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Q96PH1

- NOX5_HUMAN

UniProt

Q96PH1 - NOX5_HUMAN

Protein

NADPH oxidase 5

Gene

NOX5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    Calcium-dependent NADPH oxidase that generates superoxide. Also functions as a calcium-dependent proton channel and may regulate redox-dependent processes in lymphocytes and spermatozoa. May play a role in cell growth and apoptosis. Isoform v2 and isoform v5 are involved in endothelial generation of reactive oxygen species (ROS), proliferation and angiogenesis and contribute to endothelial response to thrombin.3 Publications

    Cofactori

    FAD.1 Publication
    Magnesium.1 Publication

    Enzyme regulationi

    Activated by calcium which induces conformational changes and interaction between the N-terminal regulatory region and the C-terminal catalytic region. Inhibited by diphenylene iodonium.1 Publication

    Kineticsi

    1. KM=1.06 µM for calcium1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi39 – 49111PROSITE-ProRule annotationAdd
    BLAST
    Calcium bindingi70 – 81122PROSITE-ProRule annotationAdd
    BLAST
    Calcium bindingi106 – 10833; first partPROSITE-ProRule annotation
    Calcium bindingi137 – 146103; second partPROSITE-ProRule annotation
    Calcium bindingi178 – 189124PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. flavin adenine dinucleotide binding Source: UniProtKB
    3. heme binding Source: UniProtKB
    4. hydrogen ion channel activity Source: UniProtKB
    5. NADP binding Source: UniProtKB
    6. protein binding Source: IntAct
    7. superoxide-generating NADPH oxidase activity Source: UniProtKB

    GO - Biological processi

    1. angiogenesis Source: UniProtKB
    2. apoptotic process Source: UniProtKB
    3. cell proliferation Source: UniProtKB
    4. cytokine secretion Source: UniProtKB
    5. cytokinesis Source: UniProtKB
    6. endothelial cell proliferation Source: UniProtKB
    7. oxidation-reduction process Source: UniProtKB
    8. positive regulation of reactive oxygen species metabolic process Source: UniProtKB
    9. proton transport Source: GOC
    10. regulation of fusion of sperm to egg plasma membrane Source: UniProtKB
    11. regulation of proton transport Source: UniProtKB
    12. superoxide anion generation Source: UniProtKB

    Keywords - Molecular functioni

    Ion channel, Oxidoreductase

    Keywords - Biological processi

    Angiogenesis, Electron transport, Ion transport, Transport

    Keywords - Ligandi

    Calcium, FAD, Flavoprotein, Metal-binding, NADP

    Protein family/group databases

    PeroxiBasei6024. HsNOx05.
    TCDBi5.B.1.1.5. the phagocyte (gp91(phox)) nadph oxidase family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADPH oxidase 5 (EC:1.6.3.-)
    Gene namesi
    Name:NOX5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:14874. NOX5.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi49 – 491E → Q: Loss of binding of 1 calcium molecule. No effect on catalytic activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA31693.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 765765NADPH oxidase 5PRO_0000224995Add
    BLAST

    Proteomic databases

    PaxDbiQ96PH1.
    PRIDEiQ96PH1.

    Expressioni

    Tissue specificityi

    Mainly expressed in pachytene spermatocytes of testis and in lymphocyte-rich areas of spleen and lymph nodes. Isoform v1 is expressed in spleen. Isoform v2 is expressed in testis. Also detected in ovary, placenta, pancreas, cardiac fibroblasts. Expressed in B-cells and prostate malignant cells. Isoform v1 and isoform v3 are expressed in epithelial colorectal adenocarcinoma cells. Isoform v2 and isoform v4 are expressed in endothelial cells. Isoform v1, isoform v2, isoform v3 and isoform v4 are expressed in pulmonary artery smooth muscle cells. Isoform v2 and isoform v5 are expressed in microvascular endothelial cells (at protein level).6 Publications

    Developmental stagei

    Expressed in fetal tissues.1 Publication

    Inductioni

    Down-regulated by TGFB1.1 Publication

    Gene expression databases

    BgeeiQ96PH1.
    CleanExiHS_NOX5.
    GenevestigatoriQ96PH1.

    Organism-specific databases

    HPAiHPA019362.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CALMP621573EBI-7305642,EBI-397403From a different organism.

    Protein-protein interaction databases

    BioGridi122660. 5 interactions.
    IntActiQ96PH1. 1 interaction.
    STRINGi9606.ENSP00000260364.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96PH1.
    SMRiQ96PH1. Positions 35-206, 567-749.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 238238CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini260 – 2667ExtracellularSequence Analysis
    Topological domaini290 – 31728CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini339 – 36224ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini384 – 39411CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini418 – 43417ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini456 – 583128CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini605 – 765161ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei239 – 25921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei267 – 28923HelicalSequence AnalysisAdd
    BLAST
    Transmembranei318 – 33821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei363 – 38321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei395 – 41723HelicalSequence AnalysisAdd
    BLAST
    Transmembranei435 – 45521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei584 – 60421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini26 – 5631EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini57 – 9236EF-hand 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini93 – 15664EF-hand 3; atypical; contains an insert of 28 residuesPROSITE-ProRule annotationAdd
    BLAST
    Domaini165 – 20036EF-hand 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini293 – 440148Ferric oxidoreductaseAdd
    BLAST
    Domaini441 – 577137FAD-binding FR-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 169169N-terminal regulatory region; interacts with the C-terminal catalytic region in a calcium-dependent mannerAdd
    BLAST
    Regioni449 – 565117C-terminal catalytic regionAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi374 – 3807Poly-Leu

    Domaini

    Isoform v1 and isoform v2 of this protein have four functional EF-hand calcium-binding domains. Isoform v3 and isoform v4 have the third EF-hand domain interrupted by an insert.

    Sequence similaritiesi

    Contains 4 EF-hand domains.PROSITE-ProRule annotation
    Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation
    Contains 1 ferric oxidoreductase domain.Curated

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG287712.
    HOVERGENiHBG082052.
    InParanoidiQ96PH1.
    OMAiVMVAKGC.
    OrthoDBiEOG7VQJC7.
    PhylomeDBiQ96PH1.
    TreeFamiTF324099.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    InterProiIPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    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]
    PfamiPF13202. EF-hand_5. 1 hit.
    PF13405. EF-hand_6. 1 hit.
    PF08022. FAD_binding_8. 1 hit.
    PF01794. Ferric_reduct. 1 hit.
    PF08030. NAD_binding_6. 1 hit.
    [Graphical view]
    SMARTiSM00054. EFh. 2 hits.
    [Graphical view]
    SUPFAMiSSF63380. SSF63380. 2 hits.
    PROSITEiPS00018. EF_HAND_1. 2 hits.
    PS50222. EF_HAND_2. 3 hits.
    PS51384. FAD_FR. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform v3 (identifier: Q96PH1-1) [UniParc]FASTAAdd to Basket

    Also known as: NOX5gamma

    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

    MNTSGDPAQT GPEGCRGTMS AEEDARWLRW VTQQFKTIAG EDGEISLQEF    50
    KAALHVKESF FAERFFALFD SDRSGTITLQ ELQEALTLLI HGSPMDKLKF 100
    LFQVYDIDVC ARQGASAGTE WGAGAGPHWA SSPLGTGSGS IDPDELRTVL 150
    QSCLRESAIS LPDEKLDQLT LALFESADAD GNGAITFEEL RDELQRFPGV 200
    MENLTISAAH WLTAPAPRPR PRRPRQLTRA YWHNHRSQLF CLATYAGLHV 250
    LLFGLAASAH RDLGASVMVA KGCGQCLNFD CSFIAVLMLR RCLTWLRATW 300
    LAQVLPLDQN IQFHQLMGYV VVGLSLVHTV AHTVNFVLQA QAEASPFQFW 350
    ELLLTTRPGI GWVHGSASPT GVALLLLLLL MFICSSSCIR RSGHFEVFYW 400
    THLSYLLVWL LLIFHGPNFW KWLLVPGILF FLEKAIGLAV SRMAAVCIME 450
    VNLLPSKVTH LLIKRPPFFH YRPGDYLYLN IPTIARYEWH PFTISSAPEQ 500
    KDTIWLHIRS QGQWTNRLYE SFKASDPLGR GSKRLSRSVT MRKSQRSSKG 550
    SEILLEKHKF CNIKCYIDGP YGTPTRRIFA SEHAVLIGAG IGITPFASIL 600
    QSIMYRHQKR KHTCPSCQHS WIEGVQDNMK LHKVDFIWIN RDQRSFEWFV 650
    SLLTKLEMDQ AEEAQYGRFL ELHMYMTSAL GKNDMKAIGL QMALDLLANK 700
    EKKDSITGLQ TRTQPGRPDW SKVFQKVAAE KKGKVQVFFC GSPALAKVLK 750
    GHCEKFGFRF FQENF 765
    Length:765
    Mass (Da):86,439
    Last modified:December 1, 2001 - v1
    Checksum:i96B57225BF919682
    GO
    Isoform v1 (identifier: Q96PH1-3) [UniParc]FASTAAdd to Basket

    Also known as: NOX5alpha

    The sequence of this isoform differs from the canonical sequence as follows:
         109-136: Missing.

    Show »
    Length:737
    Mass (Da):83,774
    Checksum:i33B3AC250C36F6E9
    GO
    Isoform v2 (identifier: Q96PH1-4) [UniParc]FASTAAdd to Basket

    Also known as: NOX5beta

    The sequence of this isoform differs from the canonical sequence as follows:
         1-18: Missing.
         109-136: Missing.

    Show »
    Length:719
    Mass (Da):82,013
    Checksum:i04F7BA7C78B1AEDB
    GO
    Isoform v4 (identifier: Q96PH1-2) [UniParc]FASTAAdd to Basket

    Also known as: NOX5delta

    The sequence of this isoform differs from the canonical sequence as follows:
         1-18: Missing.

    Show »
    Length:747
    Mass (Da):84,678
    Checksum:i86B46366672B6E4A
    GO
    Isoform v5 (identifier: Q96PH1-5) [UniParc]FASTAAdd to Basket

    Also known as: NOX5epsilon, NOX5S

    The sequence of this isoform differs from the canonical sequence as follows:
         1-200: Missing.

    Show »
    Length:565
    Mass (Da):64,652
    Checksum:i94785B98A61214F6
    GO
    Isoform v6 (identifier: Q96PH1-6) [UniParc]FASTAAdd to Basket

    Also known as: NOX5zeta

    The sequence of this isoform differs from the canonical sequence as follows:
         1-17: MNTSGDPAQTGPEGCRG → MAFVCAGLSD
         109-136: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:730
    Mass (Da):83,109
    Checksum:i93B21AF3A0A1CE79
    GO

    Sequence cautioni

    The sequence AAG33638.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAB15319.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAB84897.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti208 – 2081A → T in AAG33638. (PubMed:15994299)Curated
    Sequence conflicti272 – 2721G → S in AAI25099. (PubMed:15489334)Curated
    Sequence conflicti375 – 3751L → P in BAG37241. (PubMed:14702039)Curated
    Sequence conflicti380 – 3801L → F in BAB84884. 1 PublicationCurated
    Sequence conflicti380 – 3801L → F in BAB84897. 1 PublicationCurated
    Sequence conflicti380 – 3801L → F in BAB15319. (PubMed:14702039)Curated
    Sequence conflicti380 – 3801L → F in BAG37241. (PubMed:14702039)Curated
    Sequence conflicti380 – 3801L → F in EAW77830. 1 PublicationCurated
    Sequence conflicti380 – 3801L → F in AAI25098. (PubMed:15489334)Curated
    Sequence conflicti380 – 3801L → F in AAI25099. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti576 – 5761R → H.
    Corresponds to variant rs2277552 [ dbSNP | Ensembl ].
    VAR_055820
    Natural varianti759 – 7591R → G.
    Corresponds to variant rs7168025 [ dbSNP | Ensembl ].
    VAR_055821

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 200200Missing in isoform v5. 1 PublicationVSP_017326Add
    BLAST
    Alternative sequencei1 – 1818Missing in isoform v2 and isoform v4. 3 PublicationsVSP_017327Add
    BLAST
    Alternative sequencei1 – 1717MNTSG…EGCRG → MAFVCAGLSD in isoform v6. 1 PublicationVSP_041619Add
    BLAST
    Alternative sequencei109 – 13628Missing in isoform v1, isoform v2 and isoform v6. 2 PublicationsVSP_017328Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF325189 mRNA. Translation: AAK57193.1.
    AF325190 mRNA. Translation: AAK57194.1.
    AF353088 mRNA. Translation: AAK57338.1.
    AF353089 mRNA. Translation: AAK57339.1.
    AK074058 mRNA. Translation: BAB84884.1.
    AK074071 mRNA. Translation: BAB84897.1. Different initiation.
    AK026011 mRNA. Translation: BAB15319.1. Different initiation.
    AK314689 mRNA. Translation: BAG37241.1.
    DQ314884 Genomic DNA. Translation: ABC40743.1.
    AC027088 Genomic DNA. No translation available.
    AC087639 Genomic DNA. No translation available.
    CH471082 Genomic DNA. Translation: EAW77830.1.
    BC125097 mRNA. Translation: AAI25098.1.
    BC125098 mRNA. Translation: AAI25099.1.
    AF317889 mRNA. Translation: AAG33638.1. Different initiation.
    CCDSiCCDS32276.2. [Q96PH1-1]
    CCDS53953.1. [Q96PH1-6]
    CCDS53954.1. [Q96PH1-3]
    RefSeqiNP_001171708.1. NM_001184779.1. [Q96PH1-3]
    NP_001171709.1. NM_001184780.1. [Q96PH1-6]
    NP_078781.3. NM_024505.3. [Q96PH1-1]
    UniGeneiHs.657932.

    Genome annotation databases

    EnsembliENST00000260364; ENSP00000454143; ENSG00000255346. [Q96PH1-2]
    ENST00000388866; ENSP00000373518; ENSG00000255346. [Q96PH1-1]
    ENST00000448182; ENSP00000410887; ENSG00000255346. [Q96PH1-4]
    ENST00000455873; ENSP00000416828; ENSG00000255346. [Q96PH1-6]
    ENST00000530406; ENSP00000432440; ENSG00000255346. [Q96PH1-3]
    GeneIDi79400.
    KEGGihsa:79400.
    UCSCiuc002arp.2. human. [Q96PH1-1]
    uc002arq.2. human. [Q96PH1-4]
    uc002arr.2. human. [Q96PH1-3]
    uc010bid.2. human. [Q96PH1-6]

    Polymorphism databases

    DMDMi74717091.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF325189 mRNA. Translation: AAK57193.1 .
    AF325190 mRNA. Translation: AAK57194.1 .
    AF353088 mRNA. Translation: AAK57338.1 .
    AF353089 mRNA. Translation: AAK57339.1 .
    AK074058 mRNA. Translation: BAB84884.1 .
    AK074071 mRNA. Translation: BAB84897.1 . Different initiation.
    AK026011 mRNA. Translation: BAB15319.1 . Different initiation.
    AK314689 mRNA. Translation: BAG37241.1 .
    DQ314884 Genomic DNA. Translation: ABC40743.1 .
    AC027088 Genomic DNA. No translation available.
    AC087639 Genomic DNA. No translation available.
    CH471082 Genomic DNA. Translation: EAW77830.1 .
    BC125097 mRNA. Translation: AAI25098.1 .
    BC125098 mRNA. Translation: AAI25099.1 .
    AF317889 mRNA. Translation: AAG33638.1 . Different initiation.
    CCDSi CCDS32276.2. [Q96PH1-1 ]
    CCDS53953.1. [Q96PH1-6 ]
    CCDS53954.1. [Q96PH1-3 ]
    RefSeqi NP_001171708.1. NM_001184779.1. [Q96PH1-3 ]
    NP_001171709.1. NM_001184780.1. [Q96PH1-6 ]
    NP_078781.3. NM_024505.3. [Q96PH1-1 ]
    UniGenei Hs.657932.

    3D structure databases

    ProteinModelPortali Q96PH1.
    SMRi Q96PH1. Positions 35-206, 567-749.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122660. 5 interactions.
    IntActi Q96PH1. 1 interaction.
    STRINGi 9606.ENSP00000260364.

    Chemistry

    BindingDBi Q96PH1.
    ChEMBLi CHEMBL1926497.

    Protein family/group databases

    PeroxiBasei 6024. HsNOx05.
    TCDBi 5.B.1.1.5. the phagocyte (gp91(phox)) nadph oxidase family.

    Polymorphism databases

    DMDMi 74717091.

    Proteomic databases

    PaxDbi Q96PH1.
    PRIDEi Q96PH1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000260364 ; ENSP00000454143 ; ENSG00000255346 . [Q96PH1-2 ]
    ENST00000388866 ; ENSP00000373518 ; ENSG00000255346 . [Q96PH1-1 ]
    ENST00000448182 ; ENSP00000410887 ; ENSG00000255346 . [Q96PH1-4 ]
    ENST00000455873 ; ENSP00000416828 ; ENSG00000255346 . [Q96PH1-6 ]
    ENST00000530406 ; ENSP00000432440 ; ENSG00000255346 . [Q96PH1-3 ]
    GeneIDi 79400.
    KEGGi hsa:79400.
    UCSCi uc002arp.2. human. [Q96PH1-1 ]
    uc002arq.2. human. [Q96PH1-4 ]
    uc002arr.2. human. [Q96PH1-3 ]
    uc010bid.2. human. [Q96PH1-6 ]

    Organism-specific databases

    CTDi 79400.
    GeneCardsi GC15P069222.
    H-InvDB HIX0012384.
    HGNCi HGNC:14874. NOX5.
    HPAi HPA019362.
    MIMi 606572. gene.
    neXtProti NX_Q96PH1.
    PharmGKBi PA31693.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG287712.
    HOVERGENi HBG082052.
    InParanoidi Q96PH1.
    OMAi VMVAKGC.
    OrthoDBi EOG7VQJC7.
    PhylomeDBi Q96PH1.
    TreeFami TF324099.

    Miscellaneous databases

    GeneWikii NOX5.
    GenomeRNAii 79400.
    NextBioi 68361.
    PROi Q96PH1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q96PH1.
    CleanExi HS_NOX5.
    Genevestigatori Q96PH1.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    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 PF13202. EF-hand_5. 1 hit.
    PF13405. EF-hand_6. 1 hit.
    PF08022. FAD_binding_8. 1 hit.
    PF01794. Ferric_reduct. 1 hit.
    PF08030. NAD_binding_6. 1 hit.
    [Graphical view ]
    SMARTi SM00054. EFh. 2 hits.
    [Graphical view ]
    SUPFAMi SSF63380. SSF63380. 2 hits.
    PROSITEi PS00018. EF_HAND_1. 2 hits.
    PS50222. EF_HAND_2. 3 hits.
    PS51384. FAD_FR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A Ca(2+)-activated NADPH oxidase in testis, spleen, and lymph nodes."
      Banfi B., Molnar G., Maturana A., Steger K., Hegedus B., Demaurex N., Krause K.-H.
      J. Biol. Chem. 276:37594-37601(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS V1; V2; V3 AND V4), FUNCTION, TISSUE SPECIFICITY.
      Tissue: Spleen and Testis.
    2. "The nucleotide sequence of a long cDNA clone isolated from human spleen."
      Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.
      Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM V5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 98-765 (ISOFORMS V3/V4).
      Tissue: Spleen.
    3. "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 V4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 159-765 (ISOFORMS V1/V2/V3/V4/V6).
      Tissue: Kidney epithelium and Spleen.
    4. NHLBI resequencing and genotyping service (RS&G)
      Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM V5).
    5. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [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] (ISOFORMS V2 AND V6).
    8. "Point mutations in the proline-rich region of p22phox are dominant inhibitors of Nox1- and Nox2-dependent reactive oxygen generation."
      Kawahara T., Ritsick D., Cheng G., Lambeth J.D.
      J. Biol. Chem. 280:31859-31869(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 177-765 (ISOFORMS V1/V2/V3/V4/V6).
      Tissue: Spleen.
    9. "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: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    10. Cited for: FUNCTION, TISSUE SPECIFICITY.
    11. Cited for: ENZYME REGULATION, COFACTOR, MUTAGENESIS OF GLU-49, BIOPHYSICOCHEMICAL PROPERTIES.
    12. "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: TISSUE SPECIFICITY, INDUCTION.
    13. "Expression and activity of NOX5 in the circulating malignant B cells of hairy cell leukemia."
      Kamiguti A.S., Serrander L., Lin K., Harris R.J., Cawley J.C., Allsup D.J., Slupsky J.R., Krause K.-H., Zuzel M.
      J. Immunol. 175:8424-8430(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    14. Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiNOX5_HUMAN
    AccessioniPrimary (citable) accession number: Q96PH1
    Secondary accession number(s): B2RBJ4
    , Q08AN2, Q08AN3, Q8TEQ1, Q8TER4, Q96PH2, Q96PJ8, Q96PJ9, Q9H6E0, Q9HAM8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 7, 2006
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 111 of the entry and version 1 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 15
      Human chromosome 15: 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