PIAS4 SUMOylates RNF168 with SUMO1

Stable Identifier
R-HSA-4551661
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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PIAS4 SUMOylates RNF168 at an unknown lysine residue (Danielsen et al. 2012). Both RNF168 and HERC2 are SUMOylated at double-strand breaks in DNA. SUMOylation of RNF168 is required for its retention at double-strand breaks.

Literature References
PubMed ID Title Journal Year
22508508 DNA damage-inducible SUMOylation of HERC2 promotes RNF8 binding via a novel SUMO-binding Zinc finger

Danielsen, JR, Povlsen, LK, Villumsen, BH, Streicher, W, Nilsson, J, Wikström, M, Bekker-Jensen, S, Mailand, N

J. Cell Biol. 2012
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
SUMO transferase activity of PIAS4 [nucleoplasm]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created