MUL1 antibody

Exhibits weak E3 ubiquitin-protein ligase activity. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. Can ubiquitinate AKT1 preferentially at 'Lys-284' involving 'Lys-48'-linked polyubiquitination and seems to be involved in regulation of Akt signaling by targeting phosphorylated Akt to proteosomal degradation. Proposed to preferentially act as a SUMO E3 ligase at physiological concentrations. Plays a role in the control of mitochondrial morphology. Promotes mitochondrial fragmentation and influences mitochondrial localization. The function may implicate its ability to sumoylate DNM1L. Inhibits cell growth. When overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis. Involved in the modulation of innate immune defense against viruses by inhibiting DDX58-dependent antiviral response. Can mediate DDX58 sumoylation and disrupt its polyubiquitination.

Mitochondrial ubiquitin ligase activator of NFKB 1|E3 SUMO-protein ligase MUL1|E3 ubiquitin-protein ligase MUL1|Growth inhibition and death E3 ligase|Mitochondrial-anchored protein ligase|Protein Hades|Putative NF-kappa-B-activating protein 266|RING finger protein 218|RING-type E3 ubiquitin transferase NFKB 1|MUL1|C1orf166|GIDE|MAPL|MULAN|RNF218