| Background | domain:The zinc finger domain is required for E3 ligase activity.,function:E3 ubiquitin-protein ligase that plays a role in the control of mitochondrial morphology. Promotes mitochondrial fragmentation and influences mitochondrial localization. Inhibits cell growth. When overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis. 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.,pathway:Protein modification; protein ubiquitination.,similarity:Contains 1 RING-type zinc finger.,subcellular location:Transported in mitochondrion-derived vesicles from the mitochondrion to the peroxisome.,subunit:Homooligomer. Interacts with MAP3K7/TAK1.,tissue specificity:Widely expressed with highest levels in the heart, skeletal muscle, placenta, kidney and liver. Barely detectable in colon and thymus., |
