Ufm1-specific peptidase 2 (UFSP2)

Ufm1-specific peptidase 2 (UFSP2) is a cysteine protease enzyme that specifically cleaves the ubiquitin-like modifier UFM1 from its conjugated proteins, a process known as deufmylation[1][2][5]. UFSP2 is also responsible for processing the UFM1 precursor to expose a C-terminal glycine, which is essential for UFM1 conjugation to target proteins. By removing UFM1 after substrate modification, UFSP2 serves as a critical regulator of the UFMylation pathway, which is involved in protein homeostasis, endoplasmic reticulum function, and fine-tuning key cellular stress responses such as the DNA damage response, particularly through negative regulation of ATM kinase signaling after double-strand DNA breaks[3]. Pathogenic variants in UFSP2 have been associated with inherited skeletal disorders, including Beukes hip dysplasia, and neurodevelopmental syndromes[1][7]. UFSP2 primarily acts as a deufmylase in human cells, with no known current drug interactions or established biomarkers for patient selection or efficacy monitoring[1][2][5].

Other names

Ufm1-specific protease 2C4orf20FLJ11200BHDSEMDDRDEE106ufm1-specific peptidase 2