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NQO1 (NAD (P)H dehydrogenase, quinone 1)

Written2001-12David Ross
School of Pharmacy, University of Colorado Health Sciences Center, Denver 80262, USA
Updated2004-06David Ross
School of Pharmacy, University of Colorado Health Sciences Center, Denver 80262, USA

(Note : for Links provided by Atlas : click)

Identity

Alias_namesNMOR1
DIA4
diaphorase (NADH/NADPH) (cytochrome b-5 reductase)
NAD(P)H dehydrogenase, quinone 1
Alias_symbol (synonym)DHQU
QR1
DTD
Other aliasDT-Diaphorase
NMO1
HGNC (Hugo) NQO1
LocusID (NCBI) 1728
Atlas_Id 375
Location 16q22.1  [Link to chromosome band 16q22]
Location_base_pair Starts at 69709401 and ends at 69726668 bp from pter ( according to hg19-Feb_2009)  [Mapping NQO1.png]
 
  NQO1 (16q22) - Courtesy Mariano Rocchi, Resources for Molecular Cytogenetics.
Fusion genes
(updated 2017)		Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
FAM155A (13q33.3) / NQO1 (16q22.1)NQO1 (16q22.1) / DYRK1A (21q22.13)NQO1 (16q22.1) / NQO1 (16q22.1)
NQO1 (16q22.1) / TBRG4 (7p13)NQO1 (16q22.1) / TTC37 (5q15)NQO1 (16q22.1) / XRN1 (3q23)
SNHG6 (8q13.1) / NQO1 (16q22.1)

DNA/RNA

Description Spans approximately 20 kb consisting of 6 exons and 5 introns. Highly inducible protein and the 5' flanking region contains an AP2, ARE or EpRE(antioxidant or electrophile responsive element) and an XRE (xenobiotic responsive element).
Transcription Three mRNA sizes (1.2, 1.7 and 2.7 kb) have been observed due to multiple polyadenylation sites. An alternatively spliced form of NQO1 mRNA lacking exon 4 is also possible although the corresponding truncated protein has not been detected.

Protein

Description NQO1 is a flavoprotein which functions as a homodimer. The physiological dimer has one catalytic site per monomer. Each monomer consists of 273 amino acids.
For structures of human recombinant NQO1 with quinones complexed in the active site see Structures of recombinant human and mouse NAD(P)H:quinone oxidoreductases: species comparison and structural changes with substrate binding and release (Structure Explorer - 1D4A) and. Structure-based development of antitumor quinones. Complexes of NQO1 with three potential chemotherapeutic quinones (Structure Explorer - 1H66).
Expression NQO1 is expressed in human epithelial and endothelial tissues and at high levels throughout many human solid tumors.
Localisation NQO1 is a mainly cytosolic enzyme (approx. 90%) although it has also been localized in smaller amounts to mitochondria, endoplasmic reticulum and nucleus.
Function NQO1 catalyzes obligate two electron reduction of a wide variety of substrates. The most efficient substrates are quinones but the enzyme will also reduce quinone-imines, nitro and azo compounds. The enzyme functions via a hydride transfer mechanism and requires a pyridine nucleotide cofactor. Reduction proceeds with equal facility with both NADH and NADPH. NQO1 can generate antioxidant forms of both vitamin E and ubiquinone after free radical attack. The capability to protect cells from oxidative challenge and the ability to reduce quinones via an obligate two electron mechanism, which precludes generation of reactive oxygen radicals, demonstrates that NQO1 is a chemoprotective enzyme. NQO1 knockout mice demonstrated increased susceptibility to benzo(a)pyrene and 7,12-dimethylbenz(a) anthracene induced skin carcinogenesis. NQO1 has been proposed to stabilize the tumor suppressor gene p53 and has been shown to interact with p53 in a protein-protein interaction.

Certain compounds such as antitumor quinones, however, can be bioactivated by two electron reduction and in these cases NQO1 serves as an activating enzyme. Because of the high levels of NQO1 in certain tumors, this has led to an interest in designing compounds which can be efficiently bioactivated by NQO1 as antitumor agents.

Homology Amino acid homology across species is high (mouse/human 86%, mouse/rat -94%, human/rat 86%). NQO2 is a separate gene product demonstrating 49% and 54% similarity at the amino acid and nucleotide levels respectively.

Mutations

Germinal Two polymorphisms have been characterized. The NQO1 *2 allele represents a C609T change in the cDNA coding for a Pro187Ser change in the enzyme. The NQO1 *3 allele is a C465T change in the cDNA coding for an Arg139Trp change. The NQO1 * 2 allele is much more frequent than the *3 allele and has profound consequences for phenotype. The NQO1 *2 protein has diminished catalytic activity and the protein is rapidly degraded by the ubiquitin-proteasomal system. As a result, cells and tissues carrying the homozygous NQO1 *2 allele have no detectable NQO1 activity and at best, trace levels of NQO1 protein. The NQO1 *2/*2 genotype is effectively a null polymorphism. NQO1 is highly inducible and although NQO1 levels can vary considerably among individuals with the same genotype, the NQO1 *2 allele has been reported to show a gene dose effect since heterozygotes (NQO1 *1/*2) contained significantly less NQO1 protein than wild type (NQO1 *1/*1) samples.

Implicated in

Note
  
Entity Leukemia
Note Increased risk of leukemia has been associated with the NQO1 *2 allele and diminished NQO1 activity. Childhood leukemia (particularly with MLL fusions) , adult leukemia (ALL, AML particularly with translocations or inversions) and secondary leukemias and myelodysplasias as a result of chemotherapy have been associated with the NQO1 *2 polymorphism.
Increased benzene induced myelotoxicity in occupationally exposed individuals has also been linked to the NQO1 *2 polymorphism.
  
  
Entity Solid tumors
Note Increased risk of renal and urothelial cell carcinomas and cutaneous basal cell carcinomas have also been associated with the NQO1 *2 polymorphism but conflicting results have been obtained in colon cancer and lung cancer. A number of epidemiological studies have investigated the possible link between NQO1 and cancer and have been recently summarized [6].DISEASE
  

Bibliography

Interaction of human NAD(P)H:quinone oxidoreductase 1 (NQO1) with the tumor suppressor protein p53 in cells and cell-free systems.
Anwar A, Dehn D, Siegel D, Kepa JK, Tang LJ, Pietenpol JA, Ross D
The Journal of biological chemistry. 2003 ; 278 (12) : 10368-10373.
PMID 12529318
 
NQO1 stabilizes p53 through a distinct pathway.
Asher G, Lotem J, Kama R, Sachs L, Shaul Y
Proceedings of the National Academy of Sciences of the United States of America. 2002 ; 99 (5) : 3099-3104.
PMID 11867746
 
Nicotinamide adenine dinucleotide (phosphate): quinone oxidoreductase (DT-diaphorase) as a target for bioreductive antitumor quinones: quinone cytotoxicity and selectivity in human lung and breast cancer cell lines.
Beall HD, Murphy AM, Siegel D, Hargreaves RH, Butler J, Ross D
Molecular pharmacology. 1995 ; 48 (3) : 499-504.
PMID 7565631
 
The role of DT-diaphorase in the maintenance of the reduced antioxidant form of coenzyme Q in membrane systems.
Beyer RE, Segura-Aguilar J, Di Bernardo S, Cavazzoni M, Fato R, Fiorentini D, Galli MC, Setti M, Landi L, Lenaz G
Proceedings of the National Academy of Sciences of the United States of America. 1996 ; 93 (6) : 2528-2532.
PMID 8637908
 
DT-diaphorase.
Ernster, L
Meth Enzymol. 1967 ; 10 : 309-317.
 
Structure-based development of anticancer drugs: complexes of NAD(P)H:quinone oxidoreductase 1 with chemotherapeutic quinones.
Faig M, Bianchet MA, Winski S, Hargreaves R, Moody CJ, Hudnott AR, Ross D, Amzel LM
Structure (London, England : 1993). 2001 ; 9 (8) : 659-667.
PMID 11587640
 
NAD(P)H:quinone oxidoreductase: polymorphisms and allele frequencies in Caucasian, Chinese and Canadian Native Indian and Inuit populations.
Gaedigk A, Tyndale RF, Jurima-Romet M, Sellers EM, Grant DM, Leeder JS
Pharmacogenetics. 1998 ; 8 (4) : 305-313.
PMID 9731717
 
An alternatively spliced form of NQO1 (DT-diaphorase) messenger RNA lacking the putative quinone substrate binding site is present in human normal and tumor tissues.
Gasdaska PY, Fisher H, Powis G
Cancer research. 1995 ; 55 (12) : 2542-2547.
PMID 7780966
 
The NAD(P)H:quinone oxidoreductase locus in human colon carcinoma HCT 116 cells resistant to mitomycin C.
Hu LT, Stamberg J, Pan S
Cancer research. 1996 ; 56 (22) : 5253-5259.
PMID 8912865
 
Human NAD(P)H:quinone oxidoreductase (NQO1) gene structure and induction by dioxin.
Jaiswal AK
Biochemistry. 1991 ; 30 (44) : 10647-10653.
PMID 1657151
 
Human dioxin-inducible cytosolic NAD(P)H:menadione oxidoreductase. cDNA sequence and localization of gene to chromosome 16.
Jaiswal AK, McBride OW, Adesnik M, Nebert DW
The Journal of biological chemistry. 1988 ; 263 (27) : 13572-13578.
PMID 2843525
 
Ethnic variation in the prevalence of a common NAD(P)H quinone oxidoreductase polymorphism and its implications for anti-cancer chemotherapy.
Kelsey KT, Ross D, Traver RD, Christiani DC, Zuo ZF, Spitz MR, Wang M, Xu X, Lee BK, Schwartz BS, Wiencke JK
British journal of cancer. 1997 ; 76 (7) : 852-854.
PMID 9328142
 
Regulation and function of NAD(P)H:quinone oxidoreductase (NQO1).
Kepa JK, Traver RD, Siegel D, Winski SL, and Ross D
Reviews in Toxicology. 1997.
 
Prevalence of the inactivating 609C-->T polymorphism in the NAD(P)H:quinone oxidoreductase (NQO1) gene in patients with primary and therapy-related myeloid leukemia.
Larson RA, Wang Y, Banerjee M, Wiemels J, Hartford C, Le Beau MM, Smith MT
Blood. 1999 ; 94 (2) : 803-807.
PMID 10397748
 
The three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: mechanism of the two-electron reduction.
Li R, Bianchet MA, Talalay P, Amzel LM
Proceedings of the National Academy of Sciences of the United States of America. 1995 ; 92 (19) : 8846-8850.
PMID 7568029
 
DT-diaphorase: purification, properties, and function.
Lind C, Cadenas E, Hochstein P, Ernster L
Methods in enzymology. 1990 ; 186 : 287-301.
PMID 2233301
 
NAD(P)H:quinone oxidoreductase 1 deficiency and increased susceptibility to 7,12-dimethylbenz[a]-anthracene-induced carcinogenesis in mouse skin.
Long DJ 2nd, Waikel RL, Wang XJ, Roop DR, Jaiswal AK
Journal of the National Cancer Institute. 2001 ; 93 (15) : 1166-1170.
PMID 11481389
 
A potential mechanism underlying the increased susceptibility of individuals with a polymorphism in NAD(P)H:quinone oxidoreductase 1 (NQO1) to benzene toxicity.
Moran JL, Siegel D, Ross D
Proceedings of the National Academy of Sciences of the United States of America. 1999 ; 96 (14) : 8150-8155.
PMID 10393963
 
Analysis of genetic polymorphism in NQO1, GST-M1, GST-T1, and CYP3A4 in 469 Japanese patients with therapy-related leukemia/ myelodysplastic syndrome and de novo acute myeloid leukemia.
Naoe T, Takeyama K, Yokozawa T, Kiyoi H, Seto M, Uike N, Ino T, Utsunomiya A, Maruta A, Jin-nai I, Kamada N, Kubota Y, Nakamura H, Shimazaki C, Horiike S, Kodera Y, Saito H, Ueda R, Wiemels J, Ohno R
Clinical cancer research : an official journal of the American Association for Cancer Research. 2000 ; 6 (10) : 4091-4095.
PMID 11051261
 
NAD(P)H:quinone oxidoreductase expression and mitomycin C resistance developed by human colon cancer HCT 116 cells.
Pan SS, Forrest GL, Akman SA, Hu LT
Cancer research. 1995 ; 55 (2) : 330-335.
PMID 7812966
 
Disruption of the DT diaphorase (NQO1) gene in mice leads to increased menadione toxicity.
Radjendirane V, Joseph P, Lee YH, Kimura S, Klein-Szanto AJ, Gonzalez FJ, Jaiswal AK
The Journal of biological chemistry. 1998 ; 273 (13) : 7382-7389.
PMID 9516435
 
NAD(P)H:quinone oxidoreductases.
Ross D
Encyclopedia of Molecular Medicine. 2001.
 
Bioactivation of quinones by DT-diaphorase, molecular, biochemical, and chemical studies.
Ross D, Beall H, Traver RD, Siegel D, Phillips RM, Gibson NW
Oncology research. 1994 ; 6 (10-11) : 493-500.
PMID 7620217
 
NAD(P)H:quinone oxidoreductase 1 (NQO1): chemoprotection, bioactivation, gene regulation and genetic polymorphisms.
Ross D, Kepa JK, Winski SL, Beall HD, Anwar A, Siegel D
Chemico-biological interactions. 2000 ; 129 (1-2) : 77-97.
PMID 11154736
 
NAD(P)H:quinone oxidoreductase 1 (NQO1, DT-diaphorase), functions and pharmacogenetics.
Ross D, Siegel D
Methods in enzymology. 2004 ; 382 : 115-144.
PMID 15047100
 
Rapid polyubiquitination and proteasomal degradation of a mutant form of NAD(P)H:quinone oxidoreductase 1.
Siegel D, Anwar A, Winski SL, Kepa JK, Zolman KL, Ross D
Molecular pharmacology. 2001 ; 59 (2) : 263-268.
PMID 11160862
 
The reduction of alpha-tocopherolquinone by human NAD(P)H: quinone oxidoreductase: the role of alpha-tocopherolhydroquinone as a cellular antioxidant.
Siegel D, Bolton EM, Burr JA, Liebler DC, Ross D
Molecular pharmacology. 1997 ; 52 (2) : 300-305.
PMID 9271353
 
Genotype-phenotype relationships in studies of a polymorphism in NAD(P)H:quinone oxidoreductase 1.
Siegel D, McGuinness SM, Winski SL, Ross D
Pharmacogenetics. 1999 ; 9 (1) : 113-121.
PMID 10208650
 
Immunodetection of NAD(P)H:quinone oxidoreductase 1 (NQO1) in human tissues.
Siegel D, Ross D
Free radical biology & medicine. 2000 ; 29 (3-4) : 246-253.
PMID 11035253
 
Low NAD(P)H:quinone oxidoreductase 1 activity is associated with increased risk of acute leukemia in adults.
Smith MT, Wang Y, Kane E, Rollinson S, Wiemels JL, Roman E, Roddam P, Cartwright R, Morgan G
Blood. 2001 ; 97 (5) : 1422-1426.
PMID 11222389
 
NAD(P)H:quinone oxidoreductase gene expression in human colon carcinoma cells: characterization of a mutation which modulates DT-diaphorase activity and mitomycin sensitivity.
Traver RD, Horikoshi T, Danenberg KD, Stadlbauer TH, Danenberg PV, Ross D, Gibson NW
Cancer research. 1992 ; 52 (4) : 797-802.
PMID 1737339
 
Characterization of a polymorphism in NAD(P)H: quinone oxidoreductase (DT-diaphorase).
Traver RD, Siegel D, Beall HD, Phillips RM, Gibson NW, Franklin WA, Ross D
British journal of cancer. 1997 ; 75 (1) : 69-75.
PMID 9000600
 
A lack of a functional NAD(P)H:quinone oxidoreductase allele is selectively associated with pediatric leukemias that have MLL fusions. United Kingdom Childhood Cancer Study Investigators.
Wiemels JL, Pagnamenta A, Taylor GM, Eden OB, Alexander FE, Greaves MF
Cancer research. 1999 ; 59 (16) : 4095-4099.
PMID 10463613
 
A new screening system for NAD(P)H:quinone oxidoreductase (NQO1)-directed antitumor quinones: identification of a new aziridinylbenzoquinone, RH1, as a NQO1-directed antitumor agent.
Winski SL, Hargreaves RH, Butler J, Ross D
Clinical cancer research : an official journal of the American Association for Cancer Research. 1998 ; 4 (12) : 3083-3088.
PMID 9865924
 

Citation

This paper should be referenced as such :
Ross, D
NQO1 (NAD(P)H dehydrogenase, quinone 1)
Atlas Genet Cytogenet Oncol Haematol. 2004;8(3):215-217.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/NQO1ID375.html
History of this paper:
Ross, D. NQO1 (NAD(P)H dehydrogenase, quinone 1). Atlas Genet Cytogenet Oncol Haematol. 2002;6(2):87-89.
http://documents.irevues.inist.fr/bitstream/handle/2042/37830/12-2001-NQO1ID375.pdf

External links

Nomenclature
HGNC (Hugo)NQO1   2874
Cards
AtlasNQO1ID375
Entrez_Gene (NCBI)NQO1  1728  NAD(P)H quinone dehydrogenase 1
AliasesDHQU; DIA4; DTD; NMOR1; 
NMORI; QR1
GeneCards (Weizmann)NQO1
Ensembl hg19 (Hinxton)ENSG00000181019 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000181019 [Gene_View]  ENSG00000181019 [Sequence]  chr16:69709401-69726668 [Contig_View]  NQO1 [Vega]
ICGC DataPortalENSG00000181019
TCGA cBioPortalNQO1
AceView (NCBI)NQO1
Genatlas (Paris)NQO1
WikiGenes1728
SOURCE (Princeton)NQO1
Genetics Home Reference (NIH)NQO1
Genomic and cartography
GoldenPath hg38 (UCSC)NQO1  -     chr16:69709401-69726668 -  16q22.1   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)NQO1  -     16q22.1   [Description]    (hg19-Feb_2009)
GoldenPathNQO1 - 16q22.1 [CytoView hg19]  NQO1 - 16q22.1 [CytoView hg38]
ImmunoBaseENSG00000181019
Mapping of homologs : NCBINQO1 [Mapview hg19]  NQO1 [Mapview hg38]
OMIM125860   
Gene and transcription
Genbank (Entrez)AK223050 AK297125 AK297979 AK298896 AK307533
RefSeq transcript (Entrez)NM_000903 NM_001025433 NM_001025434 NM_001286137
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)NQO1
Cluster EST : UnigeneHs.406515 [ NCBI ]
CGAP (NCI)Hs.406515
Alternative Splicing GalleryENSG00000181019
Gene ExpressionNQO1 [ NCBI-GEO ]   NQO1 [ EBI - ARRAY_EXPRESS ]   NQO1 [ SEEK ]   NQO1 [ MEM ]
Gene Expression Viewer (FireBrowse)NQO1 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevestigatorExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)1728
GTEX Portal (Tissue expression)NQO1
Human Protein AtlasENSG00000181019-NQO1 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP15559   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP15559  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP15559
Splice isoforms : SwissVarP15559
Catalytic activity : Enzyme1.6.5.2 [ Enzyme-Expasy ]   1.6.5.21.6.5.2 [ IntEnz-EBI ]   1.6.5.2 [ BRENDA ]   1.6.5.2 [ KEGG ]   
PhosPhoSitePlusP15559
Domains : Interpro (EBI)Flavodoxin_fold    Flavoprotein-like_sf   
Domain families : Pfam (Sanger)Flavodoxin_2 (PF02525)   
Domain families : Pfam (NCBI)pfam02525   
Conserved Domain (NCBI)NQO1
DMDM Disease mutations1728
Blocks (Seattle)NQO1
PDB (RSDB)1D4A    1DXO    1GG5    1H66    1H69    1KBO    1KBQ    1QBG    2F1O    3JSX    4CET    4CF6    5A4K    5EA2    5EAI    5FUQ   
PDB Europe1D4A    1DXO    1GG5    1H66    1H69    1KBO    1KBQ    1QBG    2F1O    3JSX    4CET    4CF6    5A4K    5EA2    5EAI    5FUQ   
PDB (PDBSum)1D4A    1DXO    1GG5    1H66    1H69    1KBO    1KBQ    1QBG    2F1O    3JSX    4CET    4CF6    5A4K    5EA2    5EAI    5FUQ   
PDB (IMB)1D4A    1DXO    1GG5    1H66    1H69    1KBO    1KBQ    1QBG    2F1O    3JSX    4CET    4CF6    5A4K    5EA2    5EAI    5FUQ   
Structural Biology KnowledgeBase1D4A    1DXO    1GG5    1H66    1H69    1KBO    1KBQ    1QBG    2F1O    3JSX    4CET    4CF6    5A4K    5EA2    5EAI    5FUQ   
SCOP (Structural Classification of Proteins)1D4A    1DXO    1GG5    1H66    1H69    1KBO    1KBQ    1QBG    2F1O    3JSX    4CET    4CF6    5A4K    5EA2    5EAI    5FUQ   
CATH (Classification of proteins structures)1D4A    1DXO    1GG5    1H66    1H69    1KBO    1KBQ    1QBG    2F1O    3JSX    4CET    4CF6    5A4K    5EA2    5EAI    5FUQ   
SuperfamilyP15559
Human Protein Atlas [tissue]ENSG00000181019-NQO1 [tissue]
Peptide AtlasP15559
HPRD00518
IPIIPI00012069   IPI00910902   IPI00619898   IPI00619966   
Protein Interaction databases
DIP (DOE-UCLA)P15559
IntAct (EBI)P15559
FunCoupENSG00000181019
BioGRIDNQO1
STRING (EMBL)NQO1
ZODIACNQO1
Ontologies - Pathways
QuickGOP15559
Ontology : AmiGORNA binding  NAD(P)H dehydrogenase (quinone) activity  cytochrome-b5 reductase activity, acting on NAD(P)H  superoxide dismutase activity  protein binding  cytoplasm  cytosol  cytosol  cytosol  regulation of cellular amino acid metabolic process  xenobiotic metabolic process  nitric oxide biosynthetic process  synaptic transmission, cholinergic  aging  response to nutrient  electron transfer activity  response to toxic substance  oxidoreductase activity  removal of superoxide radicals  electron transport chain  dendrite  response to estradiol  identical protein binding  neuronal cell body  negative regulation of apoptotic process  negative regulation of catalytic activity  positive regulation of neuron apoptotic process  response to ethanol  response to electrical stimulus  cellular response to hydrogen peroxide  cellular response to metal ion  response to nitrogen compound  response to hydrogen sulfide  
Ontology : EGO-EBIRNA binding  NAD(P)H dehydrogenase (quinone) activity  cytochrome-b5 reductase activity, acting on NAD(P)H  superoxide dismutase activity  protein binding  cytoplasm  cytosol  cytosol  cytosol  regulation of cellular amino acid metabolic process  xenobiotic metabolic process  nitric oxide biosynthetic process  synaptic transmission, cholinergic  aging  response to nutrient  electron transfer activity  response to toxic substance  oxidoreductase activity  removal of superoxide radicals  electron transport chain  dendrite  response to estradiol  identical protein binding  neuronal cell body  negative regulation of apoptotic process  negative regulation of catalytic activity  positive regulation of neuron apoptotic process  response to ethanol  response to electrical stimulus  cellular response to hydrogen peroxide  cellular response to metal ion  response to nitrogen compound  response to hydrogen sulfide  
Pathways : KEGGUbiquinone and other terpenoid-quinone biosynthesis   
REACTOMEP15559 [protein]
REACTOME PathwaysR-HSA-350562 [pathway]   
NDEx NetworkNQO1
Atlas of Cancer Signalling NetworkNQO1
Wikipedia pathwaysNQO1
Orthology - Evolution
OrthoDB1728
GeneTree (enSembl)ENSG00000181019
Phylogenetic Trees/Animal Genes : TreeFamNQO1
HOGENOMP15559
Homologs : HomoloGeneNQO1
Homology/Alignments : Family Browser (UCSC)NQO1
Gene fusions - Rearrangements
Fusion : FusionGDB12588    24152    24771    24772    24773    24774    24775    24776    35148   
Fusion : Fusion_HubFAM155A--NQO1    FBLIM1--NQO1    NQO1--ADH1B    NQO1--AGK    NQO1--APOA1BP    NQO1--COA5    NQO1--DYRK1A    NQO1--NQO1    NQO1--RAD23B    NQO1--TBRG4    NQO1--THRIL    NQO1--TTC37    NQO1--XRN1    NQO1--ZNF486    RPUSD3--NQO1   
SNHG6--NQO1    WWP2--NQO1   
Fusion : QuiverNQO1
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerNQO1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)NQO1
dbVarNQO1
ClinVarNQO1
1000_GenomesNQO1 
Exome Variant ServerNQO1
ExAC (Exome Aggregation Consortium)ENSG00000181019
GNOMAD BrowserENSG00000181019
Varsome BrowserNQO1
Genetic variants : HAPMAP1728
Genomic Variants (DGV)NQO1 [DGVbeta]
DECIPHERNQO1 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisNQO1 
Mutations
ICGC Data PortalNQO1 
TCGA Data PortalNQO1 
Broad Tumor PortalNQO1
OASIS PortalNQO1 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICNQO1  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DNQO1
Mutations and Diseases : HGMDNQO1
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch NQO1
DgiDB (Drug Gene Interaction Database)NQO1
DoCM (Curated mutations)NQO1 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)NQO1 (select a term)
intoGenNQO1
NCG5 (London)NQO1
Cancer3DNQO1(select the gene name)
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM125860   
Orphanet
DisGeNETNQO1
MedgenNQO1
Genetic Testing Registry NQO1
NextProtP15559 [Medical]
TSGene1728
GENETestsNQO1
Target ValidationNQO1
Huge Navigator NQO1 [HugePedia]
snp3D : Map Gene to Disease1728
BioCentury BCIQNQO1
ClinGenNQO1
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD1728
Chemical/Pharm GKB GenePA31744
Clinical trialNQO1
Miscellaneous
canSAR (ICR)NQO1 (select the gene name)
DataMed IndexNQO1
Probes
Litterature
PubMed499 Pubmed reference(s) in Entrez
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