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MUL1 Antibody (C-term) Blocking peptide

Synthetic peptide

Product Information
Primary Accession Q969V5
Clone Names 100324079
Peptide ID 100324079
Additional Information
Gene ID 79594
Other Names Mitochondrial ubiquitin ligase activator of NFKB 1, 632-, E3 SUMO-protein ligase MUL1, E3 ubiquitin-protein ligase MUL1, Growth inhibition and death E3 ligase, Mitochondrial-anchored protein ligase, MAPL, Putative NF-kappa-B-activating protein 266, RING finger protein 218, MUL1, C1orf166, GIDE, MAPL, MULAN, RNF218
Format Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name MUL1
Synonyms C1orf166, GIDE, MAPL, MULAN, RNF218
Function 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 mitochondrial fragmentation, and influences mitochondrial localization (PubMed:19407830, PubMed:18207745, PubMed:18213395). Likely to promote mitochondrial 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).
Cellular Location Mitochondrion outer membrane; Multi-pass membrane protein. Peroxisome. Note=Transported in mitochondrion- derived vesicles from the mitochondrion to the peroxisome
Tissue Location Widely expressed with highest levels in the heart, skeletal muscle, placenta, kidney and liver. Barely detectable in colon and thymus.
Research Areas
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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.


Laure, L., et al. FEBS J. 277(20):4322-4337(2010)Braschi, E., et al. EMBO Rep. 10(7):748-754(2009)Venkatesan, K., et al. Nat. Methods 6(1):83-90(2009)Zhang, B., et al. Cell Res. 18(9):900-910(2008)Zhang, H., et al. Biochem. Biophys. Res. Commun. 366(4):898-904(2008)

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Cat# BP12811b
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