Protein function: E3 protein ligase that mediates ufmylation, the covalent attachment of the ubiquitin-like modifier UFM1 to substrate proteins, a post-translational modification on lysine residues of proteins that may play a crucial role in a number of cellular processes. Mediates DDRGK1 ufmylation and may regulate the proteasomal degradation of DDRGK1 and CDK5RAP3 thereby modulating NF-kappa-B signaling (PubMed:20018847, PubMed:20164180, PubMed:20228063, PubMed:25219498). May also through TRIP4 ufmylation play a role in nuclear receptors-mediated transcription (PubMed:25219498). May play a role in the unfolded protein response, mediating the ufmylation of multiple proteins in response to endoplasmic reticulum stress (PubMed:23152784). [The UniProt Consortium]
Anti-E3 UFM1-protein ligase 1, Anti-Novel LZAP-binding protein, Anti-E3 UFM1-protein transferase 1, Anti-Regulator of C53/LZAP and DDRGK1
Human, Mouse (Expected: Bovine)
synthetic peptide. The epitope recognized by A303-456A-T maps to a region between residue 744 and 794 of human E3 UFM1-Protein Ligase 1 using the numbering given in entry NP_056138.1 (GeneID 23376).