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:NOX1

From GONUTS
Jump to: navigation, search
Species (Taxon ID) Rattus norvegicus (Rat). (10116)
Gene Name(s) Nox1 (synonyms: Mox1, Noh1)
Protein Name(s) NADPH oxidase 1

NOX-1 Mitogenic oxidase 1 MOX-1 NADH/NADPH mitogenic oxidase subunit P65-MOX NOH-1

External Links
UniProt Q9WV87
EMBL AF152963
RefSeq NP_446135.1
UniGene Rn.220465
ProteinModelPortal Q9WV87
SMR Q9WV87
MINT MINT-4998488
STRING 10116.ENSRNOP00000065995
ChEMBL CHEMBL1075231
PeroxiBase 5408
iPTMnet Q9WV87
PhosphoSitePlus Q9WV87
PaxDb Q9WV87
GeneID 114243
KEGG rno:114243
CTD 27035
RGD 620598
eggNOG KOG0039
ENOG410XNZY
HOVERGEN HBG003760
InParanoid Q9WV87
KO K08008
PhylomeDB Q9WV87
PRO PR:Q9WV87
Proteomes UP000002494
GO GO:0030054
GO:0071438
GO:0043020
GO:0046872
GO:0016175
GO:2000379
GO:0048661
GO:0000302
GO:0007165
GO:0042554
InterPro IPR000778
IPR013112
IPR017927
IPR013130
IPR013121
IPR029650
IPR017938
PANTHER PTHR11972:SF110
Pfam PF08022
PF01794
PF08030
PRINTS PR00466
SUPFAM SSF63380
PROSITE PS51384

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0016174

NAD(P)H oxidase activity

PMID:28317735[1]

ECO:0000315

F

RAT NOX1 // Inhibition of NOX1 with 2-acetylphenothiazine resulted in a decrease of NADPH oxidase activity in cells (Fig. 2D)

complete
CACAO 12362

involved_in

GO:0048661

positive regulation of smooth muscle cell proliferation

PMID:10485709[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0042554

superoxide anion generation

PMID:10485709[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:2000379

positive regulation of reactive oxygen species metabolic process

PMID:16254042[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0043020

NADPH oxidase complex

PMID:15322091[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0007165

signal transduction

PMID:10485709[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0000302

response to reactive oxygen species

PMID:11832489[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0283531
MGI:MGI:1354184
MGI:MGI:2450016
MGI:MGI:2681162
PANTHER:PTN001735877
PomBase:SPBC1683.09c
RGD:620600
SGD:S000003128
SGD:S000004037
SGD:S000005512
TAIR:locus:2017789
TAIR:locus:2024603
TAIR:locus:2025351
TAIR:locus:2025366
TAIR:locus:2157032
TAIR:locus:2157348
TAIR:locus:2157697
TAIR:locus:2160917
TAIR:locus:2178677
TAIR:locus:2178687
UniProtKB:P04839
UniProtKB:Q96PH1
UniProtKB:Q9NPH5
UniProtKB:Q9NRD8
UniProtKB:Q9SBI0
UniProtKB:Q9Y5S8
WB:WBGene00000253
dictyBase:DDB_G0287101
dictyBase:DDB_G0289653

P

Seeded From UniProt

complete

part_of

GO:0043020

NADPH oxidase complex

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:2681162
MGI:MGI:88574
PANTHER:PTN000239643
RGD:620574
RGD:620598
RGD:620600
UniProtKB:P04839
UniProtKB:Q9Y5S8

C

Seeded From UniProt

complete

involved_in

GO:0042554

superoxide anion generation

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:1354184
MGI:MGI:2450016
MGI:MGI:2681162
PANTHER:PTN000239643
RGD:620598
UniProtKB:P04839
UniProtKB:Q96PH1
UniProtKB:Q9Y5S8
dictyBase:DDB_G0287101

P

Seeded From UniProt

complete

enables

GO:0016175

superoxide-generating NADPH oxidase activity

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:1354184
MGI:MGI:2450016
MGI:MGI:2681162
PANTHER:PTN000239643
UniProtKB:Q96PH1
UniProtKB:Q9Y5S8
dictyBase:DDB_G0287101
dictyBase:DDB_G0289653

F

Seeded From UniProt

complete

involved_in

GO:0006952

defense response

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0283531
MGI:MGI:88574
PANTHER:PTN000239643
UniProtKB:P04839
ZFIN:ZDB-GENE-091117-14
dictyBase:DDB_G0287101
dictyBase:DDB_G0289653
dictyBase:DDB_G0291117

P

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:2139422
MGI:MGI:2681162
MGI:MGI:88574
PANTHER:PTN001735877
RGD:620574
RGD:620598
RGD:620600
SGD:S000005512
TAIR:locus:2024603
TAIR:locus:2025351
TAIR:locus:2157027
TAIR:locus:2157348
TAIR:locus:2157697
TAIR:locus:2160917
UniProtKB:O81209
UniProtKB:P04839
UniProtKB:Q9Y5S8
WB:WBGene00000253

C

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000778

C

Seeded From UniProt

complete

enables

GO:0016175

superoxide-generating NADPH oxidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR029650

F

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000778
InterPro:IPR013112
InterPro:IPR013121
InterPro:IPR017927

F

Seeded From UniProt

complete

involved_in

GO:0042554

superoxide anion generation

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR029650

P

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000778
InterPro:IPR013112
InterPro:IPR013121
InterPro:IPR017927

P

Seeded From UniProt

complete

enables

GO:0016175

superoxide-generating NADPH oxidase activity

PMID:11832489[5]

ECO:0000304

author statement supported by traceable reference used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0030054

cell junction

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0965

C

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0812

C

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037
GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0249
UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

part_of

GO:0042995

cell projection

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0966

C

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:0005886

plasma membrane

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1003
UniProtKB-SubCell:SL-0039

C

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

part_of

GO:0071438

invadopodium membrane

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0290

C

Seeded From UniProt

complete

Notes

References

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

  1. Blanca, AJ et al. (2017) l-Carnitine ameliorates the oxidative stress response to angiotensin II by modulating NADPH oxidase through a reduction in protein kinase c activity and NF-κB translocation to the nucleus. Food Chem 228 356-366 PubMed GONUTS page
  2. 2.0 2.1 2.2 Suh, YA et al. (1999) Cell transformation by the superoxide-generating oxidase Mox1. Nature 401 79-82 PubMed GONUTS page
  3. Plesková, M et al. (2006) Nitric oxide down-regulates the expression of the catalytic NADPH oxidase subunit Nox1 in rat renal mesangial cells. FASEB J. 20 139-41 PubMed GONUTS page
  4. Ambasta, RK et al. (2004) Direct interaction of the novel Nox proteins with p22phox is required for the formation of a functionally active NADPH oxidase. J. Biol. Chem. 279 45935-41 PubMed GONUTS page
  5. 5.0 5.1 Katsuyama, M et al. (2002) NADPH oxidase is involved in prostaglandin F2alpha-induced hypertrophy of vascular smooth muscle cells: induction of NOX1 by PGF2alpha. J. Biol. Chem. 277 13438-42 PubMed GONUTS page
  6. 6.0 6.1 6.2 6.3 6.4 6.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page