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P15559

- NQO1_HUMAN

UniProt

P15559 - NQO1_HUMAN

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Protein

NAD(P)H dehydrogenase [quinone] 1

Gene

NQO1

Organism
Homo sapiens (Human)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei12 – 121FAD3 Publications
Binding sitei67 – 671FAD3 Publications
Binding sitei156 – 1561FAD3 Publications
Binding sitei201 – 2011FAD3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi18 – 192FAD3 Publications
Nucleotide bindingi104 – 1074FAD3 Publications
Nucleotide bindingi148 – 1514FAD3 Publications

GO - Molecular functioni

  1. cytochrome-b5 reductase activity, acting on NAD(P)H Source: ProtInc
  2. NAD(P)H dehydrogenase (quinone) activity Source: ProtInc
  3. poly(A) RNA binding Source: UniProtKB
  4. superoxide dismutase activity Source: Ensembl

GO - Biological processi

  1. aging Source: Ensembl
  2. cellular nitrogen compound metabolic process Source: Reactome
  3. negative regulation of catalytic activity Source: Ensembl
  4. nitric oxide biosynthetic process Source: ProtInc
  5. positive regulation of neuron apoptotic process Source: Ensembl
  6. regulation of cellular amino acid metabolic process Source: Reactome
  7. response to estradiol Source: Ensembl
  8. response to ethanol Source: Ensembl
  9. response to nutrient Source: Ensembl
  10. response to toxic substance Source: ProtInc
  11. small molecule metabolic process Source: Reactome
  12. synaptic transmission, cholinergic Source: ProtInc
  13. xenobiotic metabolic process Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NAD, NADP

Enzyme and pathway databases

BRENDAi1.6.5.2. 2681.
ReactomeiREACT_13565. Regulation of ornithine decarboxylase (ODC).

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
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:2874. NQO1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
  4. neuronal cell body Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31744.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 274273NAD(P)H dehydrogenase [quinone] 1PRO_0000071622Add
BLAST

Proteomic databases

MaxQBiP15559.
PaxDbiP15559.
PRIDEiP15559.

PTM databases

PhosphoSiteiP15559.

Expressioni

Inductioni

By dioxin.

Gene expression databases

BgeeiP15559.
CleanExiHS_NQO1.
ExpressionAtlasiP15559. baseline and differential.
GenevestigatoriP15559.

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.

Protein-protein interaction databases

BioGridi108072. 18 interactions.
DIPiDIP-24210N.
IntActiP15559. 3 interactions.
MINTiMINT-231407.
STRINGi9606.ENSP00000319788.

Structurei

Secondary structure

1
274
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 106Combined sources
Beta strandi15 – 173Combined sources
Helixi18 – 3215Combined sources
Beta strandi36 – 416Combined sources
Turni42 – 465Combined sources
Helixi53 – 553Combined sources
Beta strandi56 – 583Combined sources
Beta strandi63 – 653Combined sources
Helixi68 – 7811Combined sources
Helixi83 – 9412Combined sources
Beta strandi96 – 1038Combined sources
Beta strandi106 – 1083Combined sources
Helixi111 – 12010Combined sources
Turni124 – 1263Combined sources
Helixi129 – 1313Combined sources
Helixi133 – 1353Combined sources
Turni137 – 1404Combined sources
Beta strandi142 – 1487Combined sources
Helixi154 – 1563Combined sources
Beta strandi160 – 1623Combined sources
Helixi165 – 1739Combined sources
Turni174 – 1774Combined sources
Helixi178 – 1803Combined sources
Beta strandi188 – 1903Combined sources
Helixi193 – 1953Combined sources
Helixi198 – 21215Combined sources
Helixi213 – 2175Combined sources
Helixi226 – 2283Combined sources
Helixi233 – 2353Combined sources
Beta strandi237 – 2393Combined sources
Helixi241 – 2488Combined sources
Beta strandi254 – 2563Combined sources
Turni266 – 2705Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP15559.
SMRiP15559. Positions 2-274.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15559.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni126 – 1283Substrate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2249.
GeneTreeiENSGT00440000033410.
HOGENOMiHOG000149970.
HOVERGENiHBG029104.
InParanoidiP15559.
KOiK00355.
OMAiYDKGPFQ.
PhylomeDBiP15559.
TreeFamiTF300296.

Family and domain databases

Gene3Di3.40.50.360. 1 hit.
InterProiIPR003680. Flavodoxin_fold.
IPR029039. Flavoprotein-like.
[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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti252 – 2521F → S in BAG60289. (PubMed:14702039)Curated

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti139 – 1391R → W.
Corresponds to variant rs1131341 [ dbSNP | Ensembl ].
VAR_016170
Natural varianti187 – 1871P → S Lack of activity. 4 Publications
Corresponds to variant rs1800566 [ dbSNP | Ensembl ].
VAR_008384
Natural varianti269 – 2691Q → H.
Corresponds to variant rs34447156 [ dbSNP | Ensembl ].
VAR_050220

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei102 – 13938Missing in isoform 3. 1 PublicationVSP_044446Add
BLAST
Alternative sequencei140 – 17334Missing in isoform 2. 1 PublicationVSP_042716Add
BLAST

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.3. human. [P15559-1]
uc002exq.3. human. [P15559-2]
uc002exr.3. human. [P15559-3]

Polymorphism databases

DMDMi118607.

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 .
CCDSi CCDS10883.1. [P15559-1 ]
CCDS32471.1. [P15559-3 ]
CCDS32472.1. [P15559-2 ]
PIRi A41135. A30879.
RefSeqi NP_000894.1. NM_000903.2. [P15559-1 ]
NP_001020604.1. NM_001025433.1. [P15559-2 ]
NP_001020605.1. NM_001025434.1. [P15559-3 ]
UniGenei Hs.406515.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1D4A X-ray 1.70 A/B/C/D 2-274 [» ]
1DXO X-ray 2.50 A/B/C/D 2-274 [» ]
1GG5 X-ray 2.50 A/B/C/D 2-274 [» ]
1H66 X-ray 2.00 A/B/C/D 3-274 [» ]
1H69 X-ray 1.86 A/B/C/D 3-274 [» ]
1KBO X-ray 2.30 A/B/C/D 2-274 [» ]
1KBQ X-ray 1.80 A/B/C/D 2-274 [» ]
1QBG X-ray 2.30 A/B/C/D 4-274 [» ]
2F1O X-ray 2.75 A/B/C/D/E/F/G/H 2-274 [» ]
3JSX X-ray 2.45 A/B/C/D/E/F/G/H 2-274 [» ]
4CET X-ray 2.20 A 1-274 [» ]
4CF6 X-ray 2.69 A/B 1-274 [» ]
ProteinModelPortali P15559.
SMRi P15559. Positions 2-274.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108072. 18 interactions.
DIPi DIP-24210N.
IntActi P15559. 3 interactions.
MINTi MINT-231407.
STRINGi 9606.ENSP00000319788.

Chemistry

BindingDBi P15559.
ChEMBLi CHEMBL3623.
DrugBanki DB00958. Carboplatin.
DB00515. Cisplatin.
DB00266. Dicoumarol.
DB00997. Doxorubicin.
DB03147. Flavin adenine dinucleotide.
DB00170. Menadione.
DB00526. Oxaliplatin.
DB00163. Vitamin E.

PTM databases

PhosphoSitei P15559.

Polymorphism databases

DMDMi 118607.

Proteomic databases

MaxQBi P15559.
PaxDbi P15559.
PRIDEi P15559.

Protocols and materials databases

DNASUi 1728.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000320623 ; ENSP00000319788 ; ENSG00000181019 . [P15559-1 ]
ENST00000379046 ; ENSP00000368334 ; ENSG00000181019 . [P15559-3 ]
ENST00000379047 ; ENSP00000368335 ; ENSG00000181019 . [P15559-2 ]
GeneIDi 1728.
KEGGi hsa:1728.
UCSCi uc002exp.3. human. [P15559-1 ]
uc002exq.3. human. [P15559-2 ]
uc002exr.3. human. [P15559-3 ]

Organism-specific databases

CTDi 1728.
GeneCardsi GC16M069744.
HGNCi HGNC:2874. NQO1.
HPAi CAB012421.
HPA007308.
MIMi 125860. gene.
neXtProti NX_P15559.
PharmGKBi PA31744.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2249.
GeneTreei ENSGT00440000033410.
HOGENOMi HOG000149970.
HOVERGENi HBG029104.
InParanoidi P15559.
KOi K00355.
OMAi YDKGPFQ.
PhylomeDBi P15559.
TreeFami TF300296.

Enzyme and pathway databases

BRENDAi 1.6.5.2. 2681.
Reactomei REACT_13565. Regulation of ornithine decarboxylase (ODC).

Miscellaneous databases

ChiTaRSi NQO1. human.
EvolutionaryTracei P15559.
GeneWikii NAD(P)H_dehydrogenase_(quinone_1).
GenomeRNAii 1728.
NextBioi 35473648.
PROi P15559.
SOURCEi Search...

Gene expression databases

Bgeei P15559.
CleanExi HS_NQO1.
ExpressionAtlasi P15559. baseline and differential.
Genevestigatori P15559.

Family and domain databases

Gene3Di 3.40.50.360. 1 hit.
InterProi IPR003680. Flavodoxin_fold.
IPR029039. Flavoprotein-like.
[Graphical view ]
Pfami PF02525. Flavodoxin_2. 1 hit.
[Graphical view ]
SUPFAMi SSF52218. SSF52218. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human dioxin-inducible cytosolic NAD(P)H:menadione oxidoreductase. cDNA sequence and localization of gene to chromosome 16."
    Jaiswal A.K., McBride O.W., Adesnik M., Nebert D.W.
    J. Biol. Chem. 263:13572-13578(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  2. "Human NAD(P)H:quinone oxidoreductase (NQO1) gene structure and induction by dioxin."
    Jaiswal A.K.
    Biochemistry 30:10647-10653(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. NIEHS SNPs program
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-187.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), VARIANT SER-187.
    Tissue: Amygdala.
  5. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Colon.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Crystal structure of human DT-diaphorase: a model for interaction with the cytotoxic prodrug 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB1954)."
    Skelly J.V., Sanderson M.R., Suter D.A., Baumann U., Read M.A., Gregory D.S.J., Bennett M., Hobbs S.M., Neidle S.
    J. Med. Chem. 42:4325-4330(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 4-274 IN COMPLEX WITH FAD, SUBUNIT.
  10. "Structures of recombinant human and mouse NAD(P)H:quinone oxidoreductases: species comparison and structural changes with substrate binding and release."
    Faig M., Bianchet M.A., Talalay P., Chen S., Winski S., Ross D., Amzel L.M.
    Proc. Natl. Acad. Sci. U.S.A. 97:3177-3182(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH FAD AND DUROQUINONE.
  11. "Characterization of a mechanism-based inhibitor of NAD(P)H:quinone oxidoreductase 1 by biochemical, X-ray crystallographic, and mass spectrometric approaches."
    Winski S.L., Faig M., Bianchet M.A., Siegel D., Swann E., Fung K., Duncan M.W., Moody C.J., Amzel L.M., Ross D.
    Biochemistry 40:15135-15142(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH FAD AND THE INHIBITOR ES936, MASS SPECTROMETRY.
  12. "Structure-based development of anticancer drugs: complexes of NAD(P)H:quinone oxidoreductase 1 with chemotherapeutic quinones."
    Faig M., Bianchet M.A., Winski S., Hargreaves R., Moody C.J., Hudnott A.R., Ross D., Amzel L.M.
    Structure 9:659-667(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH FAD AND INHIBITORS, SUBUNIT.
  13. "The crystal structure of NAD(P)H quinone oxidoreductase 1 in complex with its potent inhibitor dicoumarol."
    Asher G., Dym O., Tsvetkov P., Adler J., Shaul Y.
    Biochemistry 45:6372-6378(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR DICOUMAROL.
  14. "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 R.D., Horikoshi T., Danenberg K.D., Stadlbauer T.H., Danenberg P.V., Ross D., Gibson N.W.
    Cancer Res. 52:797-802(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SER-187.
  15. "No linkage of P187S polymorphism in NAD(P)H: quinone oxidoreductase (NQO1/DIA4) and type 1 diabetes in the Danish population."
    Kristiansen O.P., Larsen Z.M., Johannesen J., Nerup J., Mandrup-Poulsen T., Pociot F.
    Hum. Mutat. 14:67-70(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SER-187.

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 26, 2014
This is version 162 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

External Data

Dasty 3