USP25
Description
The USP25 (ubiquitin specific peptidase 25) is a protein-coding gene located on chromosome 21.
USP25 is a protein encoded by the USP25 gene in humans. It is involved in regulating intracellular protein breakdown, cell cycle regulation, and stress response. USP25 removes ubiquitin from degraded proteins, a process that is mediated by ubiquitin-specific proteases (USPs).
USP25 is a deubiquitinating enzyme that removes ubiquitin tags from proteins, affecting various cellular processes. It plays a role in regulating inflammation and immune response by modulating the activity of signaling pathways involved in these processes. For instance, USP25 negatively regulates interleukin-17-mediated signaling and inflammation by removing ubiquitin tags from TRAF5 and TRAF6. It also prevents the degradation of TRAF3, reducing the activation of JNK and P38 pathways and the release of IL-1B, contributing to endotoxin tolerance. USP25 also regulates the Wnt/beta-catenin signaling pathway by stabilizing tankyrases TNKS1 and TNKS2, influencing cell growth and development. Additionally, USP25 participates in the defense against oxidative stress by protecting KEAP1 from degradation, leading to the activation of the NRF2 transcription factor and the upregulation of antioxidant genes. Furthermore, USP25 positively regulates innate immune signaling against RNA viruses by interacting with and deubiquitinating ERLIN1 and ERLIN2, ultimately restricting viral production.
USP25 is also known as USP21.
