TNFAIP3 (A20) deubiquitinates K63polyUb-RIPK1

Stable Identifier
R-HSA-5690856
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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TNFAIP3 (A20) removes lysine-63 (K63)-linked ubiquitin chains from Receptor interacting protein (RIPK1), an essential mediator of the proximal TNF receptor 1 (TNFR1) signalling complex. The carboxy-terminal domain of A20 then functions as a ubiquitin ligase, polyubiquitinating RIPK1 with K48-linked ubiquitin chains, thereby targeting RIPK1 for proteasomal degradation (Wertz et al. 2004) which leads to termination of TNF- or LPS-mediated activation of NF-kappa-B.

Literature References
PubMed ID Title Journal Year
15258597 De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-kappaB signalling

Wertz, IE, O'Rourke, KM, Zhou, H, Eby, M, Aravind, L, Seshagiri, S, Wu, P, Wiesmann, C, Baker, R, Boone, DL, Ma, A, Koonin, EV, Dixit, VM

Nature 2004
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Participant Of
Catalyst Activity
Catalyst Activity
Title
Lys63-specific deubiquitinase activity of TNFAIP3:K63polyUb-RIPK1 [cytosol]
Physical Entity
Activity
Orthologous Events
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