NOXO1

Protein-coding gene in the species Homo sapiens
NOXO1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2L73

Identifiers
AliasesNOXO1, P41NOX, P41NOXA, P41NOXB, P41NOXC, SH3PXD5, SNX28, NADPH oxidase organizer 1
External IDsOMIM: 611256; MGI: 1919143; HomoloGene: 12418; GeneCards: NOXO1; OMA:NOXO1 - orthologs
Gene location (Human)
Chromosome 16 (human)
Chr.Chromosome 16 (human)[1]
Chromosome 16 (human)
Genomic location for NOXO1
Genomic location for NOXO1
Band16p13.3Start1,978,917 bp[1]
End1,984,192 bp[1]
Gene location (Mouse)
Chromosome 17 (mouse)
Chr.Chromosome 17 (mouse)[2]
Chromosome 17 (mouse)
Genomic location for NOXO1
Genomic location for NOXO1
Band17 A3.3|17 12.49 cMStart24,915,208 bp[2]
End24,919,503 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • mucosa of transverse colon

  • gonad

  • testicle

  • rectum

  • appendix

  • olfactory zone of nasal mucosa

  • right hemisphere of cerebellum

  • mucosa of sigmoid colon

  • right lobe of liver

  • left testis
Top expressed in
  • Paneth cell

  • crypt of lieberkuhn of small intestine

  • spermatocyte

  • large intestine

  • colon

  • left colon

  • ileum

  • spermatid

  • jejunum

  • intestinal villus
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • enzyme binding
  • superoxide-generating NADPH oxidase activator activity
  • protein binding
  • phospholipid binding
  • identical protein binding
  • lipid binding
  • phosphatidylinositol binding
Cellular component
  • plasma membrane
  • NADPH oxidase complex
  • membrane
  • intracellular anatomical structure
Biological process
  • regulation of respiratory burst
  • extracellular matrix disassembly
  • positive regulation of catalytic activity
  • regulation of hydrogen peroxide metabolic process
  • superoxide metabolic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

124056

71893

Ensembl

ENSG00000196408

ENSMUSG00000019320

UniProt

Q8NFA2

Q8VCM2

RefSeq (mRNA)

NM_001267721
NM_144603
NM_172167
NM_172168

NM_027988
NM_001357836

RefSeq (protein)

NP_001254650
NP_653204
NP_751907
NP_751908

NP_082264
NP_001344765

Location (UCSC)Chr 16: 1.98 – 1.98 MbChr 17: 24.92 – 24.92 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

NADPH oxidase organizer 1 is an enzyme that in humans is encoded by the NOXO1 gene.[5]


References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000196408 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000019320 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ "Entrez Gene: NOXO1 NADPH oxidase organizer 1".

Further reading

  • Bánfi B, Clark RA, Steger K, Krause KH (2003). "Two novel proteins activate superoxide generation by the NADPH oxidase NOX1". J. Biol. Chem. 278 (6): 3510–3. doi:10.1074/jbc.C200613200. PMID 12473664.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Geiszt M, Lekstrom K, Witta J, Leto TL (2003). "Proteins homologous to p47phox and p67phox support superoxide production by NAD(P)H oxidase 1 in colon epithelial cells". J. Biol. Chem. 278 (22): 20006–12. doi:10.1074/jbc.M301289200. PMID 12657628.
  • Takeya R, Ueno N, Kami K, et al. (2003). "Novel human homologues of p47phox and p67phox participate in activation of superoxide-producing NADPH oxidases". J. Biol. Chem. 278 (27): 25234–46. doi:10.1074/jbc.M212856200. PMID 12716910.
  • Cheng G, Lambeth JD (2004). "NOXO1, regulation of lipid binding, localization, and activation of Nox1 by the Phox homology (PX) domain". J. Biol. Chem. 279 (6): 4737–42. doi:10.1074/jbc.M305968200. PMID 14617635.
  • Cheng G, Ritsick D, Lambeth JD (2004). "Nox3 regulation by NOXO1, p47phox, and p67phox". J. Biol. Chem. 279 (33): 34250–5. doi:10.1074/jbc.M400660200. PMID 15181005.
  • Bánfi B, Malgrange B, Knisz J, et al. (2004). "NOX3, a superoxide-generating NADPH oxidase of the inner ear". J. Biol. Chem. 279 (44): 46065–72. doi:10.1074/jbc.M403046200. PMID 15326186.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Ueno N, Takeya R, Miyano K, et al. (2005). "The NADPH oxidase Nox3 constitutively produces superoxide in a p22phox-dependent manner: its regulation by oxidase organizers and activators". J. Biol. Chem. 280 (24): 23328–39. doi:10.1074/jbc.M414548200. PMID 15824103.
  • Cheng G, Lambeth JD (2005). "Alternative mRNA splice forms of NOXO1: differential tissue expression and regulation of Nox1 and Nox3". Gene. 356: 118–26. doi:10.1016/j.gene.2005.03.008. PMID 15949904.
  • Park HS, Park D, Bae YS (2006). "Molecular interaction of NADPH oxidase 1 with betaPix and Nox Organizer 1". Biochem. Biophys. Res. Commun. 339 (3): 985–90. doi:10.1016/j.bbrc.2005.11.108. PMID 16329988.
  • Takeya R, Taura M, Yamasaki T, et al. (2006). "Expression and function of Noxo1gamma, an alternative splicing form of the NADPH oxidase organizer 1". FEBS J. 273 (16): 3663–77. doi:10.1111/j.1742-4658.2006.05371.x. PMID 16911517. S2CID 701568.
  • Yamamoto A, Kami K, Takeya R, Sumimoto H (2007). "Interaction between the SH3 domains and C-terminal proline-rich region in NADPH oxidase organizer 1 (Noxo1)". Biochem. Biophys. Res. Commun. 352 (2): 560–5. doi:10.1016/j.bbrc.2006.11.060. PMID 17126813.

External links

  • PDBe-KB provides an overview of all the structure information available in the PDB for Human NADPH oxidase organizer 1


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  • e
SNX-BAR
SNX-PX
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  • SNX10
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  • SNX20
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