Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

NAD(P)H dehydrogenase [quinone] 1

Gene

NQO1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinons 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 activityi

NAD(P)H + a quinone = NAD(P)+ + a hydroquinone.

Cofactori

Enzyme regulationi

Inhibited by dicoumarol.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei12FAD3 Publications1
Binding sitei67FAD3 Publications1
Binding sitei156FAD3 Publications1
Binding sitei201FAD3 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi18 – 19FAD3 Publications2
Nucleotide bindingi104 – 107FAD3 Publications4
Nucleotide bindingi148 – 151FAD3 Publications4

GO - Molecular functioni

  • cytochrome-b5 reductase activity, acting on NAD(P)H Source: ProtInc
  • identical protein binding Source: IntAct
  • NAD(P)H dehydrogenase (quinone) activity Source: ProtInc
  • poly(A) RNA binding Source: UniProtKB
  • superoxide dismutase activity Source: Ensembl

GO - Biological processi

  • aging Source: Ensembl
  • negative regulation of apoptotic process Source: Ensembl
  • negative regulation of catalytic activity Source: Ensembl
  • nitric oxide biosynthetic process Source: ProtInc
  • positive regulation of neuron apoptotic process Source: Ensembl
  • regulation of cellular amino acid metabolic process Source: Reactome
  • response to estradiol Source: Ensembl
  • response to ethanol Source: Ensembl
  • response to nutrient Source: Ensembl
  • response to toxic substance Source: ProtInc
  • synaptic transmission, cholinergic Source: ProtInc
  • xenobiotic metabolic process Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NAD, NADP

Enzyme and pathway databases

BioCyciZFISH:HS11566-MONOMER.
BRENDAi1.6.5.2. 2681.
ReactomeiR-HSA-350562. Regulation of ornithine decarboxylase (ODC).
SIGNORiP15559.

Names & Taxonomyi

Protein namesi
Recommended name:
NAD(P)H dehydrogenase [quinone] 1 (EC:1.6.5.2)
Alternative name(s):
Azoreductase
DT-diaphorase
Short name:
DTD
Menadione reductase
NAD(P)H:quinone oxidoreductase 1
Phylloquinone reductase
Quinone reductase 1
Short name:
QR1
Gene namesi
Name:NQO1
Synonyms:DIA4, NMOR1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:2874. NQO1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • neuronal cell body Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi1728.
OpenTargetsiENSG00000181019.
PharmGKBiPA31744.

Chemistry databases

ChEMBLiCHEMBL3623.
DrugBankiDB00958. Carboplatin.
DB00515. Cisplatin.
DB00266. Dicoumarol.
DB00997. Doxorubicin.
DB03147. Flavin adenine dinucleotide.
DB00170. Menadione.
DB00526. Oxaliplatin.
DB00163. Vitamin E.

Polymorphism and mutation databases

BioMutaiNQO1.
DMDMi118607.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000716222 – 274NAD(P)H dehydrogenase [quinone] 1Add BLAST273

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei82PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP15559.
MaxQBiP15559.
PaxDbiP15559.
PeptideAtlasiP15559.
PRIDEiP15559.
TopDownProteomicsiP15559-1. [P15559-1]

PTM databases

iPTMnetiP15559.
PhosphoSitePlusiP15559.
SwissPalmiP15559.

Expressioni

Inductioni

By dioxin.

Gene expression databases

BgeeiENSG00000181019.
CleanExiHS_NQO1.
ExpressionAtlasiP15559. baseline and differential.
GenevisibleiP15559. HS.

Organism-specific databases

HPAiCAB012421.
HPA007308.

Interactioni

Subunit structurei

Homodimer.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-3989435,EBI-3989435
ING1Q9UK533EBI-3989435,EBI-399198
Tp63O88898-22EBI-3989435,EBI-2338228From a different organism.
Tp63O88898-62EBI-3989435,EBI-2338244From a different organism.

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi108072. 24 interactors.
DIPiDIP-24210N.
IntActiP15559. 5 interactors.
MINTiMINT-231407.
STRINGi9606.ENSP00000319788.

Chemistry databases

BindingDBiP15559.

Structurei

Secondary structure

1274
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 10Combined sources6
Beta strandi15 – 17Combined sources3
Helixi18 – 32Combined sources15
Beta strandi36 – 41Combined sources6
Turni42 – 46Combined sources5
Helixi53 – 55Combined sources3
Beta strandi56 – 58Combined sources3
Helixi63 – 65Combined sources3
Helixi68 – 78Combined sources11
Helixi83 – 94Combined sources12
Beta strandi96 – 103Combined sources8
Beta strandi106 – 108Combined sources3
Helixi111 – 120Combined sources10
Turni124 – 126Combined sources3
Helixi129 – 131Combined sources3
Helixi133 – 135Combined sources3
Turni137 – 140Combined sources4
Beta strandi142 – 148Combined sources7
Helixi154 – 156Combined sources3
Beta strandi160 – 162Combined sources3
Helixi165 – 173Combined sources9
Turni174 – 177Combined sources4
Helixi178 – 180Combined sources3
Beta strandi188 – 190Combined sources3
Helixi193 – 195Combined sources3
Helixi198 – 212Combined sources15
Helixi213 – 217Combined sources5
Helixi226 – 228Combined sources3
Helixi233 – 235Combined sources3
Beta strandi237 – 239Combined sources3
Helixi241 – 248Combined sources8
Beta strandi254 – 256Combined sources3
Turni266 – 270Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D4AX-ray1.70A/B/C/D2-274[»]
1DXOX-ray2.50A/B/C/D2-274[»]
1GG5X-ray2.50A/B/C/D2-274[»]
1H66X-ray2.00A/B/C/D3-274[»]
1H69X-ray1.86A/B/C/D3-274[»]
1KBOX-ray2.30A/B/C/D2-274[»]
1KBQX-ray1.80A/B/C/D2-274[»]
1QBGX-ray2.30A/B/C/D4-274[»]
2F1OX-ray2.75A/B/C/D/E/F/G/H2-274[»]
3JSXX-ray2.45A/B/C/D/E/F/G/H2-274[»]
4CETX-ray2.20A1-274[»]
4CF6X-ray2.69A/B1-274[»]
5A4KX-ray2.09A/B/C/D1-274[»]
5EA2X-ray2.01A/C/E/G1-273[»]
5EAIX-ray2.90A/B/C/D/E/F/G/H/I/J/K/L/M/N1-274[»]
ProteinModelPortaliP15559.
SMRiP15559.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15559.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni126 – 128Substrate binding3

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IKWF. Eukaryota.
COG2249. LUCA.
GeneTreeiENSGT00440000033410.
HOGENOMiHOG000149970.
HOVERGENiHBG029104.
InParanoidiP15559.
KOiK00355.
OMAiYDKGPFQ.
OrthoDBiEOG091G183R.
PhylomeDBiP15559.
TreeFamiTF300296.

Family and domain databases

Gene3Di3.40.50.360. 1 hit.
InterProiIPR003680. Flavodoxin_fold.
IPR029039. Flavoprotein-like_dom.
[Graphical view]
PfamiPF02525. Flavodoxin_2. 1 hit.
[Graphical view]
SUPFAMiSSF52218. SSF52218. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P15559-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVGRRALIVL AHSERTSFNY AMKEAAAAAL KKKGWEVVES DLYAMNFNPI
60 70 80 90 100
ISRKDITGKL KDPANFQYPA ESVLAYKEGH LSPDIVAEQK KLEAADLVIF
110 120 130 140 150
QFPLQWFGVP AILKGWFERV FIGEFAYTYA AMYDKGPFRS KKAVLSITTG
160 170 180 190 200
GSGSMYSLQG IHGDMNVILW PIQSGILHFC GFQVLEPQLT YSIGHTPADA
210 220 230 240 250
RIQILEGWKK RLENIWDETP LYFAPSSLFD LNFQAGFLMK KEVQDEEKNK
260 270
KFGLSVGHHL GKSIPTDNQI KARK
Length:274
Mass (Da):30,868
Last modified:April 1, 1990 - v1
Checksum:iA4010462AD00F3FE
GO
Isoform 2 (identifier: P15559-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     140-173: Missing.

Note: No experimental confirmation available.
Show »
Length:240
Mass (Da):27,295
Checksum:i63EF4B34E6394793
GO
Isoform 3 (identifier: P15559-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     102-139: Missing.

Note: No experimental confirmation available.
Show »
Length:236
Mass (Da):26,365
Checksum:i8BF801EAD71D02AB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti252F → S in BAG60289 (PubMed:14702039).Curated1

Mass spectrometryi

Molecular mass is 30864±6 Da from positions 2 - 274. Determined by ESI. 1 Publication

Polymorphismi

The Ser-187 polymorphism may be linked to susceptibility to forms of cancers.

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_016170139R → W.Corresponds to variant rs1131341dbSNPEnsembl.1
Natural variantiVAR_008384187P → S Lack of activity. 4 PublicationsCorresponds to variant rs1800566dbSNPEnsembl.1
Natural variantiVAR_050220269Q → H.Corresponds to variant rs34447156dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_044446102 – 139Missing in isoform 3. 1 PublicationAdd BLAST38
Alternative sequenceiVSP_042716140 – 173Missing in isoform 2. 1 PublicationAdd BLAST34

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03934 mRNA. Translation: AAA59940.1.
M81600
, M81596, M81597, M81598, M81599 Genomic DNA. Translation: AAB60701.1.
AY281093 Genomic DNA. Translation: AAP20940.1. Sequence problems.
AK297979 mRNA. Translation: BAG60289.1.
AK312368 mRNA. Translation: BAG35286.1.
AK316246 mRNA. Translation: BAH14617.1.
AC092115 Genomic DNA. No translation available.
CH471092 Genomic DNA. Translation: EAW83283.1.
CH471092 Genomic DNA. Translation: EAW83284.1.
BC007659 mRNA. Translation: AAH07659.1.
CCDSiCCDS10883.1. [P15559-1]
CCDS32471.1. [P15559-3]
CCDS32472.1. [P15559-2]
PIRiA41135. A30879.
RefSeqiNP_000894.1. NM_000903.2. [P15559-1]
NP_001020604.1. NM_001025433.1. [P15559-2]
NP_001020605.1. NM_001025434.1. [P15559-3]
UniGeneiHs.406515.

Genome annotation databases

EnsembliENST00000320623; ENSP00000319788; ENSG00000181019. [P15559-1]
ENST00000379046; ENSP00000368334; ENSG00000181019. [P15559-3]
ENST00000379047; ENSP00000368335; ENSG00000181019. [P15559-2]
GeneIDi1728.
KEGGihsa:1728.
UCSCiuc002exp.5. human. [P15559-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03934 mRNA. Translation: AAA59940.1.
M81600
, M81596, M81597, M81598, M81599 Genomic DNA. Translation: AAB60701.1.
AY281093 Genomic DNA. Translation: AAP20940.1. Sequence problems.
AK297979 mRNA. Translation: BAG60289.1.
AK312368 mRNA. Translation: BAG35286.1.
AK316246 mRNA. Translation: BAH14617.1.
AC092115 Genomic DNA. No translation available.
CH471092 Genomic DNA. Translation: EAW83283.1.
CH471092 Genomic DNA. Translation: EAW83284.1.
BC007659 mRNA. Translation: AAH07659.1.
CCDSiCCDS10883.1. [P15559-1]
CCDS32471.1. [P15559-3]
CCDS32472.1. [P15559-2]
PIRiA41135. A30879.
RefSeqiNP_000894.1. NM_000903.2. [P15559-1]
NP_001020604.1. NM_001025433.1. [P15559-2]
NP_001020605.1. NM_001025434.1. [P15559-3]
UniGeneiHs.406515.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D4AX-ray1.70A/B/C/D2-274[»]
1DXOX-ray2.50A/B/C/D2-274[»]
1GG5X-ray2.50A/B/C/D2-274[»]
1H66X-ray2.00A/B/C/D3-274[»]
1H69X-ray1.86A/B/C/D3-274[»]
1KBOX-ray2.30A/B/C/D2-274[»]
1KBQX-ray1.80A/B/C/D2-274[»]
1QBGX-ray2.30A/B/C/D4-274[»]
2F1OX-ray2.75A/B/C/D/E/F/G/H2-274[»]
3JSXX-ray2.45A/B/C/D/E/F/G/H2-274[»]
4CETX-ray2.20A1-274[»]
4CF6X-ray2.69A/B1-274[»]
5A4KX-ray2.09A/B/C/D1-274[»]
5EA2X-ray2.01A/C/E/G1-273[»]
5EAIX-ray2.90A/B/C/D/E/F/G/H/I/J/K/L/M/N1-274[»]
ProteinModelPortaliP15559.
SMRiP15559.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108072. 24 interactors.
DIPiDIP-24210N.
IntActiP15559. 5 interactors.
MINTiMINT-231407.
STRINGi9606.ENSP00000319788.

Chemistry databases

BindingDBiP15559.
ChEMBLiCHEMBL3623.
DrugBankiDB00958. Carboplatin.
DB00515. Cisplatin.
DB00266. Dicoumarol.
DB00997. Doxorubicin.
DB03147. Flavin adenine dinucleotide.
DB00170. Menadione.
DB00526. Oxaliplatin.
DB00163. Vitamin E.

PTM databases

iPTMnetiP15559.
PhosphoSitePlusiP15559.
SwissPalmiP15559.

Polymorphism and mutation databases

BioMutaiNQO1.
DMDMi118607.

Proteomic databases

EPDiP15559.
MaxQBiP15559.
PaxDbiP15559.
PeptideAtlasiP15559.
PRIDEiP15559.
TopDownProteomicsiP15559-1. [P15559-1]

Protocols and materials databases

DNASUi1728.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000320623; ENSP00000319788; ENSG00000181019. [P15559-1]
ENST00000379046; ENSP00000368334; ENSG00000181019. [P15559-3]
ENST00000379047; ENSP00000368335; ENSG00000181019. [P15559-2]
GeneIDi1728.
KEGGihsa:1728.
UCSCiuc002exp.5. human. [P15559-1]

Organism-specific databases

CTDi1728.
DisGeNETi1728.
GeneCardsiNQO1.
HGNCiHGNC:2874. NQO1.
HPAiCAB012421.
HPA007308.
MIMi125860. gene.
neXtProtiNX_P15559.
OpenTargetsiENSG00000181019.
PharmGKBiPA31744.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IKWF. Eukaryota.
COG2249. LUCA.
GeneTreeiENSGT00440000033410.
HOGENOMiHOG000149970.
HOVERGENiHBG029104.
InParanoidiP15559.
KOiK00355.
OMAiYDKGPFQ.
OrthoDBiEOG091G183R.
PhylomeDBiP15559.
TreeFamiTF300296.

Enzyme and pathway databases

BioCyciZFISH:HS11566-MONOMER.
BRENDAi1.6.5.2. 2681.
ReactomeiR-HSA-350562. Regulation of ornithine decarboxylase (ODC).
SIGNORiP15559.

Miscellaneous databases

ChiTaRSiNQO1. human.
EvolutionaryTraceiP15559.
GeneWikiiNAD(P)H_dehydrogenase_(quinone_1).
GenomeRNAii1728.
PROiP15559.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000181019.
CleanExiHS_NQO1.
ExpressionAtlasiP15559. baseline and differential.
GenevisibleiP15559. HS.

Family and domain databases

Gene3Di3.40.50.360. 1 hit.
InterProiIPR003680. Flavodoxin_fold.
IPR029039. Flavoprotein-like_dom.
[Graphical view]
PfamiPF02525. Flavodoxin_2. 1 hit.
[Graphical view]
SUPFAMiSSF52218. SSF52218. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNQO1_HUMAN
AccessioniPrimary (citable) accession number: P15559
Secondary accession number(s): B2R5Y9
, B4DNM7, B7ZAD1, Q86UK1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: November 30, 2016
This is version 184 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Quinone reductase accepts electrons from both NADH and NADPH with equal efficiency.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.