Anti-MUL1 Antibody

Exhibits weak E3 ubiquitin-protein ligase activity (PubMed:18591963, PubMed:19407830, PubMed:22410793) . 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 (PubMed:18591963, PubMed:19407830, PubMed:22410793) . 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 (PubMed:22410793) . Proposed to preferentially act as a SUMO E3 ligase at physiological concentrations (PubMed:19407830) . Plays a role in the control of mitochondrial morphology by promoting mitchondrial fragmentation, and influences mitochondrial localization (PubMed:19407830, PubMed:18207745, PubMed:18213395) . Likely to promote mitchondrial fission through negatively regulating the mitochondrial fusion proteins MFN1 and MFN2, acting in a pathway that is parallel to the PRKN/PINK1 regulatory pathway (PubMed:24898855) . May also be involved in the sumoylation of the membrane fission protein DNM1L (PubMed:18207745, PubMed:19407830) . Inhibits cell growth (PubMed:18591963, PubMed:22410793) . When overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis (PubMed:23399697) . Involved in the modulation of innate immune defense against viruses by inhibiting DDX58-dependent antiviral response (PubMed:23399697) . Can mediate DDX58 sumoylation and disrupt its polyubiquitination (PubMed:23399697) .

Mitochondrion outer membrane; Multi-pass membrane protein. Peroxisome. Transported in mitochondrion- derived vesicles from the mitochondrion to the peroxisome.