protein
| interacting with MAP3K7/TAK1 |
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AKT1 was found to directly interact with MUL1 and to be ubiquitinated by MUL1 |
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MUL1 E3 ubiquitin ligase is a specific substrate of HTRA2, and inactivation of HTRA2 protease leads to the deregulation of mitochondrial MUL1 E3 ubiquitin ligase and increased mitophagy |
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increase in MUL1 protein levels also fragments the mitochondria through the ubiquitination and subsequent proteasomal degradation of MFN2 |
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MUL1 is a novel regulator of the DDX58-like receptor-dependent antiviral response, that otherwise functions to limit inflammation |
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MUL1 is involved in multiple biological pathways, and the interaction of GABARAP with MUL1-UBE2E3 supports the role of MUL1 as an important regulator of mitophagy and provides a plausible mechanism for its function in this process |
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MUL1, a mitochondria-localized E3 ligase, regulates selenite-induced mitophagy in an ATG5 and ULK1-dependent manner |
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specifically activated NFKB1 dependent gene expression in an E3 ligase activity-dependent manner |
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MUL1 appears to have some antagonistic functions to MARCH5 whereby MUL1 has a pro-mitophagy affect |
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in head and neck cancer (HNC) acts as negative regulator against AKT1 |
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inactivation of MUL1 ligase leads to accumulation of UBXN7, with concomitant increase in HIF1A protein levels, reduction in oxidative phosphorylation, and increased glycolysis |