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Q9NPH5

- NOX4_HUMAN

UniProt

Q9NPH5 - NOX4_HUMAN

Protein

NADPH oxidase 4

Gene

NOX4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 2 (04 Nov 2008)
      Previous versions | rss
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    Functioni

    Constitutive NADPH oxidase which generates superoxide intracellularly upon formation of a complex with CYBA/p22phox. Regulates signaling cascades probably through phosphatases inhibition. May function as an oxygen sensor regulating the KCNK3/TASK-1 potassium channel and HIF1A activity. May regulate insulin signaling cascade. May play a role in apoptosis, bone resorption and lipolysaccharide-mediated activation of NFKB. May produce superoxide in the nucleus and play a role in regulating gene expression upon cell stimulation. Isoform 3 is not functional. Isoform 5 and isoform 6 display reduced activity.
    Isoform 4: Involved in redox signaling in vascular cells. Constitutively and NADPH-dependently generates reactive oxygen species (ROS). Modulates the nuclear activation of ERK1/2 and the ELK1 transcription factor, and is capable of inducing nuclear DNA damage. Displays an increased activity relative to isoform 1.

    Enzyme regulationi

    Inhibited by plumbagin By similarity. Activated by phorbol 12-myristate 13-acetate (PMA). Activated by insulin. Inhibited by diphenylene iodonium.By similarity4 Publications

    GO - Molecular functioni

    1. electron carrier activity Source: UniProtKB
    2. flavin adenine dinucleotide binding Source: UniProtKB
    3. heme binding Source: UniProtKB
    4. modified amino acid binding Source: UniProtKB
    5. NAD(P)H oxidase activity Source: UniProtKB
    6. nucleotide binding Source: UniProtKB
    7. oxygen sensor activity Source: UniProtKB
    8. superoxide-generating NADPH oxidase activity Source: Ensembl

    GO - Biological processi

    1. bone resorption Source: Ensembl
    2. cardiocyte differentiation Source: Ensembl
    3. cell aging Source: UniProtKB
    4. cell morphogenesis Source: UniProtKB
    5. cellular response to cAMP Source: Ensembl
    6. cellular response to gamma radiation Source: Ensembl
    7. cellular response to glucose stimulus Source: Ensembl
    8. cellular response to transforming growth factor beta stimulus Source: Ensembl
    9. homocysteine metabolic process Source: UniProtKB
    10. inflammatory response Source: UniProtKB
    11. negative regulation of cell proliferation Source: UniProtKB
    12. oxidation-reduction process Source: UniProtKB
    13. positive regulation of apoptotic process Source: Ensembl
    14. positive regulation of DNA biosynthetic process Source: Ensembl
    15. positive regulation of ERK1 and ERK2 cascade Source: Ensembl
    16. positive regulation of MAP kinase activity Source: Ensembl
    17. positive regulation of protein kinase B signaling Source: Ensembl
    18. positive regulation of reactive oxygen species metabolic process Source: Ensembl
    19. positive regulation of smooth muscle cell migration Source: Ensembl
    20. positive regulation of stress fiber assembly Source: Ensembl
    21. reactive oxygen species metabolic process Source: UniProtKB
    22. response to hypoxia Source: Ensembl
    23. superoxide anion generation Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Protein family/group databases

    PeroxiBasei5967. HsNOx04.
    TCDBi5.B.1.1.2. the phagocyte (gp91(phox)) nadph oxidase family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADPH oxidase 4 (EC:1.6.3.-)
    Alternative name(s):
    Kidney oxidase-1
    Short name:
    KOX-1
    Kidney superoxide-producing NADPH oxidase
    Renal NAD(P)H-oxidase
    Gene namesi
    Name:NOX4
    Synonyms:RENOX
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:7891. NOX4.

    Subcellular locationi

    Endoplasmic reticulum membrane; Multi-pass membrane protein. Cell membrane Curated; Multi-pass membrane protein Curated. Cell junctionfocal adhesion Curated
    Note: May localize to plasma membrane and focal adhesions. According to PubMed:15927447, may also localize to the nucleus.
    Isoform 4 : Nucleus 1 Publication. Nucleusnucleolus 1 Publication

    GO - Cellular componenti

    1. apical plasma membrane Source: Ensembl
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    3. focal adhesion Source: UniProtKB-SubCell
    4. integral component of membrane Source: UniProtKB
    5. mitochondrion Source: Ensembl
    6. NADPH oxidase complex Source: Ensembl
    7. nucleolus Source: UniProtKB-SubCell
    8. perinuclear region of cytoplasm Source: Ensembl

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Endoplasmic reticulum, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi304 – 3041R → RGT: Partial loss of catalytic activity. No effect on CYBA localization. 1 Publication
    Mutagenesisi575 – 5784Missing: Partial loss of catalytic activity. No effect on CYBA localization.

    Organism-specific databases

    PharmGKBiPA31692.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 578578NADPH oxidase 4PRO_0000238980Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi133 – 1331N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi230 – 2301N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Isoform 3 and isoform 4 are N-glycosylated. Isoform 4 glycosylation is required for its proper function.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9NPH5.
    PRIDEiQ9NPH5.

    PTM databases

    PhosphoSiteiQ9NPH5.

    Expressioni

    Tissue specificityi

    Expressed by distal tubular cells in kidney cortex and in endothelial cells (at protein level). Widely expressed. Strongly expressed in kidney and to a lower extent in heart, adipocytes, hepatoma, endothelial cells, skeletal muscle, brain, several brain tumor cell lines and airway epithelial cells.4 Publications

    Developmental stagei

    Expressed in fetal kidney and fetal liver.3 Publications

    Inductioni

    By 7-ketocholesterol (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ9NPH5.
    BgeeiQ9NPH5.
    CleanExiHS_NOX4.
    GenevestigatoriQ9NPH5.

    Organism-specific databases

    HPAiHPA015475.

    Interactioni

    Subunit structurei

    Interacts with protein disulfide isomerase By similarity. Interacts with, relocalizes and stabilizes CYBA/p22phox. Interacts with TLR4.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi119078. 1 interaction.
    STRINGi9606.ENSP00000263317.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NPH5.
    SMRiQ9NPH5. Positions 409-577.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1616CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini38 – 6225ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini84 – 10320CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini125 – 15430ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini176 – 18813CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini210 – 424215ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini446 – 578133CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei17 – 3721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei63 – 8321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei104 – 12421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei155 – 17521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei189 – 20921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei425 – 44521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini58 – 303246Ferric oxidoreductaseAdd
    BLAST
    Domaini304 – 419116FAD-binding FR-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni248 – 575328Mediates interaction with TLR4Add
    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

    eggNOGiNOG265816.
    HOVERGENiHBG003760.
    InParanoidiQ9NPH5.
    OrthoDBiEOG7RZ5PZ.
    PhylomeDBiQ9NPH5.
    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 (9)i

    Sequence statusi: Complete.

    This entry describes 9 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NPH5-1) [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

    MAVSWRSWLA NEGVKHLCLF IWLSMNVLLF WKTFLLYNQG PEYHYLHQML    50
    GLGLCLSRAS ASVLNLNCSL ILLPMCRTLL AYLRGSQKVP SRRTRRLLDK 100
    SRTFHITCGV TICIFSGVHV AAHLVNALNF SVNYSEDFVE LNAARYRDED 150
    PRKLLFTTVP GLTGVCMVVV LFLMITASTY AIRVSNYDIF WYTHNLFFVF 200
    YMLLTLHVSG GLLKYQTNLD THPPGCISLN RTSSQNISLP EYFSEHFHEP 250
    FPEGFSKPAE FTQHKFVKIC MEEPRFQANF PQTWLWISGP LCLYCAERLY 300
    RYIRSNKPVT IISVMSHPSD VMEIRMVKEN FKARPGQYIT LHCPSVSALE 350
    NHPFTLTMCP TETKATFGVH LKIVGDWTER FRDLLLPPSS QDSEILPFIQ 400
    SRNYPKLYID GPFGSPFEES LNYEVSLCVA GGIGVTPFAS ILNTLLDDWK 450
    PYKLRRLYFI WVCRDIQSFR WFADLLCMLH NKFWQENRPD YVNIQLYLSQ 500
    TDGIQKIIGE KYHALNSRLF IGRPRWKLLF DEIAKYNRGK TVGVFCCGPN 550
    SLSKTLHKLS NQNNSYGTRF EYNKESFS 578
    Length:578
    Mass (Da):66,932
    Last modified:November 4, 2008 - v2
    Checksum:iD150A92CC71DD40D
    GO
    Isoform 2 (identifier: Q9NPH5-2) [UniParc]FASTAAdd to Basket

    Also known as: Nox4A

    The sequence of this isoform differs from the canonical sequence as follows:
         1-74: Missing.

    Show »
    Length:504
    Mass (Da):58,410
    Checksum:i5D1ECB62CB23ED47
    GO
    Isoform 3 (identifier: Q9NPH5-3) [UniParc]FASTAAdd to Basket

    Also known as: Nox4E

    The sequence of this isoform differs from the canonical sequence as follows:
         52-358: Missing.
         407-446: Missing.

    Show »
    Length:231
    Mass (Da):27,625
    Checksum:i548F872E16DC4D37
    GO
    Isoform 4 (identifier: Q9NPH5-4) [UniParc]FASTAAdd to Basket

    Also known as: 28 kDa, Nox4D

    The sequence of this isoform differs from the canonical sequence as follows:
         52-358: Missing.

    Show »
    Length:271
    Mass (Da):31,812
    Checksum:i9C889BAAB7E531A2
    GO
    Isoform 5 (identifier: Q9NPH5-5) [UniParc]FASTAAdd to Basket

    Also known as: Nox4C

    The sequence of this isoform differs from the canonical sequence as follows:
         211-224: GLLKYQTNLDTHPP → VQLKPKQHLGFILK
         225-578: Missing.

    Show »
    Length:224
    Mass (Da):25,761
    Checksum:i27E3A0B6890E2A67
    GO
    Isoform 6 (identifier: Q9NPH5-6) [UniParc]FASTAAdd to Basket

    Also known as: Nox4B

    The sequence of this isoform differs from the canonical sequence as follows:
         407-446: Missing.

    Show »
    Length:538
    Mass (Da):62,745
    Checksum:i2E541C48425EF25B
    GO
    Isoform 7 (identifier: Q9NPH5-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         52-54: LGL → ELS
         55-578: Missing.

    Show »
    Length:54
    Mass (Da):6,516
    Checksum:i2392A10568021769
    GO
    Isoform 8 (identifier: Q9NPH5-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-24: Missing.

    Show »
    Length:554
    Mass (Da):64,102
    Checksum:iD7469DB8BCE92821
    GO
    Isoform 9 (identifier: Q9NPH5-9) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-24: Missing.
         407-446: Missing.

    Show »
    Length:514
    Mass (Da):59,915
    Checksum:i5FFB5AA1DBE790B0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti286 – 2861W → C in BAH12756. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti315 – 3151M → I.7 Publications
    Corresponds to variant rs317139 [ dbSNP | Ensembl ].
    VAR_047114

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7474Missing in isoform 2. 1 PublicationVSP_019052Add
    BLAST
    Alternative sequencei1 – 2424Missing in isoform 8 and isoform 9. 1 PublicationVSP_053826Add
    BLAST
    Alternative sequencei52 – 358307Missing in isoform 3 and isoform 4. 1 PublicationVSP_019053Add
    BLAST
    Alternative sequencei52 – 543LGL → ELS in isoform 7. 1 PublicationVSP_019054
    Alternative sequencei55 – 578524Missing in isoform 7. 1 PublicationVSP_019055Add
    BLAST
    Alternative sequencei211 – 22414GLLKY…DTHPP → VQLKPKQHLGFILK in isoform 5. 1 PublicationVSP_019056Add
    BLAST
    Alternative sequencei225 – 578354Missing in isoform 5. 1 PublicationVSP_019057Add
    BLAST
    Alternative sequencei407 – 44640Missing in isoform 3, isoform 6 and isoform 9. 3 PublicationsVSP_019058Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF261943 mRNA. Translation: AAF87572.1.
    AF254621 mRNA. Translation: AAF68973.1.
    AB041035 mRNA. Translation: BAA95695.1.
    AY288918 mRNA. Translation: AAP41109.1.
    AJ704725 mRNA. Translation: CAG28807.1.
    AJ704726 mRNA. Translation: CAG28808.1.
    AJ704727 mRNA. Translation: CAG28809.1.
    AJ704728 mRNA. Translation: CAG28810.1.
    AJ704729 mRNA. Translation: CAG28811.1.
    AK291830 mRNA. Translation: BAF84519.1.
    AK298323 mRNA. Translation: BAH12756.1.
    AP003400 Genomic DNA. No translation available.
    AP001815 Genomic DNA. No translation available.
    AP002404 Genomic DNA. No translation available.
    BC040105 mRNA. Translation: AAH40105.1.
    BC051371 mRNA. Translation: AAH51371.1.
    CCDSiCCDS44695.1. [Q9NPH5-6]
    CCDS44696.1. [Q9NPH5-8]
    CCDS8285.1. [Q9NPH5-1]
    RefSeqiNP_001137308.1. NM_001143836.2.
    NP_001137309.1. NM_001143837.1.
    NP_001278855.1. NM_001291926.1.
    NP_001278856.1. NM_001291927.1.
    NP_058627.1. NM_016931.4.
    XP_006718914.1. XM_006718851.1. [Q9NPH5-9]
    UniGeneiHs.371036.

    Genome annotation databases

    EnsembliENST00000263317; ENSP00000263317; ENSG00000086991. [Q9NPH5-1]
    ENST00000343727; ENSP00000344747; ENSG00000086991. [Q9NPH5-8]
    ENST00000375979; ENSP00000365146; ENSG00000086991. [Q9NPH5-4]
    ENST00000393282; ENSP00000376961; ENSG00000086991. [Q9NPH5-7]
    ENST00000424319; ENSP00000412446; ENSG00000086991. [Q9NPH5-8]
    ENST00000527956; ENSP00000433797; ENSG00000086991. [Q9NPH5-8]
    ENST00000529343; ENSP00000435474; ENSG00000086991. [Q9NPH5-5]
    ENST00000531342; ENSP00000435039; ENSG00000086991. [Q9NPH5-3]
    ENST00000532825; ENSP00000434924; ENSG00000086991. [Q9NPH5-9]
    ENST00000534731; ENSP00000436892; ENSG00000086991. [Q9NPH5-6]
    GeneIDi50507.
    KEGGihsa:50507.
    UCSCiuc001pcu.3. human. [Q9NPH5-1]
    uc001pcv.3. human. [Q9NPH5-6]
    uc001pcw.3. human. [Q9NPH5-4]
    uc001pcx.3. human. [Q9NPH5-3]

    Polymorphism databases

    DMDMi212276447.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF261943 mRNA. Translation: AAF87572.1 .
    AF254621 mRNA. Translation: AAF68973.1 .
    AB041035 mRNA. Translation: BAA95695.1 .
    AY288918 mRNA. Translation: AAP41109.1 .
    AJ704725 mRNA. Translation: CAG28807.1 .
    AJ704726 mRNA. Translation: CAG28808.1 .
    AJ704727 mRNA. Translation: CAG28809.1 .
    AJ704728 mRNA. Translation: CAG28810.1 .
    AJ704729 mRNA. Translation: CAG28811.1 .
    AK291830 mRNA. Translation: BAF84519.1 .
    AK298323 mRNA. Translation: BAH12756.1 .
    AP003400 Genomic DNA. No translation available.
    AP001815 Genomic DNA. No translation available.
    AP002404 Genomic DNA. No translation available.
    BC040105 mRNA. Translation: AAH40105.1 .
    BC051371 mRNA. Translation: AAH51371.1 .
    CCDSi CCDS44695.1. [Q9NPH5-6 ]
    CCDS44696.1. [Q9NPH5-8 ]
    CCDS8285.1. [Q9NPH5-1 ]
    RefSeqi NP_001137308.1. NM_001143836.2.
    NP_001137309.1. NM_001143837.1.
    NP_001278855.1. NM_001291926.1.
    NP_001278856.1. NM_001291927.1.
    NP_058627.1. NM_016931.4.
    XP_006718914.1. XM_006718851.1. [Q9NPH5-9 ]
    UniGenei Hs.371036.

    3D structure databases

    ProteinModelPortali Q9NPH5.
    SMRi Q9NPH5. Positions 409-577.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119078. 1 interaction.
    STRINGi 9606.ENSP00000263317.

    Chemistry

    BindingDBi Q9NPH5.
    ChEMBLi CHEMBL1250375.

    Protein family/group databases

    PeroxiBasei 5967. HsNOx04.
    TCDBi 5.B.1.1.2. the phagocyte (gp91(phox)) nadph oxidase family.

    PTM databases

    PhosphoSitei Q9NPH5.

    Polymorphism databases

    DMDMi 212276447.

    Proteomic databases

    PaxDbi Q9NPH5.
    PRIDEi Q9NPH5.

    Protocols and materials databases

    DNASUi 50507.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263317 ; ENSP00000263317 ; ENSG00000086991 . [Q9NPH5-1 ]
    ENST00000343727 ; ENSP00000344747 ; ENSG00000086991 . [Q9NPH5-8 ]
    ENST00000375979 ; ENSP00000365146 ; ENSG00000086991 . [Q9NPH5-4 ]
    ENST00000393282 ; ENSP00000376961 ; ENSG00000086991 . [Q9NPH5-7 ]
    ENST00000424319 ; ENSP00000412446 ; ENSG00000086991 . [Q9NPH5-8 ]
    ENST00000527956 ; ENSP00000433797 ; ENSG00000086991 . [Q9NPH5-8 ]
    ENST00000529343 ; ENSP00000435474 ; ENSG00000086991 . [Q9NPH5-5 ]
    ENST00000531342 ; ENSP00000435039 ; ENSG00000086991 . [Q9NPH5-3 ]
    ENST00000532825 ; ENSP00000434924 ; ENSG00000086991 . [Q9NPH5-9 ]
    ENST00000534731 ; ENSP00000436892 ; ENSG00000086991 . [Q9NPH5-6 ]
    GeneIDi 50507.
    KEGGi hsa:50507.
    UCSCi uc001pcu.3. human. [Q9NPH5-1 ]
    uc001pcv.3. human. [Q9NPH5-6 ]
    uc001pcw.3. human. [Q9NPH5-4 ]
    uc001pcx.3. human. [Q9NPH5-3 ]

    Organism-specific databases

    CTDi 50507.
    GeneCardsi GC11M089057.
    HGNCi HGNC:7891. NOX4.
    HPAi HPA015475.
    MIMi 605261. gene.
    neXtProti NX_Q9NPH5.
    PharmGKBi PA31692.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG265816.
    HOVERGENi HBG003760.
    InParanoidi Q9NPH5.
    OrthoDBi EOG7RZ5PZ.
    PhylomeDBi Q9NPH5.
    TreeFami TF105354.

    Miscellaneous databases

    GeneWikii NOX4.
    GenomeRNAii 50507.
    NextBioi 35499451.
    PROi Q9NPH5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NPH5.
    Bgeei Q9NPH5.
    CleanExi HS_NOX4.
    Genevestigatori Q9NPH5.

    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 1), DEVELOPMENTAL STAGE, VARIANT ILE-315.
      Tissue: Kidney.
    2. "Homologs of gp91phox: cloning and tissue expression of Nox3, Nox4, and Nox5."
      Cheng G., Cao Z., Xu X., van Meir E.G., Lambeth J.D.
      Gene 269:131-140(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, VARIANT ILE-315.
      Tissue: Fetal kidney.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, VARIANT ILE-315.
      Tissue: Kidney.
    4. "NADPH oxidase-dependent acid production in airway epithelial cells."
      Schwarzer C., Machen T.E., Illek B., Fischer H.
      J. Biol. Chem. 279:36454-36461(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), TISSUE SPECIFICITY, VARIANT ILE-315.
    5. "Identification of novel Nox4 splice variants with impact on ROS levels in A549 cells."
      Goyal P., Weissmann N., Rose F., Grimminger F., Schaefers H.J., Seeger W., Haenze J.
      Biochem. Biophys. Res. Commun. 329:32-39(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5 AND 6), FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, VARIANT ILE-315.
      Tissue: Lung.
    6. "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] (ISOFORMS 6 AND 9), VARIANT ILE-315.
      Tissue: Pulmonary artery.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORMS 1 AND 7), VARIANT ILE-315.
      Tissue: Ovary.
    9. "Reactive oxygen species produced by NAD(P)H oxidase inhibit apoptosis in pancreatic cancer cells."
      Vaquero E.C., Edderkaoui M., Pandol S.J., Gukovsky I., Gukovskaya A.S.
      J. Biol. Chem. 279:34643-34654(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Direct interaction of TLR4 with NAD(P)H oxidase 4 isozyme is essential for lipopolysaccharide-induced production of reactive oxygen species and activation of NF-kappa B."
      Park H.S., Jung H.Y., Park E.Y., Kim J., Lee W.J., Bae Y.S.
      J. Immunol. 173:3589-3593(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TLR4.
    11. "The NAD(P)H oxidase homolog Nox4 modulates insulin-stimulated generation of H2O2 and plays an integral role in insulin signal transduction."
      Mahadev K., Motoshima H., Wu X., Ruddy J.M., Arnold R.S., Cheng G., Lambeth J.D., Goldstein B.J.
      Mol. Cell. Biol. 24:1844-1854(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION.
    12. "NAD(P)H oxidase Nox-4 mediates 7-ketocholesterol-induced endoplasmic reticulum stress and apoptosis in human aortic smooth muscle cells."
      Pedruzzi E., Guichard C., Ollivier V., Driss F., Fay M., Prunet C., Marie J.-C., Pouzet C., Samadi M., Elbim C., O'dowd Y., Bens M., Vandewalle A., Gougerot-Pocidalo M.-A., Lizard G., Ogier-Denis E.
      Mol. Cell. Biol. 24:10703-10717(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION, SUBCELLULAR LOCATION, ENZYME REGULATION.
    13. "Nox4 is critical for hypoxia-inducible factor 2-alpha transcriptional activity in von Hippel-Lindau-deficient renal cell carcinoma."
      Maranchie J.K., Zhan Y.
      Cancer Res. 65:9190-9193(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "NAD(P)H oxidase 4 mediates transforming growth factor-beta1-induced differentiation of cardiac fibroblasts into myofibroblasts."
      Cucoranu I., Clempus R., Dikalova A., Phelan P.J., Ariyan S., Dikalov S., Sorescu D.
      Circ. Res. 97:900-907(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "The superoxide-producing NAD(P)H oxidase Nox4 in the nucleus of human vascular endothelial cells."
      Kuroda J., Nakagawa K., Yamasaki T., Nakamura K., Takeya R., Kuribayashi F., Imajoh-Ohmi S., Igarashi K., Shibata Y., Sueishi K., Sumimoto H.
      Genes Cells 10:1139-1151(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ENZYME REGULATION.
    16. "Functional analysis of Nox4 reveals unique characteristics compared to other NADPH oxidases."
      Martyn K.D., Frederick L.M., von Loehneysen K., Dinauer M.C., Knaus U.G.
      Cell. Signal. 18:69-82(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CYBA, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-304 AND 575-GLU--SER-578.
    17. "NOX4 as an oxygen sensor to regulate TASK-1 activity."
      Lee Y.-M., Kim B.-J., Chun Y.-S., So I., Choi H., Kim M.-S., Park J.-W.
      Cell. Signal. 18:499-507(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION.
    18. "A 28-kDa splice variant of NADPH oxidase-4 is nuclear-localized and involved in redox signaling in vascular cells."
      Anilkumar N., San Jose G., Sawyer I., Santos C.X., Sand C., Brewer A.C., Warren D., Shah A.M.
      Arterioscler. Thromb. Vasc. Biol. 33:E104-E112(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION (ISOFORM 4), SUBCELLULAR LOCATION (ISOFORM 4).

    Entry informationi

    Entry nameiNOX4_HUMAN
    AccessioniPrimary (citable) accession number: Q9NPH5
    Secondary accession number(s): A8K715
    , B7Z520, E7EMD7, Q5K3R4, Q5K3R5, Q5K3R6, Q5K3R8, Q7Z7G3, Q86V92
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2006
    Last sequence update: November 4, 2008
    Last modified: October 1, 2014
    This is version 109 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 11
      Human chromosome 11: 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