SUMOylation of BLM with SUMO2,3

Stable Identifier
R-HSA-4568914
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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BLM is SUMOylated at lysine-317, lysine-331, lysine-344, and lysine-347 with SUMO2,3 (Eladad et al. 2005, Zhu et al. 2008, Ouyang et al. 2009, Ouyang et al. 2013, Hendriks et al. 2014). SUMOylation causes BLM to localize to PML bodies (Eladad et al. 2005). SUMOylated BLM recruits RAD51, which directly binds SUMO, and facilitates the substitution of RAD51 for RPA at stalled replication forks (Ouyang et al. 2009, 2013).

Literature References
PubMed ID Title Journal Year
24027577 BLM SUMOylation regulates ssDNA accumulation at stalled replication forks

Ouyang, KJ, Yagle, MK, Ellis, NA, Matunis, MJ

Front Genet 2013
18708356 Small ubiquitin-related modifier (SUMO) binding determines substrate recognition and paralog-selective SUMO modification

Zhu, J, Sung, KS, Choi, CY, Guzzo, CM, Zhu, S, Matunis, MJ, Ellis, NA

J. Biol. Chem. 2008
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
19956565 SUMO modification regulates BLM and RAD51 interaction at damaged replication forks

Zhu, J, Woo, LL, Ouyang, KJ, Ellis, NA, Matunis, MJ, Huo, D

PLoS Biol. 2009
15829507 Intra-nuclear trafficking of the BLM helicase to DNA damage-induced foci is regulated by SUMO modification

Ye, TZ, Beresten, S, Leversha, M, Hu, P, Ellis, NA, Matunis, MJ, Eladad, S

Hum. Mol. Genet. 2005
Participants
Participates
Catalyst Activity

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

Orthologous Events
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