SUMOylation of NPM1 with SUMO2,3

Stable Identifier
R-HSA-4086059
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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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
17535915 Sumoylation of nucleophosmin/B23 regulates its subcellular localization, mediating cell proliferation and survival

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

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

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

Mol. Cell Proteomics 2009
Participants
Participates
Catalyst Activity

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

Orthologous Events
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Reviewed
Created
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