SENP7

SENP7, or SUMO-specific protease 7, is a member of the SENP family of cysteine proteases in humans. The SENP family mediates maturation and deconjugation of small ubiquitin-like modifier (SUMO) proteins, and SENP7 contributes to the dynamic regulation of SUMOylation in the nucleus.

SENP7 functions as an isopeptidase that processes SUMO precursors and removes SUMO moieties from substrate proteins. It shows a preference for SUMO2/3 over SUMO1 and is involved in editing SUMO chains, influencing the accumulation and turnover of SUMOylated proteins.

The enzyme is predominantly localized to the nucleus, aligning with roles in chromatin-associated processes. It exists in multiple isoforms generated by alternative splicing, including long and short forms that differ in regulatory elements and subcellular distribution.

Through regulation of SUMOylation, SENP7 participates in the control of chromatin organization and gene expression, and has been studied in relation to DNA damage response and genomic stability. Like other SUMO proteases, its activity is part of a broader SUMO cycle that governs protein interactions, localization, and function.