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Q9HBY0

- NOX3_HUMAN

UniProt

Q9HBY0 - NOX3_HUMAN

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Protein

NADPH oxidase 3

Gene

NOX3

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

Functioni

NADPH oxidase which constitutively produces superoxide upon formation of a complex with CYBA/p22phox. Plays a role in the biogenesis of otoconia/otolith, which are crystalline structures of the inner ear involved in the perception of gravity.1 Publication

Enzyme regulationi

Activated by the ototoxic drug cisplatin (By similarity). Activated by NOXO1. Cooperatively activated by NCF1 and NCF2 or NOXA1 in a phorbol 12-myristate 13-acetate (PMA)-dependent manner. Inhibited by diphenyleneiodonium chloride.By similarity2 Publications

GO - Molecular functioni

  1. superoxide-generating NADPH oxidase activity Source: Ensembl

GO - Biological processi

  1. detection of gravity Source: Ensembl
  2. otolith development Source: Ensembl
  3. superoxide anion generation Source: Ensembl
  4. temperature homeostasis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Protein family/group databases

PeroxiBasei5960. HsNOx03.
TCDBi5.B.1.1.4. the phagocyte (gp91(phox)) nadph oxidase family.

Names & Taxonomyi

Protein namesi
Recommended name:
NADPH oxidase 3 (EC:1.6.3.-)
Alternative name(s):
Mitogenic oxidase 2
Short name:
MOX-2
gp91phox homolog 3
Short name:
GP91-3
Gene namesi
Name:NOX3
Synonyms:MOX2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:7890. NOX3.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. extracellular vesicular exosome Source: UniProt
  3. NADPH oxidase complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi413 – 4131P → H: Loss of catalytic activity. 1 Publication

Organism-specific databases

PharmGKBiPA31691.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 568568NADPH oxidase 3PRO_0000227596Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi163 – 1631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi238 – 2381N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9HBY0.
PRIDEiQ9HBY0.

PTM databases

PhosphoSiteiQ9HBY0.

Expressioni

Developmental stagei

Expressed in fetal kidney and to a lower extent in liver, lung and spleen.2 Publications

Gene expression databases

CleanExiHS_NOX3.
GenevestigatoriQ9HBY0.

Interactioni

Subunit structurei

Interacts with and stabilizes CYBA/p22phox.1 Publication

Protein-protein interaction databases

STRINGi9606.ENSP00000159060.

Structurei

3D structure databases

ProteinModelPortaliQ9HBY0.
SMRiQ9HBY0. Positions 383-568.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1313CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini35 – 5117ExtracellularSequence AnalysisAdd
BLAST
Topological domaini73 – 10331CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini125 – 16743ExtracellularSequence AnalysisAdd
BLAST
Topological domaini189 – 20113CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini223 – 395173ExtracellularSequence AnalysisAdd
BLAST
Topological domaini417 – 568152CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei14 – 3421HelicalSequence AnalysisAdd
BLAST
Transmembranei52 – 7221HelicalSequence AnalysisAdd
BLAST
Transmembranei104 – 12421HelicalSequence AnalysisAdd
BLAST
Transmembranei168 – 18821HelicalSequence AnalysisAdd
BLAST
Transmembranei202 – 22221HelicalSequence AnalysisAdd
BLAST
Transmembranei396 – 41621HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 284230Ferric oxidoreductaseAdd
BLAST
Domaini285 – 395111FAD-binding FR-typePROSITE-ProRule annotationAdd
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

eggNOGiNOG287712.
GeneTreeiENSGT00550000074350.
HOGENOMiHOG000216669.
HOVERGENiHBG003760.
InParanoidiQ9HBY0.
KOiK08008.
OMAiKCSEAQT.
OrthoDBiEOG71P299.
PhylomeDBiQ9HBY0.
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.
IPR029653. NOX3.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PANTHERiPTHR11972:SF12. PTHR11972:SF12. 1 hit.
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]

Sequencei

Sequence statusi: Complete.

Q9HBY0 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MMGCWILNEG LSTILVLSWL GINFYLFIDT FYWYEEEESF HYTRVILGST
60 70 80 90 100
LAWARASALC LNFNCMLILI PVSRNLISFI RGTSICCRGP WRRQLDKNLR
110 120 130 140 150
FHKLVAYGIA VNATIHIVAH FFNLERYHWS QSEEAQGLLA ALSKLGNTPN
160 170 180 190 200
ESYLNPVRTF PTNTTTELLR TIAGVTGLVI SLALVLIMTS STEFIRQASY
210 220 230 240 250
ELFWYTHHVF IVFFLSLAIH GTGRIVRGQT QDSLSLHNIT FCRDRYAEWQ
260 270 280 290 300
TVAQCPVPQF SGKEPSAWKW ILGPVVLYAC ERIIRFWRFQ QEVVITKVVS
310 320 330 340 350
HPSGVLELHM KKRGFKMAPG QYILVQCPAI SSLEWHPFTL TSAPQEDFFS
360 370 380 390 400
VHIRAAGDWT AALLEAFGAE GQALQEPWSL PRLAVDGPFG TALTDVFHYP
410 420 430 440 450
VCVCVAAGIG VTPFAALLKS IWYKCSEAQT PLKLSKVYFY WICRDARAFE
460 470 480 490 500
WFADLLLSLE TRMSEQGKTH FLSYHIFLTG WDENQALHIA LHWDENTDVI
510 520 530 540 550
TGLKQKTFYG RPNWNNEFKQ IAYNHPSSSI GVFFCGPKAL SRTLQKMCHL
560
YSSADPRGVH FYYNKESF
Length:568
Mass (Da):64,935
Last modified:March 1, 2001 - v1
Checksum:i10BCD6BEB18D0583
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti328 – 3281P → S in AAG15435. (PubMed:10974555)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti171 – 1711T → K.
Corresponds to variant rs3749930 [ dbSNP | Ensembl ].
VAR_049103

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF190122 mRNA. Translation: AAG17121.1.
AL031773 Genomic DNA. Translation: CAI19957.1.
AF229177 mRNA. Translation: AAG15435.1.
CCDSiCCDS5250.1.
RefSeqiNP_056533.1. NM_015718.2.
UniGeneiHs.247776.

Genome annotation databases

EnsembliENST00000159060; ENSP00000159060; ENSG00000074771.
GeneIDi50508.
KEGGihsa:50508.
UCSCiuc003qqm.3. human.

Polymorphism databases

DMDMi74752785.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF190122 mRNA. Translation: AAG17121.1 .
AL031773 Genomic DNA. Translation: CAI19957.1 .
AF229177 mRNA. Translation: AAG15435.1 .
CCDSi CCDS5250.1.
RefSeqi NP_056533.1. NM_015718.2.
UniGenei Hs.247776.

3D structure databases

ProteinModelPortali Q9HBY0.
SMRi Q9HBY0. Positions 383-568.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000159060.

Chemistry

ChEMBLi CHEMBL1741216.

Protein family/group databases

PeroxiBasei 5960. HsNOx03.
TCDBi 5.B.1.1.4. the phagocyte (gp91(phox)) nadph oxidase family.

PTM databases

PhosphoSitei Q9HBY0.

Polymorphism databases

DMDMi 74752785.

Proteomic databases

PaxDbi Q9HBY0.
PRIDEi Q9HBY0.

Protocols and materials databases

DNASUi 50508.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000159060 ; ENSP00000159060 ; ENSG00000074771 .
GeneIDi 50508.
KEGGi hsa:50508.
UCSCi uc003qqm.3. human.

Organism-specific databases

CTDi 50508.
GeneCardsi GC06M155716.
HGNCi HGNC:7890. NOX3.
MIMi 607105. gene.
neXtProti NX_Q9HBY0.
PharmGKBi PA31691.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG287712.
GeneTreei ENSGT00550000074350.
HOGENOMi HOG000216669.
HOVERGENi HBG003760.
InParanoidi Q9HBY0.
KOi K08008.
OMAi KCSEAQT.
OrthoDBi EOG71P299.
PhylomeDBi Q9HBY0.
TreeFami TF105354.

Miscellaneous databases

GeneWikii NOX3.
GenomeRNAii 50508.
NextBioi 53074.
PROi Q9HBY0.
SOURCEi Search...

Gene expression databases

CleanExi HS_NOX3.
Genevestigatori Q9HBY0.

Family and domain databases

InterProi IPR000778. Cyt_b245_heavy_chain.
IPR013112. FAD-bd_8.
IPR017927. Fd_Rdtase_FAD-bd.
IPR013130. Fe3_Rdtase_TM_dom.
IPR013121. Fe_red_NAD-bd_6.
IPR029653. NOX3.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view ]
PANTHERi PTHR11972:SF12. PTHR11972:SF12. 1 hit.
Pfami PF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view ]
PRINTSi PR00466. GP91PHOX.
SUPFAMi SSF63380. SSF63380. 1 hit.
PROSITEi PS51384. FAD_FR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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], DEVELOPMENTAL STAGE.
    Tissue: Fetal kidney.
  2. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "NADPH oxidase subunit, gp91phox homologue, preferentially expressed in human colon epithelial cells."
    Kikuchi H., Hikage M., Miyashita H., Fukumoto M.
    Gene 254:237-243(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 54-497, DEVELOPMENTAL STAGE.
    Tissue: Fetal kidney.
  4. "Nox3 regulation by NOXO1, p47phox, and p67phox."
    Cheng G., Ritsick D., Lambeth J.D.
    J. Biol. Chem. 279:34250-34255(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  5. "The NADPH oxidase Nox3 constitutively produces superoxide in a p22phox-dependent manner: its regulation by oxidase organizers and activators."
    Ueno N., Takeya R., Miyano K., Kikuchi H., Sumimoto H.
    J. Biol. Chem. 280:23328-23339(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF PRO-413, ENZYME REGULATION, INTERACTION WITH CYBA.

Entry informationi

Entry nameiNOX3_HUMAN
AccessioniPrimary (citable) accession number: Q9HBY0
Secondary accession number(s): Q9HBJ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: March 1, 2001
Last modified: October 29, 2014
This is version 94 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 6
    Human chromosome 6: 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