Human Gene NQO2 (ENST00000380455.11_7) from GENCODE V47lift37

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Description: N-ribosyldihydronicotinamide:quinone reductase 2, transcript variant 3 (from RefSeq NM_000904.6)
Gencode Transcript: ENST00000380455.11_7
Gencode Gene: ENSG00000124588.22_16
Transcript (Including UTRs)
Position: hg19 chr6:3,000,128-3,019,989 Size: 19,862 Total Exon Count: 7 Strand: +
Coding Region
Position: hg19 chr6:3,006,787-3,019,889 Size: 13,103 Coding Exon Count: 6

Page Index	Sequence and Links	UniProtKB Comments	Primers	MalaCards	CTD
Gene Alleles	RNA-Seq Expression	Microarray Expression	RNA Structure	Protein Structure	Other Species
GO Annotations	mRNA Descriptions	Pathways	Other Names	Model Information	Methods

Data last updated at UCSC: 2024-08-22 23:36:26

Sequence and Links to Tools and Databases

Genomic Sequence (chr6:3,000,128-3,019,989)			mRNA (may differ from genome)		Protein (231 aa)
Gene Sorter	Genome Browser	Other Species FASTA	VisiGene	Gene interactions	Table Schema
AlphaFold	BioGPS	Ensembl	Entrez Gene	ExonPrimer	GeneCards
HGNC	Malacards	MGI	OMIM	PubMed	Reactome
UniProtKB	Wikipedia	BioGrid CRISPR DB

Comments and Description Text from UniProtKB


	ID: NQO2_HUMAN DESCRIPTION: RecName: Full=Ribosyldihydronicotinamide dehydrogenase [quinone]; EC=1.10.99.2; AltName: Full=NRH dehydrogenase [quinone] 2; AltName: Full=NRH:quinone oxidoreductase 2; AltName: Full=Quinone reductase 2; Short=QR2; FUNCTION: The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis. CATALYTIC ACTIVITY: 1-(beta-D-ribofuranosyl)-1,4- dihydronicotinamide + a quinone = 1-(beta-D- ribofuranosyl)nicotinamide + a hydroquinone. COFACTOR: Binds 1 zinc ion per subunit. COFACTOR: FAD. ENZYME REGULATION: Inhibited by melatonin, resveratrol and 5- hydroxytryptamine. BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=28 uM for NRH; KM=11.6 uM for menadione; KM=252 uM for NADH; SUBUNIT: Homodimer. SUBCELLULAR LOCATION: Cytoplasm. MISCELLANEOUS: Uses dihydronicotinamide riboside (NRH) rather than NAD(P)H as an electron donor. SIMILARITY: Belongs to the NAD(P)H dehydrogenase (quinone) family. WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/nqo2/";

Primer design for this transcript

Primer3Plus can design qPCR Primers that straddle exon-exon-junctions, which amplify only cDNA, not genomic DNA.
Click here to load the transcript sequence and exon structure into Primer3Plus

Exonprimer can design one pair of Sanger sequencing primers around every exon, located in non-genic sequence.
Click here to open Exonprimer with this transcript

To design primers for a non-coding sequence, zoom to a region of interest and select from the drop-down menu: View > In External Tools > Primer3

MalaCards Disease Associations


	MalaCards Gene Search: NQO2 Diseases sorted by gene-association score: marburg hemorrhagic fever (16), alcoholic pancreatitis (8), breast cancer* (7) * = Manually curated disease association

Comparative Toxicogenomics Database (CTD)


	The following chemicals interact with this gene D013749 Tetrachlorodibenzodioxin D016604 Aflatoxin B1 D001564 Benzo(a)pyrene D016572 Cyclosporine D008550 Melatonin D024483 Vitamin K 3 C059514 resveratrol C445701 1-benzyl-1,4-dihydronicotinamide C029497 2,3-bis(3'-hydroxybenzyl)butyrolactone C016403 2,4-dinitrotoluene more ... click here to view the complete list

Common Gene Haplotype Alleles


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RNA-Seq Expression Data from GTEx (53 Tissues, 570 Donors)


	Highest median expression: 40.52 RPKM in Adrenal Gland Total median expression: 645.38 RPKM View in GTEx track of Genome Browser View at GTEx portal View GTEx Body Map

Microarray Expression Data


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mRNA Secondary Structure of 3' and 5' UTRs

Region	Fold Energy	Bases	Energy/Base	Display As
5' UTR	-120.70	277	-0.436	Picture	PostScript	Text
3' UTR	-21.70	100	-0.217	Picture	PostScript	Text

The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.

Protein Domain and Structure Information

InterPro Domains: Graphical view of domain structure
IPR003680 - Flavodoxin_fold

Pfam Domains:
PF02525 - Flavodoxin-like fold
PF03358 - NADPH-dependent FMN reductase

SCOP Domains:
52218 - Flavoproteins

Protein Data Bank (PDB) 3-D Structure
MuPIT help

1QR2 - X-ray MuPIT

1SG0 - X-ray MuPIT

1XI2 - X-ray MuPIT

1ZX1 - X-ray MuPIT

2BZS - X-ray MuPIT

2QMY - X-ray MuPIT

2QMZ - X-ray MuPIT

2QR2 - X-ray MuPIT

2QWX - X-ray MuPIT

2QX4 - X-ray MuPIT

2QX6 - X-ray MuPIT

2QX8 - X-ray MuPIT

2QX9 - X-ray MuPIT

3FW1 - X-ray MuPIT

3G5M - X-ray MuPIT

3GAM - X-ray MuPIT

3NFR - X-ray MuPIT

3NHF - X-ray MuPIT

3NHJ - X-ray MuPIT

3NHK - X-ray MuPIT

3NHL - X-ray MuPIT

3NHP - X-ray MuPIT

3NHR - X-ray MuPIT

3NHS - X-ray MuPIT

3NHU - X-ray MuPIT

3NHW - X-ray MuPIT

3NHY - X-ray MuPIT

3O2N - X-ray MuPIT

3O73 - X-ray MuPIT

3OVM - X-ray MuPIT

3OWH - X-ray MuPIT

3OWX - X-ray MuPIT

3OX1 - X-ray MuPIT

3OX2 - X-ray MuPIT

3OX3 - X-ray MuPIT

3TE7 - X-ray MuPIT

3TEM - X-ray MuPIT

3TZB - X-ray MuPIT

3UXE - X-ray MuPIT

3UXH - X-ray MuPIT

ModBase Predicted Comparative 3D Structure on P16083


Front	Top	Side

The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.

Orthologous Genes in Other Species

Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.

Mouse	Rat	Zebrafish	D. melanogaster	C. elegans	S. cerevisiae
No ortholog	No ortholog	No ortholog	No ortholog	No ortholog	No ortholog
Gene Details	Gene Details
Gene Sorter	Gene Sorter
	RGD

Gene Ontology (GO) Annotations with Structured Vocabulary


	Molecular Function: GO:0001512 dihydronicotinamide riboside quinone reductase activity GO:0005515 protein binding GO:0008270 zinc ion binding GO:0009055 electron carrier activity GO:0016491 oxidoreductase activity GO:0016661 oxidoreductase activity, acting on other nitrogenous compounds as donors GO:0031404 chloride ion binding GO:0042803 protein homodimerization activity GO:0046872 metal ion binding GO:0071949 FAD binding GO:1904408 melatonin binding GO:1905594 resveratrol binding Biological Process: GO:0006805 xenobiotic metabolic process GO:0022900 electron transport chain GO:0055114 oxidation-reduction process Cellular Component: GO:0005654 nucleoplasm GO:0005737 cytoplasm GO:0005829 cytosol GO:0070062 extracellular exosome

Descriptions from all associated GenBank mRNAs


	AB209779 - Homo sapiens mRNA for NAD(P)H dehydrogenase, quinone 2 variant protein. AK311746 - Homo sapiens cDNA, FLJ92005, Homo sapiens NAD(P)H dehydrogenase, quinone 2 (NQO2), mRNA. AK056981 - Homo sapiens cDNA FLJ32419 fis, clone SKMUS2000894, highly similar to Ribosyldihydronicotinamide dehydrogenase [quinone] (EC 1.10.99.2). J02888 - Human quinone oxidoreductase (NQO2) mRNA, complete cds. BC006096 - Homo sapiens NAD(P)H dehydrogenase, quinone 2, mRNA (cDNA clone MGC:12729 IMAGE:3507945), complete cds. AB528982 - Synthetic construct DNA, clone: pF1KE0910, Homo sapiens NQO2 gene for NAD(P)H dehydrogenase, quinone 2, without stop codon, in Flexi system. KJ897251 - Synthetic construct Homo sapiens clone ccsbBroadEn_06645 NQO2 gene, encodes complete protein. JD023394 - Sequence 4418 from Patent EP1572962. JD031386 - Sequence 12410 from Patent EP1572962. JD115759 - Sequence 96783 from Patent EP1572962. JD474060 - Sequence 455084 from Patent EP1572962. JD247166 - Sequence 228190 from Patent EP1572962. JD146092 - Sequence 127116 from Patent EP1572962.

Biochemical and Signaling Pathways


	Reactome (by CSHL, EBI, and GO) Protein P16083 (Reactome details) participates in the following event(s): R-HSA-8936519 NQO2:FAD dimer reduces quinones to hydroquinones R-HSA-211945 Phase I - Functionalization of compounds R-HSA-211859 Biological oxidations R-HSA-1430728 Metabolism

Other Names for This Gene


	Alternate Gene Symbols: B2R492, ENST00000380455.1, ENST00000380455.10, ENST00000380455.2, ENST00000380455.3, ENST00000380455.4, ENST00000380455.5, ENST00000380455.6, ENST00000380455.7, ENST00000380455.8, ENST00000380455.9, NMOR2, NM_000904, NQO2_HUMAN, P16083, Q5TD04, uc318ppi.1, uc318ppi.2 UCSC ID: ENST00000380455.11_7 RefSeq Accession: NM_000904.6 Protein: P16083 (aka NQO2_HUMAN)

Gene Model Information


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Methods, Credits, and Use Restrictions


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