| Description |
Ubiquitin-like modifier which can be covalently attached via an isopeptide bond to substrate proteins as a monomer or a lysine-linked polymer. 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). This post-translational modification on lysine residues of proteins may play a crucial role in a number of cellular processes. 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 (By similarity).
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