Anti-MUL1 from rabbit, purified by affinity chromatography

Mitochondrial ubiquitin ligase activator of NFKB 1 (UniProt: Q969V5; also known as E3 SUMO-protein ligase MUL1, E3 ubiquitin-protein ligase MUL1, Growth inhibition and death E3 ligase, Mitochondrial-anchored protein ligase, MAPL, MAPL, Putative NF-kappa-B-activating protein 266, RING finger protein 218) is encoded by the MUL1 (also known as C1orf166, GIDE, MAPL, MULAN, RNF218) gene (GeneID: 79594) in human. MUL1 is a multi-pass membrane protein located on the outer mitochondrial membrane. It plays a role in the control of mitochondrial morphology and also promotes mitochondrial fragmentation and influences mitochondrial localization. MUL1 displays a weak E3 ubiquitin-protein ligase activity. It contains a RING-type zinc finger domain (aa 302-340), which is required for its E3 ligase activity. MUL1 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. When over-expressed, MUL1 is reported to inhibit cell growth by activating JNK through MAP3K7/TAK1 and inducing caspase-dependent apoptosis. MUL1 is ubiquitinated by PARK2 during mitophagy, leading to its degradation and enhancement of mitophagy.