MUL1 Recombinant Rabbit Monoclonal Antibody [PSH15-17] (HA723721)

UNIPROT #

Q969V5

PROTEIN NAME

MUL1

SYNONYMS

0610009K11Rik antibody;AV000801 antibody;C1orf166 antibody;Chromosome 1 open reading frame 166 antibody;E3 SUMO-protein ligase MUL1 antibody;E3 ubiquitin ligase antibody;E3 ubiquitin protein ligase MUL1 antibody;E3 ubiquitin-protein ligase MUL1 antibody;FLJ12875 antibody;GIDE antibody;Growth inhibition and death E3 ligase antibody;MAPL antibody;Mitochondrial anchored protein ligase antibody;mitochondrial E3 ubiquitin ligase 1 antibody;mitochondrial E3 ubiquitin protein ligase 1 antibody;Mitochondrial ubiquitin ligase activator of NFKB 1 antibody;Mitochondrial-anchored protein ligase antibody;MUL1 antibody;MUL1_HUMAN antibody;MULAN antibody;Putative NF kappa B activating protein 266 antibody;Putative NF-kappa-B-activating protein 266 antibody;RGD1309944 antibody;RING finger protein 218 antibody;RNF218 antibody;RP11-401M16.2 antibody;RP23-25C1.10-002 antibody

SUBCELLULAR LOCATION

Mitochondrion outer membrane, Peroxisome.

FUNCTION

Mitochondrial E3 ubiquitin protein ligase 1 (MUL1) is an enzyme that in humans is encoded by the MUL1 gene on chromosome 1. This enzyme localizes to the outer mitochondrial membrane, where it regulates mitochondrial morphology and apoptosis through multiple pathways, including the Akt, JNK, and NF-κB. Its proapoptotic function thus implicates it in cancer and Parkinson's disease. 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. Is anchored in the outer mitochondrial membrane. Plays a role in the control of mitochondrial morphology. Promotes mitochondrial fragmentation and influences mitochondrial localization. The function may implicate its ability to sumoylate DNM1L. Has been observed to shuttle between the mitochondria and peroxisome, where it may also help regulate peroxisome fission. 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. Can also activate NF-κB to initiate mitochondria-to-nucleus signaling under stress.