda S.K., Venigalla R.K., Ordureau A., Patterson-Kane J.C.,
Powell D.W., Toth R., Arthur J.S., Cohen P.;
"Polyubiquitin binding to ABIN1 is required to prevent autoimmunity.";
J. Exp. Med. 208:1215-1228(2011).
[48]
INTERACTION WITH TNFAIP3.
PubMed=22099304; DOI=10.1016/j.molcel.2011.09.015;
Skaug B., Chen J., Du F., He J., Ma A., Chen Z.J.;
"Direct, noncatalytic mechanism of IKK inhibition by A20.";
Mol. Cell 44:559-571(2011).
[49]
UBIQUITINATION BY THE LUBAC COMPLEX.
PubMed=21455173; DOI=10.1038/nature09816;
Gerlach B., Cordier S.M., Schmukle A.C., Emmerich C.H., Rieser E.,
Haas T.L., Webb A.I., Rickard J.A., Anderton H., Wong W.W.,
Nachbur U., Gangoda L., Warnken U., Purcell A.W., Silke J.,
Walczak H.;
"Linear ubiquitination prevents inflammation and regulates immune
signalling.";
Nature 471:591-596(2011).
[50]
UBIQUITINATION BY THE LUBAC COMPLEX.
PubMed=21455180; DOI=10.1038/nature09815;
Tokunaga F., Nakagawa T., Nakahara M., Saeki Y., Taniguchi M.,
Sakata S., Tanaka K., Nakano H., Iwai K.;
"SHARPIN is a component of the NF-kappaB-activating linear ubiquitin
chain assembly complex.";
Nature 471:633-636(2011).
[51]
UBIQUITINATION AT LYS-277; LYS-285; LYS-309; LYS-326; LYS-111;
LYS-143; LYS-226; LYS-246; LYS-264; LYS-292 AND LYS-302 BY THE LUBAC
COMPLEX, AND UBIQUITINATION AT LYS-139 AND LYS-283.
PubMed=21455181; DOI=10.1038/nature09814;
Ikeda F., Deribe Y.L., Skanland S.S., Stieglitz B., Grabbe C.,
Franz-Wachtel M., van Wijk S.J., Goswami P., Nagy V., Terzic J.,
Tokunaga F., Androulidaki A., Nakagawa T., Pasparakis M., Iwai K.,
Sundberg J.P., Schaefer L., Rittinger K., Macek B., Dikic I.;
"SHARPIN forms a linear ubiquitin ligase complex regulating NF-kappaB
activity and apoptosis.";
Nature 471:637-641(2011).
[52]
INTERACTION WITH NLRP10.
PubMed=22672233; DOI=10.1111/j.1462-5822.2012.01822.x;
Lautz K., Damm A., Menning M., Wenger J., Adam A.C., Zigrino P.,
Kremmer E., Kufer T.A.;
"NLRP10 enhances Shigella-induced pro-inflammatory responses.";
Cell. Microbiol. 14:1568-1583(2012).
[53]
INTERACTION WITH IKBKE.
PubMed=23453969; DOI=10.1016/j.celrep.2013.01.031;
Zhou A.Y., Shen R.R., Kim E., Lock Y.J., Xu M., Chen Z.J., Hahn W.C.;
"IKKepsilon-mediated tumorigenesis requires K63-linked
polyubiquitination by a cIAP1/cIAP2/TRAF2 E3 ubiquitin ligase
complex.";
Cell Rep. 3:724-733(2013).
[54]
PHOSPHORYLATION AT SER-387.
PubMed=24012789; DOI=10.1016/j.pep.2013.08.020;
Jackson S.S., Coughlin E.E., Coon J.J., Miyamoto S.;
"Identifying post-translational modifications of NEMO by tandem mass
spectrometry after high affinity purification.";
Protein Expr. Purif. 92:48-53(2013).
[55]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[56]
INTERACTION WITH IFIT5.
PubMed=26334375; DOI=10.1016/j.cellsig.2015.08.018;
Zheng C., Zheng Z., Zhang Z., Meng J., Liu Y., Ke X., Hu Q., Wang H.;
"IFIT5 positively regulates NF-kappaB signaling through synergizing
the recruitment of IkappaB kinase (IKK) to TGF-beta-activated kinase 1
(TAK1).";
Cell. Signal. 27:2343-2354(2015).
[57]
INTERACTION WITH TANK; USP10 AND ZC3H12A, AND DEUBIQUITINATION BY
USP10.
PubMed=25861989; DOI=10.1074/jbc.M115.643767;
Wang W., Huang X., Xin H.B., Fu M., Xue A., Wu Z.H.;
"TRAF family member-associated NF-kappaB activator (TANK) inhibits
genotoxic nuclear factor kappaB activation by facilitating
deubiquitinase USP10-dependent deubiquitination of TRAF6 ligase.";
J. Biol. Chem. 290:13372-13385(2015).
[58]
STRUCTURE BY NMR OF 394-419 OF WILD-TYPE AND MUTANT PHE-417, AND
DOMAIN ZINC-FINGER.
PubMed=18313693; DOI=10.1016/j.jmb.2008.01.048;
Cordier F., Vinolo E., Veron M., Delepierre M., Agou F.;
"Solution structure of NEMO zinc finger and impact of an anhidrotic
ectodermal dysplasia with immunodeficiency-related point mutation.";
J. Mol. Biol. 377:1419-1432(2008).
[59]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 44-111 IN COMPLEX WITH CHUK
AND IKBKB, AND SUBUNIT.
PubMed=18462684; DOI=10.1016/j.str.2008.02.012;
Rushe M., Silvian L., Bixler S., Chen L.L., Cheung A., Bowes S.,
Cuervo H., Berkowitz S., Zheng T., Guckian K., Pellegrini M.,
Lugovskoy A.;
"Structure of a NEMO/IKK-associating domain reveals architecture of
the interaction site.";
Structure 16:798-808(2008).
[60]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 246-337, UBIQUITIN-BINDING,
MUTAGENESIS OF VAL-300; LEU-301; GLN-304; ILE-307; TYR-308; PHE-312;
GLN-313 AND GLN-317, CHARACTERIZATION OF VARIANT EDAID ASN-311,
CHARACTERIZATION OF VARIANT IMD33 ALA-315, AND CHARACTERIZATION OF
VARIANTS GLN-319 AND IP PRO-323.
PubMed=19185524; DOI=10.1016/j.molcel.2009.01.012;
Lo Y.C., Lin S.C., Rospigliosi C.C., Conze D.B., Wu C.J.,
Ashwell J.D., Eliezer D., Wu H.;
"Structural basis for recognition of diubiquitins by NEMO.";
Mol. Cell 33:602-615(2009).
[61]
VARIANTS EDAID ARG-417 AND PHE-417.
PubMed=11047757; DOI=10.1086/316914;
Zonana J., Elder M.E., Schneider L.C., Orlow S.J., Moss C., Golabi M.,
Shapira S.K., Farndon P.A., Wara D.W., Emmal S.A., Ferguson B.M.;
"A novel X-linked disorder of immune deficiency and hypohidrotic
ectodermal dysplasia is allelic to incontinentia pigmenti and due to
mutations in IKK-gamma (NEMO).";
Am. J. Hum. Genet. 67:1555-1562(2000).
[62]
VARIANTS IP LYS-57 AND VAL-407.
PubMed=11590134; DOI=10.1093/hmg/10.19.2171;
Aradhya S., Woffendin H., Jakins T., Bardaro T., Esposito T.,
Smahi A., Shaw C., Levy M., Munnich A., D'Urso M., Lewis R.A.,
Kenwrick S., Nelson D.L.;
"A recurrent deletion in the ubiquitously expressed NEMO (IKK-gamma)
gene accounts for the vast majority of incontinentia pigmenti
mutations.";
Hum. Mol. Genet. 10:2171-2179(2001).
[63]
INVOLVEMENT IN OLEDAID, INVOLVEMENT IN EDAID, AND VARIANTS EDAID
PRO-175; PRO-227; GLY-288; ASN-311; ARG-417 AND PHE-417.
PubMed=11242109; DOI=10.1038/85837;
Doeffinger R., Smahi A., Bessia C., Geissmann F., Feinberg J.,
Durandy A., Bodemer C., Kenwrick S.J., Dupuis-Girod S., Blanche S.,
Wood P., Rabia S.H., Headon D.J., Overbeek P.A., Le Deist F.,
Holland S.M., Belani K., Kumararatne D.S., Fischer A., Shapiro R.,
Conley M.E., Reimund E., Kalhoff H., Abinun M., Munnich A.,
Israael A., Courtois G., Casanova J.-L.;
"X-linked anhidrotic ectodermal dysplasia with immunodeficiency is
caused by impaired NF-kappa B signaling.";
Nat. Genet. 27:277-285(2001).
[64]
VARIANTS EDAID VAL-406 AND ARG-417.
PubMed=11224521; DOI=10.1038/85277;
Jain A., Ma C.A., Liu S., Brown M., Cohen J., Strober W.;
"Specific missense mutations in NEMO result in hyper-IgM syndrome with
hypohydrotic ectodermal dysplasia.";
Nat. Immunol. 2:223-228(2001).
[65]
VARIANTS EDAID ARG-153 AND ARG-417.
PubMed=12045264; DOI=10.1172/JCI0214858;
Orange J.S., Brodeur S.R., Jain A., Bonilla F.A., Schneider L.C.,
Kretschmer R., Nurko S., Rasmussen W.L., Koehler J.R., Gellis S.E.,
Ferguson B.M., Strominger J.L., Zonana J., Ramesh N., Ballas Z.K.,
Geha R.S.;
"Deficient natural killer cell cytotoxicity in patients with IKK-
gamma/NEMO mutations.";
J. Clin. Invest. 109:1501-1509(2002).
[66]
VARIANTS IP LYS-57; LYS-90 DEL AND TRP-123, VARIANT ASN-113,
CHARACTERIZATION OF VARIANTS IP LYS-57; LYS-90 DEL AND TRP-123, AND
CHARACTERIZATION OF VARIANT ASN-113.
PubMed=15229184; DOI=10.1093/hmg/ddh192;
Fusco F., Bardaro T., Fimiani G., Mercadante V., Miano M.G., Falco G.,
Israeel A., Courtois G., D'Urso M., Ursini M.V.;
"Molecular analysis of the genetic defect in a large cohort of IP
patients and identification of novel NEMO mutations interfering with
NF-kappaB activation.";
Hum. Mol. Genet. 13:1763-1773(2004).
[67]
VARIANTS EDAID ARG-153 AND ARG-417, AND VARIANT NEMOID TYR-417.
PubMed=15100680; DOI=10.1016/j.jaci.2004.01.762;
Orange J.S., Jain A., Ballas Z.K., Schneider L.C., Geha R.S.,
Bonilla F.A.;
"The presentation and natural history of immunodeficiency caused by
nuclear factor kappaB essential modulator mutation.";
J. Allergy Clin. Immunol. 113:725-733(2004).
[68]
INVOLVEMENT IN NEMOID.
PubMed=15356572; DOI=10.1016/j.jaci.2004.06.052;
Orange J.S., Levy O., Brodeur S.R., Krzewski K., Roy R.M.,
Niemela J.E., Fleisher T.A., Bonilla F.A., Geha R.S.;
"Human nuclear factor kappa B essential modulator mutation can result
in immunodeficiency without ectodermal dysplasia.";
J. Allergy Clin. Immunol. 114:650-656(2004).
[69]
VARIANTS IMD33 ALA-315 AND GLN-319.
PubMed=16818673; DOI=10.1084/jem.20060085;
Filipe-Santos O., Bustamante J., Haverkamp M.H., Vinolo E., Ku C.-L.,
Puel A., Frucht D.M., Christel K., von Bernuth H., Jouanguy E.,
Feinberg J., Durandy A., Senechal B., Chapgier A., Vogt G.,
de Beaucoudrey L., Fieschi C., Picard C., Garfa M., Chemli J.,
Bejaoui M., Tsolia M.N., Kutukculer N., Plebani A., Notarangelo L.,
Bodemer C., Geissmann F., Israeel A., Veron M., Knackstedt M.,
Barbouche R., Abel L., Magdorf K., Gendrel D., Agou F., Holland S.M.,
Casanova J.-L.;
"X-linked susceptibility to mycobacteria is caused by mutations in
NEMO impairing CD40-dependent IL-12 production.";
J. Exp. Med. 203:1745-1759(2006).
[70]
VARIANT IP PRO-323, CHARACTERIZATION OF VARIANT IP PRO-323, AND
INTERACTION WITH TRAF6.
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).
[71]
VARIANT IP HIS-183.
PubMed=20434027; DOI=10.1016/S0929-6646(10)60042-3;
Hsiao P.F., Lin S.P., Chiang S.S., Wu Y.H., Chen H.C., Lin Y.C.;
"NEMO gene mutations in Chinese patients with incontinentia
pigmenti.";
J. Formos. Med. Assoc. 109:192-200(2010).
[72]
VARIANTS IP PRO-170; GLN-173; PRO-314; PRO-322 AND TYR-413.
PubMed=24339369; DOI=10.1002/humu.22483;
Conte M.I., Pescatore A., Paciolla M., Esposito E., Miano M.G.,
Lioi M.B., McAleer M.A., Giardino G., Pignata C., Irvine A.D.,
Scheuerle A.E., Royer G., Hadj-Rabia S., Bodemer C., Bonnefont J.P.,
Munnich A., Smahi A., Steffann J., Fusco F., Ursini M.V.;
"Insight into IKBKG/NEMO locus: report of new mutations and complex
genomic rearrangements leading to incontinentia pigmenti disease.";
Hum. Mutat. 35:165-177(2014).
[73]
VARIANT IPD2 GLY-173.
PubMed=16950813; DOI=10.1136/jmg.2006.044446;
Ku C.-L., Picard C., Erdos M., Jeurissen A., Bustamante J., Puel A.,
von Bernuth H., Filipe-Santos O., Chang H.-H., Lawrence T., Raes M.,
Marodi L., Bossuyt X., Casanova J.-L.;
"IRAK4 and NEMO mutations in otherwise healthy children with recurrent
invasive pneumococcal disease.";
J. Med. Genet. 44:16-23(2007).
-!- 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. However, the specific type of
polyubiquitin recognized upon cell stimulation (either 'Lys-63'-
linked or linear polyubiquitin) and its functional importance is
reported conflictingly. 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. Essential for viral
activation of IRF3. Involved in TLR3- and IFIH1-mediated antiviral
innate response; this function requires 'Lys-27'-linked
polyubiquitination. {ECO:0000269|PubMed:14695475,
ECO:0000269|PubMed:19854139, ECO:0000269|PubMed:20724660}.
-!- 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 HTLV-1 Tax oncoprotein; the
interaction activates IKBKG. Interacts with IKBKE. Interacts with
TANK; the interaction is enhanced by IKBKE and TBK1. 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. Binds polyubiquitin; the
interaction is mediated by two domains; reports about the binding
to 'Lys-63'-linked and/or linear polyubiquitin, respective binding
affinities and stoichiometry are conflicting. Interacts with
Shigella flexneri ipah9.8; the interaction promotes TNIP1-
dependent 'Lys-27'-linked polyubiquitination of IKBKG which
perturbs NF-kappa-B activation during bacterial infection.
Interacts with NLRP10. Interacts with TANK; this interaction
increases in response to DNA damage (PubMed:25861989). Interacts
with USP10; this interaction increases in response to DNA damage
(PubMed:25861989). Interacts with ZC3H12A; this interaction
increases in response to DNA damage (PubMed:25861989). Interacts
with IFIT5; the interaction synergizes the recruitment of IKK to
MAP3K7 and enhances IKK phosphorylation (PubMed:26334375).
{ECO:0000269|PubMed:10364167, ECO:0000269|PubMed:11064457,
ECO:0000269|PubMed:11080499, ECO:0000269|PubMed:11389905,
ECO:0000269|PubMed:11418127, ECO:0000269|PubMed:11971985,
ECO:0000269|PubMed:12133833, ECO:0000269|PubMed:12917691,
ECO:0000269|PubMed:14754897, ECO:0000269|PubMed:15456791,
ECO:0000269|PubMed:16360037, ECO:0000269|PubMed:16497931,
ECO:0000269|PubMed:17728323, ECO:0000269|PubMed:17977820,
ECO:0000269|PubMed:18079694, ECO:0000269|PubMed:18164680,
ECO:0000269|PubMed:18462684, ECO:0000269|PubMed:20010814,
ECO:0000269|PubMed:22099304, ECO:0000269|PubMed:22672233,
ECO:0000269|PubMed:23453969, ECO:0000269|PubMed:25861989,
ECO:0000269|PubMed:26334375}.
-!- INTERACTION:
Self; NbExp=5; IntAct=EBI-81279, EBI-81279;
Q9NPF8:ADAP2; NbExp=2; IntAct=EBI-81279, EBI-718895;
P04083:ANXA1; NbExp=6; IntAct=EBI-81279, EBI-354007;
Q66PJ3:ARL6IP4; NbExp=2; IntAct=EBI-81279, EBI-2683099;
Q13315:ATM; NbExp=4; IntAct=EBI-81279, EBI-495465;
Q13535:ATR; NbExp=2; IntAct=EBI-81279, EBI-968983;
O95999:BCL10; NbExp=7; IntAct=EBI-81279, EBI-958922;
P05937:CALB1; NbExp=3; IntAct=EBI-81279, EBI-4286943;
Q16543:CDC37; NbExp=6; IntAct=EBI-81279, EBI-295634;
P24941:CDK2; NbExp=4; IntAct=EBI-81279, EBI-375096;
O15111:CHUK; NbExp=23; IntAct=EBI-81279, EBI-81249;
Q9UNS2:COPS3; NbExp=2; IntAct=EBI-81279, EBI-350590;
P36888:FLT3; NbExp=2; IntAct=EBI-81279, EBI-3946257;
Q14161:GIT2; NbExp=6; IntAct=EBI-81279, EBI-1046878;
P07900:HSP90AA1; NbExp=3; IntAct=EBI-81279, EBI-296047;
P08238:HSP90AB1; NbExp=3; IntAct=EBI-81279, EBI-352572;
O14920:IKBKB; NbExp=33; IntAct=EBI-81279, EBI-81266;
Q8VSC3:ipaH9.8 (xeno); NbExp=8; IntAct=EBI-81279, EBI-6125799;
P05783:KRT18; NbExp=3; IntAct=EBI-81279, EBI-297888;
P05787:KRT8; NbExp=2; IntAct=EBI-81279, EBI-297852;
Q9UDY8:MALT1; NbExp=4; IntAct=EBI-81279, EBI-1047372;
P01106:MYC; NbExp=3; IntAct=EBI-81279, EBI-447544;
P25963:NFKBIA; NbExp=6; IntAct=EBI-81279, EBI-307386;
P67775:PPP2CA; NbExp=4; IntAct=EBI-81279, EBI-712311;
Q9BYM8:RBCK1; NbExp=9; IntAct=EBI-81279, EBI-2340624;
Q13546:RIPK1; NbExp=7; IntAct=EBI-81279, EBI-358507;
Q96EP0:RNF31; NbExp=8; IntAct=EBI-81279, EBI-948111;
Q9UBF6:RNF7; NbExp=3; IntAct=EBI-81279, EBI-398632;
Q9BVN2-2:RUSC1; NbExp=4; IntAct=EBI-81279, EBI-6257338;
Q9HC62:SENP2; NbExp=3; IntAct=EBI-81279, EBI-714881;
Q9H0F6:SHARPIN; NbExp=13; IntAct=EBI-81279, EBI-3942966;
Q13501:SQSTM1; NbExp=2; IntAct=EBI-81279, EBI-307104;
P12931:SRC; NbExp=3; IntAct=EBI-81279, EBI-621482;
P63165:SUMO1; NbExp=3; IntAct=EBI-81279, EBI-80140;
P21579:SYT1; NbExp=3; IntAct=EBI-81279, EBI-524909;
Q9UHD2:TBK1; NbExp=2; IntAct=EBI-81279, EBI-356402;
P01375:TNF; NbExp=2; IntAct=EBI-81279, EBI-359977;
P21580:TNFAIP3; NbExp=4; IntAct=EBI-81279, EBI-527670;
Q15025:TNIP1; NbExp=4; IntAct=EBI-81279, EBI-357849;
Q8NFZ5:TNIP2; NbExp=6; IntAct=EBI-81279, EBI-359372;
P0CG48:UBC; NbExp=4; IntAct=EBI-81279, EBI-3390054;
Q9Y2X8:UBE2D4; NbExp=4; IntAct=EBI-81279, EBI-745527;
Q5D1E8:ZC3H12A; NbExp=2; IntAct=EBI-81279, EBI-747793;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14651848}.
Nucleus {ECO:0000269|PubMed:14651848}. Note=Sumoylated NEMO
accumulates in the nucleus in response to genotoxic stress.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9Y6K9-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y6K9-2; Sequence=VSP_041000;
Name=3;
IsoId=Q9Y6K9-3; Sequence=VSP_041001, VSP_041002;
-!- TISSUE SPECIFICITY: Heart, brain, placenta, lung, liver, skeletal
muscle, kidney and pancreas.
-!- DOMAIN: The leucine-zipper domain and the CCHC NOA-type zinc-
finger are essential for polyubiquitin binding and for the
activation of IRF3. {ECO:0000269|PubMed:18313693,
ECO:0000269|PubMed:19854139}.
-!- PTM: Phosphorylation at Ser-68 attenuates aminoterminal
homodimerization. {ECO:0000269|PubMed:17977820}.
-!- PTM: Polyubiquitinated on Lys-285 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-399 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-277 and Lys-309; 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-264,
Lys-277, Lys-285, Lys-292, Lys-302, Lys-309 and Lys-326; the head-
to-tail polyubiquitination is mediated by the LUBAC complex and
plays a key role in NF-kappa-B activation. Polyubiquitinated on
Lys-309 and Lys-321 via 'Lys-27'-linked ubiquitin by Shigella
flexneri E3 ubiquitin-protein ligase ipah9.8, leading to its
degradation by the proteasome. Deubiquitinated by USP10 in a TANK-
dependent and -independent manner, leading to the negative
regulation of NF-kappaB signaling upon DNA damage
(PubMed:25861989). {ECO:0000269|PubMed:14651848,
ECO:0000269|PubMed:14695475, ECO:0000269|PubMed:15620648,
ECO:0000269|PubMed:19136968, ECO:0000269|PubMed:20010814,
ECO:0000269|PubMed:21455181, ECO:0000269|PubMed:25861989}.
-!- PTM: Sumoylated on Lys-277 and Lys-309 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:0000269|PubMed:14651848,
ECO:0000269|PubMed:16497931, ECO:0000269|PubMed:19136968,
ECO:0000269|PubMed:20010814, ECO:0000269|PubMed:21455181}.
-!- PTM: Neddylated by TRIM40, resulting in stabilization of NFKBIA
and down-regulation of NF-kappa-B activity.
{ECO:0000269|PubMed:21474709}.
-!- DISEASE: Ectodermal dysplasia, anhidrotic, with immunodeficiency
X-linked (EDAID) [MIM:300291]: A form of ectoderma dysplasia, a
heterogeneous group of disorders due to abnormal development of
two or more ectodermal structures. Characterized by absence of
sweat glands, sparse scalp hair, rare conical teeth and
immunological abnormalities resulting in severe infectious
diseases. {ECO:0000269|PubMed:11047757,
ECO:0000269|PubMed:11224521, ECO:0000269|PubMed:11242109,
ECO:0000269|PubMed:12045264, ECO:0000269|PubMed:14651848,
ECO:0000269|PubMed:15100680, ECO:0000269|PubMed:16547522,
ECO:0000269|PubMed:19185524, ECO:0000269|PubMed:21606507}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Ectodermal dysplasia, anhidrotic, with immunodeficiency,
osteopetrosis and lymphedema (OLEDAID) [MIM:300301]: A form of
ectoderma dysplasia, a heterogeneous group of disorders due to
abnormal development of two or more ectodermal structures.
Characterized by the association of anhidrotic ectodermal
dysplasia with severe immunodeficiency, osteopetrosis and
lymphedema. {ECO:0000269|PubMed:11242109}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Immunodeficiency, NEMO-related, without anhidrotic
ectodermal dysplasia (NEMOID) [MIM:300584]: Patients manifest
immunodeficiency not associated with other abnormalities, and
resulting in increased susceptibility to infections. Patients
suffer from multiple episodes of infectious diseases.
{ECO:0000269|PubMed:15100680, ECO:0000269|PubMed:15356572}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Immunodeficiency 33 (IMD33) [MIM:300636]: A X-linked
recessive form of Mendelian susceptibility to mycobacterial
disease, a rare condition characterized by predisposition to
illness caused by moderately virulent mycobacterial species, such
as Bacillus Calmette-Guerin (BCG) vaccine, environmental non-
tuberculous mycobacteria, and by the more virulent Mycobacterium
tuberculosis. Other microorganisms rarely cause severe clinical
disease in individuals with susceptibility to mycobacterial
infections, with the exception of Salmonella which infects less
than 50% of these individuals. {ECO:0000269|PubMed:16818673,
ECO:0000269|PubMed:19185524, ECO:0000269|PubMed:19854204}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- DISEASE: Recurrent isolated invasive pneumococcal disease 2 (IPD2)
[MIM:300640]: Recurrent invasive pneumococcal disease (IPD) is
defined as two episodes of IPD occurring at least 1 month apart,
whether caused by the same or different serotypes or strains.
Recurrent IPD occurs in at least 2% of patients in most series,
making IPD the most important known risk factor for subsequent
IPD. {ECO:0000269|PubMed:16950813}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Incontinentia pigmenti (IP) [MIM:308300]: A
genodermatosis usually prenatally lethal in males. In affected
females, it causes abnormalities of the skin, hair, eyes, nails,
teeth, skeleton, heart, and central nervous system. The prominent
skin signs occur in four classic cutaneous stages: perinatal
inflammatory vesicles, verrucous patches, a distinctive pattern of
hyperpigmentation and dermal scarring.
{ECO:0000269|PubMed:10839543, ECO:0000269|PubMed:11590134,
ECO:0000269|PubMed:15229184, ECO:0000269|PubMed:17728323,
ECO:0000269|PubMed:19033441, ECO:0000269|PubMed:20434027,
ECO:0000269|PubMed:24339369}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- WEB RESOURCE: Name=IKBKGbase; Note=IKBKG mutation db;
URL="http://structure.bmc.lu.se/idbase/IKBKGbase/";
-!- WEB RESOURCE: Name=Inhibitor of kappa light polypeptide gene
enhancer in B-cells, kinase gamma (IKBKG); Note=Leiden Open
Variation Database (LOVD);
URL="http://databases.lovd.nl/shared/genes/IKBKG";
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EMBL; AF062089; AAD12183.1; -; mRNA.
EMBL; AF091453; AAD38081.1; -; mRNA.
EMBL; AF074382; AAC36330.1; -; mRNA.
EMBL; AJ271718; CAB93146.1; -; Genomic_DNA.
EMBL; AF261086; AAF99679.1; -; mRNA.
EMBL; AY114157; AAM44073.1; -; mRNA.
EMBL; AK000593; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BT019621; AAV38427.1; -; mRNA.
EMBL; AF277315; AAL27012.1; -; Genomic_DNA.
EMBL; BC000299; AAH00299.1; -; mRNA.
EMBL; BC012114; AAH12114.1; -; mRNA.
EMBL; BC046922; AAH46922.1; -; mRNA.
EMBL; BC050612; AAH50612.1; -; mRNA.
CCDS; CCDS14757.1; -. [Q9Y6K9-1]
CCDS; CCDS48196.1; -. [Q9Y6K9-2]
CCDS; CCDS48197.1; -. [Q9Y6K9-3]
RefSeq; NP_001093326.2; NM_001099856.4. [Q9Y6K9-2]
RefSeq; NP_001093327.1; NM_001099857.2. [Q9Y6K9-1]
RefSeq; NP_001138727.1; NM_001145255.2. [Q9Y6K9-3]
RefSeq; NP_001308325.1; NM_001321396.1. [Q9Y6K9-1]
RefSeq; NP_001308326.1; NM_001321397.1.
RefSeq; NP_003630.1; NM_003639.4. [Q9Y6K9-1]
UniGene; Hs.43505; -.
PDB; 2JVX; NMR; -; A=394-419.
PDB; 2JVY; NMR; -; A=394-419.
PDB; 3BRT; X-ray; 2.25 A; B/D=44-111.
PDB; 3BRV; X-ray; 2.20 A; B/D=44-111.
PDB; 3CL3; X-ray; 3.20 A; D/E=150-272.
PDB; 3FX0; X-ray; 3.20 A; A/B=246-337.
PDB; 4BWN; X-ray; 2.27 A; A/B=258-344.
PDB; 5AAY; NMR; -; A=392-419.
PDBsum; 2JVX; -.
PDBsum; 2JVY; -.
PDBsum; 3BRT; -.
PDBsum; 3BRV; -.
PDBsum; 3CL3; -.
PDBsum; 3FX0; -.
PDBsum; 4BWN; -.
PDBsum; 5AAY; -.
ProteinModelPortal; Q9Y6K9; -.
SMR; Q9Y6K9; -.
BioGrid; 114089; 324.
CORUM; Q9Y6K9; -.
DIP; DIP-27528N; -.
IntAct; Q9Y6K9; 196.
MINT; MINT-128245; -.
STRING; 9606.ENSP00000358622; -.
BindingDB; Q9Y6K9; -.
ChEMBL; CHEMBL4967; -.
DrugBank; DB04998; AGRO100.
DrugBank; DB05289; MPC-7869.
iPTMnet; Q9Y6K9; -.
PhosphoSitePlus; Q9Y6K9; -.
DMDM; 6685695; -.
EPD; Q9Y6K9; -.
PaxDb; Q9Y6K9; -.
PeptideAtlas; Q9Y6K9; -.
PRIDE; Q9Y6K9; -.
DNASU; 8517; -.
Ensembl; ENST00000594239; ENSP00000471166; ENSG00000269335. [Q9Y6K9-1]
Ensembl; ENST00000611071; ENSP00000479662; ENSG00000269335. [Q9Y6K9-1]
Ensembl; ENST00000611176; ENSP00000478616; ENSG00000269335. [Q9Y6K9-3]
Ensembl; ENST00000618670; ENSP00000483825; ENSG00000269335. [Q9Y6K9-2]
GeneID; 8517; -.
KEGG; hsa:8517; -.
UCSC; uc033fbu.1; human. [Q9Y6K9-1]
CTD; 8517; -.
DisGeNET; 8517; -.
EuPathDB; HostDB:ENSG00000269335.5; -.
GeneCards; IKBKG; -.
GeneReviews; IKBKG; -.
H-InvDB; HIX0203333; -.
HGNC; HGNC:5961; IKBKG.
HPA; CAB010373; -.
HPA; HPA000426; -.
MalaCards; IKBKG; -.
MIM; 300248; gene.
MIM; 300291; phenotype.
MIM; 300301; phenotype.
MIM; 300584; phenotype.
MIM; 300636; phenotype.
MIM; 300640; phenotype.
MIM; 308300; phenotype.
neXtProt; NX_Q9Y6K9; -.
OpenTargets; ENSG00000269335; -.
Orphanet; 69088; Anhidrotic ectodermal dysplasia - immunodeficiency - osteopetrosis - lymphedema.
Orphanet; 98813; Hypohidrotic ectodermal dysplasia with immunodeficiency.
Orphanet; 464; Incontinentia pigmenti.
Orphanet; 319612; X-linked mendelian susceptibility to mycobacterial diseases due to IKBKG deficiency.
PharmGKB; PA29777; -.
eggNOG; ENOG410IJBJ; Eukaryota.
eggNOG; ENOG410Y1FG; LUCA.
GeneTree; ENSGT00530000063808; -.
HOGENOM; HOG000293233; -.
HOVERGEN; HBG000417; -.
InParanoid; Q9Y6K9; -.
KO; K07210; -.
OMA; EFLMQKF; -.
OrthoDB; EOG091G0576; -.
PhylomeDB; Q9Y6K9; -.
TreeFam; TF326608; -.
Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
Reactome; R-HSA-168927; TICAM1, RIP1-mediated IKK complex recruitment.
Reactome; R-HSA-1810476; RIP-mediated NFkB activation via ZBP1.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-HSA-446652; Interleukin-1 family signaling.
Reactome; R-HSA-450302; activated TAK1 mediates p38 MAPK activation.
Reactome; R-HSA-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
Reactome; R-HSA-5357905; Regulation of TNFR1 signaling.
Reactome; R-HSA-5357956; TNFR1-induced NFkappaB signaling pathway.
Reactome; R-HSA-5602636; IKBKB deficiency causes SCID.
Reactome; R-HSA-5603027; IKBKG deficiency causes anhidrotic ectodermal dysplasia with immunodeficiency (EDA-ID) (via TLR).
Reactome; R-HSA-5603029; IkBA variant leads to EDA-ID.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
Reactome; R-HSA-933542; TRAF6 mediated NF-kB activation.
Reactome; R-HSA-933543; NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
Reactome; R-HSA-937039; IRAK1 recruits IKK complex.
Reactome; R-HSA-937041; IKK complex recruitment mediated by RIP1.
Reactome; R-HSA-975144; IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
SABIO-RK; Q9Y6K9; -.
SIGNOR; Q9Y6K9; -.
ChiTaRS; IKBKG; human.
EvolutionaryTrace; Q9Y6K9; -.
GeneWiki; IKBKG; -.
GenomeRNAi; 8517; -.
PRO; PR:Q9Y6K9; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000269335; -.
CleanEx; HS_IKBKG; -.
ExpressionAtlas; Q9Y6K9; baseline and differential.
Genevisible; Q9Y6K9; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0008385; C:IkappaB kinase complex; IDA:MGI.
GO; GO:0005622; C:intracellular; IDA:LIFEdb.
GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
GO; GO:0000151; C:ubiquitin ligase complex; IPI:ParkinsonsUK-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IBA:GO_Central.
GO; GO:1990450; F:linear polyubiquitin binding; IDA:ParkinsonsUK-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042975; F:peroxisome proliferator activated receptor binding; IEA:Ensembl.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0004871; F:signal transducer activity; TAS:ProtInc.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0000187; P:activation of MAPK activity; TAS:Reactome.
GO; GO:0043276; P:anoikis; ISS:BHF-UCL.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0051650; P:establishment of vesicle localization; IMP:UniProtKB.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; TAS:UniProtKB.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0006954; P:inflammatory response; TAS:UniProtKB.
GO; GO:0045087; P:innate immune response; TAS:UniProtKB.
GO; GO:0007254; P:JNK cascade; TAS:Reactome.
GO; GO:1901215; P:negative regulation of neuron death; TAS:ParkinsonsUK-UCL.
GO; GO:0070423; P:nucleotide-binding oligomerization domain containing signaling pathway; TAS:Reactome.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:MGI.
GO; GO:0016239; P:positive regulation of macroautophagy; ISS:BHF-UCL.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0010803; P:regulation of tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
GO; GO:0009615; P:response to virus; TAS:UniProtKB.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0051403; P:stress-activated MAPK cascade; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0016032; P:viral process; 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; Alternative splicing; Coiled coil; Complete proteome;
Cytoplasm; Direct protein sequencing; Disease mutation;
Disulfide bond; DNA damage; Ectodermal dysplasia;
Host-virus interaction; Isopeptide bond; Metal-binding; Nucleus;
Osteopetrosis; Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 419 NF-kappa-B essential modulator.
/FTId=PRO_0000096782.
ZN_FING 389 419 CCHC NOA-type. {ECO:0000255|PROSITE-
ProRule:PRU01142}.
REGION 44 111 Interaction with CHUK/IKBKB.
REGION 150 257 Interaction with TANK.
REGION 242 350 Ubiquitin-binding (UBD).
REGION 246 365 Self-association.
REGION 251 419 Required for interaction with TNFAIP3.
REGION 322 343 Leucine-zipper. {ECO:0000255}.
REGION 382 419 Interaction with CYLD.
{ECO:0000269|PubMed:12917691}.
COILED 49 356 {ECO:0000255}.
MOD_RES 31 31 Phosphoserine; by IKKB.
{ECO:0000269|PubMed:12657630}.
MOD_RES 43 43 Phosphoserine; by IKKB.
{ECO:0000269|PubMed:12657630}.
MOD_RES 68 68 Phosphoserine.
{ECO:0000269|PubMed:17977820}.
MOD_RES 85 85 Phosphoserine; by ATM.
{ECO:0000269|PubMed:16497931}.
MOD_RES 376 376 Phosphoserine; by IKKB.
{ECO:0000269|PubMed:12657630}.
MOD_RES 387 387 Phosphoserine.
{ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:24012789}.
DISULFID 54 54 Interchain.
{ECO:0000269|PubMed:18164680}.
DISULFID 347 347 Interchain.
{ECO:0000269|PubMed:18164680}.
CROSSLNK 111 111 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:21455181}.
CROSSLNK 139 139 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:21455181}.
CROSSLNK 143 143 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:21455181}.
CROSSLNK 226 226 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:21455181}.
CROSSLNK 246 246 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:21455181}.
CROSSLNK 264 264 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:21455181}.
CROSSLNK 277 277 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000269|PubMed:14651848}.
CROSSLNK 277 277 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate. {ECO:0000269|PubMed:14651848,
ECO:0000269|PubMed:21455181}.
CROSSLNK 283 283 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:21455181}.
CROSSLNK 285 285 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:15620648,
ECO:0000269|PubMed:19136968,
ECO:0000269|PubMed:21455181}.
CROSSLNK 292 292 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:21455181}.
CROSSLNK 302 302 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:21455181}.
CROSSLNK 309 309 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000269|PubMed:14651848}.
CROSSLNK 309 309 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate. {ECO:0000269|PubMed:14651848,
ECO:0000269|PubMed:19136968,
ECO:0000269|PubMed:20010814,
ECO:0000269|PubMed:21455181}.
CROSSLNK 321 321 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:20010814}.
CROSSLNK 325 325 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:O88522}.
CROSSLNK 326 326 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:21455181}.
CROSSLNK 399 399 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:14695475}.
VAR_SEQ 1 1 M -> MALVIQVGKLRPREVRTPQTINPSLFPSLPVKLSSI
IEVPSGGERCCSRRTLVYKARAFWKGAPLPCWM (in
isoform 2). {ECO:0000303|Ref.6}.
/FTId=VSP_041000.
VAR_SEQ 174 224 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041001.
VAR_SEQ 257 304 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041002.
VARIANT 57 57 E -> K (in IP; shows the same luciferase
activity as the control;
dbSNP:rs148695964).
{ECO:0000269|PubMed:11590134,
ECO:0000269|PubMed:15229184}.
/FTId=VAR_026491.
VARIANT 90 90 Missing (in IP; only 46.3% of the
activation obtained with the wild-type
protein). {ECO:0000269|PubMed:15229184}.
/FTId=VAR_026492.
VARIANT 113 113 D -> N (in dbSNP:rs179363896).
{ECO:0000269|PubMed:15229184}.
/FTId=VAR_026493.
VARIANT 123 123 R -> W (in IP; shows the same luciferase
activity as the control;
dbSNP:rs179363895).
{ECO:0000269|PubMed:15229184}.
/FTId=VAR_026494.
VARIANT 153 153 L -> R (in EDAID; dbSNP:rs137853328).
{ECO:0000269|PubMed:12045264,
ECO:0000269|PubMed:15100680}.
/FTId=VAR_026495.
VARIANT 170 170 L -> P (in IP).
{ECO:0000269|PubMed:24339369}.
/FTId=VAR_072603.
VARIANT 173 173 R -> G (in IPD2; dbSNP:rs179363866).
{ECO:0000269|PubMed:16950813}.
/FTId=VAR_031958.
VARIANT 173 173 R -> Q (in IP).
{ECO:0000269|PubMed:24339369}.
/FTId=VAR_072604.
VARIANT 175 175 R -> P (in EDAID; dbSNP:rs179363868).
{ECO:0000269|PubMed:11242109}.
/FTId=VAR_011320.
VARIANT 183 183 Q -> H (in IP).
{ECO:0000269|PubMed:20434027}.
/FTId=VAR_072605.
VARIANT 227 227 L -> P (in EDAID; dbSNP:rs179363869).
{ECO:0000269|PubMed:11242109}.
/FTId=VAR_011321.
VARIANT 288 288 A -> G (in EDAID; dbSNP:rs137853330).
{ECO:0000269|PubMed:11242109}.
/FTId=VAR_011322.
VARIANT 311 311 D -> N (in EDAID; abolishes binding to
polyubiquitin ('K63'-linked and linear)
and greatly impairs tandem ubiquitin
binding; dbSNP:rs179363867).
{ECO:0000269|PubMed:11242109,
ECO:0000269|PubMed:16547522,
ECO:0000269|PubMed:19185524,
ECO:0000269|PubMed:21606507}.
/FTId=VAR_011323.
VARIANT 314 314 A -> P (in IP).
{ECO:0000269|PubMed:24339369}.
/FTId=VAR_072606.
VARIANT 315 315 E -> A (in IMD33; greatly impairs tandem
ubiquitin binding. Impairs
oligomerization, impairs binding of 'Lys-
63'-linked ubiuitin and linear tetra-
ubiquitin, impairs TNF-induced NF-kappa-B
activation; dbSNP:rs137853331).
{ECO:0000269|PubMed:16818673,
ECO:0000269|PubMed:19185524,
ECO:0000269|PubMed:19854204}.
/FTId=VAR_031959.
VARIANT 319 319 R -> Q (in IMD33; impairs tandem
ubiquitin binding; dbSNP:rs137853332).
{ECO:0000269|PubMed:16818673,
ECO:0000269|PubMed:19185524}.
/FTId=VAR_031960.
VARIANT 322 322 L -> P (in IP).
{ECO:0000269|PubMed:24339369}.
/FTId=VAR_072607.
VARIANT 323 323 A -> P (in IP; diminishes interaction
with TRAF6 and polyubiquitination,
greatly impairs tandem ubiquitin binding.
Impairs oligomerization, greatly impairs
binding of 'Lys-63'-linked ubiuitin and
linear tetra-ubiquitin, impairs TNF-
induced NF-kappa-B activation;
dbSNP:rs179363865).
{ECO:0000269|PubMed:17728323,
ECO:0000269|PubMed:19185524,
ECO:0000269|PubMed:19854204}.
/FTId=VAR_042666.
VARIANT 406 406 D -> V (in EDAID; dbSNP:rs137853327).
{ECO:0000269|PubMed:11224521}.
/FTId=VAR_011324.
VARIANT 407 407 M -> V (in IP; impairs binding to
ubiquitin; dbSNP:rs137853322).
{ECO:0000269|PubMed:10839543,
ECO:0000269|PubMed:11590134,
ECO:0000269|PubMed:19033441}.
/FTId=VAR_009182.
VARIANT 413 413 H -> Y (in IP).
{ECO:0000269|PubMed:24339369}.
/FTId=VAR_072608.
VARIANT 417 417 C -> F (in EDAID; dbSNP:rs137853326).
{ECO:0000269|PubMed:11047757,
ECO:0000269|PubMed:11242109}.
/FTId=VAR_011325.
VARIANT 417 417 C -> R (in EDAID; loss of sumoylation;
dbSNP:rs137853325).
{ECO:0000269|PubMed:11047757,
ECO:0000269|PubMed:11224521,
ECO:0000269|PubMed:11242109,
ECO:0000269|PubMed:12045264,
ECO:0000269|PubMed:14651848,
ECO:0000269|PubMed:15100680}.
/FTId=VAR_011326.
VARIANT 417 417 C -> Y (in NEMOID; dbSNP:rs137853326).
{ECO:0000269|PubMed:15100680}.
/FTId=VAR_026496.
MUTAGEN 68 68 S->A: Increases formation of homodimers.
{ECO:0000269|PubMed:17977820}.
MUTAGEN 68 68 S->E: Abolishes interaction with IKBKB;
abolishes TNF-alpha induced NF-kappa-B
activity. {ECO:0000269|PubMed:17977820}.
MUTAGEN 85 85 S->A: Decreases ubiquitination and
abolishes nuclear export.
{ECO:0000269|PubMed:16497931}.
MUTAGEN 115 115 K->R: No change in the ubiquitination
level; when associated with R-399.
{ECO:0000269|PubMed:15620648}.
MUTAGEN 224 224 K->R: No change in the ubiquitination
level; when associated with R-399.
{ECO:0000269|PubMed:15620648}.
MUTAGEN 277 277 K->A: Partial abolition of sumoylation.
Abolishes sumoylation and IKK activation;
when associated with A-309.
{ECO:0000269|PubMed:14651848}.
MUTAGEN 285 285 K->R: Important decrease in the
ubiquitination level; when associated
with R-399.
{ECO:0000269|PubMed:15620648}.
MUTAGEN 296 296 E->A: No effet on oligomerization,impairs
binding of 'Lys-63'-linked ubiuitin and
linear tetra-ubiquitin, impairs TNF-
induced NF-kappa-B activation.
{ECO:0000269|PubMed:19854204}.
MUTAGEN 300 300 V->D: Greatly impairs tandem ubiquitin
binding. {ECO:0000269|PubMed:19185524}.
MUTAGEN 301 301 L->A: Impairs tandem ubiquitin binding.
{ECO:0000269|PubMed:19185524}.
MUTAGEN 304 304 Q->A: Impairs tandem ubiquitin binding.
{ECO:0000269|PubMed:19185524}.
MUTAGEN 307 307 I->N: Greatly impairs tandem ubiquitin
binding. {ECO:0000269|PubMed:19185524}.
MUTAGEN 308 308 Y->A: Greatly impairs tandem ubiquitin
binding. {ECO:0000269|PubMed:19185524}.
MUTAGEN 309 309 K->A: Partial abolition of sumoylation.
Abolishes sumoylation and IKK activation;
when associated with A-277.
{ECO:0000269|PubMed:14651848}.
MUTAGEN 312 312 F->A: Greatly impairs tandem ubiquitin
binding,impairs oligomerization, impairs
TNF-induced NF-kappa-B activation.
{ECO:0000269|PubMed:19185524,
ECO:0000269|PubMed:19854204}.
MUTAGEN 312 312 F->W: MNo effet on oligomerization,
preferentially binds tri-ubiquitin chains
('Lys-48' or 'Lys-63'-linked).
{ECO:0000269|PubMed:19185524,
ECO:0000269|PubMed:19854204}.
MUTAGEN 312 312 F->Y: Impairs tandem ubiquitin binding.
{ECO:0000269|PubMed:19185524,
ECO:0000269|PubMed:19854204}.
MUTAGEN 313 313 Q->A: Impairs tandem ubiquitin binding.
{ECO:0000269|PubMed:19185524}.
MUTAGEN 315 315 E->Q: Greatly impairs tandem ubiquitin
binding. {ECO:0000269|PubMed:19854204}.
MUTAGEN 317 317 Q->A,W: Greatly impairs tandem ubiquitin
binding. {ECO:0000269|PubMed:19185524}.
MUTAGEN 323 323 A->D: Greatly impairs tandem ubiquitin
binding. {ECO:0000269|PubMed:19854204}.
MUTAGEN 329 329 L->A: Impairs oligomerization, impairs
binding of 'Lys-63'-linked ubiuitin,
impairs TNF-induced NF-kappa-B
activation; when associated with A-336.
{ECO:0000269|PubMed:16547522,
ECO:0000269|PubMed:19854204}.
MUTAGEN 329 329 L->P: Abolishes binding to polyubiquitin.
{ECO:0000269|PubMed:16547522,
ECO:0000269|PubMed:19854204}.
MUTAGEN 336 336 L->A: Impairs oligomerization, impairs
binding of 'Lys-63'-linked ubiuitin,
impairs TNF-induced NF-kappa-B
activation; when associated with A-329.
{ECO:0000269|PubMed:19854204}.
MUTAGEN 399 399 K->R: Abolishes BCL10-mediated but not
RIPK2-mediated ubiquitination. Important
decrease in the ubiquitination level;
when associated with R-285. No change in
the ubiquitination level; when associated
with R-115 or R-224.
{ECO:0000269|PubMed:14695475,
ECO:0000269|PubMed:15620648}.
MUTAGEN 414 414 V->S: Abolishes binding to polyubiquitin.
{ECO:0000269|PubMed:19033441}.
MUTAGEN 415 415 M->S: Impairs binding to polyubiquitin.
{ECO:0000269|PubMed:19033441}.
CONFLICT 341 341 S -> R (in Ref. 1; AAD12183).
{ECO:0000305}.
CONFLICT 387 387 S -> R (in Ref. 1; AAD12183).
{ECO:0000305}.
HELIX 50 108 {ECO:0000244|PDB:3BRV}.
TURN 194 196 {ECO:0000244|PDB:3CL3}.
HELIX 197 249 {ECO:0000244|PDB:3CL3}.
HELIX 260 268 {ECO:0000244|PDB:4BWN}.
HELIX 271 295 {ECO:0000244|PDB:4BWN}.
HELIX 297 341 {ECO:0000244|PDB:4BWN}.
STRAND 394 396 {ECO:0000244|PDB:2JVY}.
TURN 398 400 {ECO:0000244|PDB:5AAY}.
STRAND 403 406 {ECO:0000244|PDB:2JVX}.
HELIX 407 416 {ECO:0000244|PDB:2JVX}.
SEQUENCE 419 AA; 48198 MW; 322D1037881447FF CRC64;
MNRHLWKSQL CEMVQPSGGP AADQDVLGEE SPLGKPAMLH LPSEQGAPET LQRCLEENQE
LRDAIRQSNQ ILRERCEELL HFQASQREEK EFLMCKFQEA RKLVERLGLE KLDLKRQKEQ
ALREVEHLKR CQQQMAEDKA SVKAQVTSLL GELQESQSRL EAATKECQAL EGRARAASEQ
ARQLESEREA LQQQHSVQVD QLRMQGQSVE AALRMERQAA SEEKRKLAQL QVAYHQLFQE
YDNHIKSSVV GSERKRGMQL EDLKQQLQQA EEALVAKQEV IDKLKEEAEQ HKIVMETVPV
LKAQADIYKA DFQAERQARE KLAEKKELLQ EQLEQLQREY SKLKASCQES ARIEDMRKRH
VEVSQAPLPP APAYLSSPLA LPSQRRSPPE EPPDFCCPKC QYQAPDMDTL QIHVMECIE


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