NADPH oxidase, EF-hand calcium binding domain 5, also known as NOX5, is a protein which in humans is encoded by the NOX5 gene.[3][4]

NOX5
Identifiers
AliasesNOX5, NADPH oxidase 5
External IDsOMIM: 606572; HomoloGene: 41568; GeneCards: NOX5; OMA:NOX5 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001184779
NM_001184780
NM_024505

n/a

RefSeq (protein)

NP_001171708
NP_001171709
NP_078781

n/a

Location (UCSC)Chr 15: 68.93 – 69.06 Mbn/a
PubMed search[2]n/a
Wikidata
View/Edit Human

Function

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NOX5 is a novel NADPH oxidase that generates superoxide.[3]

Nox5 interacts with c-abl, superoxide production leads to phosphorylation of c-abl, while inhibition of c-abl kinase activity inhibits Nox5 superoxide production.[5]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000255346Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ a b "Entrez Gene: NOX5 NADPH oxidase, EF-hand calcium binding domain 5".
  4. ^ Bánfi B, Molnár G, Maturana A, Steger K, Hegedûs B, Demaurex N, Krause KH (October 2001). "A Ca(2+)-activated NADPH oxidase in testis, spleen, and lymph nodes". J. Biol. Chem. 276 (40): 37594–601. doi:10.1074/jbc.M103034200. PMID 11483596.
  5. ^ El Jamali A, Valente AJ, Lechleiter JD, Gamez MJ, Pearson DW, Nauseef WM, Clark RA (March 2008). "Novel redox-dependent regulation of NOX5 by the tyrosine kinase c-Abl". Free Radic. Biol. Med. 44 (5): 868–81. doi:10.1016/j.freeradbiomed.2007.11.020. PMC 2278123. PMID 18160052.

Further reading

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