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Q9NPH5 (NOX4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:NOX4
Synonyms:RENOX
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length578 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3 Ref.5 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18

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. Ref.3 Ref.5 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18

Enzyme regulation

Inhibited by plumbagin By similarity. Activated by phorbol 12-myristate 13-acetate (PMA). Activated by insulin. Inhibited by diphenylene iodonium. Ref.11 Ref.12 Ref.15 Ref.17

Subunit structure

Interacts with protein disulfide isomerase By similarity. Interacts with, relocalizes and stabilizes CYBA/p22phox. Interacts with TLR4. Ref.10 Ref.16

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein Probable. Cell junctionfocal adhesion Probable. Note: May localize to plasma membrane and focal adhesions. According to Ref.16, may also localize to the nucleus. Ref.5 Ref.12 Ref.15 Ref.16 Ref.17 Ref.18

Isoform 4: Nucleus. Nucleusnucleolus Ref.5 Ref.12 Ref.15 Ref.16 Ref.17 Ref.18.

Tissue specificity

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. Ref.2 Ref.3 Ref.4 Ref.15

Developmental stage

Expressed in fetal kidney and fetal liver. Ref.1 Ref.2 Ref.3

Induction

By 7-ketocholesterol (at protein level). Ref.11 Ref.12 Ref.15 Ref.17

Post-translational modification

Isoform 3 and isoform 4 are N-glycosylated. Isoform 4 glycosylation is required for its proper function. Ref.5

Sequence similarities

Contains 1 FAD-binding FR-type domain.

Contains 1 ferric oxidoreductase domain.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Endoplasmic reticulum
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransmembrane
Transmembrane helix
   LigandNADP
   Molecular functionOxidoreductase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbone resorption

Inferred from electronic annotation. Source: Ensembl

cardiocyte differentiation

Inferred from electronic annotation. Source: Ensembl

cell aging

Inferred from sequence or structural similarity Ref.1. Source: UniProtKB

cell morphogenesis

Inferred from sequence or structural similarity Ref.1. Source: UniProtKB

cellular response to cAMP

Inferred from electronic annotation. Source: Ensembl

cellular response to gamma radiation

Inferred from electronic annotation. Source: Ensembl

cellular response to glucose stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to transforming growth factor beta stimulus

Inferred from electronic annotation. Source: Ensembl

homocysteine metabolic process

Inferred from direct assay PubMed 20031578. Source: UniProtKB

inflammatory response

Traceable author statement Ref.1. Source: UniProtKB

negative regulation of cell proliferation

Inferred from sequence or structural similarity Ref.1. Source: UniProtKB

oxidation-reduction process

Inferred from direct assay Ref.1. Source: UniProtKB

positive regulation of DNA biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of ERK1 and ERK2 cascade

Inferred from electronic annotation. Source: Ensembl

positive regulation of MAP kinase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of reactive oxygen species metabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of smooth muscle cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of stress fiber assembly

Inferred from electronic annotation. Source: Ensembl

reactive oxygen species metabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

superoxide anion generation

Inferred from sequence or structural similarity Ref.1. Source: UniProtKB

   Cellular_componentNADPH oxidase complex

Inferred from electronic annotation. Source: Ensembl

apical plasma membrane

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

focal adhesion

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Traceable author statement Ref.1. Source: UniProtKB

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionNAD(P)H oxidase activity

Traceable author statement Ref.1. Source: UniProtKB

electron carrier activity

Traceable author statement Ref.1. Source: UniProtKB

flavin adenine dinucleotide binding

Traceable author statement Ref.1. Source: UniProtKB

heme binding

Traceable author statement Ref.1. Source: UniProtKB

modified amino acid binding

Inferred from direct assay PubMed 20031578. Source: UniProtKB

nucleotide binding

Traceable author statement Ref.1. Source: UniProtKB

oxygen sensor activity

Traceable author statement Ref.1. Source: UniProtKB

superoxide-generating NADPH oxidase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 9 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NPH5-1)

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.
Isoform 2 (identifier: Q9NPH5-2)

Also known as: Nox4A;

The sequence of this isoform differs from the canonical sequence as follows:
     1-74: Missing.
Isoform 3 (identifier: Q9NPH5-3)

Also known as: Nox4E;

The sequence of this isoform differs from the canonical sequence as follows:
     52-358: Missing.
     407-446: Missing.
Isoform 4 (identifier: Q9NPH5-4)

Also known as: 28 kDa; Nox4D;

The sequence of this isoform differs from the canonical sequence as follows:
     52-358: Missing.
Isoform 5 (identifier: Q9NPH5-5)

Also known as: Nox4C;

The sequence of this isoform differs from the canonical sequence as follows:
     211-224: GLLKYQTNLDTHPP → VQLKPKQHLGFILK
     225-578: Missing.
Isoform 6 (identifier: Q9NPH5-6)

Also known as: Nox4B;

The sequence of this isoform differs from the canonical sequence as follows:
     407-446: Missing.
Isoform 7 (identifier: Q9NPH5-7)

The sequence of this isoform differs from the canonical sequence as follows:
     52-54: LGL → ELS
     55-578: Missing.
Isoform 8 (identifier: Q9NPH5-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: Missing.
Isoform 9 (identifier: Q9NPH5-9)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 578578NADPH oxidase 4
PRO_0000238980

Regions

Topological domain1 – 1616Cytoplasmic Potential
Transmembrane17 – 3721Helical; Potential
Topological domain38 – 6225Extracellular Potential
Transmembrane63 – 8321Helical; Potential
Topological domain84 – 10320Cytoplasmic Potential
Transmembrane104 – 12421Helical; Potential
Topological domain125 – 15430Extracellular Potential
Transmembrane155 – 17521Helical; Potential
Topological domain176 – 18813Cytoplasmic Potential
Transmembrane189 – 20921Helical; Potential
Topological domain210 – 424215Extracellular Potential
Transmembrane425 – 44521Helical; Potential
Topological domain446 – 578133Cytoplasmic Potential
Domain58 – 303246Ferric oxidoreductase
Domain304 – 419116FAD-binding FR-type
Region248 – 575328Mediates interaction with TLR4

Amino acid modifications

Glycosylation1331N-linked (GlcNAc...) Potential
Glycosylation2301N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 7474Missing in isoform 2.
VSP_019052
Alternative sequence1 – 2424Missing in isoform 8 and isoform 9.
VSP_053826
Alternative sequence52 – 358307Missing in isoform 3 and isoform 4.
VSP_019053
Alternative sequence52 – 543LGL → ELS in isoform 7.
VSP_019054
Alternative sequence55 – 578524Missing in isoform 7.
VSP_019055
Alternative sequence211 – 22414GLLKY…DTHPP → VQLKPKQHLGFILK in isoform 5.
VSP_019056
Alternative sequence225 – 578354Missing in isoform 5.
VSP_019057
Alternative sequence407 – 44640Missing in isoform 3, isoform 6 and isoform 9.
VSP_019058
Natural variant3151M → I. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.8
Corresponds to variant rs317139 [ dbSNP | Ensembl ].
VAR_047114

Experimental info

Mutagenesis3041R → RGT: Partial loss of catalytic activity. No effect on CYBA localization. Ref.16
Mutagenesis575 – 5784Missing: Partial loss of catalytic activity. No effect on CYBA localization. Ref.16
Sequence conflict2861W → C in BAH12756. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 4, 2008. Version 2.
Checksum: D150A92CC71DD40D

FASTA57866,932
        10         20         30         40         50         60 
MAVSWRSWLA NEGVKHLCLF IWLSMNVLLF WKTFLLYNQG PEYHYLHQML GLGLCLSRAS 

        70         80         90        100        110        120 
ASVLNLNCSL ILLPMCRTLL AYLRGSQKVP SRRTRRLLDK SRTFHITCGV TICIFSGVHV 

       130        140        150        160        170        180 
AAHLVNALNF SVNYSEDFVE LNAARYRDED PRKLLFTTVP GLTGVCMVVV LFLMITASTY 

       190        200        210        220        230        240 
AIRVSNYDIF WYTHNLFFVF YMLLTLHVSG GLLKYQTNLD THPPGCISLN RTSSQNISLP 

       250        260        270        280        290        300 
EYFSEHFHEP FPEGFSKPAE FTQHKFVKIC MEEPRFQANF PQTWLWISGP LCLYCAERLY 

       310        320        330        340        350        360 
RYIRSNKPVT IISVMSHPSD VMEIRMVKEN FKARPGQYIT LHCPSVSALE NHPFTLTMCP 

       370        380        390        400        410        420 
TETKATFGVH LKIVGDWTER FRDLLLPPSS QDSEILPFIQ SRNYPKLYID GPFGSPFEES 

       430        440        450        460        470        480 
LNYEVSLCVA GGIGVTPFAS ILNTLLDDWK PYKLRRLYFI WVCRDIQSFR WFADLLCMLH 

       490        500        510        520        530        540 
NKFWQENRPD YVNIQLYLSQ TDGIQKIIGE KYHALNSRLF IGRPRWKLLF DEIAKYNRGK 

       550        560        570 
TVGVFCCGPN SLSKTLHKLS NQNNSYGTRF EYNKESFS 

« Hide

Isoform 2 (Nox4A) [UniParc].

Checksum: 5D1ECB62CB23ED47
Show »

FASTA50458,410
Isoform 3 (Nox4E) [UniParc].

Checksum: 548F872E16DC4D37
Show »

FASTA23127,625
Isoform 4 (28 kDa) (Nox4D) [UniParc].

Checksum: 9C889BAAB7E531A2
Show »

FASTA27131,812
Isoform 5 (Nox4C) [UniParc].

Checksum: 27E3A0B6890E2A67
Show »

FASTA22425,761
Isoform 6 (Nox4B) [UniParc].

Checksum: 2E541C48425EF25B
Show »

FASTA53862,745
Isoform 7 [UniParc].

Checksum: 2392A10568021769
Show »

FASTA546,516
Isoform 8 [UniParc].

Checksum: D7469DB8BCE92821
Show »

FASTA55464,102
Isoform 9 [UniParc].

Checksum: 5FFB5AA1DBE790B0
Show »

FASTA51459,915

References

« Hide 'large scale' references
[1]"Identification of renox, an NAD(P)H oxidase in kidney."
Geiszt M., Kopp J.B., Varnai P., Leto T.L.
Proc. Natl. Acad. Sci. U.S.A. 97:8010-8014(2000) [PubMed] [Europe PMC] [Abstract]
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]"A novel superoxide-producing NAD(P)H oxidase in kidney."
Shiose A., Kuroda J., Tsuruya K., Hirai M., Hirakata H., Naito S., Hattori M., Sakaki Y., Sumimoto H.
J. Biol. Chem. 276:1417-1423(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS44695.1. [Q9NPH5-6]
CCDS8285.1. [Q9NPH5-1]
RefSeqNP_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]
UniGeneHs.371036.

3D structure databases

ProteinModelPortalQ9NPH5.
SMRQ9NPH5. Positions 409-577.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000263317.

Chemistry

BindingDBQ9NPH5.
ChEMBLCHEMBL1250375.

Protein family/group databases

PeroxiBase5967. HsNOx04.
TCDB5.B.1.1.2. the phagocyte (gp91(phox)) nadph oxidase family.

PTM databases

PhosphoSiteQ9NPH5.

Polymorphism databases

DMDM212276447.

Proteomic databases

PaxDbQ9NPH5.
PRIDEQ9NPH5.

Protocols and materials databases

DNASU50507.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263317; ENSP00000263317; ENSG00000086991. [Q9NPH5-1]
ENST00000343727; ENSP00000344747; ENSG00000086991.
ENST00000375979; ENSP00000365146; ENSG00000086991. [Q9NPH5-4]
ENST00000393282; ENSP00000376961; ENSG00000086991. [Q9NPH5-7]
ENST00000424319; ENSP00000412446; ENSG00000086991.
ENST00000527956; ENSP00000433797; ENSG00000086991.
ENST00000529343; ENSP00000435474; ENSG00000086991. [Q9NPH5-5]
ENST00000531342; ENSP00000435039; ENSG00000086991. [Q9NPH5-3]
ENST00000532825; ENSP00000434924; ENSG00000086991.
ENST00000534731; ENSP00000436892; ENSG00000086991. [Q9NPH5-6]
ENST00000535633; ENSP00000440172; ENSG00000086991.
ENST00000542487; ENSP00000439373; ENSG00000086991.
GeneID50507.
KEGGhsa:50507.
UCSCuc001pcu.3. human. [Q9NPH5-1]
uc001pcv.3. human. [Q9NPH5-6]
uc001pcw.3. human. [Q9NPH5-4]
uc001pcx.3. human. [Q9NPH5-3]

Organism-specific databases

CTD50507.
GeneCardsGC11M089057.
HGNCHGNC:7891. NOX4.
HPAHPA015475.
MIM605261. gene.
neXtProtNX_Q9NPH5.
PharmGKBPA31692.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG265816.
HOVERGENHBG003760.
InParanoidQ9NPH5.
OrthoDBEOG7RZ5PZ.
PhylomeDBQ9NPH5.
TreeFamTF105354.

Gene expression databases

ArrayExpressQ9NPH5.
BgeeQ9NPH5.
CleanExHS_NOX4.
GenevestigatorQ9NPH5.

Family and domain databases

InterProIPR000778. 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]
PfamPF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
PRINTSPR00466. GP91PHOX.
SUPFAMSSF63380. SSF63380. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiNOX4.
GenomeRNAi50507.
NextBio35499451.
PROQ9NPH5.
SOURCESearch...

Entry information

Entry nameNOX4_HUMAN
AccessionPrimary (citable) accession number: Q9NPH5
Secondary accession number(s): A8K715 expand/collapse secondary AC list , B7Z520, E7EMD7, Q5K3R4, Q5K3R5, Q5K3R6, Q5K3R8, Q7Z7G3, Q86V92
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: November 4, 2008
Last modified: July 9, 2014
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM