Anti-UFM1

UFM1 is a ubiquitin-like protein that is conjugated to target proteins by E1-like activating enzyme UBA5 (UBE1DC1, MIM 610552) and E2-like conjugating enzyme UFC1 (MIM 610554) in a manner analogous to ubiquitylation (see UBE2M, MIM 603173) (Komatsu et al., 2004 [PubMed 15071506]). Protein function: Ubiquitin-like modifier which can be covalently attached via an isopeptide bond to substrate proteins as a monomer or a lysine- linked polymer (PubMed:15071506, PubMed:20018847, PubMed:29868776). The so-called ufmylation, requires the UFM1-activating E1 enzyme UBA5, the UFM1-conjugating E2 enzyme UFC1, and the UFM1-ligase E3 enzyme UFL1 (PubMed:15071506, PubMed:20018847, PubMed:29868776). This post- translational modification on lysine residues of proteins may play a crucial role in a number of cellular processes (PubMed:15071506, PubMed:20018847). TRIP4 ufmylation may for instance play a role in nuclear receptors-mediated transcription (PubMed:25219498). Other substrates may include DDRGK1 with which it may play a role in the cellular response to endoplasmic reticulum stress (Probable). [The UniProt Consortium]