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Q9Y5S8 (NOX1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADPH oxidase 1

Short name=NOX-1
EC=1.-.-.-
Alternative name(s):
Mitogenic oxidase 1
Short name=MOX-1
NADH/NADPH mitogenic oxidase subunit P65-MOX
NOH-1
Gene names
Name:NOX1
Synonyms:MOX1, NOH1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length564 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Cofactor

NADP Potential.

FAD Potential.

Enzyme regulation

The oxidase activity is potentiated by NOXA1 and NOXO1. Ref.8 Ref.9

Subunit structure

NOX1, NOXA1, NOXO1, RAC1 and CYBA forms a functional multimeric complex supporting ROS production. Interacts with NOXA1 and NOXO1. Ref.9 Ref.10

Subcellular location

Cell projectioninvadopodium membrane; Multi-pass membrane protein Ref.11.

Tissue specificity

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.

Sequence similarities

Contains 1 FAD-binding FR-type domain.

Contains 1 ferric oxidoreductase domain.

Ontologies

Keywords
   Biological processElectron transport
Ion transport
Transport
   Cellular componentCell junction
Cell membrane
Cell projection
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransmembrane
Transmembrane helix
   LigandFAD
Flavoprotein
Heme
Iron
Metal-binding
NADP
   Molecular functionIon channel
Oxidoreductase
Voltage-gated channel
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNADP metabolic process

Inferred by curator Ref.1. Source: BHF-UCL

angiogenesis

Inferred from mutant phenotype PubMed 11805326. Source: BHF-UCL

cell migration

Inferred from mutant phenotype PubMed 18023288. Source: BHF-UCL

cellular response to acidity

Inferred from direct assay Ref.2. Source: BHF-UCL

extracellular matrix organization

Inferred from electronic annotation. Source: Ensembl

hydrogen peroxide metabolic process

Inferred from direct assay PubMed 11331784. Source: BHF-UCL

inflammatory response

Traceable author statement PubMed 18347018. Source: BHF-UCL

intracellular pH elevation

Inferred from direct assay Ref.2. Source: BHF-UCL

oxidation-reduction process

Inferred from direct assay Ref.2. Source: BHF-UCL

oxygen metabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from direct assay Ref.1. Source: BHF-UCL

positive regulation of integrin biosynthetic process

Inferred from mutant phenotype PubMed 18023288. Source: BHF-UCL

positive regulation of smooth muscle cell proliferation

Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL

positive regulation vascular endothelial growth factor production

Inferred from expression pattern PubMed 11805326. Source: BHF-UCL

proton transport

Inferred from direct assay Ref.2. Source: BHF-UCL

regulation of blood pressure

Traceable author statement PubMed 18347018. Source: BHF-UCL

regulation of systemic arterial blood pressure by renin-angiotensin

Inferred from electronic annotation. Source: Ensembl

respiratory burst

Traceable author statement Ref.10. Source: BHF-UCL

signal transduction

Traceable author statement PubMed 17673675. Source: BHF-UCL

superoxide anion generation

Inferred from direct assay Ref.1. Source: BHF-UCL

superoxide metabolic process

Inferred from mutant phenotype PubMed 18023288. Source: BHF-UCL

   Cellular_componentNADPH oxidase complex

Inferred from direct assay Ref.10. Source: BHF-UCL

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

early endosome

Inferred from direct assay PubMed 17673675. Source: BHF-UCL

integral component of membrane

Inferred by curator Ref.2. Source: BHF-UCL

invadopodium membrane

Inferred from direct assay Ref.11. Source: UniProtKB

   Molecular_functionNADP binding

Inferred by curator Ref.1. Source: BHF-UCL

Rac GTPase binding

Inferred from physical interaction Ref.10. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.10. Source: BHF-UCL

superoxide-generating NADPH oxidase activity

Traceable author statement Ref.1. Source: UniProtKB

voltage-gated proton channel activity

Inferred from direct assay Ref.2. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform NOH-1L (identifier: Q9Y5S8-1)

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 NOH-1S (identifier: Q9Y5S8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     159-190: QSRNTTVEYVTFTSIAGLTGVIMTIALILMVT → HPHITPTVYMFTVTFDMVLSSVNSNLLFLLIK
     191-564: Missing.
Isoform NOH-1LV (identifier: Q9Y5S8-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 564564NADPH oxidase 1
PRO_0000210148

Regions

Topological domain1 – 99Cytoplasmic Potential
Transmembrane10 – 3021Helical; Potential
Topological domain31 – 4414Extracellular Potential
Transmembrane45 – 7228Helical; Potential
Topological domain73 – 10230Cytoplasmic Potential
Transmembrane103 – 12321Helical; Potential
Topological domain124 – 16845Extracellular Potential
Transmembrane169 – 18921Helical; Potential
Topological domain190 – 20617Cytoplasmic Potential
Transmembrane207 – 22721Helical; Potential
Topological domain228 – 396169Extracellular Potential
Transmembrane397 – 41721Helical; Potential
Topological domain418 – 564147Cytoplasmic Potential
Domain54 – 283230Ferric oxidoreductase
Domain284 – 391108FAD-binding FR-type
Nucleotide binding338 – 3447FAD Potential
Region397 – 536140Interaction with NOXO1

Sites

Metal binding1011Iron (heme axial ligand) Probable
Metal binding1151Iron (heme axial ligand) Probable
Metal binding2091Iron (heme axial ligand) Probable
Metal binding2211Iron (heme axial ligand) Probable

Amino acid modifications

Glycosylation1621N-linked (GlcNAc...) Potential
Glycosylation2361N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence159 – 19032QSRNT…ILMVT → HPHITPTVYMFTVTFDMVLS SVNSNLLFLLIK in isoform NOH-1S.
VSP_001577
Alternative sequence191 – 564374Missing in isoform NOH-1S.
VSP_001578
Alternative sequence433 – 48149Missing in isoform NOH-1LV.
VSP_001579
Natural variant3151R → H.
Corresponds to variant rs2071756 [ dbSNP | Ensembl ].
VAR_049101
Natural variant3601D → N.
Corresponds to variant rs34688635 [ dbSNP | Ensembl ].
VAR_061176
Natural variant3781R → K.
Corresponds to variant rs35404864 [ dbSNP | Ensembl ].
VAR_049102

Experimental info

Sequence conflict1731I → V in AAD38133. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform NOH-1L [UniParc].

Last modified May 1, 2000. Version 2.
Checksum: C3BE290F4E6DBC9A

FASTA56464,871
        10         20         30         40         50         60 
MGNWVVNHWF SVLFLVVWLG LNVFLFVDAF LKYEKADKYY YTRKILGSTL ACARASALCL 

        70         80         90        100        110        120 
NFNSTLILLP VCRNLLSFLR GTCSFCSRTL RKQLDHNLTF HKLVAYMICL HTAIHIIAHL 

       130        140        150        160        170        180 
FNFDCYSRSR QATDGSLASI LSSLSHDEKK GGSWLNPIQS RNTTVEYVTF TSIAGLTGVI 

       190        200        210        220        230        240 
MTIALILMVT SATEFIRRSY FEVFWYTHHL FIFYILGLGI HGIGGIVRGQ TEESMNESHP 

       250        260        270        280        290        300 
RKCAESFEMW DDRDSHCRRP KFEGHPPESW KWILAPVILY ICERILRFYR SQQKVVITKV 

       310        320        330        340        350        360 
VMHPSKVLEL QMNKRGFSME VGQYIFVNCP SISLLEWHPF TLTSAPEEDF FSIHIRAAGD 

       370        380        390        400        410        420 
WTENLIRAFE QQYSPIPRIE VDGPFGTASE DVFQYEVAVL VGAGIGVTPF ASILKSIWYK 

       430        440        450        460        470        480 
FQCADHNLKT KKIYFYWICR ETGAFSWFNN LLTSLEQEME ELGKVGFLNY RLFLTGWDSN 

       490        500        510        520        530        540 
IVGHAALNFD KATDIVTGLK QKTSFGRPMW DNEFSTIATS HPKSVVGVFL CGPRTLAKSL 

       550        560 
RKCCHRYSSL DPRKVQFYFN KENF 

« Hide

Isoform NOH-1S [UniParc].

Checksum: 75C0B809E9AE8E3D
Show »

FASTA19021,704
Isoform NOH-1LV [UniParc].

Checksum: 1D79577159D69688
Show »

FASTA51558,972

References

« Hide 'large scale' references
[1]"Cell transformation by the superoxide-generating oxidase Mox1."
Suh Y.-A., Arnold R.S., Lassegue B., Shi J., Xu X., Sorescu D., Chung A.B., Griendling K.K., Lambeth J.D.
Nature 401:79-82(1999) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]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. expand/collapse author list , 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 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS14474.1. [Q9Y5S8-1]
CCDS14475.1. [Q9Y5S8-3]
RefSeqNP_001258744.1. NM_001271815.1.
NP_008983.2. NM_007052.4. [Q9Y5S8-1]
NP_039249.1. NM_013955.2. [Q9Y5S8-3]
UniGeneHs.592227.

3D structure databases

ProteinModelPortalQ9Y5S8.
SMRQ9Y5S8. Positions 379-564.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117966. 1 interaction.
DIPDIP-60457N.
STRING9606.ENSP00000362057.

Chemistry

BindingDBQ9Y5S8.
ChEMBLCHEMBL1287628.

Protein family/group databases

PeroxiBase5410. HsNOx01.
TCDB5.B.1.1.3. the phagocyte (gp91(phox)) nadph oxidase family.

PTM databases

PhosphoSiteQ9Y5S8.

Polymorphism databases

DMDM8134597.

Proteomic databases

PaxDbQ9Y5S8.
PRIDEQ9Y5S8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000217885; ENSP00000217885; ENSG00000007952. [Q9Y5S8-3]
ENST00000372966; ENSP00000362057; ENSG00000007952. [Q9Y5S8-1]
GeneID27035.
KEGGhsa:27035.
UCSCuc004egj.3. human. [Q9Y5S8-1]
uc004egl.4. human. [Q9Y5S8-3]

Organism-specific databases

CTD27035.
GeneCardsGC0XM100098.
HGNCHGNC:7889. NOX1.
HPAHPA035299.
HPA035300.
MIM300225. gene.
neXtProtNX_Q9Y5S8.
PharmGKBPA31690.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG287712.
HOGENOMHOG000216669.
HOVERGENHBG003760.
InParanoidQ9Y5S8.
KOK08008.
OMAMENGTSE.
OrthoDBEOG71P299.
PhylomeDBQ9Y5S8.
TreeFamTF105354.

Gene expression databases

ArrayExpressQ9Y5S8.
BgeeQ9Y5S8.
CleanExHS_NOX1.
GenevestigatorQ9Y5S8.

Family and domain databases

InterProIPR000778. Cyt_b245_heavy_chain.
IPR013112. FAD-bd_8.
IPR017927. Fd_Rdtase_FAD-bd.
IPR013130. Fe3_Rdtase_TM_dom.
IPR013121. Fe_red_NAD-bd_6.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamPF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
PRINTSPR00466. GP91PHOX.
SUPFAMSSF63380. SSF63380. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiNOX1.
GenomeRNAi27035.
NextBio49586.
PROQ9Y5S8.
SOURCESearch...

Entry information

Entry nameNOX1_HUMAN
AccessionPrimary (citable) accession number: Q9Y5S8
Secondary accession number(s): A8K836, O95691, Q2PP02
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM