ID:MUL1_HUMAN DESCRIPTION: RecName: Full=Mitochondrial ubiquitin ligase activator of NFKB 1; EC=6.3.2.-; AltName: Full=E3 SUMO-protein ligase MUL1; AltName: Full=E3 ubiquitin-protein ligase MUL1; AltName: Full=Growth inhibition and death E3 ligase; AltName: Full=Mitochondrial-anchored protein ligase; Short=MAPL; AltName: Full=Putative NF-kappa-B-activating protein 266; AltName: Full=RING finger protein 218; FUNCTION: 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. PATHWAY: Protein modification; protein ubiquitination. PATHWAY: Protein modification; protein sumoylation. SUBUNIT: Homooligomer. Interacts with MAP3K7/TAK1. Interacts with UBC9. Interacts with and sumoylates DNM1L. INTERACTION: Q92624:APPBP2; NbExp=3; IntAct=EBI-744120, EBI-743771; SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein. Peroxisome. Note=Transported in mitochondrion- derived vesicles from the mitochondrion to the peroxisome. TISSUE SPECIFICITY: Widely expressed with highest levels in the heart, skeletal muscle, placenta, kidney and liver. Barely detectable in colon and thymus. DOMAIN: The zinc finger domain is required for E3 ligase activity. SIMILARITY: Contains 1 RING-type zinc finger.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q969V5
Front
Top
Side
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.
Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Biological Process: GO:0000266 mitochondrial fission GO:0006915 apoptotic process GO:0006919 activation of cysteine-type endopeptidase activity involved in apoptotic process GO:0006996 organelle organization GO:0007257 activation of JUN kinase activity GO:0010637 negative regulation of mitochondrial fusion GO:0010821 regulation of mitochondrion organization GO:0016567 protein ubiquitination GO:0016925 protein sumoylation GO:0030308 negative regulation of cell growth GO:0031647 regulation of protein stability GO:0031648 protein destabilization GO:0033235 positive regulation of protein sumoylation GO:0043123 positive regulation of I-kappaB kinase/NF-kappaB signaling GO:0045824 negative regulation of innate immune response GO:0050689 negative regulation of defense response to virus by host GO:0050821 protein stabilization GO:0051646 mitochondrion localization GO:0051881 regulation of mitochondrial membrane potential GO:0051898 negative regulation of protein kinase B signaling GO:0060339 negative regulation of type I interferon-mediated signaling pathway GO:0071360 cellular response to exogenous dsRNA GO:0071650 negative regulation of chemokine (C-C motif) ligand 5 production GO:0090141 positive regulation of mitochondrial fission GO:1901028 regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway GO:1903861 positive regulation of dendrite extension GO:1904925 positive regulation of mitophagy in response to mitochondrial depolarization
US Server
