TNFAIP3 (A20) ubiquitinates RIPK1

Stable Identifier
R-HSA-5690827
Type
Reaction
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
Summation

The carboxy-terminal domain of TNFAIP3 (A20) functions as a ubiquitin ligase, polyubiquitinating RIPK1 with K48-linked ubiquitin chains, thereby targeting it for proteasomal degradation (Wertz et al. 2004).

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
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
ubiquitin protein ligase activity of TNFAIP3:RIPK1 [cytosol]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed