SUMOylation of SUMOylation proteins

Stable Identifier
R-HSA-4085377
DOI
10.3180/R-HSA-4085377.2
Type
Pathway
Species
Homo sapiens
Compartment
nucleoplasm, nuclear envelope
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SUMOylation of SUMOylation proteins
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SUMOylation processes themselves can be controlled by SUMOylation (reviewed in Wilkinson and Henley 2010). The SUMO E3 ligases PIAS4, RANBP2, and TOPORS are SUMOylated, as is the single SUMO E2 enzyme, UBE2I (UBC9). SUMOylation affects the subcellular location of PIAS4 and TOPORS and affects the activity of PIAS4 and UBE2I.

Literature References
PubMed ID Title Journal Year
20462400 Mechanisms, regulation and consequences of protein SUMOylation

Henley, JM, Wilkinson, KA

Biochem. J. 2010
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Orthologous Events
SUMOylation of SUMOylation proteins (Bos taurus)
SUMOylation of SUMOylation proteins (Caenorhabditis elegans)
SUMOylation of SUMOylation proteins (Danio rerio)
SUMOylation of SUMOylation proteins (Dictyostelium discoideum)
SUMOylation of SUMOylation proteins (Drosophila melanogaster)
SUMOylation of SUMOylation proteins (Gallus gallus)
SUMOylation of SUMOylation proteins (Mus musculus)
SUMOylation of SUMOylation proteins (Plasmodium falciparum)
SUMOylation of SUMOylation proteins (Rattus norvegicus)
SUMOylation of SUMOylation proteins (Saccharomyces cerevisiae)
SUMOylation of SUMOylation proteins (Schizosaccharomyces pombe)
SUMOylation of SUMOylation proteins (Xenopus tropicalis)
Cross References
GlyCosmos
Authored
May, B  (2013-08-03)
Reviewed
Niskanen, E  (2018-05-09)
Niskanen, E  (2018-08-08)
Created
May, B  (2013-08-05)
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