GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

RAT:NQO1

From GONUTS
Jump to: navigation, search
Species (Taxon ID) Rattus norvegicus (Rat). (10116)
Gene Name(s) Nqo1 (synonyms: Nmor1)
Protein Name(s) NAD(P)H dehydrogenase [quinone] 1

Azoreductase DT-diaphorase DTD Menadione reductase NAD(P)H:quinone oxidoreductase 1 Phylloquinone reductase Quinone reductase 1 QR1

External Links
UniProt P05982
EMBL J02608
J02679
M36660
J02640
M31805
M31801
M31802
M31804
M33039
M33038
BC083542
X17464
PIR A34162
RefSeq NP_058696.2
UniGene Rn.11234
PDB 1QRD
PDBsum 1QRD
ProteinModelPortal P05982
SMR P05982
IntAct P05982
STRING 10116.ENSRNOP00000017175
ChEMBL CHEMBL3091269
iPTMnet P05982
PhosphoSitePlus P05982
World-2DPAGE 0004:P05982
PaxDb P05982
PRIDE P05982
Ensembl ENSRNOT00000017174
GeneID 24314
KEGG rno:24314
UCSC RGD:2503
CTD 1728
RGD 2503
eggNOG ENOG410IKWF
COG2249
GeneTree ENSGT00440000033410
HOGENOM HOG000149970
HOVERGEN HBG029104
InParanoid P05982
KO K00355
OMA LFPIHHG
OrthoDB EOG091G183R
PhylomeDB P05982
TreeFam TF300296
BRENDA 1.6.5.2
Reactome R-RNO-350562
EvolutionaryTrace P05982
PRO PR:P05982
Proteomes UP000002494
Bgee ENSRNOG00000012772
Genevisible P05982
GO GO:0005737
GO:0005829
GO:0030425
GO:0043025
GO:0042802
GO:0003955
GO:0004784
GO:0007568
GO:0070301
GO:0071248
GO:0043066
GO:0043086
GO:0043525
GO:0051602
GO:0032355
GO:0045471
GO:1904880
GO:1901698
GO:0007584
GO:0014070
GO:0006979
GO:0006801
Gene3D 3.40.50.360
InterPro IPR003680
IPR029039
Pfam PF02525
SUPFAM SSF52218

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

involved_in

GO:1904880

response to hydrogen sulfide

PMID:29054567[1]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:1901698

response to nitrogen compound

PMID:27867096[2]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0071248

cellular response to metal ion

PMID:28722058[3]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0070301

cellular response to hydrogen peroxide

PMID:28271112[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0051602

response to electrical stimulus

PMID:28887183[5]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0045471

response to ethanol

PMID:20833713[6]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0043525

positive regulation of neuron apoptotic process

PMID:12603827[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0043066

negative regulation of apoptotic process

PMID:22227174[8]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0043025

neuronal cell body

PMID:14991562[9]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0032355

response to estradiol

PMID:14672740[10]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0030425

dendrite

PMID:28322084[11]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0014070

response to organic cyclic compound

PMID:21549141[12]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0007584

response to nutrient

PMID:21092375[13]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0007568

aging

PMID:21602469[14]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006979

response to oxidative stress

PMID:12011483[15]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006801

superoxide metabolic process

PMID:17901563[16]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:14991562[9]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:28322084[11]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004784

superoxide dismutase activity

PMID:17901563[16]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003955

NAD(P)H dehydrogenase (quinone) activity

PMID:12603827[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

PMID:21873635[17]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000024521
UniProtKB:P16083

F

Seeded From UniProt

complete

enables

GO:0009055

electron transfer activity

PMID:21873635[17]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000024521
UniProtKB:P16083

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[17]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000024521
RGD:2503
UniProtKB:P15559
UniProtKB:P16083

C

Seeded From UniProt

complete

enables

GO:0003955

NAD(P)H dehydrogenase (quinone) activity

PMID:21873635[17]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:103187
PANTHER:PTN000024521
RGD:2503
UniProtKB:Q9HUJ0

F

Seeded From UniProt

complete

involved_in

GO:0019430

removal of superoxide radicals

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0004784

P

Seeded From UniProt

complete

involved_in

GO:0022900

electron transport chain

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0009055

P

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P15559
ensembl:ENSP00000319788

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P15559
ensembl:ENSP00000319788

C

Seeded From UniProt

complete

involved_in

GO:0043086

negative regulation of catalytic activity

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q64669
ensembl:ENSMUSP00000003947

P

Seeded From UniProt

complete

involved_in

GO:0006979

response to oxidative stress

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q64669
ensembl:ENSMUSP00000003947

P

Seeded From UniProt

complete

enables

GO:0003955

NAD(P)H dehydrogenase (quinone) activity

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q64669
ensembl:ENSMUSP00000003947

F

Seeded From UniProt

complete

enables

GO:0003955

NAD(P)H dehydrogenase (quinone) activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.6.5.2

F

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Imamura, F et al. (2017) Hydrogen Sulfide Specifically Alters NAD(P)H Quinone Dehydrogenase 1 (NQO1) Olfactory Neurons in the Rat. Neuroscience 366 105-112 PubMed GONUTS page
  2. Sánchez-Rodríguez, R et al. (2017) Ptgr1 expression is regulated by NRF2 in rat hepatocarcinogenesis and promotes cell proliferation and resistance to oxidative stress. Free Radic. Biol. Med. 102 87-99 PubMed GONUTS page
  3. Zhang, L et al. (2017) Activation of Nrf2/ARE signaling pathway attenuates lanthanum chloride induced injuries in primary rat astrocytes. Metallomics 9 1120-1131 PubMed GONUTS page
  4. Peng, S et al. (2017) Activation of Nrf2-driven antioxidant enzymes by cardamonin confers neuroprotection of PC12 cells against oxidative damage. Food Funct 8 997-1007 PubMed GONUTS page
  5. Hoque, KE et al. (2017) Electrical stimulation of the hippocampal fimbria facilitates neuronal nitric oxide synthase activity in the medial shell of the rat nucleus accumbens: Modulation by dopamine D1 and D2 receptor activation. Neuropharmacology 126 151-157 PubMed GONUTS page
  6. Yeligar, SM et al. (2010) Ethanol-induced HO-1 and NQO1 are differentially regulated by HIF-1alpha and Nrf2 to attenuate inflammatory cytokine expression. J. Biol. Chem. 285 35359-73 PubMed GONUTS page
  7. 7.0 7.1 Kapinya, KJ et al. (2003) Role of NAD(P)H:quinone oxidoreductase in the progression of neuronal cell death in vitro and following cerebral ischaemia in vivo. J. Neurochem. 84 1028-39 PubMed GONUTS page
  8. Kim, YH et al. (2012) Prevention of salt-induced renal injury by activation of NAD(P)H:quinone oxidoreductase 1, associated with NADPH oxidase. Free Radic. Biol. Med. 52 880-8 PubMed GONUTS page
  9. 9.0 9.1 Stringer, JL et al. (2004) Presence and induction of the enzyme NAD(P)H: quinone oxidoreductase 1 in the central nervous system. J. Comp. Neurol. 471 289-97 PubMed GONUTS page
  10. Sanchez, RI et al. (2003) Induction of NAD(P)H quinone oxidoreductase and glutathione S-transferase activities in livers of female August-Copenhagen Irish rats treated chronically with estradiol: comparison with the Sprague-Dawley rat. J. Steroid Biochem. Mol. Biol. 87 199-206 PubMed GONUTS page
  11. 11.0 11.1 Halasy, K et al. (2017) Fine structure and synaptology of the nitrergic neurons in medial septum of the rat brain. Acta. Biol. Hung. 68 1-13 PubMed GONUTS page
  12. Kodavanti, PR et al. (2011) Toluene effects on oxidative stress in brain regions of young-adult, middle-age, and senescent Brown Norway rats. Toxicol. Appl. Pharmacol. 256 386-98 PubMed GONUTS page
  13. Krajka-Kuźniak, V et al. (2011) Modulation of rat hepatic and kidney phase II enzymes by cabbage juices: comparison with the effects of indole-3-carbinol and phenethyl isothiocyanate. Br. J. Nutr. 105 816-26 PubMed GONUTS page
  14. Ungvari, Z et al. (2011) Vascular oxidative stress in aging: a homeostatic failure due to dysregulation of NRF2-mediated antioxidant response. Am. J. Physiol. Heart Circ. Physiol. 301 H363-72 PubMed GONUTS page
  15. Koike, E et al. (2002) cDNA microarray analysis of gene expression in rat alveolar macrophages in response to organic extract of diesel exhaust particles. Toxicol. Sci. 67 241-6 PubMed GONUTS page
  16. 16.0 16.1 Zhu, H et al. (2007) The highly expressed and inducible endogenous NAD(P)H:quinone oxidoreductase 1 in cardiovascular cells acts as a potential superoxide scavenger. Cardiovasc. Toxicol. 7 202-11 PubMed GONUTS page
  17. 17.0 17.1 17.2 17.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page