NDUFS1

NADH dehydrogenase (ubiquinone) Fe-S protein 1, 75kDa (NADH-coenzyme Q reductase)
Identifiers
Symbols	NDUFS1; CI-75Kd; CI-75k; MGC26839; PRO1304
External IDs	OMIM: 157655 MGI: 2443241 HomoloGene: 3670 GeneCards: NDUFS1 Gene
EC number	1.6.5.3
Gene Ontology Molecular function • NADH dehydrogenase activity • protein binding • NADH dehydrogenase (ubiquinone) activity • NADH dehydrogenase (ubiquinone) activity • electron carrier activity • metal ion binding • 2 iron, 2 sulfur cluster binding • 4 iron, 4 sulfur cluster binding Cellular component • mitochondrion • mitochondrial inner membrane • mitochondrial respiratory chain complex I • mitochondrial respiratory chain complex I • mitochondrial respiratory chain complex I • mitochondrial intermembrane space • membrane • respiratory chain Biological process • mitochondrial electron transport, NADH to ubiquinone • transport • apoptosis • respiratory electron transport chain • ATP synthesis coupled electron transport • cellular respiration • ATP metabolic process • regulation of mitochondrial membrane potential • reactive oxygen species metabolic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	4719	227197
Ensembl	ENSG00000023228	ENSMUSG00000025968
UniProt	P28331	Q3TIU7
RefSeq (mRNA)	NM_001199981.1	NM_145518
RefSeq (protein)	NP_001186910.1	NP_663493
Location (UCSC)	Chr 2: 206.99 – 207.02 Mb	Chr 1: 63.19 – 63.22 Mb
PubMed search	[1]	[2]

NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial is an enzyme that in humans is encoded by the NDUFS1 gene.^[1][2]

Function

The protein encoded by this gene belongs to the complex I 75 kDa subunit family. Mammalian complex I is composed of 45 different subunits. It locates at the mitochondrial inner membrane. This protein has NADH dehydrogenase activity and oxidoreductase activity. It transfers electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. This protein is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized.^[2]

Clinical significance

Mutations in this gene are associated with complex I deficiency.^[2]

References

1. ^ Chow W, Ragan I, Robinson BH (Nov 1991). "Determination of the cDNA sequence for the human mitochondrial 75-kDa Fe-S protein of NADH-coenzyme Q reductase". Eur J Biochem 201 (3): 547–50. doi:10.1111/j.1432-1033.1991.tb16313.x. PMID 1935949. 
2. ^ ^{a b c} "Entrez Gene: NDUFS1 NADH dehydrogenase (ubiquinone) Fe-S protein 1, 75kDa (NADH-coenzyme Q reductase)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4719. 

Further reading

• Duncan AM, Chow W, Robinson BH (1992). "Localization of the human 75-kDal Fe-S protein of NADH-coenzyme Q reductase gene (NDUFS1) to 2q33----q34.". Cytogenet. Cell Genet. 60 (3–4): 212–3. doi:10.1159/000133340. PMID 1505218. 
• Sumegi B, Srere PA (1985). "Complex I binds several mitochondrial NAD-coupled dehydrogenases". J. Biol. Chem. 259 (24): 15040–5. PMID 6439716. 
• Loeffen JL, Triepels RH, van den Heuvel LP, et al. (1999). "cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase: human complex I cDNA characterization completed". Biochem. Biophys. Res. Commun. 253 (2): 415–22. doi:10.1006/bbrc.1998.9786. PMID 9878551. 
• Bénit P, Chretien D, Kadhom N, et al. (2001). "Large-Scale Deletion and Point Mutations of the Nuclear NDUFV1 and NDUFS1 Genes in Mitochondrial Complex I Deficiency". Am. J. Hum. Genet. 68 (6): 1344–52. doi:10.1086/320603. PMC 1226121. PMID 11349233. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1226121. 
• 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. 
• Ricci JE, Muñoz-Pinedo C, Fitzgerald P, et al. (2004). "Disruption of mitochondrial function during apoptosis is mediated by caspase cleavage of the p75 subunit of complex I of the electron transport chain". Cell 117 (6): 773–86. doi:10.1016/j.cell.2004.05.008. PMID 15186778. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• Hillier LW, Graves TA, Fulton RS, et al. (2005). "Generation and annotation of the DNA sequences of human chromosomes 2 and 4". Nature 434 (7034): 724–31. doi:10.1038/nature03466. PMID 15815621. 
• Martín MA, Blázquez A, Gutierrez-Solana LG, et al. (2005). "Leigh syndrome associated with mitochondrial complex I deficiency due to a novel mutation in the NDUFS1 gene". Arch. Neurol. 62 (4): 659–61. doi:10.1001/archneur.62.4.659. PMID 15824269. 
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. 
• Iuso A, Scacco S, Piccoli C, et al. (2006). "Dysfunctions of cellular oxidative metabolism in patients with mutations in the NDUFS1 and NDUFS4 genes of complex I". J. Biol. Chem. 281 (15): 10374–80. doi:10.1074/jbc.M513387200. PMID 16478720. 
• Piccoli C, Scacco S, Bellomo F, et al. (2006). "cAMP controls oxygen metabolism in mammalian cells". FEBS Lett. 580 (18): 4539–43. doi:10.1016/j.febslet.2006.06.085. PMID 16870178.