P16083 (NQO2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	NQO2
Synonyms:	NMOR2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	231 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.18
Catalytic activity	1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + a quinone = 1-(beta-D-ribofuranosyl)nicotinamide + a hydroquinone. Ref.19
Cofactor	Binds 1 zinc ion per subunit. FAD.
Enzyme regulation	Inhibited by melatonin, resveratrol and 5-hydroxytryptamine. Ref.18
Subunit structure	Homodimer. Ref.18
Subcellular location	Cytoplasm.
Miscellaneous	Uses dihydronicotinamide riboside (NRH) rather than NAD(P)H as an electron donor.
Sequence similarities	Belongs to the NAD(P)H dehydrogenase (quinone) family.
Biophysicochemical properties	Kinetic parameters: KM=28 µM for NRH Ref.9 Ref.12 KM=11.6 µM for menadione KM=252 µM for NADH

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	FAD Flavoprotein Metal-binding Zinc
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	memory Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA
Molecular_function	NADPH dehydrogenase (quinone) activity Traceable author statement Ref.1. Source: ProtInc dihydronicotinamide riboside quinone reductase activity Inferred from electronic annotation. Source: EC electron carrier activity Traceable author statement Ref.1. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 231

231

Ribosyldihydronicotinamide dehydrogenase [quinone]

PRO_0000071626

Regions

Nucleotide binding

18 – 21

4

FAD

Nucleotide binding

104 – 107

4

FAD

Nucleotide binding

148 – 151

4

FAD

Region

127 – 129

3

Substrate binding

Sites

Metal binding

174

1

Zinc

Metal binding

178

1

Zinc

Metal binding

223

1

Zinc

Binding site

12

1

FAD

Binding site

156

1

FAD

Binding site

194

1

FAD

Binding site

201

1

FAD

Amino acid modifications

Modified residue

80

1

Phosphoserine Ref.13

Modified residue

197

1

Phosphoserine Ref.13

Natural variations

Natural variant

16

1

K → R. Ref.4
Corresponds to variant rs28383623 [ dbSNP | Ensembl ].

VAR_021399

Natural variant

29

1

E → G. Ref.4
Corresponds to variant rs17136117 [ dbSNP | Ensembl ].

VAR_021400

Natural variant

47

1

L → F. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.7 Ref.8
Corresponds to variant rs1143684 [ dbSNP | Ensembl ].

VAR_021401

Natural variant

58

1

G → D. Ref.4
Corresponds to variant rs17300141 [ dbSNP | Ensembl ].

VAR_021402

Natural variant

184

1

V → A. Ref.4
Corresponds to variant rs28383651 [ dbSNP | Ensembl ].

VAR_021403

Experimental info

Mutagenesis

162

1

N → H: Loss of activity toward CB1954, no effect toward menadione. Ref.17

Sequence conflict

140

1

G → C in AAB60642. Ref.2

Secondary structure

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231

Helix Strand Turn

Details...

Beta strand

5 – 10

6

Helix

18 – 33

16

Beta strand

36 – 41

6

Turn

42 – 46

5

Helix

53 – 55

3

Beta strand

63 – 65

3

Helix

68 – 78

11

Helix

83 – 94

12

Beta strand

96 – 103

8

Beta strand

105 – 108

4

Helix

111 – 120

10

Turn

123 – 125

3

Beta strand

129 – 132

4

Helix

133 – 135

3

Turn

137 – 140

4

Beta strand

142 – 148

7

Turn

153 – 156

4

Beta strand

160 – 162

3

Helix

165 – 173

9

Helix

174 – 178

5

Turn

179 – 181

3

Beta strand

188 – 190

3

Turn

193 – 195

3

Helix

198 – 213

16

Helix

214 – 217

4

Helix

225 – 229

5

Sequences

	Sequence		Length	Mass (Da)
	P16083 [UniParc]. Last modified January 11, 2011. Version 5. Checksum: FE1F4D577517B972	FASTA	231	25,919
	10 20 30 40 50 60 MAGKKVLIVY AHQEPKSFNG SLKNVAVDEL SRQGCTVTVS DLYAMNLEPR 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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-197, MASS SPECTROMETRY.
[14]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00219129.

PIR

A32667.

RefSeq

NP_000895.2. NM_000904.3.

UniGene

Hs.145597.
Hs.533050.

3D structure databases

PDBe
RCSB PDB
PDBj

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	2-230	[»]
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	[»]

ProteinModelPortal

P16083.

SMR

P16083. Positions 2-231.

ModBase

Search...

Protein-protein interaction databases

IntAct

P16083. 5 interactions.

MINT

MINT-1133243.

STRING

9606.ENSP00000337773.

PTM databases

PhosphoSite

P16083.

Polymorphism databases

DMDM

9911070.

Proteomic databases

PaxDb

P16083.

PRIDE

P16083.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000338130; ENSP00000337773; ENSG00000124588.
ENST00000380430; ENSP00000369795; ENSG00000124588.
ENST00000380455; ENSP00000369822; ENSG00000124588.

GeneID

4835.

KEGG

hsa:4835.

UCSC

uc003mus.2. human.

Organism-specific databases

CTD

4835.

GeneCards

GC06P003000.

H-InvDB

HIX0018967.

HGNC

HGNC:7856. NQO2.

HPA

HPA021283.
HPA021332.

MIM

160998. gene.

neXtProt

NX_P16083.

PharmGKB

PA31745.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2249.

HOGENOM

HOG000149970.

HOVERGEN

HBG029104.

InParanoid

P16083.

KO

K08071.

OMA

AEMYTKT.

PhylomeDB

P16083.

Enzyme and pathway databases

BRENDA

1.10.99.2. 2681.

SABIO-RK

P16083.

Gene expression databases

ArrayExpress

P16083.

Bgee

P16083.

CleanEx

HS_NQO2.

Genevestigator

P16083.

GermOnline

ENSG00000124588. Homo sapiens.

Family and domain databases

InterPro

IPR003680. Flavodoxin_fold.
[Graphical view]

Pfam

PF02525. Flavodoxin_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P16083.

ChEMBL

CHEMBL3959.

DrugBank

DB00170. Menadione.
DB00157. NADH.

EvolutionaryTrace

P16083.

GenomeRNAi

4835.

NextBio

18630.

SOURCE

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Entry information

Entry name

NQO2_HUMAN

Accession

Primary (citable) accession number: P16083
Secondary accession number(s): B2R492, Q5TD04

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	January 11, 2011
Last modified:	May 1, 2013
This is version 143 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.