SUMOylation of NPM1 with SUMO2,3

Stable Identifier
R-HSA-4086059
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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NPM1 (Nucleophosmin, B23) is SUMOylated at lysine-263 with SUMO2,3 (Liu et al. 2007, Blomster et al. 2009, Hendriks et al. 2014). SUMOylation enhances binding of NPM1 to Rb and enhances nuclear residency of NPM1.

Literature References
PubMed ID Title Journal Year
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
17535915 Sumoylation of nucleophosmin/B23 regulates its subcellular localization, mediating cell proliferation and survival

Liu, X, Liu, Z, Jang, SW, Ma, Z, Shinmura, K, Kang, S, Dong, S, Chen, J, Fukasawa, K, Ye, K

Proc. Natl. Acad. Sci. U.S.A. 2007
19240082 Novel proteomics strategy brings insight into the prevalence of SUMO-2 target sites

Blomster, HA, Hietakangas, V, Wu, J, Kouvonen, P, Hautaniemi, S, Sistonen, L

Mol. Cell Proteomics 2009
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
SUMO transferase activity of UBE2I:SUMO2,UBE2I:SUMO3 [nucleoplasm]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created