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P16083

- NQO2_HUMAN

UniProt

P16083 - NQO2_HUMAN

Protein

Ribosyldihydronicotinamide dehydrogenase [quinone]

Gene

NQO2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 5 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Catalytic activityi

    1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + a quinone = 1-(beta-D-ribofuranosyl)nicotinamide + a hydroquinone.1 Publication

    Cofactori

    Binds 1 zinc ion per subunit.
    FAD.

    Enzyme regulationi

    Inhibited by melatonin, resveratrol and 5-hydroxytryptamine.1 Publication

    Kineticsi

    1. KM=28 µM for NRH2 Publications
    2. KM=11.6 µM for menadione2 Publications
    3. KM=252 µM for NADH2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei12 – 121FAD2 Publications
    Binding sitei156 – 1561FAD2 Publications
    Metal bindingi174 – 1741Zinc
    Metal bindingi178 – 1781Zinc
    Binding sitei194 – 1941FAD2 Publications
    Binding sitei201 – 2011FAD2 Publications
    Metal bindingi223 – 2231Zinc

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi18 – 214FAD2 Publications
    Nucleotide bindingi104 – 1074FAD2 Publications
    Nucleotide bindingi148 – 1514FAD2 Publications

    GO - Molecular functioni

    1. dihydronicotinamide riboside quinone reductase activity Source: UniProtKB-EC
    2. electron carrier activity Source: UniProtKB
    3. metal ion binding Source: UniProtKB-KW
    4. NADPH dehydrogenase (quinone) activity Source: ProtInc

    GO - Biological processi

    1. memory Source: Ensembl

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi1.10.99.2. 2681.
    SABIO-RKP16083.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribosyldihydronicotinamide dehydrogenase [quinone] (EC:1.10.99.2)
    Alternative name(s):
    NRH dehydrogenase [quinone] 2
    NRH:quinone oxidoreductase 2
    Quinone reductase 2
    Short name:
    QR2
    Gene namesi
    Name:NQO2
    Synonyms:NMOR2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:7856. NQO2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. extracellular vesicular exosome Source: UniProt
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi162 – 1621N → H: Loss of activity toward CB1954, no effect toward menadione. 1 Publication

    Organism-specific databases

    PharmGKBiPA31745.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 231231Ribosyldihydronicotinamide dehydrogenase [quinone]PRO_0000071626Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei80 – 801Phosphoserine1 Publication
    Modified residuei197 – 1971Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP16083.
    PaxDbiP16083.
    PRIDEiP16083.

    PTM databases

    PhosphoSiteiP16083.

    Expressioni

    Gene expression databases

    ArrayExpressiP16083.
    BgeeiP16083.
    CleanExiHS_NQO2.
    GenevestigatoriP16083.

    Organism-specific databases

    HPAiHPA021283.
    HPA021332.

    Interactioni

    Subunit structurei

    Homodimer.4 Publications

    Protein-protein interaction databases

    BioGridi110898. 9 interactions.
    IntActiP16083. 7 interactions.
    MINTiMINT-1133243.
    STRINGi9606.ENSP00000337773.

    Structurei

    Secondary structure

    1
    231
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 106
    Helixi18 – 3316
    Beta strandi36 – 416
    Turni42 – 465
    Helixi53 – 553
    Beta strandi63 – 653
    Helixi68 – 7710
    Helixi83 – 9412
    Beta strandi96 – 1038
    Beta strandi105 – 1084
    Helixi111 – 12010
    Turni123 – 1253
    Beta strandi129 – 1324
    Helixi133 – 1353
    Turni137 – 1404
    Beta strandi142 – 1487
    Turni153 – 1564
    Beta strandi160 – 1623
    Helixi165 – 1739
    Helixi174 – 1785
    Turni179 – 1813
    Beta strandi188 – 1903
    Turni193 – 1953
    Helixi198 – 21215
    Helixi213 – 2175
    Helixi225 – 2295

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QR2X-ray2.10A/B2-231[»]
    1SG0X-ray1.50A/B2-231[»]
    1XI2X-ray1.50A/B2-231[»]
    1ZX1X-ray2.16A/B1-231[»]
    2BZSX-ray2.00A/B2-231[»]
    2QMYX-ray2.50A/B2-231[»]
    2QMZX-ray2.10A/B2-231[»]
    2QR2X-ray2.45A/B2-231[»]
    2QWXX-ray1.50A/B1-231[»]
    2QX4X-ray1.65A/B2-231[»]
    2QX6X-ray1.75A/B2-231[»]
    2QX8X-ray1.60A/B2-231[»]
    2QX9X-ray2.31A/B2-231[»]
    3FW1X-ray1.75A1-231[»]
    3G5MX-ray1.84A/B1-231[»]
    3GAMX-ray1.98A/B1-231[»]
    3NFRX-ray1.57A/B2-231[»]
    3NHFX-ray2.00A/B2-231[»]
    3NHJX-ray2.33A/B2-231[»]
    3NHKX-ray1.96A/B2-231[»]
    3NHLX-ray1.57A/B2-231[»]
    3NHPX-ray1.70A/B2-231[»]
    3NHRX-ray1.80A/B2-231[»]
    3NHSX-ray1.78A/B2-231[»]
    3NHUX-ray1.90A/B2-231[»]
    3NHWX-ray1.65A/B2-231[»]
    3NHYX-ray1.90A/B2-231[»]
    3O2NX-ray1.60A/B2-231[»]
    3O73X-ray2.00A/B1-231[»]
    3OVMX-ray2.09A/B1-231[»]
    3OWHX-ray2.28A/B1-231[»]
    3OWXX-ray1.85A/B1-231[»]
    3OX1X-ray2.00A/B1-231[»]
    3OX2X-ray2.41A/B1-231[»]
    3OX3X-ray1.80A/B1-231[»]
    3TE7X-ray1.70A/B3-230[»]
    3TEMX-ray1.45A/B3-230[»]
    3TZBX-ray2.19A/B/C/D3-230[»]
    3UXEX-ray1.50A/B2-231[»]
    3UXHX-ray1.53A/B2-231[»]
    4FGJX-ray1.35A/B1-231[»]
    4FGKX-ray1.40A/B1-231[»]
    4FGLX-ray1.20A/B/C/D1-231[»]
    4GQIX-ray1.95A/B2-231[»]
    4GR9X-ray2.29A/B2-231[»]
    DisProtiDP00727.
    ProteinModelPortaliP16083.
    SMRiP16083. Positions 1-231.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP16083.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni127 – 1293Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG2249.
    HOGENOMiHOG000149970.
    HOVERGENiHBG029104.
    InParanoidiP16083.
    KOiK08071.
    OMAiDGWKSEI.
    PhylomeDBiP16083.
    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.

    Sequencei

    Sequence statusi: Complete.

    P16083-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGKKVLIVY AHQEPKSFNG SLKNVAVDEL SRQGCTVTVS DLYAMNLEPR    50
    ATDKDITGTL SNPEVFNYGV ETHEAYKQRS LASDITDEQK KVREADLVIF 100
    QFPLYWFSVP AILKGWMDRV LCQGFAFDIP GFYDSGLLQG KLALLSVTTG 150
    GTAEMYTKTG VNGDSRYFLW PLQHGTLHFC GFKVLAPQIS FAPEIASEEE 200
    RKGMVAAWSQ RLQTIWKEEP IPCTAHWHFG Q 231
    Length:231
    Mass (Da):25,919
    Last modified:January 11, 2011 - v5
    Checksum:iFE1F4D577517B972
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti140 – 1401G → C in AAB60642. (PubMed:8182056)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti16 – 161K → R.1 Publication
    Corresponds to variant rs28383623 [ dbSNP | Ensembl ].
    VAR_021399
    Natural varianti29 – 291E → G.1 Publication
    Corresponds to variant rs17136117 [ dbSNP | Ensembl ].
    VAR_021400
    Natural varianti47 – 471L → F.7 Publications
    Corresponds to variant rs1143684 [ dbSNP | Ensembl ].
    VAR_021401
    Natural varianti58 – 581G → D.1 Publication
    Corresponds to variant rs17300141 [ dbSNP | Ensembl ].
    VAR_021402
    Natural varianti184 – 1841V → A.1 Publication
    Corresponds to variant rs28383651 [ dbSNP | Ensembl ].
    VAR_021403

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02888 mRNA. Translation: AAA60239.1.
    AY299456 Genomic DNA. Translation: AAB60642.3.
    AB050248 Genomic DNA. Translation: BAB16974.1.
    AY855291 Genomic DNA. Translation: AAW29945.1.
    AK311746 mRNA. Translation: BAG34689.1.
    AL133351 Genomic DNA. Translation: CAI23294.1.
    CH471087 Genomic DNA. Translation: EAW55107.1.
    BC006096 mRNA. Translation: AAH06096.1.
    CCDSiCCDS4481.1.
    PIRiA32667.
    RefSeqiNP_000895.2. NM_000904.4.
    NP_001277150.1. NM_001290221.1.
    XP_005249205.1. XM_005249148.2.
    XP_005249206.1. XM_005249149.2.
    XP_005249207.1. XM_005249150.2.
    XP_005249208.1. XM_005249151.2.
    XP_006715163.1. XM_006715100.1.
    XP_006715164.1. XM_006715101.1.
    UniGeneiHs.145597.
    Hs.533050.

    Genome annotation databases

    EnsembliENST00000338130; ENSP00000337773; ENSG00000124588.
    ENST00000380430; ENSP00000369795; ENSG00000124588.
    ENST00000380455; ENSP00000369822; ENSG00000124588.
    GeneIDi4835.
    KEGGihsa:4835.
    UCSCiuc003mus.2. human.

    Polymorphism databases

    DMDMi317373581.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02888 mRNA. Translation: AAA60239.1 .
    AY299456 Genomic DNA. Translation: AAB60642.3 .
    AB050248 Genomic DNA. Translation: BAB16974.1 .
    AY855291 Genomic DNA. Translation: AAW29945.1 .
    AK311746 mRNA. Translation: BAG34689.1 .
    AL133351 Genomic DNA. Translation: CAI23294.1 .
    CH471087 Genomic DNA. Translation: EAW55107.1 .
    BC006096 mRNA. Translation: AAH06096.1 .
    CCDSi CCDS4481.1.
    PIRi A32667.
    RefSeqi NP_000895.2. NM_000904.4.
    NP_001277150.1. NM_001290221.1.
    XP_005249205.1. XM_005249148.2.
    XP_005249206.1. XM_005249149.2.
    XP_005249207.1. XM_005249150.2.
    XP_005249208.1. XM_005249151.2.
    XP_006715163.1. XM_006715100.1.
    XP_006715164.1. XM_006715101.1.
    UniGenei Hs.145597.
    Hs.533050.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1QR2 X-ray 2.10 A/B 2-231 [» ]
    1SG0 X-ray 1.50 A/B 2-231 [» ]
    1XI2 X-ray 1.50 A/B 2-231 [» ]
    1ZX1 X-ray 2.16 A/B 1-231 [» ]
    2BZS X-ray 2.00 A/B 2-231 [» ]
    2QMY X-ray 2.50 A/B 2-231 [» ]
    2QMZ X-ray 2.10 A/B 2-231 [» ]
    2QR2 X-ray 2.45 A/B 2-231 [» ]
    2QWX X-ray 1.50 A/B 1-231 [» ]
    2QX4 X-ray 1.65 A/B 2-231 [» ]
    2QX6 X-ray 1.75 A/B 2-231 [» ]
    2QX8 X-ray 1.60 A/B 2-231 [» ]
    2QX9 X-ray 2.31 A/B 2-231 [» ]
    3FW1 X-ray 1.75 A 1-231 [» ]
    3G5M X-ray 1.84 A/B 1-231 [» ]
    3GAM X-ray 1.98 A/B 1-231 [» ]
    3NFR X-ray 1.57 A/B 2-231 [» ]
    3NHF X-ray 2.00 A/B 2-231 [» ]
    3NHJ X-ray 2.33 A/B 2-231 [» ]
    3NHK X-ray 1.96 A/B 2-231 [» ]
    3NHL X-ray 1.57 A/B 2-231 [» ]
    3NHP X-ray 1.70 A/B 2-231 [» ]
    3NHR X-ray 1.80 A/B 2-231 [» ]
    3NHS X-ray 1.78 A/B 2-231 [» ]
    3NHU X-ray 1.90 A/B 2-231 [» ]
    3NHW X-ray 1.65 A/B 2-231 [» ]
    3NHY X-ray 1.90 A/B 2-231 [» ]
    3O2N X-ray 1.60 A/B 2-231 [» ]
    3O73 X-ray 2.00 A/B 1-231 [» ]
    3OVM X-ray 2.09 A/B 1-231 [» ]
    3OWH X-ray 2.28 A/B 1-231 [» ]
    3OWX X-ray 1.85 A/B 1-231 [» ]
    3OX1 X-ray 2.00 A/B 1-231 [» ]
    3OX2 X-ray 2.41 A/B 1-231 [» ]
    3OX3 X-ray 1.80 A/B 1-231 [» ]
    3TE7 X-ray 1.70 A/B 3-230 [» ]
    3TEM X-ray 1.45 A/B 3-230 [» ]
    3TZB X-ray 2.19 A/B/C/D 3-230 [» ]
    3UXE X-ray 1.50 A/B 2-231 [» ]
    3UXH X-ray 1.53 A/B 2-231 [» ]
    4FGJ X-ray 1.35 A/B 1-231 [» ]
    4FGK X-ray 1.40 A/B 1-231 [» ]
    4FGL X-ray 1.20 A/B/C/D 1-231 [» ]
    4GQI X-ray 1.95 A/B 2-231 [» ]
    4GR9 X-ray 2.29 A/B 2-231 [» ]
    DisProti DP00727.
    ProteinModelPortali P16083.
    SMRi P16083. Positions 1-231.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110898. 9 interactions.
    IntActi P16083. 7 interactions.
    MINTi MINT-1133243.
    STRINGi 9606.ENSP00000337773.

    Chemistry

    BindingDBi P16083.
    ChEMBLi CHEMBL3959.
    DrugBanki DB00170. Menadione.
    DB00157. NADH.

    PTM databases

    PhosphoSitei P16083.

    Polymorphism databases

    DMDMi 317373581.

    Proteomic databases

    MaxQBi P16083.
    PaxDbi P16083.
    PRIDEi P16083.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000338130 ; ENSP00000337773 ; ENSG00000124588 .
    ENST00000380430 ; ENSP00000369795 ; ENSG00000124588 .
    ENST00000380455 ; ENSP00000369822 ; ENSG00000124588 .
    GeneIDi 4835.
    KEGGi hsa:4835.
    UCSCi uc003mus.2. human.

    Organism-specific databases

    CTDi 4835.
    GeneCardsi GC06P003006.
    H-InvDB HIX0018967.
    HGNCi HGNC:7856. NQO2.
    HPAi HPA021283.
    HPA021332.
    MIMi 160998. gene.
    neXtProti NX_P16083.
    PharmGKBi PA31745.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2249.
    HOGENOMi HOG000149970.
    HOVERGENi HBG029104.
    InParanoidi P16083.
    KOi K08071.
    OMAi DGWKSEI.
    PhylomeDBi P16083.
    TreeFami TF300296.

    Enzyme and pathway databases

    BRENDAi 1.10.99.2. 2681.
    SABIO-RK P16083.

    Miscellaneous databases

    EvolutionaryTracei P16083.
    GeneWikii NAD(P)H_dehydrogenase,_quinone_2.
    GenomeRNAii 4835.
    NextBioi 18630.
    PROi P16083.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P16083.
    Bgeei P16083.
    CleanExi HS_NQO2.
    Genevestigatori P16083.

    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. "Nucleotide and deduced amino acid sequence of a human cDNA (NQO2) corresponding to a second member of the NAD(P)H:quinone oxidoreductase gene family. Extensive polymorphism at the NQO2 gene locus on chromosome 6."
      Jaiswal A.K., Burnett P., Adesnik M., McBride O.W.
      Biochemistry 29:1899-1906(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PHE-47.
      Tissue: Liver.
    2. "Human NAD(P)H:quinone oxidoreductase 2. Gene structure, activity, and tissue-specific expression."
      Jaiswal A.K.
      J. Biol. Chem. 269:14502-14508(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PHE-47.
      Tissue: Liver.
    3. "Human NRH:quinone oxidoreductase 2, complete genomic sequence."
      Iida A., Osawa S., Kitamura Y., Kitamoto T., Koyama K., Nakamura Y.
      Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PHE-47.
    4. NIEHS SNPs program
      Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-16; GLY-29; PHE-47; ASP-58 AND ALA-184.
    5. "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], VARIANT PHE-47.
      Tissue: Cerebellum.
    6. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PHE-47.
    8. "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], VARIANT PHE-47.
      Tissue: Brain.
    9. "Catalytic properties of NAD(P)H:quinone oxidoreductase-2 (NQO2), a dihydronicotinamide riboside dependent oxidoreductase."
      Wu K., Knox R., Sun X.Z., Joseph P., Jaiswal A.K., Zhang D., Deng P.S.-K., Chen S.
      Arch. Biochem. Biophys. 347:221-228(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES.
    10. "Unexpected genetic and structural relationships of a long-forgotten flavoenzyme to NAD(P)H:quinone reductase (DT-diaphorase)."
      Zhao Q., Yang X.L., Holtzclaw W.D., Talalay P.
      Proc. Natl. Acad. Sci. U.S.A. 94:1669-1674(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    11. Erratum
      Zhao Q., Yang X.L., Holtzclaw W.D., Talalay P.
      Proc. Natl. Acad. Sci. U.S.A. 94:5979-5979(1997)
    12. "Kinetic mechanism of quinone oxidoreductase 2 and its inhibition by the antimalarial quinolines."
      Kwiek J.J., Haystead T.A.J., Rudolph J.
      Biochemistry 43:4538-4547(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-197, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Crystal structure of human quinone reductase type 2, a metalloflavoprotein."
      Foster C.E., Bianchet M.A., Talalay P., Zhao Q., Amzel L.M.
      Biochemistry 38:9881-9886(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
    16. "Crystal structure of quinone reductase 2 in complex with resveratrol."
      Buryanovskyy L., Fu Y., Boyd M., Ma Y., Hsieh T.-C., Wu J.M., Zhang Z.
      Biochemistry 43:11417-11426(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH RESVERATROL.
    17. "Crystal structure of quinone reductase 2 in complex with cancer prodrug CB1954."
      Fu Y., Buryanovskyy L., Zhang Z.
      Biochem. Biophys. Res. Commun. 336:332-338(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH CB1954, MUTAGENESIS OF ASN-162.
    18. "Kinetic, thermodynamic and X-ray structural insights into the interaction of melatonin and analogues with quinone reductase 2."
      Calamini B., Santarsiero B.D., Boutin J.A., Mesecar A.D.
      Biochem. J. 413:81-91(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH MELATONIN AND FAD, FUNCTION, SUBUNIT, ENZYME REGULATION.
    19. "Quinone reductase 2 is a catechol quinone reductase."
      Fu Y., Buryanovskyy L., Zhang Z.
      J. Biol. Chem. 283:23829-23835(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH DOPAMINE AND ADRENOCHROME, ENZYME ACTIVITY.
    20. "The structure of the leukemia drug imatinib bound to human quinone reductase 2 (NQO2)."
      Winger J.A., Hantschel O., Superti-Furga G., Kuriyan J.
      BMC Struct. Biol. 9:7-7(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH ZINC IONS; FAD AND IMATINIB.

    Entry informationi

    Entry nameiNQO2_HUMAN
    AccessioniPrimary (citable) accession number: P16083
    Secondary accession number(s): B2R492, Q5TD04
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 158 of the entry and version 5 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

    Uses dihydronicotinamide riboside (NRH) rather than NAD(P)H as an electron donor.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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