Ubiquitin specific peptidase 31 (USP31)

Ubiquitin specific peptidase 31 (USP31) is a cysteine-type deubiquitinating enzyme, part of the larger ubiquitin-specific protease family[1]. It catalyzes the removal of ubiquitin moieties from substrate proteins by cleaving the bond at the C-terminal glycine of ubiquitin, influencing protein degradation pathways via the ubiquitin-proteasome system. USP31 plays an important regulatory role in intracellular signaling, most notably influencing NF-kappa-B signaling by deubiquitinating factors such as TRAF2, thereby impacting inflammatory and immune responses[1]. USP31 is predominantly localized in the nucleus and may function as a biomarker for prognosis and immune response, particularly in clear cell renal cell carcinoma; it has also been implicated in rare diseases like mouth disease and Waardenburg syndrome, type 4A[1]. Additionally, USP31 participates in the translation of viral proteins during specific viral infections by interacting with internal ribosomal entry sites on viral genomes[1]. Drugs targeting deubiquitinases like USP31 are of interest in cancer and immunity, but there are currently no known approved small molecule drugs specifically targeting USP31[5][1].

Other names

Ubiquitin carboxyl-terminal hydrolase 31Deubiquitinating enzyme 31Ubiquitin thioesterase 31Ubiquitin-specific-processing protease 31KIAA1203ubiquitin specific proteinase 31ubiquitin thiolesterase 31

Inhibitors would act through inhibition of deubiquitinase (DUB) activity, leading to accumulation of ubiquitinated proteins and altered proteolysis. Modulation of NF-kappa-B signaling via deubiquitination of pathway components (such as TRAF2).