Mitochondrial ubiquitin ligase activator of NFKB 1 (EC 2.3.2.27) (E3 SUMO-protein ligase MUL1) (E3 ubiquitin-protein ligase MUL1) (Growth inhibition and death E3 ligase) (Mitochondrial-anchored protein ligase) (Protein Hades) (Putative NF-kappa-B-activating protein 266) (RING finger protein 218) (RING-type E3 ubiquitin transferase NFKB 1)
1_MESGG 6_ RPSLC 11_ QFILL 16_ GTTSV 21_ VTAAL 26_ YSVYR 31_ QKARV 36_ SQELK 41_ GAKKV 46_ HLGED 51_ LKSIL 56_ SEAPG 61_ KCVPY 66_ AVIEG 71_ AVRSV 76_ KETLN 81_ SQFVE 86_ NCKGV 91_ IQRLT 96_ LQEHK 101_ MVWNR 106_ TTHLW 111_ NDCSK 116_ IIHQR 121_ TNTVP 126_ FDLVP 131_ HEDGV 136_ DVAVR 141_ VLKPL 146_ DSVDL 151_ GLETV 156_ YEKFH 161_ PSIQS 166_ FTDVI 171_ GHYIS 176_ GERPK 181_ GIQET 186_ EEMLK 191_ VGATL 196_ TGVGE 201_ LVLDN 206_ NSVRL 211_ QPPKQ 216_ GMQYY 221_ LSSQD 226_ FDSLL 231_ QRQES 236_ SVRLW 241_ KVLAL 246_ VFGFA 251_ TCATL 256_ FFILR 261_ KQYLQ 266_ RQERL 271_ RLKQM 276_ QEEFQ 281_ EHEAQ 286_ LLSRA 291_ KPEDR 296_ ESLKS 301_ ACVVC 306_ LSSFK 311_ SCVFL 316_ ECGHV 321_ CSCTE 326_ CYRAL 331_ PEPKK 336_ CPICR 341_ QAITR 346_VIPLY
1: 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 proteasomal 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: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). 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)