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Mul1

Gene
mul1
Protein
Mitochondrial ubiquitin ligase activator of nfkb 1
Organism
Xenopus laevis
Length
353 amino acids
Function
E3 ubiquitin-protein ligase that plays a role in the control of mitochondrial morphology. Promotes mitochondrial fragmentation and influences mitochondrial localization. Inhibits cell growth. 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.
Mass
40.359 kDa
Sequence
MENGGRPSVGQVILLTTSSAITALFYSIYRHKYRSVQTLKEAKKFCLTDDLPAVLSDLPGKCVPYAVIEGAVTSVKEVLNSQYVENCKGVIQRLSLKEHKMVWNRTTHLWNDHEKIIHQRSNTVPFDLAPENPGESGVSVRVLRPLEAVDLGLETIYEKFHPAVQSFSNILGHYMTGERPKGVQETEEMLKIGATITGVGELVLDNKTIKLQPPKDGMLFYLSSMDYEGLLEKQEVQMRWWRILSIVFGVASCITLFFILRRKYRHYKEKQHLKNLQREFEESRARQRVQQEPQNKEEVQNPCSICLSTEKSCVFLECGHVCSCISCYQALPSPKKCPICRNFIDRIVPLYNS

Gene
MUL1
Protein
Mitochondrial ubiquitin ligase activator of NFKB 1
Organism
Homo sapiens
Length
352 amino acids
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).
Mass
39.8 kDa
Sequence
MESGGRPSLCQFILLGTTSVVTAALYSVYRQKARVSQELKGAKKVHLGEDLKSILSEAPGKCVPYAVIEGAVRSVKETLNSQFVENCKGVIQRLTLQEHKMVWNRTTHLWNDCSKIIHQRTNTVPFDLVPHEDGVDVAVRVLKPLDSVDLGLETVYEKFHPSIQSFTDVIGHYISGERPKGIQETEEMLKVGATLTGVGELVLDNNSVRLQPPKQGMQYYLSSQDFDSLLQRQESSVRLWKVLALVFGFATCATLFFILRKQYLQRQERLRLKQMQEEFQEHEAQLLSRAKPEDRESLKSACVVCLSSFKSCVFLECGHVCSCTECYRALPEPKKCPICRQAITRVIPLYNS

Gene
MUL1
Protein
Mitochondrial ubiquitin ligase activator of NFKB 1
Organism
Macaca fascicularis
Length
352 amino acids
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.
Mass
39.827 kDa
Sequence
MENGGRPSLCQFILLGTTSVVTAALYSVYRQKAWVSQELKGAKKVHLGEDLKSILSEAPGKCVPYAVIEGAVRSVKETLNSQFVENCKGVIQRLTLQEHKMVWNRTTHLWNDCSKIIHQRTNTVPFDLVPHEDGVDVAVRVLKPLDSVDLGLEAVYEKFHPSIQSFTDVIGHYISGERPKGIQETEEMLKVGATLTGVGELVLDNNSVRLQPPKQGMQYYLSSQDFDSLLQRQESSVRLWKVLALVFGFATCATLFFILRKQYLQRQERLRLKQMQEEFQEHEAQLLSRAKPEDRESLKSACVVCLSSFKSCVFLECGHVCSCTECYRALPEPKKCPICRQAITRVIPLYNS

Gene
Mul1
Protein
Mitochondrial ubiquitin ligase activator of NFKB 1
Organism
Mus musculus
Length
352 amino acids
Function
Exhibits weak E3 ubiquitin-protein ligase activity (By similarity). 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 (By similarity). 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 (By similarity). Proposed to preferentially act as a SUMO E3 ligase at physiological concentrations (By similarity). Plays a role in the control of mitochondrial morphology by promoting mitochondrial fragmentation, and influences mitochondrial localization (By similarity). 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 (By similarity). Inhibits cell growth (By similarity). When overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis (By similarity). Involved in the modulation of innate immune defense against viruses by inhibiting DDX58-dependent antiviral response (By similarity). Can mediate DDX58 sumoylation and disrupt its polyubiquitination (By similarity).
Mass
39.835 kDa
Sequence
MESGSRPSLGQVILLGTSSMVTAVLYSIYRQKAQVAQELKGAKKIHLGEDLKGILSEAPGKCVPYAVIEGAVRSVKETLNSQFVENCKGVIQRLSLQEHKMVWNRTTHLWNDYSKIIHQRTNTVPFDLVPHEDGVAVSVRVLKPLDSVDLGLETVYEKFHPSVQSFTDAIGHYISGERPKGIQETEEMLKVGATLTGIGELVLDNNAVRLQPPKQGMQYYLSSQDFDSLLHRQESSVRLWKILVLVFGFATCATLFFILRKQYLHRQERLRQQQLQEEFLEHEAQLLSQASPEDRESLKSACVVCLSNFKSCVFLECGHVCSCRQCYLALPEPKRCPICRREITRVIPLYNS

Gene
Mul1
Protein
Mitochondrial E3 ubiquitin protein ligase 1
Organism
Drosophila melanogaster
Length
338 amino acids
Function
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. Plays a role in the control of mitochondrial morphology by promoting mitochondrial fission. Negatively regulates the mitochondrial fusion protein marf by promoting its ubiquitination, acting in a pathway that is parallel to the park/pink1 regulatory pathway.
Mass
37.844 kDa
Sequence
MEFLHESVALGVDLLILGLCAREYVHYKRTAKVLKAAPQYNIDGDLKSVVERQRDKKIPYAVIRGTVTPIGVPLRSSLVPSVSGVLQIVKLHEHRVTRGFAGFWTEQHKLLHESANEMPFELRNQSHGVEIVDALSAAVLDVDVVYDNYEPSNLSLFDHVFGFFSGVRQRGLQTTEEVLREGSFLTAIGELELDGDTLRMQPSNEGPLFLTTATKSTLIKRFEDAKTTTILKLVVCSTISAILVAFIAKKLYRKRKQEREEAKIRERLDTERRERRARSRPHTLSQDQLCVVCSTNPKEIILLPCGHVCLCEDCAQKISVTCPVCRGSIVSKAAAFIA