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UniProtKB/Swiss-Prot entry P16083


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NQO2_HUMAN
Primary accession number P16083
Secondary accession numbers None
Integrated into Swiss-Prot on April 1, 1990
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    September 23, 2008 (Entry version 95)
Name and origin of the protein
Protein name Ribosyldihydronicotinamide dehydrogenase [quinone]
Synonyms EC 1.10.99.2
NRH dehydrogenase [quinone] 2
NRH:quinone oxidoreductase 2
Quinone reductase 2
QR2
Gene name
Name: NQO2
Synonyms: NMOR2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
DOI=10.1021/bi00459a034; PubMed=1691923 [NCBI, ExPASy, EBI, Israel, Japan]
Jaiswal A.K., Burnett P., Adesnik M., McBride O.W.;
"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.";
Biochemistry 29:1899-1906(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Liver;
PubMed=8182056 [NCBI, ExPASy, EBI, Israel, Japan]
Jaiswal A.K.;
"Human NAD(P)H:quinone oxidoreductase 2. Gene structure, activity, and tissue-specific expression.";
J. Biol. Chem. 269:14502-14508(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Iida A., Osawa S., Kitamura Y., Kitamoto T., Koyama K., Nakamura Y.;
"Human NRH:quinone oxidoreductase 2, complete genomic sequence.";
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-16; GLY-29; LEU-47; ASP-58 AND ALA-184.
Livingston R.J., Rieder M.J., Chung M.-W., Ritchie T.K., Olson A.N., Nguyen C.P., Gildersleeve H., Cassidy C.M., Johnson E.J., Swanson J.E., McFarland I., Yool B., Park C., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
CHARACTERIZATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
DOI=10.1006/abbi.1997.0344; PubMed=9367528 [NCBI, ExPASy, EBI, Israel, Japan]
Wu K., Knox R., Sun X.Z., Joseph P., Jaiswal A.K., Zhang D., Deng P.S.-K., Chen S.;
"Catalytic properties of NAD(P)H:quinone oxidoreductase-2 (NQO2), a dihydronicotinamide riboside dependent oxidoreductase.";
Arch. Biochem. Biophys. 347:221-228(1997).
[7]
CHARACTERIZATION.
DOI=10.1073/pnas.94.5.1669; PubMed=9050836 [NCBI, ExPASy, EBI, Israel, Japan]
Zhao Q., Yang X.L., Holtzclaw W.D., Talalay P.;
"Unexpected genetic and structural relationships of a long-forgotten flavoenzyme to NAD(P)H:quinone reductase (DT-diaphorase).";
Proc. Natl. Acad. Sci. U.S.A. 94:1669-1674(1997).
[8]
ERRATUM.
Zhao Q., Yang X.L., Holtzclaw W.D., Talalay P.;
Proc. Natl. Acad. Sci. U.S.A. 94:5979-5979(1997).
[9]
BIOPHYSICOCHEMICAL PROPERTIES.
DOI=10.1021/bi035923w; PubMed=15078100 [NCBI, ExPASy, EBI, Israel, Japan]
Kwiek J.J., Haystead T.A.J., Rudolph J.;
"Kinetic mechanism of quinone oxidoreductase 2 and its inhibition by the antimalarial quinolines.";
Biochemistry 43:4538-4547(2004).
[10]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
DOI=10.1021/bi990799v; PubMed=10433694 [NCBI, ExPASy, EBI, Israel, Japan]
Foster C.E., Bianchet M.A., Talalay P., Zhao Q., Amzel L.M.;
"Crystal structure of human quinone reductase type 2, a metalloflavoprotein.";
Biochemistry 38:9881-9886(1999).
[11]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH RESVERATROL.
DOI=10.1021/bi049162o; PubMed=15350128 [NCBI, ExPASy, EBI, Israel, Japan]
Buryanovskyy L., Fu Y., Boyd M., Ma Y., Hsieh T.-C., Wu J.M., Zhang Z.;
"Crystal structure of quinone reductase 2 in complex with resveratrol.";
Biochemistry 43:11417-11426(2004).
[12]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH CB1954, AND MUTANT HIS-162.
DOI=10.1016/j.bbrc.2005.08.081; PubMed=16129418 [NCBI, ExPASy, EBI, Israel, Japan]
Fu Y., Buryanovskyy L., Zhang Z.;
"Crystal structure of quinone reductase 2 in complex with cancer prodrug CB1954.";
Biochem. Biophys. Res. Commun. 336:332-338(2005).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J02888; AAA60239.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY299456; AAB60642.3; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB050248; BAB16974.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY855291; AAW29945.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC006096; AAH06096.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A32667; A32667.
RefSeq NP_000895.2; -.
UniGene Hs.533050
3D structure databases
PDB
1QR2; X-ray; 2.10 A; A/B=1-231.[ExPASy / RCSB / EBI]
1SG0; X-ray; 1.50 A; A/B=1-231.[ExPASy / RCSB / EBI]
1XI2; X-ray; 1.50 A; A/B=1-231.[ExPASy / RCSB / EBI]
1ZX1; X-ray; 2.16 A; A/B=1-231.[ExPASy / RCSB / EBI]
2BZS; X-ray; 2.00 A; A/B=1-231.[ExPASy / RCSB / EBI]
2QMY; X-ray; 2.50 A; A/B=2-231.[ExPASy / RCSB / EBI]
2QMZ; X-ray; 2.10 A; A/B=2-231.[ExPASy / RCSB / EBI]
2QR2; X-ray; 2.45 A; A/B=1-231.[ExPASy / RCSB / EBI]
2QWX; X-ray; 1.50 A; A/B=1-231.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1QR2; -.
1SG0; -.
1XI2; -.
1ZX1; -.
2BZS; -.
2QMY; -.
2QMZ; -.
2QR2; -.
2QWX; -.
ModBase P16083.
Protein-protein interaction databases
IntAct P16083; -.
Polymorphism databases
NIEHS-SNPs NQO2.
Organism-specific databases
H-InvDB HIX0018967; -.
HGNC HGNC:7856; NQO2.
GenAtlas NQO2.
MIM 160998; gene. [NCBI / EBI]
PharmGKB PA31745; -.
GeneCards P16083.
Gene expression databases
ArrayExpress P16083; -.
CleanEx HS_NQO2; -.
GermOnline ENSG00000124588; Homo sapiens.
Ontologies
GO
GO:0009055; Molecular function: electron carrier activity (traceable author statement from UniProtKB).
GO:0008753; Molecular function: NADPH dehydrogenase (quinone) activity (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR003680; Flavodoxin_fold.
Graphical view of domain structure.
Pfam PF02525; Flavodoxin_2; 1.
Pfam graphical view of domain structure.
BLOCKS P16083.
Genome annotation databases
Ensembl ENSG00000124588; Homo sapiens. [Contig view]
GeneID 4835; -.
KEGG hsa:4835; -.
Phylogenomic databases
HOGENOM P16083; -.
HOVERGEN P16083; -.
Other
DrugBank DB00170; Menadione.
DB00157; NADH.
LinkHub P16083; -.
SOURCE NQO2; Homo sapiens.
ProtoNet P16083.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; FAD; Flavoprotein; Metal-binding; Oxidoreductase; Polymorphism; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   231  230     Ribosyldihydronicotinamide dehydrogenase [quinone]. PRO_0000071626
METAL   174   174        Zinc. 
METAL   178   178        Zinc. 
METAL   223   223        Zinc. 
VARIANT   16    16  1     K -> R (in dbSNP:rs28383623 [NCBI]). VAR_021399 [3D]
VARIANT   29    29  1     E -> G (in dbSNP:rs17136117 [NCBI]). VAR_021400 [3D]
VARIANT   47    47  1     F -> L (in dbSNP:rs1143684 [NCBI]). VAR_021401 [3D]
VARIANT   58    58  1     G -> D (in dbSNP:rs17300141 [NCBI]). VAR_021402 [3D]
VARIANT   184   184  1     V -> A (in dbSNP:rs28383651 [NCBI]). VAR_021403 [3D]
MUTAGEN   162   162        N->H: Loss of activity toward CB1954, no effect toward menadione. 
CONFLICT   140   140        G -> C (in Ref. 2). 
STRAND   5    10  6      
HELIX   18    32  15      
STRAND   36    41  6      
HELIX   42    45  4      
HELIX   53    55  3      
HELIX   68    77  10      
HELIX   83    94  12      
STRAND   96   103  8      
HELIX   111   120  10      
TURN   123   125  3      
HELIX   133   135  3      
TURN   137   140  4      
STRAND   142   148  7      
TURN   153   156  4      
STRAND   160   162  3      
HELIX   165   173  9      
TURN   174   177  4      
HELIX   178   180  3      
STRAND   188   190  3      
HELIX   193   195  3      
HELIX   198   213  16      
HELIX   214   217  4      
HELIX   225   229  5      
Sequence information
Length: 231 AA [This is the length of the unprocessed precursor] Molecular weight: 25953 Da [This is the MW of the unprocessed precursor] CRC64: FAF549B991FDB978 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAGKKVLIVY AHQEPKSFNG SLKNVAVDEL SRQGCTVTVS DLYAMNFEPR ATDKDITGTL 

        70         80         90        100        110        120 
SNPEVFNYGV ETHEAYKQRS LASDITDEQK KVREADLVIF QFPLYWFSVP AILKGWMDRV 

       130        140        150        160        170        180 
LCQGFAFDIP GFYDSGLLQG KLALLSVTTG GTAEMYTKTG VNGDSRYFLW PLQHGTLHFC 

       190        200        210        220        230 
GFKVLAPQIS FAPEIASEEE RKGMVAAWSQ RLQTIWKEEP IPCTAHWHFG Q 

P16083 in FASTA format

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