SUMOylation of NOP58 with SUMO2

Stable Identifier
R-HSA-4570489
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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NOP58 (NOP5) is SUMOylated at lysine-467 and lysine-497 with SUMO2 (Matic et al. 2010, Westman et al. 2010, Westman and Lamond 2011, Hendriks et al. 2014, Impens et al. 2014, Tammsalu et al. 2014). (Two molecules of SUMO2 are shown for each modification in order to represent the oligomeric chains of SUMO2 that are attached to a target protein.) SUMOylation of NOP58 is required for high affinity binding of snoRNAs by NOP58

Literature References
PubMed ID Title Journal Year
20797634 Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif

Matic, I, Schimmel, J, Hendriks, IA, van Santen, MA, van de Rijke, F, van Dam, H, Gnad, F, Mann, M, Vertegaal, AC

Mol. Cell 2010
24782567 Proteome-wide identification of SUMO2 modification sites

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

Sci Signal 2014
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
20797632 A proteomic screen for nucleolar SUMO targets shows SUMOylation modulates the function of Nop5/Nop58

Westman, BJ, Verheggen, C, Hutten, S, Lam, YW, Bertrand, E, Lamond, AI

Mol. Cell 2010
25114211 Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli

Impens, F, Radoshevich, L, Cossart, P, Ribet, D

Proc. Natl. Acad. Sci. U.S.A. 2014
21647297 A role for SUMOylation in snoRNP biogenesis revealed by quantitative proteomics

Westman, BJ, Lamond, AI

Nucleus 2011
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
SUMO transferase activity of SUMO2:UBE2I [nucleoplasm]
Physical Entity
Activity
Orthologous Events
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Reviewed
Created