SUMOylation of TDG with SUMO1

Stable Identifier
Reaction [transition]
Homo sapiens
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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
18691969 Ubc9 sumoylation regulates SUMO target discrimination

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

Mol. Cell 2008
11889051 Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover

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

EMBO J. 2002
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, Léger, H, Eilebrecht, S, Benecke, A, Wieruszeski, JM

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

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

Nature 2005
Catalyst Activity

SUMO transferase activity of SUMO1:C93-UBE2I [cytoplasm]

Orthologous Events
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