AIFM2 — Apoptosis inducing factor mitochondria associated 2
AIFM2 belongs to a gene co-expression module in 1 of 30 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.
AIFM2's module in each cell type
| Cell type | Module | Shares the module with | |
|---|---|---|---|
| Colonocytes | Colonocyte Detoxification Nutrient processing | ADORA2B, AKR1B10, ATL3, ATP6V0D1, CBLC, CDH17, CSTB, FUOM +21 more | View in SCUBA |
About the gene
| Synonyms | AMID, FLJ14497, FSP1, PRG3 |
|---|---|
| Chromosome | 10: 70098223-70132934 |
| Predicted location | Intracellular |
| Essential gene | No |
| Protein class | Predicted intracellular proteins |
| Molecular function | DNA-binding, Oxidoreductase |
Function
A NAD(P)H-dependent oxidoreductase that acts as a key inhibitor of ferroptosis. At the plasma membrane, catalyzes reduction of coenzyme Q/ubiquinone-10 to ubiquinol-10, a lipophilic radical-trapping antioxidant that prevents lipid oxidative damage and consequently ferroptosis. Acts in parallel to GPX4 to suppress phospholipid peroxidation and ferroptosis. This anti-ferroptotic function is independent of cellular glutathione levels. Also acts as a potent radical-trapping antioxidant by mediating warfarin-resistant vitamin K reduction in the canonical vitamin K cycle: catalyzes NAD(P)H-dependent reduction of vitamin K (phylloquinone, menaquinone-4 and menadione) to hydroquinone forms. Hydroquinones act as potent radical-trapping antioxidants inhibitor of phospholipid peroxidation and ferroptosis. May play a role in mitochondrial stress signaling. Upon oxidative stress, associates with the lipid peroxidation end product 4-hydroxy-2-nonenal (HNE) forming a lipid adduct devoid of oxidoreductase activity, which then translocates from mitochondria into the nucleus triggering DNA damage and cell death. Capable of DNA binding in a non-sequence specific way.
Human Protein Atlas · Open Targets · UniProt
Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.