SUMOylation of TDG with SUMO2,3

Stable Identifier
Reaction [transition]
Homo sapiens
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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
Catalyst Activity

SUMO transferase activity of UBE2I:SUMO2,UBE2I:SUMO3 [nucleoplasm]

Orthologous Events
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