SUMOylation of TDG with SUMO2,3

Stable Identifier
R-HSA-4551738
Type
Reaction
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
Summation

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
24782567 Proteome-wide identification of SUMO2 modification sites

Tammsalu, T, Matic, I, Jaffray, EG, Ibrahim, AF, Tatham, MH, Hay, RT

Sci Signal 2014
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
16626738 Crystal structure of SUMO-3-modified thymine-DNA glycosylase

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

J. Mol. Biol. 2006
25218447 Uncovering global SUMOylation signaling networks in a site-specific manner

Hendriks, IA, D'Souza, RC, Yang, B, Verlaan-de Vries, M, Mann, M, Vertegaal, AC

Nat. Struct. Mol. Biol. 2014
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
SUMO transferase activity of UBE2I:SUMO2,UBE2I:SUMO3 [nucleoplasm]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed