NOXA1

NADPH oxidase activator 1
Identifiers
Symbols	NOXA1 ; NY-CO-31; SDCCAG31; p51NOX
External IDs	OMIM: 611255 MGI: 2449980 HomoloGene: 18156 GeneCards: NOXA1 Gene
Gene ontology Molecular function • protein binding • superoxide-generating NADPH oxidase activator activity • SH3 domain binding • enzyme binding • Rac GTPase binding Cellular component • cytosol • NADPH oxidase complex Biological process • superoxide metabolic process • small GTPase mediated signal transduction • regulation of hydrogen peroxide metabolic process • positive regulation of catalytic activity • regulation of respiratory burst Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	10811	241275
Ensembl	ENSG00000188747	ENSMUSG00000036805
UniProt	Q86UR1	Q8CJ00
RefSeq (mRNA)	NM_001256067	NM_001163626
RefSeq (protein)	NP_001242996	NP_001157098
Location (UCSC)	Chr 9: 137.42 – 137.43 Mb	Chr 2: 25.09 – 25.1 Mb
PubMed search

NADPH oxidase activator 1 is an enzyme that in humans is encoded by the NOXA1 gene.^[1][2]

References

1. Scanlan MJ, Chen YT, Williamson B, Gure AO, Stockert E, Gordan JD, Türeci O, Sahin U, Pfreundschuh M, Old LJ (May 1998). "Characterization of human colon cancer antigens recognized by autologous antibodies". International Journal of Cancer. Journal International Du Cancer 76 (5): 652–8. doi:10.1002/(SICI)1097-0215(19980529)76:5<652::AID-IJC7>3.0.CO;2-P. PMID 9610721.
2. "Entrez Gene: NOXA1 NADPH oxidase activator 1".

Further reading

• Opitz N, Drummond GR, Selemidis S, Meurer S, Schmidt HH (Jan 2007). "The 'A's and 'O's of NADPH oxidase regulation: a commentary on "Subcellular localization and function of alternatively spliced Noxo1 isoforms"". Free Radical Biology & Medicine 42 (2): 175–9. doi:10.1016/j.freeradbiomed.2006.11.003. PMID 17189823.
• Kim JS, Diebold BA, Babior BM, Knaus UG, Bokoch GM (Nov 2007). "Regulation of Nox1 activity via protein kinase A-mediated phosphorylation of NoxA1 and 14-3-3 binding". The Journal of Biological Chemistry 282 (48): 34787–800. doi:10.1074/jbc.M704754200. PMID 17913709.
• Valente AJ, El Jamali A, Epperson TK, Gamez MJ, Pearson DW, Clark RA (Aug 2007). "NOX1 NADPH oxidase regulation by the NOXA1 SH3 domain". Free Radical Biology & Medicine 43 (3): 384–96. doi:10.1016/j.freeradbiomed.2007.04.022. PMID 17602954.
• Lim J, Hao T, Shaw C, Patel AJ, Szabó G, Rual JF, Fisk CJ, Li N, Smolyar A, Hill DE, Barabási AL, Vidal M, Zoghbi HY (May 2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569.
• Takeya R, Ueno N, Kami K, Taura M, Kohjima M, Izaki T, Nunoi H, Sumimoto H (Jul 2003). "Novel human homologues of p47phox and p67phox participate in activation of superoxide-producing NADPH oxidases". The Journal of Biological Chemistry 278 (27): 25234–46. doi:10.1074/jbc.M212856200. PMID 12716910.
• Geiszt M, Lekstrom K, Witta J, Leto TL (May 2003). "Proteins homologous to p47phox and p67phox support superoxide production by NAD(P)H oxidase 1 in colon epithelial cells". The Journal of Biological Chemistry 278 (22): 20006–12. doi:10.1074/jbc.M301289200. PMID 12657628.
• Bánfi B, Clark RA, Steger K, Krause KH (Feb 2003). "Two novel proteins activate superoxide generation by the NADPH oxidase NOX1". The Journal of Biological Chemistry 278 (6): 3510–3. doi:10.1074/jbc.C200613200. PMID 12473664.