Search Results
Overview
| Uniprot ID | O95831 |
|---|---|
| Protein Name | Apoptosis-inducing factor 1, mitochondrial |
| Gene Name | AIFM1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 109 | LGLTPEQKQKKAALS |
| 112 | TPEQKQKKAALSASE |
| 189 | SDDPNVTKTLRFKQW |
| 199 | RFKQWNGKERSIYFQ |
| 232 | VAVLTGKKVVQLDVR |
| 388 | IKLKDGRKVETDHIV |
| 518 | ATAQDNPKSATEQSG |
| 593 | PIARKIIKDGEQHED |
Function
Functions both as NADH oxidoreductase and as regulator of apoptosis (PubMed:17094969, PubMed:20362274, PubMed:23217327, PubMed:33168626). In response to apoptotic stimuli, it is released from the mitochondrion intermembrane space into the cytosol and to the nucleus, where it functions as a proapoptotic factor in a caspase-independent pathway (PubMed:20362274). Release into the cytoplasm is mediated upon binding to poly-ADP-ribose chains (By similarity). The soluble form (AIFsol) found in the nucleus induces 'parthanatos' i.e. caspase-independent fragmentation of chromosomal DNA (PubMed:20362274). Binds to DNA in a sequence-independent manner (PubMed:27178839). Interacts with EIF3G, and thereby inhibits the EIF3 machinery and protein synthesis, and activates caspase-7 to amplify apoptosis (PubMed:17094969). Plays a critical role in caspase-independent, pyknotic cell death in hydrogen peroxide-exposed cells (PubMed:19418225). In contrast, participates in normal mitochondrial metabolism. Plays an important role in the regulation of respiratory chain biogenesis by interacting with CHCHD4 and controlling CHCHD4 mitochondrial import (PubMed:26004228)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005743 | mitochondrial inner membrane |
| Cellular Component | GO:0005758 | mitochondrial intermembrane space |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0048471 | perinuclear region of cytoplasm |
| Molecular Function | GO:0003677 | DNA binding |
| Molecular Function | GO:0071949 | FAD binding |
| Molecular Function | GO:0016174 | NAD(P)H oxidase H2O2-forming activity |
| Molecular Function | GO:0003954 | NADH dehydrogenase activity |
| Molecular Function | GO:0016651 | oxidoreductase activity, acting on NAD(P)H |
| Molecular Function | GO:0072572 | poly-ADP-D-ribose binding |
| Molecular Function | GO:0046983 | protein dimerization activity |
| Biological Process | GO:0006915 | apoptotic process |
| Biological Process | GO:1904045 | cellular response to aldosterone |
| Biological Process | GO:0071392 | cellular response to estradiol stimulus |
| Biological Process | GO:0070301 | cellular response to hydrogen peroxide |
| Biological Process | GO:0071456 | cellular response to hypoxia |
| Biological Process | GO:0071732 | cellular response to nitric oxide |
| Biological Process | GO:0070059 | intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress |
| Biological Process | GO:0160203 | mitochondrial disulfide relay system |
| Biological Process | GO:0033108 | mitochondrial respiratory chain complex assembly |
| Biological Process | GO:0030182 | neuron differentiation |
| Biological Process | GO:0043065 | positive regulation of apoptotic process |
| Biological Process | GO:0060545 | positive regulation of necroptotic process |
| Biological Process | GO:0043525 | positive regulation of neuron apoptotic process |
| Biological Process | GO:0045041 | protein import into mitochondrial intermembrane space |
| Biological Process | GO:0002931 | response to ischemia |
| Biological Process | GO:1902065 | response to L-glutamate |
| Biological Process | GO:0009636 | response to toxic substance |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.
[3] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.