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Q96PH1 (NOX5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADPH oxidase 5

EC=1.6.3.-
Gene names
Name:NOX5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length765 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.10 Ref.14

Cofactor

FAD. Ref.11

Magnesium. Ref.11

Enzyme regulation

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. Ref.11

Subcellular location

Membrane; Multi-pass membrane protein Potential Ref.14.

Isoform v2: Endoplasmic reticulum Ref.14.

Isoform v5: Endoplasmic reticulum Ref.14.

Tissue specificity

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). Ref.1 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14

Developmental stage

Expressed in fetal tissues. Ref.9

Induction

Down-regulated by TGFB1. Ref.11 Ref.12

Domain

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 similarities

Contains 4 EF-hand domains.

Contains 1 FAD-binding FR-type domain.

Contains 1 ferric oxidoreductase domain.

Biophysicochemical properties

Kinetic parameters:

KM=1.06 µM for calcium Ref.11

Sequence caution

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.

Ontologies

Keywords
   Biological processAngiogenesis
Electron transport
Ion transport
Transport
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandCalcium
FAD
Flavoprotein
Metal-binding
NADP
   Molecular functionIon channel
Oxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from direct assay Ref.14. Source: UniProtKB

apoptotic process

Non-traceable author statement Ref.1. Source: UniProtKB

cell proliferation

Non-traceable author statement Ref.1. Source: UniProtKB

cytokine secretion

Non-traceable author statement Ref.1. Source: UniProtKB

cytokinesis

Non-traceable author statement Ref.1. Source: UniProtKB

endothelial cell proliferation

Inferred from direct assay Ref.14. Source: UniProtKB

oxidation-reduction process

Inferred from direct assay Ref.1. Source: UniProtKB

positive regulation of reactive oxygen species metabolic process

Inferred from direct assay Ref.14. Source: UniProtKB

proton transport

Inferred from direct assay Ref.1. Source: GOC

regulation of fusion of sperm to egg plasma membrane

Non-traceable author statement Ref.1. Source: UniProtKB

regulation of proton transport

Non-traceable author statement Ref.1. Source: UniProtKB

superoxide anion generation

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentendoplasmic reticulum

Inferred from direct assay Ref.14. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionNADP binding

Non-traceable author statement Ref.1. Source: UniProtKB

calcium ion binding

Inferred from electronic annotation. Source: InterPro

flavin adenine dinucleotide binding

Non-traceable author statement Ref.1. Source: UniProtKB

heme binding

Non-traceable author statement Ref.1. Source: UniProtKB

hydrogen ion channel activity

Inferred from direct assay Ref.1. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 17346712. Source: IntAct

superoxide-generating NADPH oxidase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CALMP621573EBI-7305642,EBI-397403From a different organism.

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform v3 (identifier: Q96PH1-1)

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.
Isoform v1 (identifier: Q96PH1-3)

Also known as: NOX5alpha;

The sequence of this isoform differs from the canonical sequence as follows:
     109-136: Missing.
Isoform v2 (identifier: Q96PH1-4)

Also known as: NOX5beta;

The sequence of this isoform differs from the canonical sequence as follows:
     1-18: Missing.
     109-136: Missing.
Isoform v4 (identifier: Q96PH1-2)

Also known as: NOX5delta;

The sequence of this isoform differs from the canonical sequence as follows:
     1-18: Missing.
Isoform v5 (identifier: Q96PH1-5)

Also known as: NOX5epsilon; NOX5S;

The sequence of this isoform differs from the canonical sequence as follows:
     1-200: Missing.
Isoform v6 (identifier: Q96PH1-6)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 765765NADPH oxidase 5
PRO_0000224995

Regions

Topological domain1 – 238238Cytoplasmic Potential
Transmembrane239 – 25921Helical; Potential
Topological domain260 – 2667Extracellular Potential
Transmembrane267 – 28923Helical; Potential
Topological domain290 – 31728Cytoplasmic Potential
Transmembrane318 – 33821Helical; Potential
Topological domain339 – 36224Extracellular Potential
Transmembrane363 – 38321Helical; Potential
Topological domain384 – 39411Cytoplasmic Potential
Transmembrane395 – 41723Helical; Potential
Topological domain418 – 43417Extracellular Potential
Transmembrane435 – 45521Helical; Potential
Topological domain456 – 583128Cytoplasmic Potential
Transmembrane584 – 60421Helical; Potential
Topological domain605 – 765161Extracellular Potential
Domain26 – 5631EF-hand 1
Domain57 – 9236EF-hand 2
Domain93 – 15664EF-hand 3; atypical; contains an insert of 28 residues
Domain165 – 20036EF-hand 4
Domain293 – 440148Ferric oxidoreductase
Domain441 – 577137FAD-binding FR-type
Calcium binding39 – 49111 Potential
Calcium binding70 – 81122 Potential
Calcium binding106 – 10833; first part Potential
Calcium binding137 – 146103; second part Potential
Calcium binding178 – 189124 Potential
Region1 – 169169N-terminal regulatory region; interacts with the C-terminal catalytic region in a calcium-dependent manner
Region449 – 565117C-terminal catalytic region
Compositional bias374 – 3807Poly-Leu

Natural variations

Alternative sequence1 – 200200Missing in isoform v5.
VSP_017326
Alternative sequence1 – 1818Missing in isoform v2 and isoform v4.
VSP_017327
Alternative sequence1 – 1717MNTSG…EGCRG → MAFVCAGLSD in isoform v6.
VSP_041619
Alternative sequence109 – 13628Missing in isoform v1, isoform v2 and isoform v6.
VSP_017328
Natural variant5761R → H.
Corresponds to variant rs2277552 [ dbSNP | Ensembl ].
VAR_055820
Natural variant7591R → G.
Corresponds to variant rs7168025 [ dbSNP | Ensembl ].
VAR_055821

Experimental info

Mutagenesis491E → Q: Loss of binding of 1 calcium molecule. No effect on catalytic activity. Ref.11
Sequence conflict2081A → T in AAG33638. Ref.8
Sequence conflict2721G → S in AAI25099. Ref.7
Sequence conflict3751L → P in BAG37241. Ref.3
Sequence conflict3801L → F in BAB84884. Ref.2
Sequence conflict3801L → F in BAB84897. Ref.2
Sequence conflict3801L → F in BAB15319. Ref.3
Sequence conflict3801L → F in BAG37241. Ref.3
Sequence conflict3801L → F in EAW77830. Ref.6
Sequence conflict3801L → F in AAI25098. Ref.7
Sequence conflict3801L → F in AAI25099. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform v3 (NOX5gamma) [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 96B57225BF919682

FASTA76586,439
        10         20         30         40         50         60 
MNTSGDPAQT GPEGCRGTMS AEEDARWLRW VTQQFKTIAG EDGEISLQEF KAALHVKESF 

        70         80         90        100        110        120 
FAERFFALFD SDRSGTITLQ ELQEALTLLI HGSPMDKLKF LFQVYDIDVC ARQGASAGTE 

       130        140        150        160        170        180 
WGAGAGPHWA SSPLGTGSGS IDPDELRTVL QSCLRESAIS LPDEKLDQLT LALFESADAD 

       190        200        210        220        230        240 
GNGAITFEEL RDELQRFPGV MENLTISAAH WLTAPAPRPR PRRPRQLTRA YWHNHRSQLF 

       250        260        270        280        290        300 
CLATYAGLHV LLFGLAASAH RDLGASVMVA KGCGQCLNFD CSFIAVLMLR RCLTWLRATW 

       310        320        330        340        350        360 
LAQVLPLDQN IQFHQLMGYV VVGLSLVHTV AHTVNFVLQA QAEASPFQFW ELLLTTRPGI 

       370        380        390        400        410        420 
GWVHGSASPT GVALLLLLLL MFICSSSCIR RSGHFEVFYW THLSYLLVWL LLIFHGPNFW 

       430        440        450        460        470        480 
KWLLVPGILF FLEKAIGLAV SRMAAVCIME VNLLPSKVTH LLIKRPPFFH YRPGDYLYLN 

       490        500        510        520        530        540 
IPTIARYEWH PFTISSAPEQ KDTIWLHIRS QGQWTNRLYE SFKASDPLGR GSKRLSRSVT 

       550        560        570        580        590        600 
MRKSQRSSKG SEILLEKHKF CNIKCYIDGP YGTPTRRIFA SEHAVLIGAG IGITPFASIL 

       610        620        630        640        650        660 
QSIMYRHQKR KHTCPSCQHS WIEGVQDNMK LHKVDFIWIN RDQRSFEWFV SLLTKLEMDQ 

       670        680        690        700        710        720 
AEEAQYGRFL ELHMYMTSAL GKNDMKAIGL QMALDLLANK EKKDSITGLQ TRTQPGRPDW 

       730        740        750        760 
SKVFQKVAAE KKGKVQVFFC GSPALAKVLK GHCEKFGFRF FQENF 

« Hide

Isoform v1 (NOX5alpha) [UniParc].

Checksum: 33B3AC250C36F6E9
Show »

FASTA73783,774
Isoform v2 (NOX5beta) [UniParc].

Checksum: 04F7BA7C78B1AEDB
Show »

FASTA71982,013
Isoform v4 (NOX5delta) [UniParc].

Checksum: 86B46366672B6E4A
Show »

FASTA74784,678
Isoform v5 (NOX5epsilon) (NOX5S) [UniParc].

Checksum: 94785B98A61214F6
Show »

FASTA56564,652
Isoform v6 (NOX5zeta) [UniParc].

Checksum: 93B21AF3A0A1CE79
Show »

FASTA73083,109

References

« Hide 'large scale' references
[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. 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] (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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"NOX5 NAD(P)H oxidase regulates growth and apoptosis in DU 145 prostate cancer cells."
Brar S.S., Corbin Z., Kennedy T.P., Hemendinger R., Thornton L., Bommarius B., Arnold R.S., Whorton A.R., Sturrock A.B., Huecksteadt T.P., Quinn M.T., Krenitsky K., Ardie K.G., Lambeth J.D., Hoidal J.R.
Am. J. Physiol. 285:C353-C369(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[11]"Mechanism of Ca2+ activation of the NADPH oxidase 5 (NOX5)."
Banfi B., Tirone F., Durussel I., Knisz J., Moskwa P., Molnar G.Z., Krause K.-H., Cox J.A.
J. Biol. Chem. 279:18583-18591(2004) [PubMed] [Europe PMC] [Abstract]
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]"NOX5 variants are functionally active in endothelial cells."
BelAiba R.S., Djordjevic T., Petry A., Diemer K., Bonello S., Banfi B., Hess J., Pogrebniak A., Bickel C., Gorlach A.
Free Radic. Biol. Med. 42:446-459(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS32276.2. [Q96PH1-1]
CCDS53953.1. [Q96PH1-6]
CCDS53954.1. [Q96PH1-3]
RefSeqNP_001171708.1. NM_001184779.1. [Q96PH1-3]
NP_001171709.1. NM_001184780.1. [Q96PH1-6]
NP_078781.3. NM_024505.3. [Q96PH1-1]
UniGeneHs.657932.

3D structure databases

ProteinModelPortalQ96PH1.
SMRQ96PH1. Positions 35-206, 567-749.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122660. 5 interactions.
IntActQ96PH1. 1 interaction.
STRING9606.ENSP00000260364.

Chemistry

BindingDBQ96PH1.
ChEMBLCHEMBL1926497.

Protein family/group databases

PeroxiBase6024. HsNOx05.
TCDB5.B.1.1.5. the phagocyte (gp91(phox)) nadph oxidase family.

Polymorphism databases

DMDM74717091.

Proteomic databases

PaxDbQ96PH1.
PRIDEQ96PH1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260364; ENSP00000454143; ENSG00000255346. [Q96PH1-2]
ENST00000388866; ENSP00000373518; ENSG00000255346. [Q96PH1-1]
ENST00000448182; ENSP00000410887; ENSG00000255346. [Q96PH1-4]
ENST00000455873; ENSP00000416828; ENSG00000255346. [Q96PH1-6]
ENST00000530406; ENSP00000432440; ENSG00000255346. [Q96PH1-3]
GeneID79400.
KEGGhsa:79400.
UCSCuc002arp.2. human. [Q96PH1-1]
uc002arq.2. human. [Q96PH1-4]
uc002arr.2. human. [Q96PH1-3]
uc010bid.2. human. [Q96PH1-6]

Organism-specific databases

CTD79400.
GeneCardsGC15P069222.
H-InvDBHIX0012384.
HGNCHGNC:14874. NOX5.
HPAHPA019362.
MIM606572. gene.
neXtProtNX_Q96PH1.
PharmGKBPA31693.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG287712.
HOVERGENHBG082052.
InParanoidQ96PH1.
OMAVMVAKGC.
OrthoDBEOG7VQJC7.
PhylomeDBQ96PH1.
TreeFamTF324099.

Gene expression databases

BgeeQ96PH1.
CleanExHS_NOX5.
GenevestigatorQ96PH1.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
InterProIPR011992. 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]
PfamPF13202. 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]
SMARTSM00054. EFh. 2 hits.
[Graphical view]
SUPFAMSSF63380. SSF63380. 2 hits.
PROSITEPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
PS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiNOX5.
GenomeRNAi79400.
NextBio68361.
PROQ96PH1.
SOURCESearch...

Entry information

Entry nameNOX5_HUMAN
AccessionPrimary (citable) accession number: Q96PH1
Secondary accession number(s): B2RBJ4 expand/collapse secondary AC list , Q08AN2, Q08AN3, Q8TEQ1, Q8TER4, Q96PH2, Q96PJ8, Q96PJ9, Q9H6E0, Q9HAM8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 110 of the entry and version 1 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 15

Human chromosome 15: entries, gene names and cross-references to MIM