Search Results
Overview
| Uniprot ID | P49189 |
|---|---|
| Protein Name | 4-trimethylaminobutyraldehyde dehydrogenase |
| Gene Name | ALDH9A1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 298 | GTRVFVQKEILDKFT |
| 30 | ADASGTEKAFEPATG |
| 303 | VQKEILDKFTEEVVK |
| 310 | KFTEEVVKQTQRIKI |
| 316 | VKQTQRIKIGDPLLE |
| 344 | ERVLGFVKVAKEQGA |
| 347 | LGFVKVAKEQGAKVL |
| 352 | VAKEQGAKVLCGGDI |
| 366 | IYVPEDPKLKDGYYM |
| 49 | TFTCSGEKEVNLAVQ |
| 59 | NLAVQNAKAAFKIWS |
| 68 | AFKIWSQKSGMERCR |
Function
Converts gamma-trimethylaminobutyraldehyde into gamma-butyrobetaine with high efficiency (in vitro). Can catalyze the irreversible oxidation of a broad range of aldehydes to the corresponding acids in an NAD-dependent reaction, but with low efficiency. Catalyzes the oxidation of aldehydes arising from biogenic amines and polyamines
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005739 | mitochondrion |
| Molecular Function | GO:0047105 | 4-trimethylammoniobutyraldehyde 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:0018467 | formaldehyde dehydrogenase (NAD+) activity |
| Molecular Function | GO:0036094 | small molecule binding |
| Biological Process | GO:0006081 | aldehyde metabolic process |
| Biological Process | GO:0045329 | carnitine biosynthetic process |
| Biological Process | GO:0051289 | protein homotetramerization |
| Biological Process | GO:0042429 | serotonin catabolic 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] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.
[4] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.