Ubiquitin-fold modifier 1 (UFM1)

Ubiquitin-fold modifier 1 (UFM1) is a highly conserved ubiquitin-like protein involved in a distinct post-translational modification pathway termed UFMylation, which is structurally and mechanistically analogous to ubiquitination but biochemically unique[1][2][3][4][5][7]. UFM1 is synthesized as an inactive precursor and is processed to its mature form by the cysteine proteases UFSP1 and UFSP2, exposing a C-terminal glycine essential for activation[1][2]. The UFM1 modification cycle involves the sequential action of a dedicated E1 (UBA5), E2 (UFC1), and E3 (UFL1) enzyme cascade that covalently attaches UFM1 to lysine residues on substrate proteins[2][3][5]. UFMylation regulates protein function, stability, localization, and interactions, and is essential for normal development and cellular homeostasis in multicellular organisms, with disruption leading to defects such as hematopoietic failure and altered immune response[1][2][3][5]. Disease associations include roles in cancer progression, immune modulation, and possibly neurodevelopmental or other cellular stress-linked pathologies[2][3][5]. No specific drugs currently target UFM1 directly, but the pathway's importance makes it a potential therapeutic target for the future[2][3][5].

Other names

C13orf20BM-002bA131P10.1HLD14ubiquitin-fold modifier 1UFM1

Not applicable (no clinically approved drugs targeting UFM1 specifically as of latest available information)