NOXA1

NOXA1
Identifiers
Aliases	NOXA1 , NY-CO-31, SDCCAG31, p51NOX, NADPH oxidase activator 1
External IDs	OMIM: 611255; MGI: 2449980; HomoloGene: 18156; GeneCards: NOXA1; OMA:NOXA1 - orthologs
Gene location (Human) Chr. Chromosome 9 (human) [1] Band 9q34.3 Start 137,423,350 bp [1] End 137,434,406 bp [1]
Gene location (Mouse) Chr. Chromosome 2 (mouse) [2] Band 2|2 A3 Start 24,975,679 bp [2] End 24,985,161 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in pancreatic ductal cell mucosa of transverse colon right uterine tube right frontal lobe anterior pituitary Brodmann area 9 nucleus accumbens body of pancreas right hemisphere of cerebellum cingulate gyrus Top expressed in ileum colon duodenum jejunum stomach embryo embryo uterus lung liver More reference expression data BioGPS n/a
Gene ontology Molecular function SH3 domain binding enzyme binding superoxide-generating NADPH oxidase activator activity protein binding Cellular component cytoplasm cytosol plasma membrane membrane NADPH oxidase complex Biological process regulation of respiratory burst superoxide metabolic process regulation of hydrogen peroxide metabolic process positive regulation of catalytic activity superoxide anion generation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10811 241275 Ensembl ENSG00000188747 ENSMUSG00000036805 UniProt Q86UR1 Q8CJ00 RefSeq (mRNA) NM_001256067 NM_001256068 NM_006647 NM_001163626 NM_172204 RefSeq (protein) NP_001242996 NP_001242997 NP_006638 NP_001157098 NP_757341 Location (UCSC) Chr 9: 137.42 – 137.43 Mb Chr 2: 24.98 – 24.99 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

NADPH oxidase activator 1 is an enzyme that in humans is encoded by the NOXA1 gene. ^{[5] [6]}

References

1. GRCh38: Ensembl release 89: ENSG00000188747 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000036805 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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. 76 (5): 652–8. doi: 10.1002/(SICI)1097-0215(19980529)76:5<652::AID-IJC7>3.0.CO;2-P . PMID   9610721.
6. "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. S2CID   13709685.
• 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.