Search Results
Overview
| Uniprot ID | P15559 |
|---|---|
| Protein Name | NAD(P)H dehydrogenase [quinone] 1 |
| Gene Name | NQO1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 209 | IQILEGWKKRLENIW |
| 23 | TSFNYAMKEAAAAAL |
| 251 | QDEEKNKKFGLSVGH |
| 262 | SVGHHLGKSIPTDNQ |
| 271 | IPTDNQIKARK**** |
| 31 | EAAAAALKKKGWEVV |
| 32 | AAAAALKKKGWEVVE |
| 90 | PDIVAEQKKLEAADL |
Function
Flavin-containing quinone reductase that catalyzes two-electron reduction of quinones to hydroquinones using either NADH or NADPH as electron donors. In a ping-pong kinetic mechanism, the electrons are sequentially transferred from NAD(P)H to flavin cofactor and then from reduced flavin to the quinone, bypassing the formation of semiquinone and reactive oxygen species (By similarity) (PubMed:8999809, PubMed:9271353). Regulates cellular redox state primarily through quinone detoxification. Reduces components of plasma membrane redox system such as coenzyme Q and vitamin quinones, producing antioxidant hydroquinone forms. In the process may function as superoxide scavenger to prevent hydroquinone oxidation and facilitate excretion (PubMed:15102952, PubMed:8999809, PubMed:9271353). Alternatively, can activate quinones and their derivatives by generating redox reactive hydroquinones with DNA cross-linking antitumor potential (PubMed:8999809). Acts as a gatekeeper of the core 20S proteasome known to degrade proteins with unstructured regions. Upon oxidative stress, interacts with tumor suppressors TP53 and TP73 in a NADH-dependent way and inhibits their ubiquitin-independent degradation by the 20S proteasome (PubMed:15687255, PubMed:28291250)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0045202 | synapse |
| Molecular Function | GO:0004128 | cytochrome-b5 reductase activity, acting on NAD(P)H |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0003955 | NAD(P)H dehydrogenase (quinone) activity |
| Molecular Function | GO:0050136 | NADH dehydrogenase (quinone) (non-electrogenic) activity |
| Molecular Function | GO:0008753 | NADPH dehydrogenase (quinone) activity |
| Molecular Function | GO:0003723 | RNA binding |
| Biological Process | GO:0045454 | cell redox homeostasis |
| Biological Process | GO:0034599 | cellular response to oxidative stress |
| Biological Process | GO:0045087 | innate immune response |
| Biological Process | GO:0110076 | negative regulation of ferroptosis |
| Biological Process | GO:0042177 | negative regulation of protein catabolic process |
| Biological Process | GO:0006809 | nitric oxide biosynthetic process |
| Biological Process | GO:0030163 | protein catabolic process |
| Biological Process | GO:0000209 | protein polyubiquitination |
| Biological Process | GO:0019430 | removal of superoxide radicals |
| Biological Process | GO:0032496 | response to lipopolysaccharide |
| Biological Process | GO:0006979 | response to oxidative stress |
| Biological Process | GO:0009636 | response to toxic substance |
| Biological Process | GO:0007271 | synaptic transmission, cholinergic |
| Biological Process | GO:0006743 | ubiquinone metabolic process |
| Biological Process | GO:0042360 | vitamin E metabolic process |
| Biological Process | GO:0042373 | vitamin K metabolic process |
| Biological Process | GO:0006805 | xenobiotic 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] 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.
[3] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.