Anti-UFL1 antibody - N-terminal

Target data

E3 protein ligase that mediates ufmylation, the covalent attachment of the ubiquitin-like modifier UFM1 to lysine residues on target proteins, and which plays a key role in various processes, such as ribosome recycling, response to DNA damage, interferon response or reticulophagy (also called ER-phagy) (PubMed : 20018847, PubMed : 20164180, PubMed : 20228063, PubMed : 25219498, PubMed : 27351204, PubMed : 30626644, PubMed : 30783677, PubMed : 32160526, PubMed : 32807901, PubMed : 35394863, PubMed : 36121123, PubMed : 36543799, PubMed : 36893266, PubMed : 37036982, PubMed : 37311461, PubMed : 37595036, PubMed : 37795761, PubMed : 38377992, PubMed : 38383785, PubMed : 38383789). Catalyzes ufmylation of many protein, such as CD274/PD-L1, CDK5RAP3, CYB5R3, DDRGK1, EIF6, histone H4, MRE11, P4HB, PDCD1/PD-1, TRIP4, RPN1, RPS20/uS10, RPL10/uL16, RPL26/uL24, SYVN1/HRD1 and TP53/p53 (PubMed : 20018847, PubMed : 20531390, PubMed : 25219498, PubMed : 30783677, PubMed : 30886146, PubMed : 32160526, PubMed : 35753586, PubMed : 36543799, PubMed : 36893266, PubMed : 37036982, PubMed : 37595036, PubMed : 37795761, PubMed : 38383785, PubMed : 38383789). As part of the UREL complex, plays a key role in ribosome recycling by catalyzing mono-ufmylation of RPL26/uL24 subunit of the 60S ribosome (PubMed : 38383785, PubMed : 38383789). Ufmylation of RPL26/uL24 occurs on free 60S ribosomes following ribosome dissociation : it weakens the junction between post-termination 60S subunits and SEC61 translocons, promoting release and recycling of the large ribosomal subunit from the endoplasmic reticulum membrane (PubMed : 38383785, PubMed : 38383789). Ufmylation of RPL26/uL24 and subsequent 60S ribosome recycling either take place after normal termination of translation or after ribosome stalling during cotranslational translocation at the endoplasmic reticulum (PubMed : 37036982, PubMed : 37595036, PubMed : 38383785, PubMed : 38383789). Involved in reticulophagy in response to endoplasmic reticulum stress by mediating ufmylation of proteins such as CYB5R3 and RPN1, thereby promoting lysosomal degradation of ufmylated proteins (PubMed : 23152784, PubMed : 32160526, PubMed : 36543799). Ufmylation in response to endoplasmic reticulum stress is essential for processes such as hematopoiesis, blood vessel morphogenesis or inflammatory response (PubMed : 32050156). Mediates ufmylation of DDRGK1 and CDK5RAP3; the role of these modifications is however unclear : as both DDRGK1 and CDK5RAP3 act as substrate adapters for ufmylation, it is uncertain whether ufmylation of these proteins is, a collateral effect or is required for ufmylation (PubMed : 20018847, PubMed : 20531390). Acts as a negative regulator of T-cell activation by mediating ufmylation and stabilization of PDCD1/PD-1 (PubMed : 38377992). Also involved in the response to DNA damage : recruited to double-strand break sites following DNA damage and mediates monoufmylation of histone H4 and ufmylation of MRE11 (PubMed : 30783677, PubMed : 30886146). Mediates ufmylation of TP53/p53, promoting its stability (PubMed : 32807901). Catalyzes ufmylation of TRIP4, thereby playing a role in nuclear receptor-mediated transcription (PubMed : 25219498). Required for hematopoietic stem cell function and hematopoiesis (By similarity).