UFL1 Antibodies

Target Information

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. May also play a role in nuclear receptor-mediated transcription through TRIP4 ufmylation. May play a role in the unfolded protein response, mediating the ufmylation of multiple proteins in response to endoplasmic reticulum stress. Anchors CDK5RAP3 in the cytoplasm, preventing its translocation to the nucleus which allows expression of the CCND1 cyclin and progression of cells through the G1/S transition. Belongs to the UFL1 family. Ubiquitously expressed, with a high expression in liver (at protein level). Low expression in several invasive hepatocellular carcinomas, such Hep-G2, Hep 3B2.1-7, HLE and PLC. 3 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.

Alternate Names

E3 UFM1-protein ligase 1; E3 UFM1-protein transferase 1; hypothetical protein LOC23376; KIAA0776; LZAP-binding protein; MAXER; Multiple alpha-helix protein located at ER; NLBP; novel LZAP-binding protein; RCAD; Regulator of C53/LZAP and DDRGK1; Regulator of CDK5RAP3 and DDRGK1; RP3-393D12.1; UFL1; UFM1 specific ligase 1