SubmitCancel

Skip Header

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

P16083

- NQO2_HUMAN

UniProt

P16083 - NQO2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Ribosyldihydronicotinamide dehydrogenase [quinone]
Gene
NQO2, NMOR2
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 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 menadione
  3. KM=252 µM for NADH

Sites

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

Regions

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

GO - Molecular functioni

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

GO - Biological processi

  1. memory Source: Ensembl
Complete GO annotation...

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
Complete GO annotation...

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.1 Publication

Protein-protein interaction databases

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

Structurei

Secondary structure

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.

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti140 – 1401G → C in AAB60642. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 157 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

Similar proteinsi