Ubiquitin-fold modifier-conjugating enzyme 1 (UFC1)

Ubiquitin-fold modifier-conjugating enzyme 1 (UFC1) is a E2-like enzyme of the *ufmylation* pathway, a post-translational protein modification system analogous to ubiquitylation. UFC1 receives activated UFM1 from the E1-like enzyme UBA5 and facilitates its conjugation to substrate proteins, often mediated by the E3 ligase UFL1. UFC1 consists of a canonical E2 catalytic core domain and an additional N-terminal helix, with the active site Cys116 required for thioester bond formation with UFM1. The *ufmylation* system regulates fundamental processes such as protein homeostasis, stress responses, ER-phagy, and developmental pathways. Disruption of UFC1 function can affect ribosome recycling, DNA repair, and cell survival. There are currently no drugs or clinical agents that selectively modulate UFC1, and no validated biomarkers or safety data for clinical applications targeting UFC1 are available. UFC1 is evolutionarily conserved in multicellular organisms and is a topic of research in disease mechanisms and post-translational modification biology.

Other names

UFC1CGI-126HSPC155Ufm1-conjugating enzyme 1NEDSG

Not applicable for existing drugs. Any future drugs would likely act by inhibiting the E2-like conjugation activity, blocking UFM1 transfer to target proteins.