NOXA1

NOXA1
Identifiers
Aliases	NOXA1 , NY-CO-31, SDCCAG31, p51NOX, NADPH oxidase activator 1
External IDs	OMIM: 611255 MGI: 2449980 HomoloGene: 18156 GeneCards: NOXA1
Gene location (Human)
Chr.	Chromosome 9 (human)
End	137,434,406 bp
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)
End	25,095,149 bp
Gene ontology
Molecular function	• SH3 domain binding ; • enzyme binding ; • superoxide-generating NADPH oxidase activator activity ; • GO:0001948 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 ; • GO:0048554 positive regulation of catalytic activity ; • superoxide anion generation ;
	Sources:Amigo / QuickGO
Orthologs
	10811
	241275
	ENSG00000188747
	ENSMUSG00000036805
	Q86UR1
	Q8CJ00
	NM_001256067 ; NM_001256068 ; NM_006647
	NM_001163626 ; NM_172204
	NP_001242996 ; NP_001242997 ; NP_006638
	NP_001157098 ; NP_757341
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated July 06, 2021

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

Related Research Articles

Respiratory burst is the rapid release of the reactive oxygen species (ROS), superoxide anion and hydrogen peroxide, from different cell types.

NADPH oxidase is a membrane-bound enzyme complex that faces the extracellular space. It can be found in the plasma membrane as well as in the membranes of phagosomes used by neutrophil white blood cells to engulf microorganisms. Human isoforms of the catalytic component of the complex include NOX1, NOX2, NOX3, NOX4, NOX5, DUOX1, and DUOX2.

NADPH oxidase 2 (Nox2), also known as cytochrome b(558) subunit beta or Cytochrome b-245 heavy chain, is a protein that in humans is encoded by the NOX2 gene. The protein is a super-oxide generating enzyme which forms reactive oxygen species (ROS).

Neutrophil cytosol factor 2 is a protein that in humans is encoded by the NCF2 gene.

Neutrophil cytosol factor 1, also known as p47phox, is a protein that in humans is encoded by the NCF1 gene.

Nucleotide-binding oligomerization domain-containing protein 1 (NOD1) is a protein receptor that in humans is encoded by the NOD1 gene. It recognizes bacterial molecules and stimulates an immune reaction.

NADPH oxidase 1 is an enzyme that in humans is encoded by the NOX1 gene.

NADPH oxidase 4 is an enzyme that in humans is encoded by the NOX4 gene, and is a member of the NOX family of NADPH oxidases.

Cytochrome b-245 light chain is a protein that in humans is encoded by the CYBA gene involved in superoxide production and phagocytosis.

Rac2 is a small signaling G protein, and is a member of the Rac subfamily of the family Rho family of GTPases. It is encoded by the gene RAC2.

Neutrophil cytosol factor 4 is a protein that in humans is encoded by the NCF4 gene.

Peroxiredoxin-6 is a protein that in humans is encoded by the PRDX6 gene. It is a member of the peroxiredoxin family of antioxidant enzymes.

Dual specificity mitogen-activated protein kinase kinase 5 is an enzyme that in humans is encoded by the MAP2K5 gene.

Dual oxidase 2, also known as DUOX2 or ThOX2, is an enzyme that in humans is encoded by the DUOX2 gene. Dual oxidase is an enzyme that was first identified in the mammalian thyroid gland. In humans, two isoforms are found; hDUOX1 and hDUOX2. The protein location is not exclusive to thyroid tissue; hDUOX1 is prominent in airway epithelial cells and hDUOX2 in the salivary glands and gastrointestinal tract.

Dual oxidase 1, also known as DUOX1 or ThOX1, is an enzyme which in humans is encoded by the DUOX1 gene. DUOX1 was first identified in the mammalian thyroid gland. In humans, two isoforms are found; hDUOX1 and hDUOX2. Human DUOX protein localization is not exclusive to thyroid tissue; hDUOX1 is prominent in airway epithelial cells and hDUOX2 in the salivary glands and gastrointestinal tract.

NADPH oxidase, EF-hand calcium binding domain 5, also known as NOX5, is a protein which in humans is encoded by the NOX5 gene.

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

Synaptotagmin-like protein 1 is a protein that in humans is encoded by the SYTL1 gene.

NADPH oxidase 3 is an enzyme that in humans is encoded by the NOX3 gene.

Edgar Pick is an Israeli immunologist who is Professor Emeritus of Immunology in the Department of Clinical Microbiology and Immunology at the Sackler Faculty of Medicine at Tel Aviv University, Israel.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000188747 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000036805 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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.
↑ "Entrez Gene: NOXA1 NADPH oxidase activator 1".

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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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000188747 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 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.

[pmid9610721-5] 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.

[entrez-6] "Entrez Gene: NOXA1 NADPH oxidase activator 1".

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NOXA1

Related Research Articles

References

Further reading