重组人E3 ubiquitin-protein ligase MUL1
Recombinant Human E3 ubiquitin-protein ligase MUL1
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Recombinant Human E3 ubiquitin-protein ligase MUL1 is a Human Full Length protein, in the 1 to 352 aa range, expressed in Wheat germ, suitable for ELISA, WB.
查看别名
C1orf166, GIDE, MAPL, MULAN, RNF218, MUL1, Mitochondrial ubiquitin ligase activator of NFKB 1, 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
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human E3 ubiquitin-protein ligase MUL1 (AB153508)
ab153508 on a 12.5% SDS-PAGE stained with Coomassie Blue.
反应性数据
序列信息
性能和储存信息
运输条件
推荐的短期储存条件
推荐的长期储存条件
分装信息
储存信息
补充信息
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
MUL1 regulates numerous cellular processes such as apoptosis mitophagy and the mitochondrial dynamics by modulating the stability of target proteins. MUL1 operates independently and does not require a specific E2 enzyme for its function. Additionally it participates in cellular homeostasis by mediating the degradation of proteins that impact mitochondrial fusion and fission events. Since MUL1 forms part of the regulatory mechanisms governing cellular adaptation and survival its levels and activity are finely controlled within the cell.
Pathways
MUL1 is actively involved in the mitophagy and DNA damage response pathways. Its role in the mitophagy pathway links MUL1 to PINK1 and PARKIN proteins that are critical for the removal of damaged mitochondria. In the context of the DNA damage response MUL1 functions to reprogram metabolic pathways yielding protection against cellular stress. This activity associates it with proteins like p53 a well-known tumor suppressor anchoring its presence in mechanisms of cellular defense.
特殊说明
形式
Liquid
常规信息
功能
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).
翻译后修饰
Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30.
亚细胞定位
Mitochondrion outer membrane
靶点信息
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