NDUFS2

NADH dehydrogenase (ubiquinone) Fe-S protein 2, 49kDa (NADH-coenzyme Q reductase)
Identifiers
Symbols	NDUFS2;
External IDs	OMIM: 602985 MGI: 2385112 HomoloGene: 56659 GeneCards: NDUFS2 Gene
EC number	1.6.5.3
Gene Ontology Molecular function • NADH dehydrogenase activity • protein binding • NADH dehydrogenase (ubiquinone) activity • electron carrier activity • metal ion binding • quinone binding • NAD binding • 4 iron, 4 sulfur cluster binding Cellular component • mitochondrion • mitochondrion • mitochondrial inner membrane • mitochondrial respiratory chain complex I • mitochondrial respiratory chain complex I • mitochondrial respiratory chain complex I • membrane • respiratory chain Biological process • mitochondrial electron transport, NADH to ubiquinone • transport • response to oxidative stress • respiratory electron transport chain Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	4720	226646
Ensembl	ENSG00000158864	ENSMUSG00000013593
UniProt	O75306	Q3U5Y9
RefSeq (mRNA)	NM_001166159.1	NM_153064.4
RefSeq (protein)	NP_001159631.1	NP_694704.1
Location (UCSC)	Chr 1: 161.17 – 161.18 Mb	Chr 1: 173.16 – 173.18 Mb
PubMed search	[1]	[2]

NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial also known as NADH-ubiquinone oxidoreductase 49 kDa subunit is an enzyme that in humans is encoded by the NDUFS2 gene.^[1][2][3]

Function

Mitochondrial complex I is the first multimeric complex of the respiratory chain that catalyzes the NADH oxidation with concomitant ubiquinone reduction and proton ejection out of the mitochondria. Mammalian mitochondrial complex I is an assembly of at least 43 different subunits. Seven of the subunits are encoded by the mitochondrial genome; the remainder are the products of nuclear genes. The iron-sulfur protein (IP) fraction of complex I is made up of 7 subunits, including NDUFS2.^[3]

See also

• NDUFS1

References

1. ^ Fearnley IM, Finel M, Skehel JM, Walker JE (Oct 1991). "NADH:ubiquinone oxidoreductase from bovine heart mitochondria. cDNA sequences of the import precursors of the nuclear-encoded 39 kDa and 42 kDa subunits". Biochem J. 278 ( Pt 3): 821–9. PMC 1151420. PMID 1832859. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1151420. 
2. ^ Procaccio V, de Sury R, Martinez P, Depetris D, Rabilloud T, Soularue P, Lunardi J, Issartel J (Jun 1998). "Mapping to 1q23 of the human gene (NDUFS2) encoding the 49-kDa subunit of the mitochondrial respiratory Complex I and immunodetection of the mature protein in mitochondria". Mamm Genome 9 (6): 482–4. doi:10.1007/s003359900803. PMID 9585441. 
3. ^ ^{a b} "Entrez Gene: NDUFS2 NADH dehydrogenase (ubiquinone) Fe-S protein 2, 49kDa (NADH-coenzyme Q reductase)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4720. 

Further reading

• 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. 
• 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. 
• Loeffen J, van den Heuvel L, Smeets R, et al. (1998). "cDNA sequence and chromosomal localization of the remaining three human nuclear encoded iron sulphur protein (IP) subunits of complex I: the human IP fraction is completed.". Biochem. Biophys. Res. Commun. 247 (3): 751–8. doi:10.1006/bbrc.1998.8882. PMID 9647766. 
• 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. 
• Triepels RH, Hanson BJ, van den Heuvel LP, et al. (2001). "Human complex I defects can be resolved by monoclonal antibody analysis into distinct subunit assembly patterns.". J. Biol. Chem. 276 (12): 8892–7. doi:10.1074/jbc.M009903200. PMID 11112787. 
• Loeffen J, Elpeleg O, Smeitink J, et al. (2001). "Mutations in the complex I NDUFS2 gene of patients with cardiomyopathy and encephalomyopathy.". Ann. Neurol. 49 (2): 195–201. doi:10.1002/1531-8249(20010201)49:2<195::AID-ANA39>3.0.CO;2-M. PMID 11220739. 
• 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. 
• Murray J, Taylor SW, Zhang B, et al. (2003). "Oxidative damage to mitochondrial complex I due to peroxynitrite: identification of reactive tyrosines by mass spectrometry.". J. Biol. Chem. 278 (39): 37223–30. doi:10.1074/jbc.M305694200. PMID 12857734. 
• Ugalde C, Janssen RJ, van den Heuvel LP, et al. (2004). "Differences in assembly or stability of complex I and other mitochondrial OXPHOS complexes in inherited complex I deficiency.". Hum. Mol. Genet. 13 (6): 659–67. doi:10.1093/hmg/ddh071. PMID 14749350. 
• Bourges I, Ramus C, Mousson de Camaret B, et al. (2005). "Structural organization of mitochondrial human complex I: role of the ND4 and ND5 mitochondria-encoded subunits and interaction with prohibitin.". Biochem. J. 383 (Pt. 3): 491–9. doi:10.1042/BJ20040256. PMC 1133742. PMID 15250827. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1133742. 
• 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. 
• Ma J, Dempsey AA, Stamatiou D, et al. (2007). "Identifying leukocyte gene expression patterns associated with plasma lipid levels in human subjects.". Atherosclerosis 191 (1): 63–72. doi:10.1016/j.atherosclerosis.2006.05.032. PMID 16806233. 
• Vogel RO, Dieteren CE, van den Heuvel LP, et al. (2007). "Identification of mitochondrial complex I assembly intermediates by tracing tagged NDUFS3 demonstrates the entry point of mitochondrial subunits.". J. Biol. Chem. 282 (10): 7582–90. doi:10.1074/jbc.M609410200. PMID 17209039.