InterPro domain: IPR018611

The ubiquitin fold modifier 1 (Ufm1) is the most recently discovered ubiquitin-like modifier whose conjugation (ufmylation) system is conserved in multicellular organisms. Ufm1 is known to covalently attach with cellular protein(s) via a specific E1-activating enzyme (Uba5), an E2-conjugating enzyme (Ufc1), and a E3-ligating enzyme [ 1 ]. This entry represents E3 UFM1-protein ligase 1 (Ufl1) which mediates the covalent attachment of the ubiquitin-like modifier UFM1 to lysine residues on target proteins and plays a key role in reticulophagy (also called ER-phagy) induced in response to endoplasmic reticulum stress [ 2 , 2 , 3 , 4 , 5 ].

1. A novel type of E3 ligase for the Ufm1 conjugation system. J. Biol. Chem. 285, 5417-27
2. A novel LZAP-binding protein, NLBP, inhibits cell invasion. J Biol Chem 285, 12232-40
3. A novel C53/LZAP-interacting protein regulates stability of C53/LZAP and DDRGK domain-containing Protein 1 (DDRGK1) and modulates NF-kappaB signaling. J. Biol. Chem. 285, 15126-36
4. Modification of ASC1 by UFM1 is crucial for ERα transactivation and breast cancer development. Mol. Cell 56, 261-274
5. A Genome-wide ER-phagy Screen Highlights Key Roles of Mitochondrial Metabolism and ER-Resident UFMylation. Cell 180, 1160-1177.e20