SCO1

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SCO cytochrome oxidase deficient homolog 1 (yeast)
File:PBB Protein SCO1 image.jpg
PDB rendering based on 1wp0.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols SCO1 ; SCOD1
External IDs Template:OMIM5 Template:MGI HomoloGene3374
RNA expression pattern
File:PBB GE SCO1 gnf1h00058 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

SCO cytochrome oxidase deficient homolog 1 (yeast), also known as SCO1, is a human gene.[1]

Mammalian cytochrome c oxidase (COX) catalyzes the transfer of reducing equivalents from cytochrome c to molecular oxygen and pumps protons across the inner mitochondrial membrane. In yeast, 2 related COX assembly genes, SCO1 and SCO2 (synthesis of cytochrome c oxidase), enable subunits 1 and 2 to be incorporated into the holoprotein. This gene is the human homolog to the yeast SCO1 gene.[1]

References

  1. 1.0 1.1 "Entrez Gene: SCO1 SCO cytochrome oxidase deficient homolog 1 (yeast)".

Further reading

  • Shoubridge EA (2001). "Cytochrome c oxidase deficiency". Am. J. Med. Genet. 106 (1): 46–52. doi:10.1002/ajmg.1378. PMID 11579424.
  • Schulze M, Rödel G (1989). "Accumulation of the cytochrome c oxidase subunits I and II in yeast requires a mitochondrial membrane-associated protein, encoded by the nuclear SCO1 gene". Mol. Gen. Genet. 216 (1): 37–43. PMID 2543907.
  • Schulze M, Rödel G (1988). "SCO1, a yeast nuclear gene essential for accumulation of mitochondrial cytochrome c oxidase subunit II". Mol. Gen. Genet. 211 (3): 492–8. PMID 2835635.
  • Andersson B, Wentland MA, Ricafrente JY; et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
  • Yu W, Andersson B, Worley KC; et al. (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. PMID 9110174.
  • Petruzzella V, Tiranti V, Fernandez P; et al. (1999). "Identification and characterization of human cDNAs specific to BCS1, PET112, SCO1, COX15, and COX11, five genes involved in the formation and function of the mitochondrial respiratory chain". Genomics. 54 (3): 494–504. doi:10.1006/geno.1998.5580. PMID 9878253.
  • Paret C, Ostermann K, Krause-Buchholz U; et al. (1999). "Human members of the SCO1 gene family: complementation analysis in yeast and intracellular localization". FEBS Lett. 447 (1): 65–70. PMID 10218584.
  • Papadopoulou LC, Sue CM, Davidson MM; et al. (1999). "Fatal infantile cardioencephalomyopathy with COX deficiency and mutations in SCO2, a COX assembly gene". Nat. Genet. 23 (3): 333–7. doi:10.1038/15513. PMID 10545952.
  • Valnot I, Osmond S, Gigarel N; et al. (2000). "Mutations of the SCO1 gene in mitochondrial cytochrome c oxidase deficiency with neonatal-onset hepatic failure and encephalopathy". Am. J. Hum. Genet. 67 (5): 1104–9. PMID 11013136.
  • Horvath R, Lochmüller H, Stucka R; et al. (2000). "Characterization of human SCO1 and COX17 genes in mitochondrial cytochrome-c-oxidase deficiency". Biochem. Biophys. Res. Commun. 276 (2): 530–3. doi:10.1006/bbrc.2000.3495. PMID 11027508.
  • 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.
  • Leary SC, Kaufman BA, Pellecchia G; et al. (2005). "Human SCO1 and SCO2 have independent, cooperative functions in copper delivery to cytochrome c oxidase". Hum. Mol. Genet. 13 (17): 1839–48. doi:10.1093/hmg/ddh197. PMID 15229189.
  • 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.
  • Williams JC, Sue C, Banting GS; et al. (2005). "Crystal structure of human SCO1: implications for redox signaling by a mitochondrial cytochrome c oxidase "assembly" protein". J. Biol. Chem. 280 (15): 15202–11. doi:10.1074/jbc.M410705200. PMID 15659396.
  • Horng YC, Leary SC, Cobine PA; et al. (2005). "Human Sco1 and Sco2 function as copper-binding proteins". J. Biol. Chem. 280 (40): 34113–22. doi:10.1074/jbc.M506801200. PMID 16091356.
  • Cobine PA, Pierrel F, Leary SC; et al. (2006). "The P174L mutation in human Sco1 severely compromises Cox17-dependent metallation but does not impair copper binding". J. Biol. Chem. 281 (18): 12270–6. doi:10.1074/jbc.M600496200. PMID 16520371.
  • Banci L, Bertini I, Calderone V; et al. (2006). "A hint for the function of human Sco1 from different structures". Proc. Natl. Acad. Sci. U.S.A. 103 (23): 8595–600. doi:10.1073/pnas.0601375103. PMID 16735468.
  • Leary SC, Cobine PA, Kaufman BA; et al. (2007). "The human cytochrome c oxidase assembly factors SCO1 and SCO2 have regulatory roles in the maintenance of cellular copper homeostasis". Cell Metab. 5 (1): 9–20. doi:10.1016/j.cmet.2006.12.001. PMID 17189203.

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