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Q96PH1

- NOX5_HUMAN

UniProt

Q96PH1 - NOX5_HUMAN

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Protein

NADPH oxidase 5

Gene

NOX5

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

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

Protein has several cofactor binding sites:

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. 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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 238238CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei239 – 25921HelicalSequence AnalysisAdd
BLAST
Topological domaini260 – 2667ExtracellularSequence Analysis
Transmembranei267 – 28923HelicalSequence AnalysisAdd
BLAST
Topological domaini290 – 31728CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei318 – 33821HelicalSequence AnalysisAdd
BLAST
Topological domaini339 – 36224ExtracellularSequence AnalysisAdd
BLAST
Transmembranei363 – 38321HelicalSequence AnalysisAdd
BLAST
Topological domaini384 – 39411CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei395 – 41723HelicalSequence AnalysisAdd
BLAST
Topological domaini418 – 43417ExtracellularSequence AnalysisAdd
BLAST
Transmembranei435 – 45521HelicalSequence AnalysisAdd
BLAST
Topological domaini456 – 583128CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei584 – 60421HelicalSequence AnalysisAdd
BLAST
Topological domaini605 – 765161ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

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...

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.
GeneTreeiENSGT00550000074350.
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.
IPR029648. NOX5.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PANTHERiPTHR11972:SF36. PTHR11972:SF36. 1 hit.
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

        10         20         30         40         50
MNTSGDPAQT GPEGCRGTMS AEEDARWLRW VTQQFKTIAG EDGEISLQEF
60 70 80 90 100
KAALHVKESF FAERFFALFD SDRSGTITLQ ELQEALTLLI HGSPMDKLKF
110 120 130 140 150
LFQVYDIDVC ARQGASAGTE WGAGAGPHWA SSPLGTGSGS IDPDELRTVL
160 170 180 190 200
QSCLRESAIS LPDEKLDQLT LALFESADAD GNGAITFEEL RDELQRFPGV
210 220 230 240 250
MENLTISAAH WLTAPAPRPR PRRPRQLTRA YWHNHRSQLF CLATYAGLHV
260 270 280 290 300
LLFGLAASAH RDLGASVMVA KGCGQCLNFD CSFIAVLMLR RCLTWLRATW
310 320 330 340 350
LAQVLPLDQN IQFHQLMGYV VVGLSLVHTV AHTVNFVLQA QAEASPFQFW
360 370 380 390 400
ELLLTTRPGI GWVHGSASPT GVALLLLLLL MFICSSSCIR RSGHFEVFYW
410 420 430 440 450
THLSYLLVWL LLIFHGPNFW KWLLVPGILF FLEKAIGLAV SRMAAVCIME
460 470 480 490 500
VNLLPSKVTH LLIKRPPFFH YRPGDYLYLN IPTIARYEWH PFTISSAPEQ
510 520 530 540 550
KDTIWLHIRS QGQWTNRLYE SFKASDPLGR GSKRLSRSVT MRKSQRSSKG
560 570 580 590 600
SEILLEKHKF CNIKCYIDGP YGTPTRRIFA SEHAVLIGAG IGITPFASIL
610 620 630 640 650
QSIMYRHQKR KHTCPSCQHS WIEGVQDNMK LHKVDFIWIN RDQRSFEWFV
660 670 680 690 700
SLLTKLEMDQ AEEAQYGRFL ELHMYMTSAL GKNDMKAIGL QMALDLLANK
710 720 730 740 750
EKKDSITGLQ TRTQPGRPDW SKVFQKVAAE KKGKVQVFFC GSPALAKVLK
760
GHCEKFGFRF FQENF
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.Curated
The sequence BAB15319.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB84897.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
GeneTreei ENSGT00550000074350.
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.
IPR029648. NOX5.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view ]
PANTHERi PTHR11972:SF36. PTHR11972:SF36. 1 hit.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 113 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