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Protein

NADPH oxidase 4

Gene

NOX4

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

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

  • electron carrier activity Source: UniProtKB
  • flavin adenine dinucleotide binding Source: UniProtKB
  • heme binding Source: UniProtKB
  • modified amino acid binding Source: UniProtKB
  • NAD(P)H oxidase activity Source: UniProtKB
  • nucleotide binding Source: UniProtKB
  • oxygen sensor activity Source: UniProtKB
  • superoxide-generating NADPH oxidase activity Source: Ensembl

GO - Biological processi

  • bone resorption Source: Ensembl
  • cardiac muscle cell differentiation Source: Ensembl
  • cell aging Source: UniProtKB
  • cell morphogenesis Source: UniProtKB
  • cellular response to cAMP Source: Ensembl
  • cellular response to gamma radiation Source: Ensembl
  • cellular response to glucose stimulus Source: Ensembl
  • cellular response to transforming growth factor beta stimulus Source: Ensembl
  • gene expression Source: CACAO
  • homocysteine metabolic process Source: UniProtKB
  • inflammatory response Source: UniProtKB
  • negative regulation of cell proliferation Source: UniProtKB
  • oxidation-reduction process Source: UniProtKB
  • positive regulation of apoptotic process Source: Ensembl
  • positive regulation of DNA biosynthetic process Source: Ensembl
  • positive regulation of ERK1 and ERK2 cascade Source: Ensembl
  • positive regulation of MAP kinase activity Source: Ensembl
  • positive regulation of protein kinase B signaling Source: Ensembl
  • positive regulation of reactive oxygen species metabolic process Source: Ensembl
  • positive regulation of smooth muscle cell migration Source: Ensembl
  • positive regulation of stress fiber assembly Source: Ensembl
  • reactive oxygen species metabolic process Source: UniProtKB
  • response to hypoxia Source: Ensembl
  • superoxide anion generation Source: UniProtKB
  • superoxide metabolic process Source: CACAO
Complete GO annotation...

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 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:7891. NOX4.

Subcellular locationi

Isoform 4 :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1616CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei17 – 3721HelicalSequence AnalysisAdd
BLAST
Topological domaini38 – 6225ExtracellularSequence AnalysisAdd
BLAST
Transmembranei63 – 8321HelicalSequence AnalysisAdd
BLAST
Topological domaini84 – 10320CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei104 – 12421HelicalSequence AnalysisAdd
BLAST
Topological domaini125 – 15430ExtracellularSequence AnalysisAdd
BLAST
Transmembranei155 – 17521HelicalSequence AnalysisAdd
BLAST
Topological domaini176 – 18813CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei189 – 20921HelicalSequence AnalysisAdd
BLAST
Topological domaini210 – 424215ExtracellularSequence AnalysisAdd
BLAST
Transmembranei425 – 44521HelicalSequence AnalysisAdd
BLAST
Topological domaini446 – 578133CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

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. 1 Publication

Organism-specific databases

PharmGKBiPA31692.

Polymorphism and mutation databases

BioMutaiNOX4.
DMDMi212276447.

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

BgeeiQ9NPH5.
CleanExiHS_NOX4.
ExpressionAtlasiQ9NPH5. baseline and differential.
GenevisibleiQ9NPH5. HS.

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

STRINGi9606.ENSP00000263317.

Structurei

3D structure databases

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

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.
GeneTreeiENSGT00550000074350.
HOGENOMiHOG000216669.
HOVERGENiHBG003760.
InParanoidiQ9NPH5.
OMAiTDGIQQK.
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. AlignAdd to basket

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

        10         20         30         40         50
MAVSWRSWLA NEGVKHLCLF IWLSMNVLLF WKTFLLYNQG PEYHYLHQML
60 70 80 90 100
GLGLCLSRAS ASVLNLNCSL ILLPMCRTLL AYLRGSQKVP SRRTRRLLDK
110 120 130 140 150
SRTFHITCGV TICIFSGVHV AAHLVNALNF SVNYSEDFVE LNAARYRDED
160 170 180 190 200
PRKLLFTTVP GLTGVCMVVV LFLMITASTY AIRVSNYDIF WYTHNLFFVF
210 220 230 240 250
YMLLTLHVSG GLLKYQTNLD THPPGCISLN RTSSQNISLP EYFSEHFHEP
260 270 280 290 300
FPEGFSKPAE FTQHKFVKIC MEEPRFQANF PQTWLWISGP LCLYCAERLY
310 320 330 340 350
RYIRSNKPVT IISVMSHPSD VMEIRMVKEN FKARPGQYIT LHCPSVSALE
360 370 380 390 400
NHPFTLTMCP TETKATFGVH LKIVGDWTER FRDLLLPPSS QDSEILPFIQ
410 420 430 440 450
SRNYPKLYID GPFGSPFEES LNYEVSLCVA GGIGVTPFAS ILNTLLDDWK
460 470 480 490 500
PYKLRRLYFI WVCRDIQSFR WFADLLCMLH NKFWQENRPD YVNIQLYLSQ
510 520 530 540 550
TDGIQKIIGE KYHALNSRLF IGRPRWKLLF DEIAKYNRGK TVGVFCCGPN
560 570
SLSKTLHKLS NQNNSYGTRF EYNKESFS
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:
EMBLi
GenBanki
DDBJi
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]
CCDS73361.1. [Q9NPH5-9]
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_001287924.1. NM_001300995.1. [Q9NPH5-9]
NP_058627.1. NM_016931.4.
XP_011541159.1. XM_011542857.1. [Q9NPH5-8]
XP_011541160.1. XM_011542858.1. [Q9NPH5-9]
XP_011541161.1. XM_011542859.1. [Q9NPH5-2]
UniGeneiHs.371036.

Genome annotation databases

EnsembliENST00000263317; ENSP00000263317; ENSG00000086991.
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]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
CCDS73361.1. [Q9NPH5-9]
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_001287924.1. NM_001300995.1. [Q9NPH5-9]
NP_058627.1. NM_016931.4.
XP_011541159.1. XM_011542857.1. [Q9NPH5-8]
XP_011541160.1. XM_011542858.1. [Q9NPH5-9]
XP_011541161.1. XM_011542859.1. [Q9NPH5-2]
UniGeneiHs.371036.

3D structure databases

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

Protein-protein interaction databases

STRINGi9606.ENSP00000263317.

Chemistry

BindingDBiQ9NPH5.
ChEMBLiCHEMBL1250375.

Protein family/group databases

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

PTM databases

PhosphoSiteiQ9NPH5.

Polymorphism and mutation databases

BioMutaiNOX4.
DMDMi212276447.

Proteomic databases

PaxDbiQ9NPH5.
PRIDEiQ9NPH5.

Protocols and materials databases

DNASUi50507.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263317; ENSP00000263317; ENSG00000086991.
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]

Organism-specific databases

CTDi50507.
GeneCardsiGC11M089057.
HGNCiHGNC:7891. NOX4.
HPAiHPA015475.
MIMi605261. gene.
neXtProtiNX_Q9NPH5.
PharmGKBiPA31692.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG265816.
GeneTreeiENSGT00550000074350.
HOGENOMiHOG000216669.
HOVERGENiHBG003760.
InParanoidiQ9NPH5.
OMAiTDGIQQK.
OrthoDBiEOG7RZ5PZ.
PhylomeDBiQ9NPH5.
TreeFamiTF105354.

Miscellaneous databases

GeneWikiiNOX4.
GenomeRNAii50507.
NextBioi35499451.
PROiQ9NPH5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NPH5.
CleanExiHS_NOX4.
ExpressionAtlasiQ9NPH5. baseline and differential.
GenevisibleiQ9NPH5. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 116 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.