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Q9Y5S8

- NOX1_HUMAN

UniProt

Q9Y5S8 - NOX1_HUMAN

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Protein

NADPH oxidase 1

Gene

NOX1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

NOH-1S is a voltage-gated proton channel that mediates the H+ currents of resting phagocytes and other tissues. It participates in the regulation of cellular pH and is blocked by zinc. NOH-1L is a pyridine nucleotide-dependent oxidoreductase that generates superoxide and might conduct H+ ions as part of its electron transport mechanism, whereas NOH-1S does not contain an electron transport chain.

Cofactori

NADP.Curated
FAD.Curated

Enzyme regulationi

The oxidase activity is potentiated by NOXA1 and NOXO1.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi101 – 1011Iron (heme axial ligand)Curated
Metal bindingi115 – 1151Iron (heme axial ligand)Curated
Metal bindingi209 – 2091Iron (heme axial ligand)Curated
Metal bindingi221 – 2211Iron (heme axial ligand)Curated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi338 – 3447FADSequence Analysis

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. NADP binding Source: BHF-UCL
  3. Rac GTPase binding Source: BHF-UCL
  4. superoxide-generating NADPH oxidase activity Source: UniProtKB
  5. voltage-gated proton channel activity Source: BHF-UCL

GO - Biological processi

  1. angiogenesis Source: BHF-UCL
  2. cell migration Source: BHF-UCL
  3. cellular response to hyperoxia Source: Ensembl
  4. cellular stress response to acidic pH Source: BHF-UCL
  5. extracellular matrix organization Source: Ensembl
  6. hydrogen peroxide metabolic process Source: BHF-UCL
  7. inflammatory response Source: BHF-UCL
  8. intracellular pH elevation Source: BHF-UCL
  9. NADP metabolic process Source: BHF-UCL
  10. oxidation-reduction process Source: BHF-UCL
  11. oxygen metabolic process Source: Ensembl
  12. positive regulation of cell proliferation Source: BHF-UCL
  13. positive regulation of integrin biosynthetic process Source: BHF-UCL
  14. positive regulation of JNK cascade Source: Ensembl
  15. positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: Ensembl
  16. positive regulation of smooth muscle cell proliferation Source: BHF-UCL
  17. positive regulation vascular endothelial growth factor production Source: BHF-UCL
  18. proton transport Source: BHF-UCL
  19. regulation of blood pressure Source: BHF-UCL
  20. regulation of systemic arterial blood pressure by renin-angiotensin Source: Ensembl
  21. respiratory burst Source: BHF-UCL
  22. signal transduction Source: BHF-UCL
  23. superoxide anion generation Source: BHF-UCL
  24. superoxide metabolic process Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Oxidoreductase, Voltage-gated channel

Keywords - Biological processi

Electron transport, Ion transport, Transport

Keywords - Ligandi

FAD, Flavoprotein, Heme, Iron, Metal-binding, NADP

Protein family/group databases

PeroxiBasei5410. HsNOx01.
TCDBi5.B.1.1.3. the phagocyte (gp91(phox)) nadph oxidase family.

Names & Taxonomyi

Protein namesi
Recommended name:
NADPH oxidase 1 (EC:1.-.-.-)
Short name:
NOX-1
Alternative name(s):
Mitogenic oxidase 1
Short name:
MOX-1
NADH/NADPH mitogenic oxidase subunit P65-MOX
NOH-1
Gene namesi
Name:NOX1
Synonyms:MOX1, NOH1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:7889. NOX1.

Subcellular locationi

Cell projectioninvadopodium membrane 1 Publication; Multi-pass membrane protein 1 Publication

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. early endosome Source: BHF-UCL
  3. integral component of membrane Source: BHF-UCL
  4. invadopodium membrane Source: UniProtKB
  5. NADPH oxidase complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31690.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 564564NADPH oxidase 1PRO_0000210148Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi162 – 1621N-linked (GlcNAc...)1 Publication
Glycosylationi236 – 2361N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9Y5S8.
PRIDEiQ9Y5S8.

PTM databases

PhosphoSiteiQ9Y5S8.

Expressioni

Tissue specificityi

NOH-1L is detected in colon, uterus, prostate, and colon carcinoma, but not in peripheral blood leukocytes. NOH-1S is detected only in colon and colon carcinoma cells.

Gene expression databases

BgeeiQ9Y5S8.
CleanExiHS_NOX1.
ExpressionAtlasiQ9Y5S8. baseline and differential.
GenevestigatoriQ9Y5S8.

Organism-specific databases

HPAiHPA035299.
HPA035300.

Interactioni

Subunit structurei

NOX1, NOXA1, NOXO1, RAC1 and CYBA forms a functional multimeric complex supporting ROS production. Interacts with NOXA1 and NOXO1.2 Publications

Protein-protein interaction databases

BioGridi117966. 1 interaction.
DIPiDIP-60457N.
STRINGi9606.ENSP00000362057.

Structurei

3D structure databases

ProteinModelPortaliQ9Y5S8.
SMRiQ9Y5S8. Positions 379-564.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 99CytoplasmicSequence Analysis
Topological domaini31 – 4414ExtracellularSequence AnalysisAdd
BLAST
Topological domaini73 – 10230CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini124 – 16845ExtracellularSequence AnalysisAdd
BLAST
Topological domaini190 – 20617CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini228 – 396169ExtracellularSequence AnalysisAdd
BLAST
Topological domaini418 – 564147CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei10 – 3021HelicalSequence AnalysisAdd
BLAST
Transmembranei45 – 7228HelicalSequence AnalysisAdd
BLAST
Transmembranei103 – 12321HelicalSequence AnalysisAdd
BLAST
Transmembranei169 – 18921HelicalSequence AnalysisAdd
BLAST
Transmembranei207 – 22721HelicalSequence AnalysisAdd
BLAST
Transmembranei397 – 41721HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini54 – 283230Ferric oxidoreductaseAdd
BLAST
Domaini284 – 391108FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni397 – 536140Interaction with NOXO1Add
BLAST

Sequence similaritiesi

Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation
Contains 1 ferric oxidoreductase domain.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG287712.
GeneTreeiENSGT00550000074350.
HOGENOMiHOG000216669.
HOVERGENiHBG003760.
InParanoidiQ9Y5S8.
KOiK08008.
OMAiMENGTSE.
OrthoDBiEOG71P299.
PhylomeDBiQ9Y5S8.
TreeFamiTF105354.

Family and domain databases

InterProiIPR000778. Cyt_b245_heavy_chain.
IPR013112. FAD-bd_8.
IPR017927. Fd_Rdtase_FAD-bd.
IPR013130. Fe3_Rdtase_TM_dom.
IPR013121. Fe_red_NAD-bd_6.
IPR029650. NOX1.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PANTHERiPTHR11972:SF10. PTHR11972:SF10. 1 hit.
PfamiPF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
PRINTSiPR00466. GP91PHOX.
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform NOH-1L (identifier: Q9Y5S8-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MGNWVVNHWF SVLFLVVWLG LNVFLFVDAF LKYEKADKYY YTRKILGSTL
60 70 80 90 100
ACARASALCL NFNSTLILLP VCRNLLSFLR GTCSFCSRTL RKQLDHNLTF
110 120 130 140 150
HKLVAYMICL HTAIHIIAHL FNFDCYSRSR QATDGSLASI LSSLSHDEKK
160 170 180 190 200
GGSWLNPIQS RNTTVEYVTF TSIAGLTGVI MTIALILMVT SATEFIRRSY
210 220 230 240 250
FEVFWYTHHL FIFYILGLGI HGIGGIVRGQ TEESMNESHP RKCAESFEMW
260 270 280 290 300
DDRDSHCRRP KFEGHPPESW KWILAPVILY ICERILRFYR SQQKVVITKV
310 320 330 340 350
VMHPSKVLEL QMNKRGFSME VGQYIFVNCP SISLLEWHPF TLTSAPEEDF
360 370 380 390 400
FSIHIRAAGD WTENLIRAFE QQYSPIPRIE VDGPFGTASE DVFQYEVAVL
410 420 430 440 450
VGAGIGVTPF ASILKSIWYK FQCADHNLKT KKIYFYWICR ETGAFSWFNN
460 470 480 490 500
LLTSLEQEME ELGKVGFLNY RLFLTGWDSN IVGHAALNFD KATDIVTGLK
510 520 530 540 550
QKTSFGRPMW DNEFSTIATS HPKSVVGVFL CGPRTLAKSL RKCCHRYSSL
560
DPRKVQFYFN KENF
Length:564
Mass (Da):64,871
Last modified:May 1, 2000 - v2
Checksum:iC3BE290F4E6DBC9A
GO
Isoform NOH-1S (identifier: Q9Y5S8-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     159-190: QSRNTTVEYVTFTSIAGLTGVIMTIALILMVT → HPHITPTVYMFTVTFDMVLSSVNSNLLFLLIK
     191-564: Missing.

Show »
Length:190
Mass (Da):21,704
Checksum:i75C0B809E9AE8E3D
GO
Isoform NOH-1LV (identifier: Q9Y5S8-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     433-481: Missing.

Show »
Length:515
Mass (Da):58,972
Checksum:i1D79577159D69688
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti173 – 1731I → V in AAD38133. (PubMed:10615049)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti315 – 3151R → H.
Corresponds to variant rs2071756 [ dbSNP | Ensembl ].
VAR_049101
Natural varianti360 – 3601D → N.
Corresponds to variant rs34688635 [ dbSNP | Ensembl ].
VAR_061176
Natural varianti378 – 3781R → K.
Corresponds to variant rs35404864 [ dbSNP | Ensembl ].
VAR_049102

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei159 – 19032QSRNT…ILMVT → HPHITPTVYMFTVTFDMVLS SVNSNLLFLLIK in isoform NOH-1S. 1 PublicationVSP_001577Add
BLAST
Alternative sequencei191 – 564374Missing in isoform NOH-1S. 1 PublicationVSP_001578Add
BLAST
Alternative sequencei433 – 48149Missing in isoform NOH-1LV. 1 PublicationVSP_001579Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF127763 mRNA. Translation: AAD38133.1.
AF166326 mRNA. Translation: AAF23232.1.
AF166327 mRNA. Translation: AAF23233.1.
AF166328 mRNA. Translation: AAF23234.1.
DQ314883 Genomic DNA. Translation: ABC40742.1.
AK292201 mRNA. Translation: BAF84890.1.
Z83819 Genomic DNA. Translation: CAI42336.1.
Z83819 Genomic DNA. Translation: CAI42337.1.
CH471115 Genomic DNA. Translation: EAX02820.1.
BC075014 mRNA. Translation: AAH75014.1.
BC075015 mRNA. Translation: AAH75015.1.
CCDSiCCDS14474.1. [Q9Y5S8-1]
CCDS14475.1. [Q9Y5S8-3]
RefSeqiNP_001258744.1. NM_001271815.1.
NP_008983.2. NM_007052.4. [Q9Y5S8-1]
NP_039249.1. NM_013955.2. [Q9Y5S8-3]
UniGeneiHs.592227.

Genome annotation databases

EnsembliENST00000217885; ENSP00000217885; ENSG00000007952. [Q9Y5S8-3]
ENST00000372966; ENSP00000362057; ENSG00000007952. [Q9Y5S8-1]
GeneIDi27035.
KEGGihsa:27035.
UCSCiuc004egj.3. human. [Q9Y5S8-1]
uc004egl.4. human. [Q9Y5S8-3]

Polymorphism databases

DMDMi8134597.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF127763 mRNA. Translation: AAD38133.1 .
AF166326 mRNA. Translation: AAF23232.1 .
AF166327 mRNA. Translation: AAF23233.1 .
AF166328 mRNA. Translation: AAF23234.1 .
DQ314883 Genomic DNA. Translation: ABC40742.1 .
AK292201 mRNA. Translation: BAF84890.1 .
Z83819 Genomic DNA. Translation: CAI42336.1 .
Z83819 Genomic DNA. Translation: CAI42337.1 .
CH471115 Genomic DNA. Translation: EAX02820.1 .
BC075014 mRNA. Translation: AAH75014.1 .
BC075015 mRNA. Translation: AAH75015.1 .
CCDSi CCDS14474.1. [Q9Y5S8-1 ]
CCDS14475.1. [Q9Y5S8-3 ]
RefSeqi NP_001258744.1. NM_001271815.1.
NP_008983.2. NM_007052.4. [Q9Y5S8-1 ]
NP_039249.1. NM_013955.2. [Q9Y5S8-3 ]
UniGenei Hs.592227.

3D structure databases

ProteinModelPortali Q9Y5S8.
SMRi Q9Y5S8. Positions 379-564.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117966. 1 interaction.
DIPi DIP-60457N.
STRINGi 9606.ENSP00000362057.

Chemistry

BindingDBi Q9Y5S8.
ChEMBLi CHEMBL1287628.

Protein family/group databases

PeroxiBasei 5410. HsNOx01.
TCDBi 5.B.1.1.3. the phagocyte (gp91(phox)) nadph oxidase family.

PTM databases

PhosphoSitei Q9Y5S8.

Polymorphism databases

DMDMi 8134597.

Proteomic databases

PaxDbi Q9Y5S8.
PRIDEi Q9Y5S8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000217885 ; ENSP00000217885 ; ENSG00000007952 . [Q9Y5S8-3 ]
ENST00000372966 ; ENSP00000362057 ; ENSG00000007952 . [Q9Y5S8-1 ]
GeneIDi 27035.
KEGGi hsa:27035.
UCSCi uc004egj.3. human. [Q9Y5S8-1 ]
uc004egl.4. human. [Q9Y5S8-3 ]

Organism-specific databases

CTDi 27035.
GeneCardsi GC0XM100098.
HGNCi HGNC:7889. NOX1.
HPAi HPA035299.
HPA035300.
MIMi 300225. gene.
neXtProti NX_Q9Y5S8.
PharmGKBi PA31690.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG287712.
GeneTreei ENSGT00550000074350.
HOGENOMi HOG000216669.
HOVERGENi HBG003760.
InParanoidi Q9Y5S8.
KOi K08008.
OMAi MENGTSE.
OrthoDBi EOG71P299.
PhylomeDBi Q9Y5S8.
TreeFami TF105354.

Miscellaneous databases

GeneWikii NOX1.
GenomeRNAii 27035.
NextBioi 49586.
PROi Q9Y5S8.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y5S8.
CleanExi HS_NOX1.
ExpressionAtlasi Q9Y5S8. baseline and differential.
Genevestigatori Q9Y5S8.

Family and domain databases

InterProi IPR000778. Cyt_b245_heavy_chain.
IPR013112. FAD-bd_8.
IPR017927. Fd_Rdtase_FAD-bd.
IPR013130. Fe3_Rdtase_TM_dom.
IPR013121. Fe_red_NAD-bd_6.
IPR029650. NOX1.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view ]
PANTHERi PTHR11972:SF10. PTHR11972:SF10. 1 hit.
Pfami PF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view ]
PRINTSi PR00466. GP91PHOX.
SUPFAMi SSF63380. SSF63380. 1 hit.
PROSITEi PS51384. FAD_FR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM NOH-1L).
    Tissue: Colon epithelium.
  2. "A mammalian H+ channel, generated through alternative splicing of the NADPH oxidase homolog NOH-1."
    Banfi B., Maturana A., Jaconi S., Arnaudeau S., Laforge T., Sinha B., Ligeti E., Demaurex N., Krause K.-H.
    Science 287:138-142(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS NOH-1L; NOH-1LV AND NOH-1S).
  3. NHLBI resequencing and genotyping service (RS&G)
    Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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] (ISOFORM NOH-1L).
    Tissue: Colon.
  5. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. 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 NOH-1L).
  8. "NOXO1, regulation of lipid binding, localization, and activation of Nox1 by the Phox homology (PX) domain."
    Cheng G., Lambeth J.D.
    J. Biol. Chem. 279:4737-4742(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  9. "Molecular interaction of NADPH oxidase 1 with betaPix and Nox Organizer 1."
    Park H.S., Park D., Bae Y.S.
    Biochem. Biophys. Res. Commun. 339:985-990(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NOXO1, ENZYME REGULATION.
  10. "Nox1-dependent reactive oxygen generation is regulated by Rac1."
    Cheng G., Diebold B.A., Hughes Y., Lambeth J.D.
    J. Biol. Chem. 281:17718-17726(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX CONTAINING NOX1; NOXO1; NOXA1 AND RAC1.
  11. "Novel p47(phox)-related organizers regulate localized NADPH oxidase 1 (Nox1) activity."
    Gianni D., Diaz B., Taulet N., Fowler B., Courtneidge S.A., Bokoch G.M.
    Sci. Signal. 2:RA54-RA54(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  12. "N-Linked glycosylation of the superoxide-producing NADPH oxidase Nox1."
    Miyano K., Sumimoto H.
    Biochem. Biophys. Res. Commun. 443:1060-1065(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-162 AND ASN-236.

Entry informationi

Entry nameiNOX1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5S8
Secondary accession number(s): A8K836, O95691, Q2PP02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3