SUMOylation of TDG with SUMO1

Stable Identifier
R-HSA-4551648
Type
Reaction
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
Summation

TDG is SUMOylated at lysine-330 with SUMO1 by UBE2I (Hardeland et al. 2002, Baba et al. 2005, Steinacher et al. 2005, Knipscheer et al. 2008, Smet-Nocca et al. 2011). Conjugation of SUMO1 to TDG induces dissociation of TDG from its product, an abasic site, and increases turnover of TDG with G:U substrate but abolishes activity with G:T substrate (Hardeland et al. 2002).

Literature References
PubMed ID Title Journal Year
11889051 Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover

Hardeland, U, Steinacher, R, Jiricny, J, Schär, P

EMBO J. 2002
18691969 Ubc9 sumoylation regulates SUMO target discrimination

Knipscheer, P, Flotho, A, Klug, H, Olsen, JV, van Dijk, WJ, Fish, A, Johnson, ES, Mann, M, Sixma, TK, Pichler, A

Mol. Cell 2008
15823533 Functionality of human thymine DNA glycosylase requires SUMO-regulated changes in protein conformation

Steinacher, R, Schär, P

Curr. Biol. 2005
21284855 SUMO-1 regulates the conformational dynamics of thymine-DNA Glycosylase regulatory domain and competes with its DNA binding activity

Smet-Nocca, C, Wieruszeski, JM, Léger, H, Eilebrecht, S, Benecke, A

BMC Biochem. 2011
15959518 Crystal structure of thymine DNA glycosylase conjugated to SUMO-1

Baba, D, Maita, N, Jee, JG, Uchimura, Y, Saitoh, H, Sugasawa, K, Hanaoka, F, Tochio, H, Hiroaki, H, Shirakawa, M

Nature 2005
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
SUMO transferase activity of SUMO1:C93-UBE2I [nucleoplasm]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed