Protein Name:
E3 ubiquitin-protein ligase MARCHF5
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UniprotKB/SwissProt ID: Q3KNM2 (Q3KNM2)
Gene Name:
Marchf5
Organism: Mus musculus (Mouse)
Function: Mitochondrial E3 ubiquitin-protein ligase that plays a crucial role in the control of mitochondrial morphology by acting as a positive regulator of mitochondrial fission and as an important regulator of immune response. Plays a crucial role in maintaining mitochondrial homeostasis by regulating the dynamics of mitochondria through the ubiquitination of key proteins involved in fission and fusion such as FIS1, DNM1L and MFN1 (By similarity). Acts as a critical determinant of mitotic apoptosis through both MCL1-dependent and -independent pathways (PubMed:36329234). Turns off persistent immune signaling by degrading oligomeric complexes of retinoic acid-inducible gene I/DDX58 and mitochondrial antiviral-signaling protein/MAVS formed upon RNA virus infection. Promotes STING-mediated type-I interferon production via 'Lys-63'-linked ubiquitination of STING1 thereby preserving its activity and preventing the formation of inactive STING1 polymers. Plays also an essential role in the formation of PEX3-containing vesicles in the de novo biogenesis of peroxisomes from mitochondria. Acts as a regulator of NLRP3 inflammasome activation on the mitochondria by mediating the 'Lys-27'-linked polyubiquitination of NLRP3, positively regulating the NLRP3-NEK7 complex formation and NLRP3 oligomerization (PubMed:37575012)
Other Modifications: View all modification sites in dbPTM
Protein Subcellular Localization: Mitochondrion outer membrane. Endoplasmic reticulum membrane
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Graphical Visualization of S-nitrosylation Sites:
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The S-nitrosylation sites of Q3KNM2
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| No. |
Position |
S-nitrosylated Peptide |
Secondary Structure of S-nitrosylated Peptide |
Solvent Accessibility of nitrosylated Site |
PubMed ID |
| 1 |
46 |
RGSTKWVHQA C LQRWVDEKQR |
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