TNFAIP3 (A20) ubiquitinates RIPK1

Stable Identifier
R-HSA-5690827
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
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

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

Nature 2004
Participants
Participates
Catalyst Activity

ubiquitin protein ligase activity of TNFAIP3:RIPK1 [cytosol]

Orthologous Events
Authored
Reviewed
Created
Cite Us!