TNFAIP3

Also known as A20, OTUD7C, TNFA1P2, AISBL, TNF alpha induced protein 3, AIFBL1

Tumor necrosis factor, alpha-induced protein 3 or A20 is a protein that in humans is encoded by the TNFAIP3 gene.

Gene data

TNFAIP3

Name: TNF alpha induced protein 3
Type: protein-coding
Position: 137,866,383–137,885,836 (+)
Aliases: A20, AIFBL1, AISBL, OTUD7C, TNFA1P2
Ensembl: ENSG00000118503
RefSeq RNA: NM_001270507.2, NM_001270508.2, NM_006290.4, XM_005267119.1, XM_011536095.2
RefSeq protein: NP_001257436.1, NP_001257437.1, NP_006281.1, XP_005267176.1, XP_011534397.1

This gene was identified as a gene whose expression is rapidly induced by the tumor necrosis factor (TNF). The protein encoded by this gene is a zinc finger protein and ubiqitin-editing enzyme, and has been shown to inhibit NF-kappa B activation as well as TNF-mediated apoptosis. The encoded protein, which has both ubiquitin ligase and deubiquitinase activities, is involved in the cytokine-mediated immune and inflammatory responses. Several transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2012].

Gene Ontology

Biological process

B-1 B cell homeostasis

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Article

7 sections

Contents

Interactions
Association with rheumatoid arthritis
Other diseases
See also
References
Further reading
External links

Tumor necrosis factor, alpha-induced protein 3 or A20 is a protein that in humans is encoded by the TNFAIP3 gene.

This gene was identified as a gene whose expression is rapidly induced by the tumor necrosis factor (TNF). The protein encoded by this gene is a zinc finger protein and a deubiquitinating enzyme, and has been shown to inhibit NF-kappa B activation as well as TNF-mediated apoptosis. The A20 protein is ancient, and protein homolog can be found as far back as cnidaria (corals, jellyfish, anemones) with a conserved protein domain composition. Using knockout mouse models of TNFAIP3 and its transcriptional repressor (i.e. KCHIP3), TNFAIP3 has been shown to be critical for limiting inflammation by terminating endotoxin- and TNF-induced NF-kappa B responses. In brief, deubiquitinase function of TNFAIP3 was shown to remove ubiquitin chains from VE-cadherin to prevent loss of VE-cadherin at the endothelial adherens junctions.