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Q9Y5S8

- NOX1_HUMAN

UniProt

Q9Y5S8 - NOX1_HUMAN

Protein

NADPH oxidase 1

Gene

NOX1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (01 May 2000)
      Previous versions | rss
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    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. protein binding Source: BHF-UCL
    4. Rac GTPase binding Source: BHF-UCL
    5. superoxide-generating NADPH oxidase activity Source: UniProtKB
    6. 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 acidic pH Source: BHF-UCL
    4. extracellular matrix organization Source: Ensembl
    5. hydrogen peroxide metabolic process Source: BHF-UCL
    6. inflammatory response Source: BHF-UCL
    7. intracellular pH elevation Source: BHF-UCL
    8. NADP metabolic process Source: BHF-UCL
    9. oxidation-reduction process Source: BHF-UCL
    10. oxygen metabolic process Source: Ensembl
    11. positive regulation of cell proliferation Source: BHF-UCL
    12. positive regulation of integrin biosynthetic process Source: BHF-UCL
    13. positive regulation of smooth muscle cell proliferation Source: BHF-UCL
    14. positive regulation vascular endothelial growth factor production Source: BHF-UCL
    15. proton transport Source: BHF-UCL
    16. regulation of blood pressure Source: BHF-UCL
    17. regulation of systemic arterial blood pressure by renin-angiotensin Source: Ensembl
    18. respiratory burst Source: BHF-UCL
    19. signal transduction Source: BHF-UCL
    20. superoxide anion generation Source: BHF-UCL
    21. superoxide metabolic process Source: BHF-UCL

    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

    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...)Sequence Analysis
    Glycosylationi236 – 2361N-linked (GlcNAc...)Sequence Analysis

    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

    ArrayExpressiQ9Y5S8.
    BgeeiQ9Y5S8.
    CleanExiHS_NOX1.
    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.
    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.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view]
    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

    MGNWVVNHWF SVLFLVVWLG LNVFLFVDAF LKYEKADKYY YTRKILGSTL    50
    ACARASALCL NFNSTLILLP VCRNLLSFLR GTCSFCSRTL RKQLDHNLTF 100
    HKLVAYMICL HTAIHIIAHL FNFDCYSRSR QATDGSLASI LSSLSHDEKK 150
    GGSWLNPIQS RNTTVEYVTF TSIAGLTGVI MTIALILMVT SATEFIRRSY 200
    FEVFWYTHHL FIFYILGLGI HGIGGIVRGQ TEESMNESHP RKCAESFEMW 250
    DDRDSHCRRP KFEGHPPESW KWILAPVILY ICERILRFYR SQQKVVITKV 300
    VMHPSKVLEL QMNKRGFSME VGQYIFVNCP SISLLEWHPF TLTSAPEEDF 350
    FSIHIRAAGD WTENLIRAFE QQYSPIPRIE VDGPFGTASE DVFQYEVAVL 400
    VGAGIGVTPF ASILKSIWYK FQCADHNLKT KKIYFYWICR ETGAFSWFNN 450
    LLTSLEQEME ELGKVGFLNY RLFLTGWDSN IVGHAALNFD KATDIVTGLK 500
    QKTSFGRPMW DNEFSTIATS HPKSVVGVFL CGPRTLAKSL RKCCHRYSSL 550
    DPRKVQFYFN KENF 564
    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.
    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

    ArrayExpressi Q9Y5S8.
    Bgeei Q9Y5S8.
    CleanExi HS_NOX1.
    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.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view ]
    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

    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.

    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 1, 2014
    This is version 132 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