Mouse Tumor necrosis factor alpha-induced protein 3,TNFAIP3 ELI

Ubiquitin-editing enzyme that contains both ubiquitin ligase and deubiquitinase activities.

Involved in immune and inflammatory responses signaled by cytokines, such as TNF-alpha and IL-1 beta, or pathogens via Toll-like receptors (TLRs) through terminating NF-kappa-B activity.

Essential component of a ubiquitin-editing protein complex, comprising also RNF11, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways.

In cooperation with TAX1BP1 promotes disassembly of E2-E3 ubiquitin protein ligase complexes in IL-1R and TNFR-1 pathways; affected are at least E3 ligases TRAF6, TRAF2 and BIRC2, and E2 ubiquitin-conjugating enzymes UBE2N and UBE2D3.

In cooperation with TAX1BP1 promotes ubiquitination of UBE2N and proteasomal degradation of UBE2N and UBE2D3.

Upon TNF stimulation, deubiquitinates 'Lys-63'-polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains.

This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B.

Deubiquitinates TRAF6 probably acting on 'Lys-63'-linked polyubiquitin.

Upon T-cell receptor (TCR)-mediated T-cell activation, deubiquitinates 'Lys-63'-polyubiquitin chains on MALT1 thereby mediating disassociation of the CBM (CARD11:BCL10:MALT1) and IKK complexes and preventing sustained IKK activation.

Deubiquitinates NEMO/IKBKG; the function is facilitated by TNIP1 and leads to inhibition of NF-kappa-B activation.

Upon stimulation by bacterial peptidoglycans, probably deubiquitinates RIPK2.

Can also inhibit I-kappa-B-kinase (IKK) through a non-catalytic mechanism which involves polyubiquitin; polyubiquitin promotes association with IKBKG and prevents IKK MAP3K7-mediated phosphorylation.

Targets TRAF2 for lysosomal degradation.

In vitro able to deubiquitinate 'Lys-11'-, 'Lys-48'- and 'Lys-63' polyubiquitin chains.

Inhibitor of programmed cell death.

Has a role in the function of the lymphoid system.

Required for LPS-induced production of proinflammatory cytokines and IFN beta in LPS-tolerized macrophages.

{ECO:0000269|PubMed:10385526, ECO:0000269|PubMed:11389905, ECO:0000269|PubMed:15334086, ECO:0000269|PubMed:18342009, ECO:0000269|PubMed:20185725, ECO:0000269|PubMed:23609450}.