UFM1
Description
The UFM1 (ubiquitin fold modifier 1) is a protein-coding gene located on chromosome 13.
UFM1, also known as Ubiquitin-fold modifier 1, is a protein encoded by the UFM1 gene in humans. It is a ubiquitin-like protein that is attached to target proteins by a process called UFMylation, which involves the enzymes UBA5 (E1-like) and UFC1 (E2-like). UFM1 shares similarities with ubiquitin, including its tertiary structure, but lacks sequence similarity. It is initially produced as an inactive precursor (pro-UFM1) and requires activation by its cognate E1 enzyme (Uba5) to become active. This activation involves the formation of a high-energy thiolester bond in the presence of ATP. The activated UFM1 is then transferred to its cognate E2-like enzyme (Ufc1), which facilitates its conjugation to target proteins. UFM1 forms complexes with unidentified proteins.
UFM1, a ubiquitin-like modifier, can be attached to lysine residues on target proteins as a single unit or a chain. This process, known as ufmylation, requires the enzymes UBA5 (E1), UFC1 (E2), and UFL1 (E3). Ufmylation plays a role in several cellular processes, including the removal of damaged ribosomes, DNA damage response, gene transcription, and reticulophagy, a process that removes damaged endoplasmic reticulum. Ufmylation of the protein TRIP4 influences gene transcription mediated by nuclear receptors.
UFM1 is also known as BM-002, C13orf20, HLD14.
