NOXA1

NADPH oxidase activator 1

Identifiers

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	• cytoplasm • NADPH oxidase complex
Biological process	• superoxide metabolic process • regulation of hydrogen peroxide metabolic process • positive regulation of catalytic activity • regulation of respiratory burst
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

ENSG00000188747

ENSMUSG00000036805

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 9:
140.32 – 140.33 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

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

Further reading

Opitz N, Drummond GR, Selemidis S et al. (2007). "The 'A's and 'O's of NADPH oxidase regulation: a commentary on "Subcellular localization and function of alternatively spliced Noxo1 isoforms".". Free Radic. Biol. Med. 42 (2): 175–9. doi:10.1016/j.freeradbiomed.2006.11.003. PMID 17189823.
Kim JS, Diebold BA, Babior BM et al. (2008). "Regulation of Nox1 activity via protein kinase A-mediated phosphorylation of NoxA1 and 14-3-3 binding.". J. Biol. Chem. 282 (48): 34787–800. doi:10.1074/jbc.M704754200. PMID 17913709.
Valente AJ, El Jamali A, Epperson TK et al. (2007). "NOX1 NADPH oxidase regulation by the NOXA1 SH3 domain.". Free Radic. Biol. Med. 43 (3): 384–96. doi:10.1016/j.freeradbiomed.2007.04.022. PMID 17602954.
Lim J, Hao T, Shaw C et al. (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.
Ota T, Suzuki Y, Nishikawa T et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
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.
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.
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.
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.