| UniProt ID | AL3A1_HUMAN | |
|---|---|---|
| UniProt AC | P30838 | |
| Protein Name | Aldehyde dehydrogenase, dimeric NADP-preferring | |
| Gene Name | ALDH3A1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 453 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde (Probable). They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation (Probable). Oxidizes medium and long chain aldehydes into non-toxic fatty acids. [PubMed: 1737758 Preferentially oxidizes aromatic aldehyde substrates] | |
| Protein Sequence | MSKISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEEVVYVLEEIEYMIQKLPEWAADEPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYLDKDLYPVINGGVPETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIEGQKVAYGGTGDAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIVHITLHSLPFGGVGNSGMGSYHGKKSFETFSHRRSCLVRPLMNDEGLKVRYPPSPAKMTQH | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MSKISEAVK ------CCHHHHHHH | 38.40 | 20068231 | |
| 2 | Acetylation | ------MSKISEAVK ------CCHHHHHHH | 38.40 | 22814378 | |
| 3 | Acetylation | -----MSKISEAVKR -----CCHHHHHHHH | 49.29 | 19608861 | |
| 5 | Phosphorylation | ---MSKISEAVKRAR ---CCHHHHHHHHHH | 24.20 | 22496350 | |
| 163 | Phosphorylation | QYLDKDLYPVINGGV HHHCCCCHHHHCCCC | 12.94 | 110743635 | |
| 178 | Acetylation | PETTELLKERFDHIL CCHHHHHHHHCCEEE | 60.51 | 19608861 | |
| 178 | Ubiquitination | PETTELLKERFDHIL CCHHHHHHHHCCEEE | 60.51 | 19608861 | |
| 186 | Phosphorylation | ERFDHILYTGSTGVG HHCCEEEEECCCCHH | 14.41 | 71735 | |
| 194 | Acetylation | TGSTGVGKIIMTAAA ECCCCHHHHHHHHHH | 27.01 | 19608861 | |
| 198 | Phosphorylation | GVGKIIMTAAAKHLT CHHHHHHHHHHHHCC | 11.61 | 110743641 | |
| 202 | Acetylation | IIMTAAAKHLTPVTL HHHHHHHHHCCCEEE | 34.13 | 25825284 | |
| 205 | Phosphorylation | TAAAKHLTPVTLELG HHHHHHCCCEEEEEC | 18.55 | 110743647 | |
| 208 | Phosphorylation | AKHLTPVTLELGGKS HHHCCCEEEEECCCC | 18.73 | 22817900 | |
| 214 | Ubiquitination | VTLELGGKSPCYVDK EEEEECCCCCCCCCC | 49.80 | - | |
| 221 | Ubiquitination | KSPCYVDKNCDLDVA CCCCCCCCCCCCCHH | 49.81 | - | |
| 269 | Ubiquitination | EKLKKSLKEFYGEDA HHHHHHHHHHHCCHH | 53.52 | 19608861 | |
| 269 | Acetylation | EKLKKSLKEFYGEDA HHHHHHHHHHHCCHH | 53.52 | 19608861 | |
| 272 | Phosphorylation | KKSLKEFYGEDAKKS HHHHHHHHCCHHHHH | 22.24 | 110743653 | |
| 277 | Ubiquitination | EFYGEDAKKSRDYGR HHHCCHHHHHCCHHH | 64.70 | - | |
| 287 | Phosphorylation | RDYGRIISARHFQRV CCHHHHHCHHHHHHH | 19.51 | 24719451 | |
| 302 | Ubiquitination | MGLIEGQKVAYGGTG HHHHCCEEEECCCCC | 39.42 | - | |
| 305 | Phosphorylation | IEGQKVAYGGTGDAA HCCEEEECCCCCCHH | 21.05 | 18083107 | |
| 399 | Phosphorylation | IVHITLHSLPFGGVG EEEEEEECCCCCCCC | 40.63 | 46162019 | |
| 427 | Phosphorylation | ETFSHRRSCLVRPLM CCCCCCCCEEEEECC | 16.26 | 28188228 | |
| 443 | Phosphorylation | DEGLKVRYPPSPAKM CCCCCEECCCCCCCC | 23.60 | 29396449 | |
| 446 | Phosphorylation | LKVRYPPSPAKMTQH CCEECCCCCCCCCCC | 32.74 | 27422710 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AL3A1_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of AL3A1_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| SRF_HUMAN | SRF | physical | 21988832 | |
| CYHR1_HUMAN | CYHR1 | physical | 21988832 | |
| FXL12_HUMAN | FBXL12 | physical | 26124079 | |
| ZN446_HUMAN | ZNF446 | physical | 28514442 | |
| AL3A2_HUMAN | ALDH3A2 | physical | 28514442 | |
| IGLL5_HUMAN | IGLL5 | physical | 28514442 | |
| H2A2C_HUMAN | HIST2H2AC | physical | 28514442 | |
| RCCD1_HUMAN | RCCD1 | physical | 28514442 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3; LYS-178; LYS-194 ANDLYS-269, AND MASS SPECTROMETRY. | |