NOXO1

From Wikipedia, the free encyclopedia

NADPH oxidase organizer 1

Identifiers

NOXO1; MGC20258; P41NOX; P41NOXA; P41NOXB; P41NOXC; SH3PXD5

External IDs

MGI: 1919143 HomoloGene: 12418

Gene ontology
Molecular Function:	• protein binding • lipid binding • superoxide-generating NADPH oxidase activator activity • phosphoinositide binding
Cellular Component:	• membrane
Biological Process:	• superoxide metabolic process • cell communication

Orthologs

Human

Mouse

Refseq

NM_144603 (mRNA)
NP_653204 (protein)

NM_027988 (mRNA)
NP_082264 (protein)

Location

Chr 16: 1.97 - 1.97 Mb

Chr 17: 24.42 - 24.43 Mb

Pubmed search

[1]

[2]

NADPH oxidase organizer 1, also known as NOXO1, is a human gene.^[1]

[edit] References

^ Entrez Gene: NOXO1 NADPH oxidase organizer 1.

[edit] 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. 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. 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.
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.