Developer site: The content shown here is test data.

MyEClinic
MyEClinic
Health Dictionary AI Health Chat Find an Online Doctor
A serene Zen garden with raked sand and smooth stones, symbolising clarity and calm

Health Dictionary

Reliable, easy-to-read patient information on common medical conditions — written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.

Back to skin conditions

SCO2

Introduction

SCO cytochrome oxidase deficient homolog 2 (yeast), also known as SCO2, 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 of the yeast SCO2 gene.[1]

References

References

  1. ↑ 1.0 1.1 “Entrez Gene: SCO2 SCO cytochrome oxidase deficient homolog 2 (yeast)”.
Further reading

Further reading

  • 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.
  • Jaksch M, Ogilvie I, Yao J; et al. (2000). “Mutations in SCO2 are associated with a distinct form of hypertrophic cardiomyopathy and cytochrome c oxidase deficiency”. Hum. Mol. Genet. 9 (5): 795–801. PMID 10749987.
  • Jaksch M, Horvath R, Horn N; et al. (2001). “Homozygosity (E140K) in SCO2 causes delayed infantile onset of cardiomyopathy and neuropathy”. Neurology. 57 (8): 1440–6. PMID 11673586.
  • Jaksch M, Paret C, Stucka R; et al. (2002). “Cytochrome c oxidase deficiency due to mutations in SCO2, encoding a mitochondrial copper-binding protein, is rescued by copper in human myoblasts”. Hum. Mol. Genet. 10 (26): 3025–35. PMID 11751685.
  • Salviati L, Hernandez-Rosa E, Walker WF; et al. (2002). “Copper supplementation restores cytochrome c oxidase activity in cultured cells from patients with SCO2 mutations”. Biochem. J. 363 (Pt 2): 321–7. PMID 11931660.
  • Salviati L, Sacconi S, Rasalan MM; et al. (2002). “Cytochrome c oxidase deficiency due to a novel SCO2 mutation mimics Werdnig-Hoffmann disease”. Arch. Neurol. 59 (5): 862–5. PMID 12020273.
  • 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.
  • Collins JE, Goward ME, Cole CG; et al. (2003). “Reevaluating human gene annotation: a second-generation analysis of chromosome 22”. Genome Res. 13 (1): 27–36. doi:10.1101/gr.695703. PMID 12529303.
  • Sacconi S, Salviati L, Sue CM; et al. (2003). “Mutation screening in patients with isolated cytochrome c oxidase deficiency”. Pediatr. Res. 53 (2): 224–30. PMID 12538779.
  • Tarnopolsky MA, Bourgeois JM, Fu MH; et al. (2004). “Novel SCO2 mutation (G1521A) presenting as a spinal muscular atrophy type I phenotype”. Am. J. Med. Genet. A. 125 (3): 310–4. doi:10.1002/ajmg.a.20466. PMID 14994243.
  • Brandenberger R, Wei H, Zhang S; et al. (2005). “Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation”. Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197.
  • 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.
  • Collins JE, Wright CL, Edwards CA; et al. (2005). “A genome annotation-driven approach to cloning the human ORFeome”. Genome Biol. 5 (10): R84. doi:10.1186/gb-2004-5-10-r84. PMID 15461802.
  • 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.
  • Stiburek L, Vesela K, Hansikova H; et al. (2006). “Tissue-specific cytochrome c oxidase assembly defects due to mutations in SCO2 and SURF1”. Biochem. J. 392 (Pt 3): 625–32. doi:10.1042/BJ20050807. PMID 16083427.
  • 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.
  • Matoba S, Kang JG, Patino WD; et al. (2006). “p53 regulates mitochondrial respiration”. Science. 312 (5780): 1650–3. doi:10.1126/science.1126863. PMID 16728594.
  • 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.
  • Banci L, Bertini I, Ciofi-Baffoni S; et al. (2007). “A structural characterization of human SCO2”. Structure. 15 (9): 1132–40. doi:10.1016/j.str.2007.07.011. PMID 17850752.

Template:WikiDoc Sources