NDOR1

NADPH dependent diflavin oxidoreductase 1
Identifiers
Symbols	NDOR1; MGC138148; NR1; bA350O14.9
External IDs	OMIM: 606073 MGI: 1926047 HomoloGene: 7144 GeneCards: NDOR1 Gene
EC number	1.6.-.-
Gene Ontology Molecular function • iron ion binding • protein binding • FMN binding • oxidoreductase activity • flavin adenine dinucleotide binding • NADP binding Cellular component • nucleus • cytoplasm • cytosol • intermediate filament cytoskeleton • perinuclear region of cytoplasm Biological process • cell death • oxidation-reduction process Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	27158	78797
Ensembl	ENSG00000188566	ENSMUSG00000006471
UniProt	Q9UHB4	n/a
RefSeq (mRNA)	NM_001144026.1	NM_001082476.1
RefSeq (protein)	NP_001137498.1	NP_001075945.1
Location (UCSC)	Chr 9: 140.1 – 140.11 Mb	Chr 2: 25.1 – 25.11 Mb
PubMed search	[1]	[2]

NADPH-dependent diflavin oxidoreductase 1 is an enzyme that in humans is encoded by the NDOR1 gene.^[1][2][3]

References

1. ^ Paine MJ, Garner AP, Powell D, Sibbald J, Sales M, Pratt N, Smith T, Tew DG, Wolf CR (Feb 2000). "Cloning and characterization of a novel human dual flavin reductase". J Biol Chem 275 (2): 1471–8. doi:10.1074/jbc.275.2.1471. PMID 10625700. 
2. ^ Finn RD, Basran J, Roitel O, Wolf CR, Munro AW, Paine MJ, Scrutton NS (Mar 2003). "Determination of the redox potentials and electron transfer properties of the FAD- and FMN-binding domains of the human oxidoreductase NR1". Eur J Biochem 270 (6): 1164–75. doi:10.1046/j.1432-1033.2003.03474.x. PMID 12631275. 
3. ^ "Entrez Gene: NDOR1 NADPH dependent diflavin oxidoreductase 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27158. 

Further reading

• Kwasnicka DA, Krakowiak A, Thacker C, et al. (2003). "Coordinate expression of NADPH-dependent flavin reductase, Fre-1, and Hint-related 7meGMP-directed hydrolase, DCS-1.". J. Biol. Chem. 278 (40): 39051–8. doi:10.1074/jbc.M306355200. PMC 2556063. PMID 12871939. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2556063. 
• Olteanu H, Banerjee R (2003). "Redundancy in the pathway for redox regulation of mammalian methionine synthase: reductive activation by the dual flavoprotein, novel reductase 1.". J. Biol. Chem. 278 (40): 38310–4. doi:10.1074/jbc.M306282200. PMID 12871938. 
• 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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
• Kornau HC, Schenker LT, Kennedy MB, Seeburg PH (1995). "Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95.". Science 269 (5231): 1737–40. doi:10.1126/science.7569905. PMID 7569905. 

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