MUL1 blocking peptide

MUL1 Antibody (C-term) Blocking peptide

• Gene Names: MUL1; GIDE; MAPL; MULAN; RNF218; C1orf166
• Synonyms: MUL1; MUL1 Antibody (C-term) Blocking peptide; 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; C1orf166; GIDE; MULAN; RNF218; MUL1 blocking peptide

• Form/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.
• Sequence Length: 352

• 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.
• Preparation and Storage: Maintain refrigerated at 2-8 degree C for up to 6 months. For long term storage store at -20 degree C.

Related Product Information for MUL1 blocking peptide

Exhibits weak E3 ubiquitin-protein ligase activity. 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. 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. Proposed to preferentially act as a SUMO E3 ligase at physiological concentrations. Plays a role in the control of mitochondrial morphology. Promotes mitochondrial fragmentation and influences mitochondrial localization. The function may implicate its abilty to sumoylate DNM1L. Inhibits cell growth. When overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis. Involved in the modulation of innate immune defense against viruses by inhibiting DDX58-dependent antiviral response. Can mediate DDX58 sumoylation and disrupt its polyubiquitination.

NCBI and Uniprot Product Information

• NCBI GI #: 74760689
• NCBI GeneID: 79594
• UniProt Accession #: Q969V5; Q7Z431; Q9H9B5; B5M497
• Molecular Weight: 39,800 Da
• NCBI Official Full Name: Mitochondrial ubiquitin ligase activator of NFKB 1
• NCBI Official Synonym Full Names: mitochondrial E3 ubiquitin protein ligase 1
• NCBI Official Symbol: MUL1
• NCBI Official Synonym Symbols: GIDE; MAPL; MULAN; RNF218; C1orf166
• NCBI Protein Information: mitochondrial ubiquitin ligase activator of NFKB 1
• UniProt Protein Name: Mitochondrial ubiquitin ligase activator of NFKB 1
• Protein Family: Mitochondrial ubiquitin ligase activator
• UniProt Gene Name: MUL1
• UniProt Synonym Gene Names: C1orf166; GIDE; MAPL; MULAN; RNF218; MAPL
• UniProt Entry Name: MUL1_HUMAN

Uniprot Description

MULAN: 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.

Protein type: Membrane protein, multi-pass; Apoptosis; Membrane protein, integral; Ubiquitin ligase; Mitochondrial; EC 6.3.2.-; EC 6.3.2.19; Ubiquitin conjugating system; Ligase

Chromosomal Location of Human Ortholog: 1p36.12

Cellular Component: axon; cell soma; cytoplasm; integral to mitochondrial outer membrane; membrane; mitochondrion; nucleoplasm; peroxisome

Molecular Function: identical protein binding; protein binding; signal transducer activity; SUMO ligase activity; ubiquitin protein ligase binding; ubiquitin-protein ligase activity

Biological Process: activation of JNK activity; caspase activation; mitochondrial fission; mitochondrion localization; negative regulation of cell growth; negative regulation of defense response to virus by host; negative regulation of innate immune response; negative regulation of protein kinase B signaling cascade; positive regulation of I-kappaB kinase/NF-kappaB cascade; positive regulation of protein sumoylation; protein destabilization; protein stabilization; protein ubiquitination