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P15559

- NQO1_HUMAN

UniProt

P15559 - NQO1_HUMAN

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
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    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

    FAD.

    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. protein binding Source: IntAct
    5. 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

    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

    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

    ArrayExpressiP15559.
    BgeeiP15559.
    CleanExiHS_NQO1.
    GenevestigatoriP15559.

    Organism-specific databases

    HPAiCAB012421.
    HPA007308.

    Interactioni

    Subunit structurei

    Homodimer.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    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 – 106
    Beta strandi15 – 173
    Helixi18 – 3215
    Beta strandi36 – 416
    Turni42 – 465
    Helixi53 – 553
    Beta strandi56 – 583
    Beta strandi63 – 653
    Helixi68 – 7811
    Helixi83 – 9412
    Beta strandi96 – 1038
    Beta strandi106 – 1083
    Helixi111 – 12010
    Turni124 – 1263
    Helixi129 – 1313
    Helixi133 – 1353
    Turni137 – 1404
    Beta strandi142 – 1487
    Helixi154 – 1563
    Beta strandi160 – 1623
    Helixi165 – 1739
    Turni174 – 1774
    Helixi178 – 1803
    Beta strandi188 – 1903
    Helixi193 – 1953
    Helixi198 – 21215
    Helixi213 – 2175
    Helixi226 – 2283
    Helixi233 – 2353
    Beta strandi237 – 2393
    Helixi241 – 2488
    Beta strandi254 – 2563
    Turni266 – 2705

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    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.
    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

    MVGRRALIVL AHSERTSFNY AMKEAAAAAL KKKGWEVVES DLYAMNFNPI    50
    ISRKDITGKL KDPANFQYPA ESVLAYKEGH LSPDIVAEQK KLEAADLVIF 100
    QFPLQWFGVP AILKGWFERV FIGEFAYTYA AMYDKGPFRS KKAVLSITTG 150
    GSGSMYSLQG IHGDMNVILW PIQSGILHFC GFQVLEPQLT YSIGHTPADA 200
    RIQILEGWKK RLENIWDETP LYFAPSSLFD LNFQAGFLMK KEVQDEEKNK 250
    KFGLSVGHHL GKSIPTDNQI KARK 274
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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 [» ]
    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 DB00266. Dicumarol.
    DB00170. Menadione.

    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.
    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

    ArrayExpressi P15559.
    Bgeei P15559.
    CleanExi HS_NQO1.
    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

    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: October 1, 2014
    This is version 160 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