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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.
17-JUN-2020, entry version 223.
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=10.1159/000025378;
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 (MICROBIAL INFECTION).
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 (MICROBIAL INFECTION).
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 EDAID1 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 PIDD1.
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
EDAID1 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 OF PUBMED:16547522.
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 (MICROBIAL INFECTION), 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 EDAID1 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]
INTERACTION WITH ARFIP2.
PubMed=26296658; DOI=10.1016/j.cellsig.2015.08.012;
You D.J., Park C.R., Furlong M., Koo O., Lee C., Ahn C., Seong J.Y.,
Hwang J.I.;
"Dimer of arfaptin 2 regulates NF-kappaB signaling by interacting with
IKKbeta/NEMO and inhibiting IKKbeta kinase activity.";
Cell. Signal. 27:2173-2181(2015).
[59]
INTERACTION WITH MOLLUSCUM CONTAGIOSUM VIRUS PROTEIN MC005 (MICROBIAL
INFECTION).
PubMed=28490597; DOI=10.1128/jvi.00545-17;
Brady G., Haas D.A., Farrell P.J., Pichlmair A., Bowie A.G.;
"Molluscum contagiosum virus protein MC005 inhibits NF-kappaB activation by
targeting NEMO-regulated IkappaB kinase activation.";
J. Virol. 91:0-0(2017).
[60]
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).
[61]
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).
[62]
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 EDAID1 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).
[63]
VARIANTS EDAID1 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).
[64]
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).
[65]
INVOLVEMENT IN OLEDAID, INVOLVEMENT IN EDAID1, AND VARIANTS EDAID1 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).
[66]
VARIANTS EDAID1 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).
[67]
VARIANTS EDAID1 ARG-153 AND ARG-417.
PubMed=12045264; DOI=10.1172/jci14858;
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).
[68]
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).
[69]
VARIANTS EDAID1 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).
[70]
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).
[71]
INTERACTION WITH TRIM13.
PubMed=25152375; DOI=10.1016/j.cellsig.2014.08.008;
Tomar D., Singh R.;
"TRIM13 regulates ubiquitination and turnover of NEMO to suppress TNF
induced NF-kappaB activation.";
Cell. Signal. 26:2606-2613(2014).
[72]
CLEAVAGE BY HAV PROTEASE 3C (MICROBIAL INFECTION), CLEAVAGE SITES, AND
MUTAGENESIS OF GLN-304.
PubMed=24920812; DOI=10.1128/jvi.00869-14;
Wang D., Fang L., Wei D., Zhang H., Luo R., Chen H., Li K., Xiao S.;
"Hepatitis A virus 3C protease cleaves NEMO to impair induction of beta
interferon.";
J. Virol. 88:10252-10258(2014).
[73]
INTERACTION WITH TRIM29.
PubMed=27695001; DOI=10.1038/ni.3580;
Xing J., Weng L., Yuan B., Wang Z., Jia L., Jin R., Lu H., Li X.C.,
Liu Y.J., Zhang Z.;
"Identification of a role for TRIM29 in the control of innate immunity in
the respiratory tract.";
Nat. Immunol. 17:1373-1380(2016).
[74]
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).
[75]
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).
[76]
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).
[77]
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).
[78]
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 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 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 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). Interacts with TRIM29;
this interaction induces IKBKG/NEMO ubiquitination and proteolytic
degradation (PubMed:27695001). Interacts with TRIM13; this interaction
leads to IKBKG/NEMO ubiquitination (PubMed:25152375). Interacts with
ARFIP2 (PubMed:26296658). Interacts with RIPK1 (By similarity).
{ECO:0000250|UniProtKB:O88522, 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:22099304, ECO:0000269|PubMed:22672233,
ECO:0000269|PubMed:23453969, ECO:0000269|PubMed:25861989,
ECO:0000269|PubMed:26296658, ECO:0000269|PubMed:26334375,
ECO:0000269|PubMed:27695001}.
-!- SUBUNIT: (Microbial infection) Interacts with Molluscum contagiosum
virus protein MC005; this interaction inhibits NF-kappa-B activation.
{ECO:0000269|PubMed:28490597}.
-!- SUBUNIT: (Microbial infection) Interacts with HTLV-1 Tax oncoprotein;
the interaction activates IKBKG. {ECO:0000269|PubMed:10364167,
ECO:0000269|PubMed:11064457}.
-!- SUBUNIT: (Microbial infection) 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. {ECO:0000269|PubMed:20010814}.
-!- INTERACTION:
Q9Y6K9; Q9NPF8: ADAP2; NbExp=2; IntAct=EBI-81279, EBI-718895;
Q9Y6K9; Q4VCS5: AMOT; NbExp=3; IntAct=EBI-81279, EBI-2511319;
Q9Y6K9; P04083: ANXA1; NbExp=6; IntAct=EBI-81279, EBI-354007;
Q9Y6K9; Q66PJ3: ARL6IP4; NbExp=2; IntAct=EBI-81279, EBI-2683099;
Q9Y6K9; Q13315: ATM; NbExp=4; IntAct=EBI-81279, EBI-495465;
Q9Y6K9; Q13535: ATR; NbExp=2; IntAct=EBI-81279, EBI-968983;
Q9Y6K9; O95999: BCL10; NbExp=7; IntAct=EBI-81279, EBI-958922;
Q9Y6K9; P05937: CALB1; NbExp=3; IntAct=EBI-81279, EBI-4286943;
Q9Y6K9; Q16543: CDC37; NbExp=6; IntAct=EBI-81279, EBI-295634;
Q9Y6K9; P24941: CDK2; NbExp=4; IntAct=EBI-81279, EBI-375096;
Q9Y6K9; O15111: CHUK; NbExp=25; IntAct=EBI-81279, EBI-81249;
Q9Y6K9; Q9UNS2: COPS3; NbExp=2; IntAct=EBI-81279, EBI-350590;
Q9Y6K9; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-81279, EBI-5453285;
Q9Y6K9; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-81279, EBI-744099;
Q9Y6K9; P36888: FLT3; NbExp=2; IntAct=EBI-81279, EBI-3946257;
Q9Y6K9; Q14161: GIT2; NbExp=6; IntAct=EBI-81279, EBI-1046878;
Q9Y6K9; Q92917: GPKOW; NbExp=3; IntAct=EBI-81279, EBI-746309;
Q9Y6K9; Q7Z4H3: HDDC2; NbExp=3; IntAct=EBI-81279, EBI-6163836;
Q9Y6K9; P07900: HSP90AA1; NbExp=3; IntAct=EBI-81279, EBI-296047;
Q9Y6K9; P08238: HSP90AB1; NbExp=3; IntAct=EBI-81279, EBI-352572;
Q9Y6K9; O14920: IKBKB; NbExp=35; IntAct=EBI-81279, EBI-81266;
Q9Y6K9; Q9Y6K9: IKBKG; NbExp=7; IntAct=EBI-81279, EBI-81279;
Q9Y6K9; P05783: KRT18; NbExp=3; IntAct=EBI-81279, EBI-297888;
Q9Y6K9; P05787: KRT8; NbExp=2; IntAct=EBI-81279, EBI-297852;
Q9Y6K9; Q96PV6: LENG8; NbExp=3; IntAct=EBI-81279, EBI-739546;
Q9Y6K9; Q9UDY8: MALT1; NbExp=4; IntAct=EBI-81279, EBI-1047372;
Q9Y6K9; Q99558: MAP3K14; NbExp=3; IntAct=EBI-81279, EBI-358011;
Q9Y6K9; P01106: MYC; NbExp=3; IntAct=EBI-81279, EBI-447544;
Q9Y6K9; P25963: NFKBIA; NbExp=6; IntAct=EBI-81279, EBI-307386;
Q9Y6K9; Q9UJX0: OSGIN1; NbExp=3; IntAct=EBI-81279, EBI-9057006;
Q9Y6K9; P67775: PPP2CA; NbExp=4; IntAct=EBI-81279, EBI-712311;
Q9Y6K9; Q99633: PRPF18; NbExp=3; IntAct=EBI-81279, EBI-2798416;
Q9Y6K9; P28074: PSMB5; NbExp=3; IntAct=EBI-81279, EBI-357828;
Q9Y6K9; Q9BYM8: RBCK1; NbExp=9; IntAct=EBI-81279, EBI-2340624;
Q9Y6K9; Q13546: RIPK1; NbExp=8; IntAct=EBI-81279, EBI-358507;
Q9Y6K9; Q96EP0: RNF31; NbExp=10; IntAct=EBI-81279, EBI-948111;
Q9Y6K9; Q9UBF6: RNF7; NbExp=3; IntAct=EBI-81279, EBI-398632;
Q9Y6K9; Q9BVN2-2: RUSC1; NbExp=4; IntAct=EBI-81279, EBI-6257338;
Q9Y6K9; Q9HC62: SENP2; NbExp=3; IntAct=EBI-81279, EBI-714881;
Q9Y6K9; Q9H0F6: SHARPIN; NbExp=14; IntAct=EBI-81279, EBI-3942966;
Q9Y6K9; O95391: SLU7; NbExp=3; IntAct=EBI-81279, EBI-750559;
Q9Y6K9; Q13573: SNW1; NbExp=3; IntAct=EBI-81279, EBI-632715;
Q9Y6K9; Q13501: SQSTM1; NbExp=2; IntAct=EBI-81279, EBI-307104;
Q9Y6K9; P12931: SRC; NbExp=3; IntAct=EBI-81279, EBI-621482;
Q9Y6K9; P63165: SUMO1; NbExp=3; IntAct=EBI-81279, EBI-80140;
Q9Y6K9; P21579: SYT1; NbExp=3; IntAct=EBI-81279, EBI-524909;
Q9Y6K9; Q92844: TANK; NbExp=5; IntAct=EBI-81279, EBI-356349;
Q9Y6K9; Q9UHD2: TBK1; NbExp=4; IntAct=EBI-81279, EBI-356402;
Q9Y6K9; P01375: TNF; NbExp=3; IntAct=EBI-81279, EBI-359977;
Q9Y6K9; P21580: TNFAIP3; NbExp=5; IntAct=EBI-81279, EBI-527670;
Q9Y6K9; Q15025: TNIP1; NbExp=6; IntAct=EBI-81279, EBI-357849;
Q9Y6K9; Q8NFZ5: TNIP2; NbExp=8; IntAct=EBI-81279, EBI-359372;
Q9Y6K9; P0CG48: UBC; NbExp=4; IntAct=EBI-81279, EBI-3390054;
Q9Y6K9; Q9Y2X8: UBE2D4; NbExp=3; IntAct=EBI-81279, EBI-745527;
Q9Y6K9; Q5D1E8: ZC3H12A; NbExp=2; IntAct=EBI-81279, EBI-747793;
Q9Y6K9; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-81279, EBI-6427977;
Q9Y6K9; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-81279, EBI-5667516;
Q9Y6K9; Q8VSC3: ipaH9.8; Xeno; NbExp=8; IntAct=EBI-81279, EBI-6125799;
-!- 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. Deubiquitinated by USP10 in a TANK-dependent and
-independent manner, leading to the negative regulation of NF-kappa-B
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}.
-!- PTM: (Microbial infection) Cleaved by hepatitis A virus (HAV) protease
3C allowing the virus to disrupt the host innate immune signaling.
{ECO:0000269|PubMed:24920812}.
-!- PTM: (Microbial infection) 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.
{ECO:0000269|PubMed:20010814}.
-!- DISEASE: Ectodermal dysplasia and immunodeficiency 1 (EDAID1)
[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]: An 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]
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.
PDB; 5LDE; X-ray; 3.38 A; R/S=230-249.
PDB; 6MI3; X-ray; 1.78 A; A/B=38-129.
PDB; 6MI4; X-ray; 2.50 A; A/B=38-129.
PDBsum; 2JVX; -.
PDBsum; 2JVY; -.
PDBsum; 3BRT; -.
PDBsum; 3BRV; -.
PDBsum; 3CL3; -.
PDBsum; 3FX0; -.
PDBsum; 4BWN; -.
PDBsum; 5AAY; -.
PDBsum; 5LDE; -.
PDBsum; 6MI3; -.
PDBsum; 6MI4; -.
SMR; Q9Y6K9; -.
BioGRID; 114089; 379.
ComplexPortal; CPX-3269; IkappaB kinase complex.
CORUM; Q9Y6K9; -.
DIP; DIP-27528N; -.
IntAct; Q9Y6K9; 242.
MINT; Q9Y6K9; -.
STRING; 9606.ENSP00000483825; -.
BindingDB; Q9Y6K9; -.
ChEMBL; CHEMBL4967; -.
DrugBank; DB04998; AGRO100.
DrugBank; DB05289; Tarenflurbil.
MoonDB; Q9Y6K9; Predicted.
iPTMnet; Q9Y6K9; -.
PhosphoSitePlus; Q9Y6K9; -.
BioMuta; IKBKG; -.
DMDM; 6685695; -.
CPTAC; CPTAC-1044; -.
CPTAC; CPTAC-806; -.
EPD; Q9Y6K9; -.
jPOST; Q9Y6K9; -.
MassIVE; Q9Y6K9; -.
PaxDb; Q9Y6K9; -.
PeptideAtlas; Q9Y6K9; -.
PRIDE; Q9Y6K9; -.
ProteomicsDB; 86716; -. [Q9Y6K9-1]
ProteomicsDB; 86717; -. [Q9Y6K9-2]
ProteomicsDB; 86718; -. [Q9Y6K9-3]
Antibodypedia; 73338; 1206 antibodies.
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; -.
HGNC; HGNC:5961; IKBKG.
HPA; ENSG00000269335; Tissue enhanced (blood).
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 syndrome.
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; -.
InParanoid; Q9Y6K9; -.
KO; K07210; -.
OMA; AHPSFHL; -.
OrthoDB; 745047at2759; -.
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-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-4755510; SUMOylation of immune response proteins.
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-9020702; Interleukin-1 signaling.
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; -.
BioGRID-ORCS; 8517; 36 hits in 417 CRISPR screens.
ChiTaRS; IKBKG; human.
EvolutionaryTrace; Q9Y6K9; -.
GeneWiki; IKBKG; -.
GenomeRNAi; 8517; -.
Pharos; Q9Y6K9; Tbio.
PRO; PR:Q9Y6K9; -.
Proteomes; UP000005640; Chromosome X.
RNAct; Q9Y6K9; protein.
Bgee; ENSG00000269335; Expressed in blood and 89 other tissues.
ExpressionAtlas; Q9Y6K9; baseline and differential.
Genevisible; Q9Y6K9; HS.
GO; GO:0005623; C:cell; IEA:GOC.
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:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; 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:0044877; F:protein-containing complex binding; IEA:Ensembl.
GO; GO:1990459; F:transferrin receptor binding; IPI:ARUK-UCL.
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:0070498; P:interleukin-1-mediated signaling pathway; TAS:Reactome.
GO; GO:0007254; P:JNK cascade; TAS:Reactome.
GO; GO:0002756; P:MyD88-independent toll-like receptor signaling pathway; 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 by RNA polymerase II; IDA:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0065003; P:protein-containing complex assembly; IDA:UniProtKB.
GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
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:Reactome.
GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DisProt; DP02269; -.
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; 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
/note="NF-kappa-B essential modulator"
/id="PRO_0000096782"
ZN_FING 389..419
/note="CCHC NOA-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01142"
REGION 44..111
/note="Interaction with CHUK/IKBKB"
REGION 150..257
/note="Interaction with TANK"
REGION 242..350
/note="Ubiquitin-binding (UBD)"
REGION 246..365
/note="Self-association"
REGION 251..419
/note="Required for interaction with TNFAIP3"
REGION 322..343
/note="Leucine-zipper"
/evidence="ECO:0000255"
REGION 382..419
/note="Interaction with CYLD"
/evidence="ECO:0000269|PubMed:12917691"
COILED 49..356
/evidence="ECO:0000255"
MOD_RES 31
/note="Phosphoserine; by IKKB"
/evidence="ECO:0000269|PubMed:12657630"
MOD_RES 43
/note="Phosphoserine; by IKKB"
/evidence="ECO:0000269|PubMed:12657630"
MOD_RES 68
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:17977820"
MOD_RES 85
/note="Phosphoserine; by ATM"
/evidence="ECO:0000269|PubMed:16497931"
MOD_RES 376
/note="Phosphoserine; by IKKB"
/evidence="ECO:0000269|PubMed:12657630"
MOD_RES 387
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:24012789"
DISULFID 54
/note="Interchain"
/evidence="ECO:0000269|PubMed:18164680"
DISULFID 347
/note="Interchain"
/evidence="ECO:0000269|PubMed:18164680"
CROSSLNK 111
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000269|PubMed:21455181"
CROSSLNK 139
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000269|PubMed:21455181"
CROSSLNK 143
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000269|PubMed:21455181"
CROSSLNK 226
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000269|PubMed:21455181"
CROSSLNK 246
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000269|PubMed:21455181"
CROSSLNK 264
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000269|PubMed:21455181"
CROSSLNK 277
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO); alternate"
/evidence="ECO:0000269|PubMed:14651848"
CROSSLNK 277
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin); alternate"
/evidence="ECO:0000269|PubMed:14651848,
ECO:0000269|PubMed:21455181"
CROSSLNK 283
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000269|PubMed:21455181"
CROSSLNK 285
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000269|PubMed:15620648,
ECO:0000269|PubMed:19136968, ECO:0000269|PubMed:21455181"
CROSSLNK 292
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000269|PubMed:21455181"
CROSSLNK 302
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000269|PubMed:21455181"
CROSSLNK 309
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO); alternate"
/evidence="ECO:0000269|PubMed:14651848"
CROSSLNK 309
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin); alternate"
/evidence="ECO:0000269|PubMed:14651848,
ECO:0000269|PubMed:19136968, ECO:0000269|PubMed:20010814,
ECO:0000269|PubMed:21455181"
CROSSLNK 321
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000269|PubMed:20010814"
CROSSLNK 325
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000250|UniProtKB:O88522"
CROSSLNK 326
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000269|PubMed:21455181"
CROSSLNK 399
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000269|PubMed:14695475"
VAR_SEQ 1
/note="M -> MALVIQVGKLRPREVRTPQTINPSLFPSLPVKLSSIIEVPSGGERCC
SRRTLVYKARAFWKGAPLPCWM (in isoform 2)"
/evidence="ECO:0000303|Ref.6"
/id="VSP_041000"
VAR_SEQ 174..224
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_041001"
VAR_SEQ 257..304
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_041002"
VARIANT 57
/note="E -> K (in IP; shows the same luciferase activity as
the control; dbSNP:rs148695964)"
/evidence="ECO:0000269|PubMed:11590134,
ECO:0000269|PubMed:15229184"
/id="VAR_026491"
VARIANT 90
/note="Missing (in IP; only 46.3% of the activation
obtained with the wild-type protein)"
/evidence="ECO:0000269|PubMed:15229184"
/id="VAR_026492"
VARIANT 113
/note="D -> N (in dbSNP:rs179363896)"
/evidence="ECO:0000269|PubMed:15229184"
/id="VAR_026493"
VARIANT 123
/note="R -> W (in IP; shows the same luciferase activity as
the control; dbSNP:rs179363895)"
/evidence="ECO:0000269|PubMed:15229184"
/id="VAR_026494"
VARIANT 153
/note="L -> R (in EDAID1; dbSNP:rs137853328)"
/evidence="ECO:0000269|PubMed:12045264,
ECO:0000269|PubMed:15100680"
/id="VAR_026495"
VARIANT 170
/note="L -> P (in IP)"
/evidence="ECO:0000269|PubMed:24339369"
/id="VAR_072603"
VARIANT 173
/note="R -> G (in IPD2; dbSNP:rs179363866)"
/evidence="ECO:0000269|PubMed:16950813"
/id="VAR_031958"
VARIANT 173
/note="R -> Q (in IP; dbSNP:rs1057520292)"
/evidence="ECO:0000269|PubMed:24339369"
/id="VAR_072604"
VARIANT 175
/note="R -> P (in EDAID1; dbSNP:rs179363868)"
/evidence="ECO:0000269|PubMed:11242109"
/id="VAR_011320"
VARIANT 183
/note="Q -> H (in IP; dbSNP:rs1198984417)"
/evidence="ECO:0000269|PubMed:20434027"
/id="VAR_072605"
VARIANT 227
/note="L -> P (in EDAID1; dbSNP:rs179363869)"
/evidence="ECO:0000269|PubMed:11242109"
/id="VAR_011321"
VARIANT 288
/note="A -> G (in EDAID1; dbSNP:rs137853330)"
/evidence="ECO:0000269|PubMed:11242109"
/id="VAR_011322"
VARIANT 311
/note="D -> N (in EDAID1; abolishes binding to
polyubiquitin ('K63'-linked and linear) and greatly impairs
tandem ubiquitin binding; dbSNP:rs179363867)"
/evidence="ECO:0000269|PubMed:11242109,
ECO:0000269|PubMed:16547522, ECO:0000269|PubMed:19185524,
ECO:0000269|PubMed:21606507"
/id="VAR_011323"
VARIANT 314
/note="A -> P (in IP)"
/evidence="ECO:0000269|PubMed:24339369"
/id="VAR_072606"
VARIANT 315
/note="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)"
/evidence="ECO:0000269|PubMed:16818673,
ECO:0000269|PubMed:19185524, ECO:0000269|PubMed:19854204"
/id="VAR_031959"
VARIANT 319
/note="R -> Q (in IMD33; impairs tandem ubiquitin binding;
dbSNP:rs137853332)"
/evidence="ECO:0000269|PubMed:16818673,
ECO:0000269|PubMed:19185524"
/id="VAR_031960"
VARIANT 322
/note="L -> P (in IP)"
/evidence="ECO:0000269|PubMed:24339369"
/id="VAR_072607"
VARIANT 323
/note="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)"
/evidence="ECO:0000269|PubMed:17728323,
ECO:0000269|PubMed:19185524, ECO:0000269|PubMed:19854204"
/id="VAR_042666"
VARIANT 406
/note="D -> V (in EDAID1; dbSNP:rs137853327)"
/evidence="ECO:0000269|PubMed:11224521"
/id="VAR_011324"
VARIANT 407
/note="M -> V (in IP; impairs binding to ubiquitin;
dbSNP:rs137853322)"
/evidence="ECO:0000269|PubMed:10839543,
ECO:0000269|PubMed:11590134, ECO:0000269|PubMed:19033441"
/id="VAR_009182"
VARIANT 413
/note="H -> Y (in IP)"
/evidence="ECO:0000269|PubMed:24339369"
/id="VAR_072608"
VARIANT 417
/note="C -> F (in EDAID1; dbSNP:rs137853326)"
/evidence="ECO:0000269|PubMed:11047757,
ECO:0000269|PubMed:11242109"
/id="VAR_011325"
VARIANT 417
/note="C -> R (in EDAID1; loss of sumoylation;
dbSNP:rs137853325)"
/evidence="ECO:0000269|PubMed:11047757,
ECO:0000269|PubMed:11224521, ECO:0000269|PubMed:11242109,
ECO:0000269|PubMed:12045264, ECO:0000269|PubMed:14651848,
ECO:0000269|PubMed:15100680"
/id="VAR_011326"
VARIANT 417
/note="C -> Y (in NEMOID; dbSNP:rs137853326)"
/evidence="ECO:0000269|PubMed:15100680"
/id="VAR_026496"
MUTAGEN 68
/note="S->A: Increases formation of homodimers."
/evidence="ECO:0000269|PubMed:17977820"
MUTAGEN 68
/note="S->E: Abolishes interaction with IKBKB; abolishes
TNF-alpha induced NF-kappa-B activity."
/evidence="ECO:0000269|PubMed:17977820"
MUTAGEN 85
/note="S->A: Decreases ubiquitination and abolishes nuclear
export."
/evidence="ECO:0000269|PubMed:16497931"
MUTAGEN 115
/note="K->R: No change in the ubiquitination level; when
associated with R-399."
/evidence="ECO:0000269|PubMed:15620648"
MUTAGEN 224
/note="K->R: No change in the ubiquitination level; when
associated with R-399."
/evidence="ECO:0000269|PubMed:15620648"
MUTAGEN 277
/note="K->A: Partial abolition of sumoylation. Abolishes
sumoylation and IKK activation; when associated with A-
309."
/evidence="ECO:0000269|PubMed:14651848"
MUTAGEN 285
/note="K->R: Important decrease in the ubiquitination
level; when associated with R-399."
/evidence="ECO:0000269|PubMed:15620648"
MUTAGEN 296
/note="E->A: No effet on oligomerization,impairs binding of
'Lys-63'-linked ubiuitin and linear tetra-ubiquitin,
impairs TNF-induced NF-kappa-B activation."
/evidence="ECO:0000269|PubMed:19854204"
MUTAGEN 300
/note="V->D: Greatly impairs tandem ubiquitin binding."
/evidence="ECO:0000269|PubMed:19185524"
MUTAGEN 301
/note="L->A: Impairs tandem ubiquitin binding."
/evidence="ECO:0000269|PubMed:19185524"
MUTAGEN 304
/note="Q->A: Complete loss of cleavage by HAV protease 3c."
/evidence="ECO:0000269|PubMed:24920812"
MUTAGEN 304
/note="Q->A: Impairs tandem ubiquitin binding."
/evidence="ECO:0000269|PubMed:19185524"
MUTAGEN 307
/note="I->N: Greatly impairs tandem ubiquitin binding."
/evidence="ECO:0000269|PubMed:19185524"
MUTAGEN 308
/note="Y->A: Greatly impairs tandem ubiquitin binding."
/evidence="ECO:0000269|PubMed:19185524"
MUTAGEN 309
/note="K->A: Partial abolition of sumoylation. Abolishes
sumoylation and IKK activation; when associated with A-
277."
/evidence="ECO:0000269|PubMed:14651848"
MUTAGEN 312
/note="F->A: Greatly impairs tandem ubiquitin
binding,impairs oligomerization, impairs TNF-induced NF-
kappa-B activation."
/evidence="ECO:0000269|PubMed:19185524,
ECO:0000269|PubMed:19854204"
MUTAGEN 312
/note="F->W: MNo effet on oligomerization, preferentially
binds tri-ubiquitin chains ('Lys-48' or 'Lys-63'-linked)."
/evidence="ECO:0000269|PubMed:19185524,
ECO:0000269|PubMed:19854204"
MUTAGEN 312
/note="F->Y: Impairs tandem ubiquitin binding."
/evidence="ECO:0000269|PubMed:19185524,
ECO:0000269|PubMed:19854204"
MUTAGEN 313
/note="Q->A: Impairs tandem ubiquitin binding."
/evidence="ECO:0000269|PubMed:19185524"
MUTAGEN 315
/note="E->Q: Greatly impairs tandem ubiquitin binding."
/evidence="ECO:0000269|PubMed:19854204"
MUTAGEN 317
/note="Q->A,W: Greatly impairs tandem ubiquitin binding."
/evidence="ECO:0000269|PubMed:19185524"
MUTAGEN 323
/note="A->D: Greatly impairs tandem ubiquitin binding."
/evidence="ECO:0000269|PubMed:19854204"
MUTAGEN 329
/note="L->A: Impairs oligomerization, impairs binding of
'Lys-63'-linked ubiuitin, impairs TNF-induced NF-kappa-B
activation; when associated with A-336."
/evidence="ECO:0000269|PubMed:16547522,
ECO:0000269|PubMed:19854204"
MUTAGEN 329
/note="L->P: Abolishes binding to polyubiquitin."
/evidence="ECO:0000269|PubMed:16547522,
ECO:0000269|PubMed:19854204"
MUTAGEN 336
/note="L->A: Impairs oligomerization, impairs binding of
'Lys-63'-linked ubiuitin, impairs TNF-induced NF-kappa-B
activation; when associated with A-329."
/evidence="ECO:0000269|PubMed:19854204"
MUTAGEN 399
/note="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."
/evidence="ECO:0000269|PubMed:14695475,
ECO:0000269|PubMed:15620648"
MUTAGEN 414
/note="V->S: Abolishes binding to polyubiquitin."
/evidence="ECO:0000269|PubMed:19033441"
MUTAGEN 415
/note="M->S: Impairs binding to polyubiquitin."
/evidence="ECO:0000269|PubMed:19033441"
CONFLICT 341
/note="S -> R (in Ref. 1; AAD12183)"
/evidence="ECO:0000305"
CONFLICT 387
/note="S -> R (in Ref. 1; AAD12183)"
/evidence="ECO:0000305"
HELIX 38..129
/evidence="ECO:0000244|PDB:6MI3"
TURN 194..196
/evidence="ECO:0000244|PDB:3CL3"
HELIX 197..249
/evidence="ECO:0000244|PDB:3CL3"
HELIX 260..268
/evidence="ECO:0000244|PDB:4BWN"
HELIX 271..295
/evidence="ECO:0000244|PDB:4BWN"
HELIX 297..341
/evidence="ECO:0000244|PDB:4BWN"
STRAND 394..396
/evidence="ECO:0000244|PDB:2JVY"
TURN 398..400
/evidence="ECO:0000244|PDB:5AAY"
STRAND 403..406
/evidence="ECO:0000244|PDB:2JVX"
HELIX 407..416
/evidence="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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U1953b CLIA kit Bos taurus,Bovine,I-kappa-B kinase 2,I-kappa-B-kinase beta,IkBKB,IKBKB,IKK2,IKK-B,IKK-beta,Inhibitor of nuclear factor kappa-B kinase subunit beta,NFKBIKB,Nuclear factor NF-kappa-B inhibitor 96T
U1953r CLIA 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 inhibitor kinase beta,Rat,R 96T
E1953r ELISA kit 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 inhibitor kinase beta 96T
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
WP253: Glycolysis
WP868: estrogen signalling
WP542: Electron Transport Chain
WP1644: DNA replication
WP1722: Th1/Th2
WP1844: MAP kinase cascade
WP1567: Glycolysis and Gluconeogenesis
WP1693: Purine metabolism
WP1243: EBV LMP1 signaling
WP1328: EBV LMP1 signaling

Related Genes :
[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) (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 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)

Bibliography :
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