MUL1
entrez
79594
canonical
uniprot
Q969V5
canonical
ensembl
ENSG00000090432
resolver
ensp
ENSP00000264198
resolver
enst
ENST00000264198
resolver
genesymbol
MUL1
resolver
genesymbol_syn
C1orf166
resolver
genesymbol_syn
GIDE
resolver
genesymbol_syn
MAPL
resolver
genesymbol_syn
MULAN
resolver
genesymbol_syn
RNF218
resolver
hgnc
HGNC:25762
resolver
uniprot
B5M497
resolver
uniprot
Q7Z431
resolver
uniprot
Q9H9B5
resolver
uniprot_entry
MUL1_HUMAN
resolver
uniprot_sec
B5M497
resolver
uniprot_sec
Q7Z431
resolver
uniprot_sec
Q9H9B5
resolver
amino_acid_sequence
MESGGRPSLCQFILLGTTSVVTAALYSVYRQKARVSQELKGAKKVHLGEDLKSILSEAPGKCVPYAVIEGAVRSVKETLNSQFVENCKGVIQRLTLQEHKMVWNRTTHLWNDCSKIIHQRTNTVPFDLVPHEDGVDVAVRVLKPLDSVDLGLETVYEKFHPSIQSFTDVIGHYISGERPKGIQETEEMLKVGATLTGVGELVLDNNSVRLQPPKQGMQYYLSSQDFDSLLQRQESSVRLWKVLALVFGFATCATLFFILRKQYLQRQERLRLKQMQEEFQEHEAQLLSRAKPEDRESLKSACVVCLSSFKSCVFLECGHVCSCTECYRALPEPKKCPICRQAITRVIPLYNS
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: E3 ubiquitin-protein ligase activity, which accepts 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 proteasomal degradation (PubMed:22410793). Mediates polyubiquitination of cytoplasmic p53/TP53 at 'Lys-24' which targets TP53 for proteasomal degradation, thus reducing TP53 levels in the cytoplasm and mitochondrion (PubMed:21597459). Also involved in antiviral immunity by mediating 'Lys-63'-linked ubiquitination of STING1, promoting production of type I interferon (IFN-alpha and IFN-beta), whitout activating STING1-dependent NF-kappa-B signaling (PubMed:28763789). Proposed to preferentially act as a SUMO E3 ligase at physiological concentrations (PubMed:19407830). Involved in the modulation of innate immune defense against viruses by inhibiting RIGI-dependent antiviral response (PubMed:23399697). Can mediate RIGI sumoylation and disrupt its polyubiquitination (PubMed:23399697). Plays a role in the control of mitochondrial morphology by promoting mitochondrial fragmentation, and influences mitochondrial localization (PubMed:18207745, PubMed:18213395, PubMed:19407830). 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). {ECO:0000269|PubMed:18207745, ECO:0000269|PubMed:18213395, ECO:0000269|PubMed:18591963, ECO:0000269|PubMed:19407830, ECO:0000269|PubMed:22410793, ECO:0000269|PubMed:23399697, ECO:0000269|PubMed:24898855, ECO:0000269|PubMed:28763789}.
uniprot
proteins
mass_dalton
39800
uniprot
proteins
mutagenesis
MUTAGEN 260; /note="R->A: Protein is targeted to the ER; when associated with A-261."; /evidence="ECO:0000269|PubMed:18213395"; MUTAGEN 261; /note="K->A: Protein is targeted to the ER; when associated with A-260."; /evidence="ECO:0000269|PubMed:18213395"; MUTAGEN 302; /note="C->S: Failure to reduce TP53 levels and abolishes ligase activity; when associated with S-305."; /evidence="ECO:0000269|PubMed:21597459"; MUTAGEN 305; /note="C->S: Failure to reduce TP53 levels and abolishes ligase activity; when associated with S-302."; /evidence="ECO:0000269|PubMed:21597459"; MUTAGEN 319; /note="H->A: Abolishes E3 ubiquitin-protein ligase activity. No effect on mitochondrial localization."; /evidence="ECO:0000269|PubMed:18591963, ECO:0000269|PubMed:23399697"; MUTAGEN 339; /note="C->A: Abolishes ligase activity."; /evidence="ECO:0000269|PubMed:18213395
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:21597459, ECO:0000269|PubMed:28763789}.; PATHWAY: Protein modification; protein sumoylation. {ECO:0000269|PubMed:19407830}.
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30. {ECO:0000269|PubMed:25621951}.
uniprot
proteins
pubmed
12761501
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18207745
uniprot
proteins
pubmed
18213395
uniprot
proteins
pubmed
18591963
uniprot
proteins
pubmed
19407830
uniprot
proteins
pubmed
21597459
uniprot
proteins
pubmed
22410793
uniprot
proteins
pubmed
23399697
uniprot
proteins
pubmed
24898855
uniprot
proteins
pubmed
25621951
uniprot
proteins
pubmed
28763789
uniprot
proteins
pubmed
40105103
uniprot
proteins
sequence_length
352
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:18207745, ECO:0000269|PubMed:18213395, ECO:0000269|PubMed:18591963, ECO:0000269|PubMed:21597459}; Multi-pass membrane protein {ECO:0000255}. Peroxisome {ECO:0000269|PubMed:18207745}. Note=Transported in mitochondrion-derived vesicles from the mitochondrion to the peroxisome. {ECO:0000269|PubMed:18207745}.
uniprot
proteins
transmembrane_region
TRANSMEM 9..29; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 239..259; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins