Reactome | SUMOylation of TDG with SUMO1

SUMOylation of TDG with SUMO1

Stable Identifier

R-HSA-4551648

Type

Reaction [transition]

Species

Homo sapiens

Compartment

nucleoplasm

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

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