PIAS4 SUMOylates RNF168 with SUMO1

Stable Identifier
R-HSA-4551661
Type
Reaction [transition]
Species
Homo sapiens
Compartment
nucleoplasm
ReviewStatus
5/5
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PIAS4 SUMOylates RNF168 with SUMO1
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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

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

J. Cell Biol. 2012
Participants
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Output
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Catalyst Activity

SUMO transferase activity of PIAS4 [nucleoplasm]

Physical Entity
PIAS4 [nucleoplasm] (Homo sapiens)
Activity
SUMO transferase activity (GO:0019789)
Orthologous Events
PIAS4 SUMOylates RNF168 with SUMO1 (Bos taurus)
PIAS4 SUMOylates RNF168 with SUMO1 (Caenorhabditis elegans)
PIAS4 SUMOylates RNF168 with SUMO1 (Danio rerio)
PIAS4 SUMOylates RNF168 with SUMO1 (Gallus gallus)
PIAS4 SUMOylates RNF168 with SUMO1 (Mus musculus)
PIAS4 SUMOylates RNF168 with SUMO1 (Rattus norvegicus)
PIAS4 SUMOylates RNF168 with SUMO1 (Sus scrofa)
PIAS4 SUMOylates RNF168 with SUMO1 (Xenopus tropicalis)
Authored
May, B  (2013-09-13)
Reviewed
Ferrari, S  (2015-02-21)
Created
May, B  (2013-09-14)
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