FEATURES

DESCRIPTION

Also known as NEMO_MOUSE, Ikbkg, Nemo. 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 (PubMed:9927690). Its binding to scaffolding polyubiquitin plays a key role in IKK activation by multiple signaling receptor pathways. Can recognize and bind both 'Lys-63'-linked and linear polyubiquitin upon cell stimulation, with a much highr affinity for linear polyubiquitin. 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 (By similarity). Homodimer; disulfide-linked (By similarity). 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 (PubMed:11080499). The IKK core complex seems to associate with regulatory or adapter proteins to form a IKK-signalosome holo-complex (PubMed:11080499). The IKK complex associates with TERF2IP/RAP1, leading to promote IKK-mediated phosphorylation of RELA/p65 (PubMed:20622870). Part of a complex composed of NCOA2, NCOA3, CHUK/IKKA, IKBKB, IKBKG and CREBBP (By similarity). Interacts with COPS3, CYLD, NALP2, TRPC4AP and PIDD1 (By similarity). Interacts with ATM; the complex is exported from the nucleus (By similarity). Interacts with TRAF6 (By similarity). Interacts with IKBKE (By similarity). Interacts with TANK; the interaction is enhanced by IKBKE and TBK1 (By similarity). Part of a ternary complex consisting of TANK, IKBKB and IKBKG (PubMed:12133833). Interacts with ZFAND5 (By similarity). Interacts with RIPK2 (By similarity). Interacts with TNIP1 and TNFAIP3; TNIP1 facilitates the TNFAIP3-mediated de-ubiquitination of IKBKG (By similarity). Interacts with TNFAIP3; the interaction is induced by TNF stimulation and by polyubiquitin (By similarity). Binds (via UBAN region) polyubiquitin; binds both 'Lys-63'-linked and linear polyubiquitin, with higher affinity for linear ubiquitin (PubMed:19303852, PubMed:19854204). Interacts with NLRP10 (By similarity). Interacts with TANK; this interaction increases in response to DNA damage (By similarity). Interacts with USP10; this interaction increases in response to DNA damage (By similarity). Interacts with ZC3H12A; this interaction increases in response to DNA damage (By similarity). Interacts with IFIT5; the interaction synergizes the recruitment of IKK to MAP3K7 and enhances IKK phosphorylation (By similarity). Interacts with TRIM29; this interaction induces IKBKG/NEMO ubiquitination and proteolytic degradation (By similarity). Interacts with TRIM13; this interaction leads to IKBKG/NEMO ubiquitination (By similarity). Interacts with ARFIP2 (By similarity). Interacts with RIPK1 (PubMed:31519886). Interacts with (ubiquitinated) BCL10; interaction with polyubiquitinated BCL10 via both 'Lys-63'-linked and linear ubiquitin is required for TCR-induced NF-kappa-B activation (By similarity).

EXTERNAL LINKS

Ikbkg

NF-kappa-B essential modulator

Ikbkg

Molecular Synopsis