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{{Underlinked|date=June 2016}}
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{{Infobox_gene}}
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'''NADPH oxidase organizer 1''' is an [[enzyme]] that in humans is encoded by the ''NOXO1'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NOXO1 NADPH oxidase organizer 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=124056| accessdate = }}</ref>
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{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = NADPH oxidase organizer 1
| HGNCid = 19404
| Symbol = NOXO1
| AltSymbols =; MGC20258; P41NOX; P41NOXA; P41NOXB; P41NOXC; SH3PXD5
| OMIM = 
| ECnumber = 
| Homologene = 12418
| MGIid = 1919143
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008289 |text = lipid binding}} {{GNF_GO|id=GO:0016176 |text = superoxide-generating NADPH oxidase activator activity}} {{GNF_GO|id=GO:0035091 |text = phosphoinositide binding}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006801 |text = superoxide metabolic process}} {{GNF_GO|id=GO:0007154 |text = cell communication}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 124056
    | Hs_Ensembl = ENSG00000196408
    | Hs_RefseqProtein = NP_653204
    | Hs_RefseqmRNA = NM_144603
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 16
    | Hs_GenLoc_start = 1968920
    | Hs_GenLoc_end = 1971441
    | Hs_Uniprot = Q8NFA2
    | Mm_EntrezGene = 71893
    | Mm_Ensembl = ENSMUSG00000019320
    | Mm_RefseqmRNA = NM_027988
    | Mm_RefseqProtein = NP_082264
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 17
    | Mm_GenLoc_start = 24423874
    | Mm_GenLoc_end = 24428127
    | Mm_Uniprot = Q0VDT6
  }}
}}
'''NADPH oxidase organizer 1''', also known as '''NOXO1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NOXO1 NADPH oxidase organizer 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=124056| accessdate = }}</ref>


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==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Bánfi B, Clark RA, Steger K, Krause KH |title=Two novel proteins activate superoxide generation by the NADPH oxidase NOX1. |journal=J. Biol. Chem. |volume=278 |issue= 6 |pages= 3510-3 |year= 2003 |pmid= 12473664 |doi= 10.1074/jbc.C200613200 }}
*{{cite journal  | vauthors=Bánfi B, Clark RA, Steger K, Krause KH |title=Two novel proteins activate superoxide generation by the NADPH oxidase NOX1. |journal=J. Biol. Chem. |volume=278 |issue= 6 |pages= 3510–3 |year= 2003 |pmid= 12473664 |doi= 10.1074/jbc.C200613200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
*{{cite journal  | author=Geiszt M, Lekstrom K, Witta J, Leto TL |title=Proteins homologous to p47phox and p67phox support superoxide production by NAD(P)H oxidase 1 in colon epithelial cells. |journal=J. Biol. Chem. |volume=278 |issue= 22 |pages= 20006-12 |year= 2003 |pmid= 12657628 |doi= 10.1074/jbc.M301289200 }}
*{{cite journal  | vauthors=Geiszt M, Lekstrom K, Witta J, Leto TL |title=Proteins homologous to p47phox and p67phox support superoxide production by NAD(P)H oxidase 1 in colon epithelial cells. |journal=J. Biol. Chem. |volume=278 |issue= 22 |pages= 20006–12 |year= 2003 |pmid= 12657628 |doi= 10.1074/jbc.M301289200 }}
*{{cite journal | author=Takeya R, Ueno N, Kami K, ''et al.'' |title=Novel human homologues of p47phox and p67phox participate in activation of superoxide-producing NADPH oxidases. |journal=J. Biol. Chem. |volume=278 |issue= 27 |pages= 25234-46 |year= 2003 |pmid= 12716910 |doi= 10.1074/jbc.M212856200 }}
*{{cite journal   |vauthors=Takeya R, Ueno N, Kami K, etal |title=Novel human homologues of p47phox and p67phox participate in activation of superoxide-producing NADPH oxidases. |journal=J. Biol. Chem. |volume=278 |issue= 27 |pages= 25234–46 |year= 2003 |pmid= 12716910 |doi= 10.1074/jbc.M212856200 }}
*{{cite journal  | author=Cheng G, Lambeth JD |title=NOXO1, regulation of lipid binding, localization, and activation of Nox1 by the Phox homology (PX) domain. |journal=J. Biol. Chem. |volume=279 |issue= 6 |pages= 4737-42 |year= 2004 |pmid= 14617635 |doi= 10.1074/jbc.M305968200 }}
*{{cite journal  | vauthors=Cheng G, Lambeth JD |title=NOXO1, regulation of lipid binding, localization, and activation of Nox1 by the Phox homology (PX) domain. |journal=J. Biol. Chem. |volume=279 |issue= 6 |pages= 4737–42 |year= 2004 |pmid= 14617635 |doi= 10.1074/jbc.M305968200 }}
*{{cite journal  | author=Cheng G, Ritsick D, Lambeth JD |title=Nox3 regulation by NOXO1, p47phox, and p67phox. |journal=J. Biol. Chem. |volume=279 |issue= 33 |pages= 34250-5 |year= 2004 |pmid= 15181005 |doi= 10.1074/jbc.M400660200 }}
*{{cite journal  | vauthors=Cheng G, Ritsick D, Lambeth JD |title=Nox3 regulation by NOXO1, p47phox, and p67phox. |journal=J. Biol. Chem. |volume=279 |issue= 33 |pages= 34250–5 |year= 2004 |pmid= 15181005 |doi= 10.1074/jbc.M400660200 }}
*{{cite journal | author=Bánfi B, Malgrange B, Knisz J, ''et al.'' |title=NOX3, a superoxide-generating NADPH oxidase of the inner ear. |journal=J. Biol. Chem. |volume=279 |issue= 44 |pages= 46065-72 |year= 2004 |pmid= 15326186 |doi= 10.1074/jbc.M403046200 }}
*{{cite journal   |vauthors=Bánfi B, Malgrange B, Knisz J, etal |title=NOX3, a superoxide-generating NADPH oxidase of the inner ear. |journal=J. Biol. Chem. |volume=279 |issue= 44 |pages= 46065–72 |year= 2004 |pmid= 15326186 |doi= 10.1074/jbc.M403046200 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
*{{cite journal | author=Ueno N, Takeya R, Miyano K, ''et al.'' |title=The NADPH oxidase Nox3 constitutively produces superoxide in a p22phox-dependent manner: its regulation by oxidase organizers and activators. |journal=J. Biol. Chem. |volume=280 |issue= 24 |pages= 23328-39 |year= 2005 |pmid= 15824103 |doi= 10.1074/jbc.M414548200 }}
*{{cite journal   |vauthors=Ueno N, Takeya R, Miyano K, etal |title=The NADPH oxidase Nox3 constitutively produces superoxide in a p22phox-dependent manner: its regulation by oxidase organizers and activators. |journal=J. Biol. Chem. |volume=280 |issue= 24 |pages= 23328–39 |year= 2005 |pmid= 15824103 |doi= 10.1074/jbc.M414548200 }}
*{{cite journal  | author=Cheng G, Lambeth JD |title=Alternative mRNA splice forms of NOXO1: differential tissue expression and regulation of Nox1 and Nox3. |journal=Gene |volume=356 |issue=  |pages= 118-26 |year= 2005 |pmid= 15949904 |doi= 10.1016/j.gene.2005.03.008 }}
*{{cite journal  | vauthors=Cheng G, Lambeth JD |title=Alternative mRNA splice forms of NOXO1: differential tissue expression and regulation of Nox1 and Nox3. |journal=Gene |volume=356 |issue=  |pages= 118–26 |year= 2005 |pmid= 15949904 |doi= 10.1016/j.gene.2005.03.008 }}
*{{cite journal  | author=Park HS, Park D, Bae YS |title=Molecular interaction of NADPH oxidase 1 with betaPix and Nox Organizer 1. |journal=Biochem. Biophys. Res. Commun. |volume=339 |issue= 3 |pages= 985-90 |year= 2006 |pmid= 16329988 |doi= 10.1016/j.bbrc.2005.11.108 }}
*{{cite journal  | vauthors=Park HS, Park D, Bae YS |title=Molecular interaction of NADPH oxidase 1 with betaPix and Nox Organizer 1. |journal=Biochem. Biophys. Res. Commun. |volume=339 |issue= 3 |pages= 985–90 |year= 2006 |pmid= 16329988 |doi= 10.1016/j.bbrc.2005.11.108 }}
*{{cite journal | author=Takeya R, Taura M, Yamasaki T, ''et al.'' |title=Expression and function of Noxo1gamma, an alternative splicing form of the NADPH oxidase organizer 1. |journal=FEBS J. |volume=273 |issue= 16 |pages= 3663-77 |year= 2006 |pmid= 16911517 |doi= 10.1111/j.1742-4658.2006.05371.x }}
*{{cite journal   |vauthors=Takeya R, Taura M, Yamasaki T, etal |title=Expression and function of Noxo1gamma, an alternative splicing form of the NADPH oxidase organizer 1. |journal=FEBS J. |volume=273 |issue= 16 |pages= 3663–77 |year= 2006 |pmid= 16911517 |doi= 10.1111/j.1742-4658.2006.05371.x }}
*{{cite journal  | author=Yamamoto A, Kami K, Takeya R, Sumimoto H |title=Interaction between the SH3 domains and C-terminal proline-rich region in NADPH oxidase organizer 1 (Noxo1). |journal=Biochem. Biophys. Res. Commun. |volume=352 |issue= 2 |pages= 560-5 |year= 2007 |pmid= 17126813 |doi= 10.1016/j.bbrc.2006.11.060 }}
*{{cite journal  | vauthors=Yamamoto A, Kami K, Takeya R, Sumimoto H |title=Interaction between the SH3 domains and C-terminal proline-rich region in NADPH oxidase organizer 1 (Noxo1). |journal=Biochem. Biophys. Res. Commun. |volume=352 |issue= 2 |pages= 560–5 |year= 2007 |pmid= 17126813 |doi= 10.1016/j.bbrc.2006.11.060 }}
}}
}}
{{refend}}
{{refend}}


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Latest revision as of 13:11, 5 September 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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


References

  1. ↑ "Entrez Gene: NOXO1 NADPH oxidase organizer 1".

Further reading



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