NOXO1

Protein-coding gene in the species Homo sapiens

NOXO1

| Available structures

PDB| Ortholog search: PDBe RCSB
| List of PDB id codes

2L73

Identifiers
Aliases| NOXO1, P41NOX, P41NOXA, P41NOXB, P41NOXC, SH3PXD5, SNX28, NADPH oxidase organizer 1
External IDs| OMIM: 611256 MGI: 1919143 HomoloGene: 12418 GeneCards: NOXO1
| Gene location (Human)

Chr.| Chromosome 16 (human)[1]

Band| 16p13.3| Start| 1,978,917 bp[1]
End| 1,984,192 bp[1]
| Gene location (Mouse)

Chr.| Chromosome 17 (mouse)[2]

Band| 17 A3.3|17 12.49 cM| Start| 24,915,208 bp[2]
End| 24,919,503 bp[2]
| RNA expression pattern

Bgee| | Human| Mouse (ortholog)

|

| Top expressed in

* rectum

* appendix

* right lobe of liver

* ganglionic eminence

* putamen

* nucleus accumbens

* salivary gland

* duodenum

* minor salivary gland

* caudate nucleus

| Top expressed in

* Paneth cell

* crypt of lieberkuhn of small intestine

* spermatocyte

* large intestine

* colon

* left colon

* ileum

* spermatid

* jejunum

* intestinal villus

More reference expression data
BioGPS| | n/a

| Gene ontology

Molecular function|

* enzyme binding
* superoxide-generating NADPH oxidase activator activity
* protein binding
* phospholipid binding
* identical protein binding
* lipid binding
* phosphatidylinositol binding

Cellular component|

* plasma membrane
* NADPH oxidase complex
* membrane
* intracellular anatomical structure

Biological process|

* regulation of respiratory burst
* extracellular matrix disassembly
* positive regulation of catalytic activity
* regulation of hydrogen peroxide metabolic process
* superoxide metabolic process

Sources:Amigo / QuickGO
| Orthologs

Species| Human| Mouse
Entrez| |

124056

71893

Ensembl| |

ENSG00000196408

ENSMUSG00000019320

UniProt| |

Q8NFA2

Q8VCM2

RefSeq (mRNA)| |

NM_001267721
NM_144603
NM_172167
NM_172168

NM_027988
NM_001357836

RefSeq (protein)| |

NP_001254650
NP_653204
NP_751907
NP_751908

NP_082264
NP_001344765

Location (UCSC)| Chr 16: 1.98 – 1.98 Mb| Chr 17: 24.92 – 24.92 Mb
PubMed search| [3]| [4]
Wikidata
| View/Edit Human| View/Edit Mouse

|

NADPH oxidase organizer 1 is an enzyme that in humans is encoded by the NOXO1 gene.[5]

## References[edit]

1. ^ a b c GRCh38: Ensembl release 89: ENSG00000196408 \- Ensembl, May 2017
2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000019320 \- 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. ^ "Entrez Gene: NOXO1 NADPH oxidase organizer 1".

## Further reading[edit]

* Bánfi B, Clark RA, Steger K, Krause KH (2003). "Two novel proteins activate superoxide generation by the NADPH oxidase NOX1". J. Biol. Chem. 278 (6): 3510–3. doi:10.1074/jbc.C200613200. PMID 12473664.
* Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
* Geiszt M, Lekstrom K, Witta J, Leto TL (2003). "Proteins homologous to p47phox and p67phox support superoxide production by NAD(P)H oxidase 1 in colon epithelial cells". J. Biol. Chem. 278 (22): 20006–12. doi:10.1074/jbc.M301289200. PMID 12657628.
* Takeya R, Ueno N, Kami K, et al. (2003). "Novel human homologues of p47phox and p67phox participate in activation of superoxide-producing NADPH oxidases". J. Biol. Chem. 278 (27): 25234–46. doi:10.1074/jbc.M212856200. PMID 12716910.
* Cheng G, Lambeth JD (2004). "NOXO1, regulation of lipid binding, localization, and activation of Nox1 by the Phox homology (PX) domain". J. Biol. Chem. 279 (6): 4737–42. doi:10.1074/jbc.M305968200. PMID 14617635.
* Cheng G, Ritsick D, Lambeth JD (2004). "Nox3 regulation by NOXO1, p47phox, and p67phox". J. Biol. Chem. 279 (33): 34250–5. doi:10.1074/jbc.M400660200. PMID 15181005.
* Bánfi B, Malgrange B, Knisz J, et al. (2004). "NOX3, a superoxide-generating NADPH oxidase of the inner ear". J. Biol. Chem. 279 (44): 46065–72. doi:10.1074/jbc.M403046200. PMID 15326186.
* Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
* Ueno N, Takeya R, Miyano K, et al. (2005). "The NADPH oxidase Nox3 constitutively produces superoxide in a p22phox-dependent manner: its regulation by oxidase organizers and activators". J. Biol. Chem. 280 (24): 23328–39. doi:10.1074/jbc.M414548200. PMID 15824103.
* Cheng G, Lambeth JD (2005). "Alternative mRNA splice forms of NOXO1: differential tissue expression and regulation of Nox1 and Nox3". Gene. 356: 118–26. doi:10.1016/j.gene.2005.03.008. PMID 15949904.
* Park HS, Park D, Bae YS (2006). "Molecular interaction of NADPH oxidase 1 with betaPix and Nox Organizer 1". Biochem. Biophys. Res. Commun. 339 (3): 985–90. doi:10.1016/j.bbrc.2005.11.108. PMID 16329988.
* Takeya R, Taura M, Yamasaki T, et al. (2006). "Expression and function of Noxo1gamma, an alternative splicing form of the NADPH oxidase organizer 1". FEBS J. 273 (16): 3663–77. doi:10.1111/j.1742-4658.2006.05371.x. PMID 16911517. S2CID 701568.
* Yamamoto A, Kami K, Takeya R, Sumimoto H (2007). "Interaction between the SH3 domains and C-terminal proline-rich region in NADPH oxidase organizer 1 (Noxo1)". Biochem. Biophys. Res. Commun. 352 (2): 560–5. doi:10.1016/j.bbrc.2006.11.060. PMID 17126813.

## External links[edit]

* PDBe-KB provides an overview of all the structure information available in the PDB for Human NADPH oxidase organizer 1

* v
* t
* e

Sorting nexins

SNX-BAR|

* SNX1
* SNX2
* SNX4
* SNX5
* SNX6
* SNX7
* SNX8
* SNX9
* SNX18
* SNX30
* SNX32
* SNX33

SNX-PX|

* SNX3
* SNX10
* SNX11
* SNX12
* SNX16
* SNX20
* SNX21
* SNX22
* SNX24
* SNX29

SNX-Other|

* SNX13
* SNX14
* SNX15
* SNX17
* SNX19
* SNX23
* SNX25
* SNX26
* SNX27
* SNX28
* SNX31

Related articles|

* PX domain
* BAR domain
* Retromer

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