SUMOylation of NOP58 with SUMO2

Stable Identifier
Reaction [transition]
Homo sapiens
Locations in the PathwayBrowser
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
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
24782567 Proteome-wide identification of SUMO2 modification sites

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

Sci Signal 2014
20797634 Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif

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

Mol. Cell 2010
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
20797632 A proteomic screen for nucleolar SUMO targets shows SUMOylation modulates the function of Nop5/Nop58

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

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

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

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

Lamond, AI, Westman, BJ

Nucleus 2011
Catalyst Activity

SUMO transferase activity of SUMO2:UBE2I [nucleoplasm]

Orthologous Events
Cite Us!