NDUFS2

From Wikipedia, the free encyclopedia

NADH dehydrogenase (ubiquinone) Fe-S protein 2, 49kDa (NADH-coenzyme Q reductase)

Identifiers

External IDs

OMIM: 602985 MGI: 2385112 HomoloGene: 56659

Gene ontology
Molecular Function:	• NADH dehydrogenase activity • iron ion binding • NADH dehydrogenase (ubiquinone) activity • metal ion binding • NAD binding • 4 iron, 4 sulfur cluster binding
Cellular Component:	• membrane fraction • mitochondrion
Biological Process:	• mitochondrial electron transport, NADH to ubiquinone

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_004550 (mRNA)
NP_004541 (protein)

NM_153064 (mRNA)
NP_694704 (protein)

Location

Chr 1: 159.44 - 159.45 Mb

Chr 1: 173.07 - 173.08 Mb

Pubmed search

[1]

[2]

NADH dehydrogenase (ubiquinone) Fe-S protein 2, 49kDa (NADH-coenzyme Q reductase), also known as NDUFS2, is a human gene.^[1]

Mitochondrial complex I (NADH-ubiquinone reductase; EC 1.6.5.3) 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. See NDUFS1 (MIM 157655).[supplied by OMIM]^[1]

[edit] References

^ ^a ^b Entrez Gene: NDUFS2 NADH dehydrogenase (ubiquinone) Fe-S protein 2, 49kDa (NADH-coenzyme Q reductase).

[edit] Further reading

Fearnley IM, Finel M, Skehel JM, Walker JE (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. PMID 1832859.
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. 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. PMID 9373149.
Procaccio V, de Sury R, Martinez P, et al. (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. PMID 9585441.
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. 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. PMID 12477932.
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. PMID 15250827.
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. PMID 15489334.
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.