Search Results
Overview
| Uniprot ID | P00352 |
|---|---|
| Protein Name | Aldehyde dehydrogenase 1A1 |
| Gene Name | ALDH1A1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 139 | YCAGWADKIQGRTIP |
| 22 | DLKIQYTKIFINNEW |
| 252 | TGSTEVGKLIKEAAG |
| 255 | TEVGKLIKEAAGKSN |
| 260 | LIKEAAGKSNLKRVT |
| 329 | RSVERAKKYILGNPL |
| 348 | TQGPQIDKEQYDKIL |
| 36 | WHDSVSGKKFPVFNP |
| 362 | LDLIESGKKEGAKLE |
| 367 | SGKKEGAKLECGGGP |
| 37 | HDSVSGKKFPVFNPA |
| 398 | TDEMRIAKEEIFGPV |
| 410 | GPVQQIMKFKSLDDV |
| 412 | VQQIMKFKSLDDVIK |
| 419 | KSLDDVIKRANNTFY |
| 435 | LSAGVFTKDIDKAIT |
| 490 | FHEYTEVKTVTVKIS |
| 495 | EVKTVTVKISQKNS* |
| 62 | GDKEDVDKAVKAARQ |
| 91 | ERGRLLYKLADLIER |
Function
Cytosolic dehydrogenase that catalyzes the irreversible oxidation of a wide range of aldehydes to their corresponding carboxylic acid (PubMed:12941160, PubMed:15623782, PubMed:17175089, PubMed:19296407, PubMed:25450233, PubMed:26373694, PubMed:25413692). Functions downstream of retinol dehydrogenases and catalyzes the oxidation of retinaldehyde into retinoic acid, the second step in the oxidation of retinol/vitamin A into retinoic acid (PubMed:25413692). This pathway is crucial to control the levels of retinol and retinoic acid, two important molecules which excess can be teratogenic and cytotoxic (PubMed:25413692). Also oxidizes aldehydes resulting from lipid peroxidation like (E)-4-hydroxynon-2-enal/HNE, malonaldehyde and hexanal that form protein adducts and are highly cytotoxic. By participating for instance to the clearance of (E)-4-hydroxynon-2-enal/HNE in the lens epithelium prevents the formation of HNE-protein adducts and lens opacification (PubMed:12941160, PubMed:15623782, PubMed:19296407). Also functions downstream of fructosamine-3-kinase in the fructosamine degradation pathway by catalyzing the oxidation of 3-deoxyglucosone, the carbohydrate product of fructosamine 3-phosphate decomposition, which is itself a potent glycating agent that may react with lysine and arginine side-chains of proteins (PubMed:17175089). Also has an aminobutyraldehyde dehydrogenase activity and is probably part of an alternative pathway for the biosynthesis of GABA/4-aminobutanoate in midbrain, thereby playing a role in GABAergic synaptic transmission (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0030424 | axon |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0045202 | synapse |
| Molecular Function | GO:0106373 | 3-deoxyglucosone dehydrogenase activity |
| Molecular Function | GO:0140087 | acetaldehyde dehydrogenase (NAD+) activity |
| Molecular Function | GO:0004029 | aldehyde dehydrogenase (NAD+) activity |
| Molecular Function | GO:0019145 | aminobutyraldehyde dehydrogenase (NAD+) activity |
| Molecular Function | GO:0005497 | androgen binding |
| Molecular Function | GO:0018479 | benzaldehyde dehydrogenase (NAD+) activity |
| Molecular Function | GO:0005096 | GTPase activator activity |
| Molecular Function | GO:0051287 | NAD binding |
| Molecular Function | GO:0001758 | retinal dehydrogenase (NAD+) activity |
| Biological Process | GO:0006081 | aldehyde metabolic process |
| Biological Process | GO:0110095 | cellular detoxification of aldehyde |
| Biological Process | GO:0030392 | fructosamine catabolic process |
| Biological Process | GO:0009449 | gamma-aminobutyric acid biosynthetic process |
| Biological Process | GO:0036438 | maintenance of lens transparency |
| Biological Process | GO:0120163 | negative regulation of cold-induced thermogenesis |
| Biological Process | GO:0001523 | retinoid metabolic process |
| Biological Process | GO:0042572 | retinol metabolic process |
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.