Exhibits weak E3 ubiquitin-protein ligase activity, but preferentially acts as a SUMO E3 ligase at physiological concentrations. 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.
Widely expressed with highest levels in the heart, skeletal muscle, placenta, kidney and liver. Barely detectable in colon and thymus.
Protein modification; protein ubiquitination. Protein modification; protein sumoylation.
Contains 1 RING-type zinc finger.
The zinc finger domain is required for E3 ligase activity.
Mitochondrion outer membrane. Peroxisome. Transported in mitochondrion-derived vesicles from the mitochondrion to the peroxisome.