NOXO1

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2L73

Identifiers

Aliases

NOXO1, P41NOX, P41NOXA, P41NOXB, P41NOXC, SH3PXD5, SNX28, NADPH oxidase organizer 1

External IDs

MGI: 1919143 HomoloGene: 12418 GeneCards: NOXO1

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
Biological process	• regulation of respiratory burst • extracellular matrix disassembly • positive regulation of catalytic activity • regulation of hydrogen peroxide metabolic process • superoxide metabolic process • oxidation-reduction process
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


124056


71893

Ensembl


ENSG00000196408


ENSMUSG00000019320

UniProt


Q8NFA2


Q8VCM2

RefSeq (mRNA)


NM_001267721 NM_144603 NM_172167 NM_172168


NM_027988

RefSeq (protein)


NP_001254650.1 NP_653204.1 NP_751907.1 NP_751908.1


NP_082264.2

Location (UCSC)

Chr 16: 1.98 – 1.98 Mb

Chr 17: 24.7 – 24.7 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

NADPH oxidase organizer 1 is an enzyme that in humans is encoded by the NOXO1 gene.^[3]

References

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.
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.
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.

Sorting nexins

SNX-BAR	SNX1 SNX2 SNX4 SNX5 SNX6 SNX7 SNX8 SNX9 SNX18 SNX30 SNX32 SNX33

SNX-PX	SNX3 SNX10 SNX11 SNX12 SNX16 SNX20 SNX21 SNX22 SNX24 SNX29

SNX-Other	SNX13 SNX14 SNX15 SNX17 SNX19 SNX23 SNX25 SNX26 SNX27 SNX28 SNX31

Related articles	PX domain BAR domain Retromer

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NOXO1

References

Further reading