MUL1 (Vector Vector will be determined during the manufacturing process, either pENTR223.1 or pUC, A

Length: 1059 Sequence: atggagagcg gagggcggcc ctcgctgtgc cagttcatcc tcctgggcac cacctctgtg gtcaccgccg ccctgtactc cgtgtaccgg cagaaggccc gggtctccca agagctcaag ggagctaaaa aagttcattt gggtgaagat ttaaagagta ttctttcaga agctccagga aaatgcgtgc cttatgctgt tatagaagga gctgtgcggt ctgttaaaga aacgcttaac agccagtttg tggaaaactg caagggggta attcagcggc tgacacttca ggagcacaag atggtgtgga atcgaaccac ccacctttgg aatgattgct caaagatcat tcatcagagg accaacacag tgccctttga cctggtgccc cacgaggatg gcgtggatgt ggctgtgcga gtgctgaagc ccctggactc agtggatctg ggtctagaga ctgtgtatga gaagttccac ccctcgattc agtccttcac cgatgtcatc ggccactaca tcagcggtga gcggcccaaa ggcatccaag agaccgagga gatgctgaag gtgggggcca ccctcacagg ggttggcgaa ctggtcctgg acaacaactc tgtccgcctg cagccgccca aacaaggcat gcagtactat ctaagcagcc aggacttcga cagcctgctg cagaggcagg agtcgagcgt caggctctgg aaggtgctgg cgctggtttt tggctttgcc acatgtgcca ccctcttctt cattctccgg aagcagtatc tgcagcggca ggagcgcctg cgcctcaagc agatgcagga ggagttccag gagcatgagg cccagctgct gagccgagcc aagcctgagg acagggagag tctgaagagc gcctgtgtag tgtgtctgag cagcttcaag tcctgcgtct ttctggagtg tgggcacgtt tgttcctgca ccgagtgcta ccgcgccttg ccagagccca agaagtgccc tatctgcaga caggcgatca cccgggtgat acccctgtac Protein 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). Mediates polyubiquitination of cytoplasmic TP53 at 'Lys-24' which targets TP53 for proteasomal degradation, thus reducing TP53 levels in the cytoplasm and mitochondrion (PubMed:21597459). 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). [The UniProt Consortium]