SUMOylation of ubiquitinylation proteins

Stable Identifier
R-HSA-3232142
DOI
10.3180/R-HSA-3232142.2
Type
Pathway
Species
Homo sapiens
Compartment
nucleoplasm
ReviewStatus
5/5
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SUMOylation of ubiquitinylation proteins
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Several ubiquitin E3 ligases are regulated by SUMOylation (reviewed in Wilson and Heaton 2008). SUMOylation appears to be necessary for nuclear import of MDM2, the E3 ligase that ubiquitinylates TP53 (p53). SUMOylation of VHL abolishes its ubiquitin ligase activity. HERC2, RNF168, and BRCA1 are ubiquitin ligases that are SUMOylated during DNA damage response and repair.
Literature References
PubMed ID Title Journal Year
18282128 Ubiquitin proteolytic system: focus on SUMO

Wilson, VG, Heaton, PR

Expert Rev Proteomics 2008
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Events
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Orthologous Events
SUMOylation of ubiquitinylation proteins (Bos taurus)
SUMOylation of ubiquitinylation proteins (Caenorhabditis elegans)
SUMOylation of ubiquitinylation proteins (Danio rerio)
SUMOylation of ubiquitinylation proteins (Gallus gallus)
SUMOylation of ubiquitinylation proteins (Mus musculus)
SUMOylation of ubiquitinylation proteins (Rattus norvegicus)
SUMOylation of ubiquitinylation proteins (Sus scrofa)
SUMOylation of ubiquitinylation proteins (Xenopus tropicalis)
Authored
May, B  (2013-03-23)
Reviewed
Niskanen, E  (2018-05-09)
Niskanen, E  (2018-08-08)
Created
May, B  (2013-03-27)
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