Search Results
Overview
| Uniprot ID | Q13268 |
|---|---|
| Protein Name | Dehydrogenase/reductase SDR family member 2, mitochondrial |
| Gene Name | DHRS2 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 206 | LALELAPKDIRVNCV |
| 224 | IIKTDFSKVFHGNES |
| 234 | HGNESLWKNFKEHHQ |
| 237 | ESLWKNFKEHHQLQR |
| 31 | SSTGIDRKGVLANRV |
| 69 | HVVISSRKQQNVDRA |
| 79 | NVDRAMAKLQGEGLS |
| 96 | GIVCHVGKAEDREQL |
Function
NADPH-dependent oxidoreductase which catalyzes the reduction of dicarbonyl compounds. Displays reductase activity in vitro with 3,4-hexanedione, 2,3-heptanedione and 1-phenyl-1,2-propanedione as substrates (PubMed:16685466). May function as a dicarbonyl reductase in the enzymatic inactivation of reactive carbonyls involved in covalent modification of cellular components (PubMed:16685466). Also displays a minor hydroxysteroid dehydrogenase activity toward bile acids such as ursodeoxycholic acid (UDCA) and isoursodeoxycholic acid (isoUDCA), which makes it unlikely to control hormone levels (PubMed:16685466). Doesn't show any activity in vitro with retinoids and sugars as substrates (PubMed:16685466). Attenuates MDM2-mediated p53/TP53 degradation, leading to p53/TP53 stabilization and increased transcription activity, resulting in the accumulation of MDM2 and CDKN1A/p21 (PubMed:20547751). Reduces proliferation, migration and invasion of cancer cells and well as the production of ROS in cancer (PubMed:29106393)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Biological Process | GO:0009636 | response to toxic substance |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005759 | mitochondrial matrix |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0005635 | nuclear envelope |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0004090 | carbonyl reductase (NADPH) activity |
| Molecular Function | GO:0016616 | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| Biological Process | GO:0008207 | C21-steroid hormone metabolic process |
| Biological Process | GO:0034599 | cellular response to oxidative stress |
| Biological Process | GO:0022900 | electron transport chain |
| Biological Process | GO:0043011 | myeloid dendritic cell differentiation |
| Biological Process | GO:0043066 | negative regulation of apoptotic process |
| Biological Process | GO:0008285 | negative regulation of cell population proliferation |
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] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.