Recombinant Human SENP7/SSP2 protein

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

SENP7 also known as SSP2 functions mechanically as a SUMO protease with a mass of approximately 126 kDa. It belongs to the SENP family of proteases responsible for deSUMOylation which involves the removal of SUMO groups from target proteins. SENP7 shows expression in various tissues with particular prevalence in the brain and skeletal muscle. It plays an essential role in post-translational modification by regulating the SUMOylation state influencing protein activity stability and interactions.

Biological function summary

DeSUMOylation is critical for regulating protein function and SENP7 plays a significant role in this process. It removes small ubiquitin-related modifier (SUMO) proteins from substrates therefore modulating protein function and interactions. SENP7 is not known to be part of large multiprotein complexes unlike some other members of the SUMO protease family. The precise SUMO motifs and substrates of SENP7 influence cellular functions such as DNA repair signal transduction and transcriptional regulation responding to cellular stress.

Pathways

SENP7 acts within the SUMOylation pathway a post-translational modification pathway known for regulating a variety of protein functions. It is particularly associated with pathways controlling cellular stress responses and chromatin dynamics similar to other members of the SENP family such as SENP1 and SENP2. This involvement in chromatin remodeling links SENP7 to regulating genes associated with cellular stress resilience. It helps maintain the balance of SUMO-conjugated proteins in response to environmental changes impacting cell cycle regulation and apoptosis.

Associated diseases and disorders

SENP7 connects with several conditions like cancer and neurological disorders. Aberrant SENP7 activity can lead to dysregulated SUMOylation contributing to the progression of these diseases. In cancer changes in SENP7 function relate to the altered expression of proteins involved in cell proliferation such as p53 a well-known tumor suppressor. In neurological diseases SENP7 might interact with proteins like tau influencing their SUMOylation state and aggregation tendencies which are critical in neurodegenerative disorders like Alzheimer's disease.