NOX5

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
Gene location (Human)
Chr.Chromosome 15 (human)[1]
Band15q23Start68,930,525 bp[1]
End69,062,762 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

79400

n/a

Ensembl

ENSG00000255346

n/a

UniProt

Q96PH1

n/a

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

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

  1. GRCh38: Ensembl release 89: ENSG00000255346 - Ensembl, May 2017
  2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. "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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