NOXO1

NADPH oxidase organizer 1
Identifiers
Symbols	NOXO1; MGC20258; P41NOX; P41NOXA; P41NOXB; P41NOXC; SH3PXD5; SNX28
External IDs	OMIM: 611256 MGI: 1919143 HomoloGene: 12418 GeneCards: NOXO1 Gene
Gene Ontology Molecular function • protein binding • phospholipid binding • superoxide-generating NADPH oxidase activator activity • enzyme binding • phosphatidylinositol binding Cellular component • plasma membrane • NADPH oxidase complex Biological process • superoxide metabolic process • cell communication • regulation of hydrogen peroxide metabolic process • regulation of respiratory burst Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	124056	71893
Ensembl	ENSG00000196408	ENSMUSG00000019320
UniProt	Q8NFA2	Q0VDT6
RefSeq (mRNA)	NM_144603.2	NM_027988.4
RefSeq (protein)	NP_653204.1	NP_082264.2
Location (UCSC)	Chr 16: 2.03 – 2.03 Mb	Chr 17: 24.83 – 24.84 Mb
PubMed search	[1]	[2]

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

References

1. ^ "Entrez Gene: NOXO1 NADPH oxidase organizer 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=124056. 

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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• 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. 
• 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.