NDOR1

NADPH-dependent diflavin oxidoreductase 1 is an enzyme that in humans is encoded by the NDOR1 gene.[4][5][6]

NDOR1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4H2D
Identifiers
Aliases	NDOR1, NR1, bA350O14.9, NADPH dependent diflavin oxidoreductase 1, CIAE1
External IDs	OMIM: 606073 MGI: 1926047 HomoloGene: 7144 GeneCards: NDOR1
Gene location (Human) Chr. Chromosome 9 (human)[1] Band 9q34.3 Start 137,205,685 bp[1] End 137,217,009 bp[1]
Gene ontology Molecular function • oxidoreductase activity • FMN binding • NADPH-hemoprotein reductase activity • GO:0001948 protein binding • flavin adenine dinucleotide binding • NADP binding • oxidoreductase activity, acting on NAD(P)H Cellular component • cytoplasm • perinuclear region of cytoplasm • cytosol • intermediate filament cytoskeleton • cell nucleus Biological process • cell death • cellular response to menadione • oxidation-reduction process • iron-sulfur cluster assembly Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	27158	78797
Ensembl	ENSG00000188566	n/a
UniProt	Q9UHB4	A2AI05
RefSeq (mRNA)	NM_001144026 NM_001144027 NM_001144028 NM_014434	NM_001082476 NM_001252541 NM_001252542 NM_178239
RefSeq (protein)	NP_001137498 NP_001137499 NP_001137500 NP_055249	NP_001075945 NP_001239470 NP_001239471
Location (UCSC)	Chr 9: 137.21 – 137.22 Mb	n/a
PubMed search	[2]	[3]
Wikidata
View/Edit Human View/Edit Mouse

References

1. GRCh38: Ensembl release 89: ENSG00000188566 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. 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.
5. 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.
6. "Entrez Gene: NDOR1 NADPH dependent diflavin oxidoreductase 1".

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.
• 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• 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. Bibcode:1995Sci...269.1737K. doi:10.1126/science.7569905. PMID 7569905.