NOXA1

Protein-coding gene in the species Homo sapiens
NOXA1
Identifiers
AliasesNOXA1, NY-CO-31, SDCCAG31, p51NOX, NADPH oxidase activator 1
External IDsOMIM: 611255; MGI: 2449980; HomoloGene: 18156; GeneCards: NOXA1; OMA:NOXA1 - orthologs
Gene location (Human)
Chromosome 9 (human)
Chr.Chromosome 9 (human)[1]
Chromosome 9 (human)
Genomic location for NOXA1
Genomic location for NOXA1
Band9q34.3Start137,423,350 bp[1]
End137,434,406 bp[1]
Gene location (Mouse)
Chromosome 2 (mouse)
Chr.Chromosome 2 (mouse)[2]
Chromosome 2 (mouse)
Genomic location for NOXA1
Genomic location for NOXA1
Band2|2 A3Start24,975,679 bp[2]
End24,985,161 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
SpeciesHumanMouse
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 MbChr 2: 24.98 – 24.99 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000188747 – Ensembl, May 2017
  2. ^ a b c 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.


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