SUMOylation of BLM with SUMO2,3

Stable Identifier
R-HSA-4568914
Type
Reaction
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
Summation

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

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

Hum. Mol. Genet. 2005
18708356 Small ubiquitin-related modifier (SUMO) binding determines substrate recognition and paralog-selective SUMO modification

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

J. Biol. Chem. 2008
24027577 BLM SUMOylation regulates ssDNA accumulation at stalled replication forks

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

Front Genet 2013
19956565 SUMO modification regulates BLM and RAD51 interaction at damaged replication forks

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

PLoS Biol. 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