Reactome | SUMOylation of TDG with SUMO2,3

SUMOylation of TDG with SUMO2,3

Stable Identifier

R-HSA-4551738

Type

Reaction [transition]

Species

Homo sapiens

Compartment

nucleoplasm

ReviewStatus

5/5

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TDG is SUMOylated at lysine-330 with SUMO2,3 by UBE2I and perhaps another E3 ligase (Hardeland et al. 2002, Baba et al. 2006, Hendriks et al. 2014, Tammsalu et al. 2014). SUMOylation increases turnover of TDG with G:U substrate and 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 Steinacher, R, Hardeland, U, Schär, P, Jiricny, J	EMBO J.	2002
24782567	Proteome-wide identification of SUMO2 modification sites Tatham, MH, Hay, RT, Tammsalu, T, Ibrahim, AF, Jaffray, EG, Matic, I	Sci Signal	2014
16626738	Crystal structure of SUMO-3-modified thymine-DNA glycosylase Shirakawa, M, Baba, D, Hiroaki, H, Maita, N, Tochio, H, Uchimura, Y, Sugasawa, K, Hanaoka, F, Saitoh, H, Jee, JG	J. Mol. Biol.	2006
25218447	Uncovering global SUMOylation signaling networks in a site-specific manner Yang, B, Hendriks, IA, Verlaan-de Vries, M, Vertegaal, AC, D'Souza, RC, Mann, M	Nat. Struct. Mol. Biol.	2014