P15559 (NQO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	NQO1
Synonyms:	DIA4, NMOR1

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	274 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	NAD(P)H + a quinone = NAD(P)+ + a hydroquinone.
Cofactor	FAD.
Enzyme regulation	Inhibited by dicoumarol.
Subunit structure	Homodimer. Ref.9 Ref.12
Subcellular location	Cytoplasm.
Induction	By dioxin.
Polymorphism	The Ser-187 polymorphism may be linked to susceptibility to forms of cancers.
Miscellaneous	Quinone reductase accepts electrons from both NADH and NADPH with equal efficiency.
Sequence similarities	Belongs to the NAD(P)H dehydrogenase (quinone) family.
Mass spectrometry	Molecular mass is 30864±6 Da from positions 1 - 274. Determined by ESI. Ref.11

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	FAD Flavoprotein NAD NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aging Inferred from electronic annotation. Source: Compara negative regulation of catalytic activity Inferred from electronic annotation. Source: Compara nitric oxide biosynthetic process Traceable author statement PubMed 9579781. Source: ProtInc positive regulation of neuron apoptotic process Inferred from electronic annotation. Source: Compara regulation of cellular amino acid metabolic process Traceable author statement. Source: Reactome response to estradiol stimulus Inferred from electronic annotation. Source: Compara response to ethanol Inferred from electronic annotation. Source: Compara response to nutrient Inferred from electronic annotation. Source: Compara response to oxidative stress Inferred from electronic annotation. Source: Compara response to toxin Traceable author statement PubMed 10393963. Source: ProtInc small molecule metabolic process Traceable author statement. Source: Reactome superoxide metabolic process Inferred from electronic annotation. Source: Compara synaptic transmission, cholinergic Traceable author statement PubMed 9579781. Source: ProtInc xenobiotic metabolic process Traceable author statement PubMed 10393963. Source: ProtInc
Cellular_component	cytosol Traceable author statement. Source: Reactome neuronal cell body Inferred from electronic annotation. Source: Compara
Molecular_function	NAD(P)H dehydrogenase (quinone) activity Traceable author statement PubMed 10393963. Source: ProtInc cytochrome-b5 reductase activity, acting on NAD(P)H Traceable author statement PubMed 9579781. Source: ProtInc superoxide dismutase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Tp63	O88898-2	2	EBI-3989435,EBI-2338228	From a different organism.
Tp63	O88898-6	2	EBI-3989435,EBI-2338244	From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P15559-1)

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.

Isoform 2 (identifier: P15559-2)

The sequence of this isoform differs from the canonical sequence as follows:
     140-173: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: P15559-3)

The sequence of this isoform differs from the canonical sequence as follows:
     102-139: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 274

273

NAD(P)H dehydrogenase [quinone] 1

PRO_0000071622

Regions

Nucleotide binding

18 – 19

2

FAD

Nucleotide binding

104 – 107

4

FAD

Nucleotide binding

148 – 151

4

FAD

Region

126 – 128

3

Substrate binding

Sites

Binding site

12

1

FAD

Binding site

67

1

FAD

Binding site

156

1

FAD

Binding site

201

1

FAD

Natural variations

Alternative sequence

102 – 139

38

Missing in isoform 3.

VSP_044446

Alternative sequence

140 – 173

34

Missing in isoform 2.

VSP_042716

Natural variant

139

1

R → W.
Corresponds to variant rs1131341 [ dbSNP | Ensembl ].

VAR_016170

Natural variant

187

1

P → S Lack of activity. Ref.3 Ref.4 Ref.14 Ref.15
Corresponds to variant rs1800566 [ dbSNP | Ensembl ].

VAR_008384

Natural variant

269

1

Q → H.
Corresponds to variant rs34447156 [ dbSNP | Ensembl ].

VAR_050220

Experimental info

Sequence conflict

252

1

F → S in BAG60289. Ref.4

Secondary structure

1

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274

Helix Strand Turn

Details...

Beta strand

5 – 10

6

Beta strand

15 – 17

3

Helix

18 – 32

15

Beta strand

36 – 41

6

Turn

42 – 46

5

Helix

53 – 55

3

Beta strand

56 – 58

3

Beta strand

63 – 65

3

Helix

68 – 78

11

Helix

83 – 94

12

Beta strand

96 – 103

8

Beta strand

106 – 108

3

Helix

111 – 120

10

Turn

124 – 126

3

Helix

129 – 131

3

Helix

133 – 135

3

Turn

137 – 140

4

Beta strand

142 – 148

7

Helix

154 – 156

3

Beta strand

160 – 162

3

Helix

165 – 173

9

Turn

174 – 177

4

Helix

178 – 180

3

Beta strand

188 – 190

3

Helix

193 – 195

3

Helix

198 – 212

15

Helix

213 – 217

5

Helix

226 – 228

3

Helix

233 – 235

3

Beta strand

237 – 239

3

Helix

241 – 248

8

Beta strand

254 – 256

3

Turn

266 – 270

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: A4010462AD00F3FE	FASTA	274	30,868
	10 20 30 40 50 60 MVGRRALIVL AHSERTSFNY AMKEAAAAAL KKKGWEVVES DLYAMNFNPI ISRKDITGKL 70 80 90 100 110 120 KDPANFQYPA ESVLAYKEGH LSPDIVAEQK KLEAADLVIF QFPLQWFGVP AILKGWFERV 130 140 150 160 170 180 FIGEFAYTYA AMYDKGPFRS KKAVLSITTG GSGSMYSLQG IHGDMNVILW PIQSGILHFC 190 200 210 220 230 240 GFQVLEPQLT YSIGHTPADA RIQILEGWKK RLENIWDETP LYFAPSSLFD LNFQAGFLMK 250 260 270 KEVQDEEKNK KFGLSVGHHL GKSIPTDNQI KARK
	Isoform 2 [UniParc]. Checksum: 63EF4B34E6394793	FASTA	240	27,295
	10 20 30 40 50 60 MVGRRALIVL AHSERTSFNY AMKEAAAAAL KKKGWEVVES DLYAMNFNPI ISRKDITGKL 70 80 90 100 110 120 KDPANFQYPA ESVLAYKEGH LSPDIVAEQK KLEAADLVIF QFPLQWFGVP AILKGWFERV 130 140 150 160 170 180 FIGEFAYTYA AMYDKGPFRS GILHFCGFQV LEPQLTYSIG HTPADARIQI LEGWKKRLEN 190 200 210 220 230 240 IWDETPLYFA PSSLFDLNFQ AGFLMKKEVQ DEEKNKKFGL SVGHHLGKSI PTDNQIKARK
	Isoform 3 [UniParc]. Checksum: 8BF801EAD71D02AB	FASTA	236	26,365
	10 20 30 40 50 60 MVGRRALIVL AHSERTSFNY AMKEAAAAAL KKKGWEVVES DLYAMNFNPI ISRKDITGKL 70 80 90 100 110 120 KDPANFQYPA ESVLAYKEGH LSPDIVAEQK KLEAADLVIF QSKKAVLSIT TGGSGSMYSL 130 140 150 160 170 180 QGIHGDMNVI LWPIQSGILH FCGFQVLEPQ LTYSIGHTPA DARIQILEGW KKRLENIWDE 190 200 210 220 230 TPLYFAPSSL FDLNFQAGFL MKKEVQDEEK NKKFGLSVGH HLGKSIPTDN QIKARK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	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].
[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]	"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].
[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.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00012069.
IPI00619898.
IPI00619966.

PIR

A30879. A41135.

RefSeq

NP_000894.1. NM_000903.2.
NP_001020604.1. NM_001025433.1.
NP_001020605.1. NM_001025434.1.

UniGene

Hs.406515.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P15559.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-24210N.

IntAct

P15559. 2 interactions.

MINT

MINT-231407.

STRING

9606.ENSP00000319788.

PTM databases

PhosphoSite

P15559.

Polymorphism databases

DMDM

118607.

Proteomic databases

PaxDb

P15559.

PRIDE

P15559.

Protocols and materials databases

DNASU

1728.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000320623; ENSP00000319788; ENSG00000181019.
ENST00000379046; ENSP00000368334; ENSG00000181019.
ENST00000379047; ENSP00000368335; ENSG00000181019.

GeneID

1728.

KEGG

hsa:1728.

UCSC

uc002exp.3. human.

Organism-specific databases

CTD

1728.

GeneCards

GC16M069744.

HGNC

HGNC:2874. NQO1.

HPA

CAB012421.
HPA007308.

MIM

125860. gene.

neXtProt

NX_P15559.

PharmGKB

PA31744.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2249.

HOGENOM

HOG000149970.

HOVERGEN

HBG029104.

InParanoid

P15559.

KO

K00355.

OMA

GILHYPG.

OrthoDB

EOG44BB36.

PhylomeDB

P15559.

Enzyme and pathway databases

BRENDA

1.6.5.2. 2681.

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

P15559.

Bgee

P15559.

CleanEx

HS_NQO1.

Genevestigator

P15559.

GermOnline

ENSG00000181019. Homo sapiens.

Family and domain databases

InterPro

IPR003680. Flavodoxin_fold.
[Graphical view]

Pfam

PF02525. Flavodoxin_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P15559.

ChEMBL

CHEMBL3623.

ChiTaRS

NQO1. human.

DrugBank

DB00266. Dicumarol.
DB00170. Menadione.

EvolutionaryTrace

P15559.

GenomeRNAi

1728.

NextBio

35473648.

SOURCE

Search...

Entry information

Entry name

NQO1_HUMAN

Accession

Primary (citable) accession number: P15559
Secondary accession number(s): B2R5Y9 , B4DNM7, B7ZAD1, Q86UK1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	May 1, 2013
This is version 145 of the entry and version 1 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.