SUMO modification of proteins other than transcription factors.
A wide range of eukaryotic proteins has been shown to be sumoylated. Most, but not all of these proteins are nuclear. In all cases documented so far, sumoylation has been shown to occur on lysine residues. In general these are located within the consensus sequence psiKxE, although there are some exceptions to this. The role of sumoylation has been investigated for a number of identified targets. Unlike the situation with ubiquitination, sumoylation does not appear to target proteins for proteasome-mediated degradation. In contrast, the effect of SUMO modification appears to depend on the target protein and includes roles in altering protein activity, protein-protein interactions or protein localisation.
Watts
Felicity Z
FZ
Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, Brighton BN1 9QG, UK. f.z.watts@sussex.ac.uk
D000818:Animals; D003593:Cytoplasm / Q000378:metabolism; D006801:Humans; D009687:Nuclear Proteins / Q000378:metabolism; D011485:Protein Binding; D011506:Proteins / Q000378:metabolism*; D025841:Small Ubiquitin-Related Modifier Proteins / Q000378:metabolism*
D009687:Nuclear Proteins; D011506:Proteins; D025841:Small Ubiquitin-Related Modifier Proteins