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Gene Review

COQ7  -  coenzyme Q7 homolog, ubiquinone (yeast)

Homo sapiens

Synonyms: CAT5, CLK-1, CLK1, Coenzyme Q biosynthesis protein 7 homolog, Timing protein clk-1 homolog, ...
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Disease relevance of COQ7


High impact information on COQ7

  • Coq7p, the Saccharomyces cerevisiae homologue, is essential for ubiquinone (coenzyme Q or Q) synthesis and therefore respiration [2].
  • In yeast, mutation of the COQ7 gene results in the absence of UQ biosynthesis and demonstrates a role for this gene in the step leading to the hydroxylation of 5-demethoxyubiquinone [1].
  • Here we identify Coq7 as belonging to a family of a di-iron containing oxidases/hydroxylases based on a conserved sequence motif for the iron ligands, supporting a direct function of Coq7 as a hydroxylase [1].
  • The Saccharomyces cerevisiae homologue COQ7/CAT5 is essential for several metabolic pathways including ubiquinone biosynthesis, respiration, and gluconeogenic gene activation [3].
  • Further investigations are necessary to elucidate the exact role of CS-1 and ubiquinone biosynthesis protein COQ7 in the setting of hypertension-induced LVH [4].

Biological context of COQ7

  • Zoo blot analysis implied that the COQ7 gene was well conserved among mammal, bird, and reptile genomes [5].
  • Genomic analyses revealed that the human COQ7 gene is composed of six exons spanning 11 kb of human genome as a single-copy gene [5].
  • The number and location of human CLK1 introns were determined, and the location of introns II and IV are the same as in C. elegans [6].

Anatomical context of COQ7

  • Tissue blot analysis showed that human COQ7 is dominantly transcribed in heart and skeletal muscle [5].
  • Biochemical analysis revealed that COQ7 is targeted to mitochondria where it is processed to mature form [7].
  • In the light, when glyoxysomes were transformed to leaf-type peroxisomes, the five more-basic forms (CAT 1 through CAT 5) became more prominent, while amounts of the three more-acidic forms (CAT 6 through CAT 8) decreased considerably [8].

Associations of COQ7 with chemical compounds


Analytical, diagnostic and therapeutic context of COQ7


  1. A new member of the family of di-iron carboxylate proteins. Coq7 (clk-1), a membrane-bound hydroxylase involved in ubiquinone biosynthesis. Stenmark, P., Grünler, J., Mattsson, J., Sindelar, P.J., Nordlund, P., Berthold, D.A. J. Biol. Chem. (2001) [Pubmed]
  2. A dietary source of coenzyme Q is essential for growth of long-lived Caenorhabditis elegans clk-1 mutants. Jonassen, T., Larsen, P.L., Clarke, C.F. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  3. Yeast Clk-1 homologue (Coq7/Cat5) is a mitochondrial protein in coenzyme Q synthesis. Jonassen, T., Proft, M., Randez-Gil, F., Schultz, J.R., Marbois, B.N., Entian, K.D., Clarke, C.F. J. Biol. Chem. (1998) [Pubmed]
  4. Proteomic analysis of early left ventricular hypertrophy secondary to hypertension: modulation by antihypertensive therapies. Gallego-Delgado, J., Lazaro, A., Osende, J.I., Esteban, V., Barderas, M.G., Gomez-Guerrero, C., Vega, R., Vivanco, F., Egido, J. J. Am. Soc. Nephrol. (2006) [Pubmed]
  5. Orthologues of the Caenorhabditis elegans longevity gene clk-1 in mouse and human. Asaumi, S., Kuroyanagi, H., Seki, N., Shirasawa, T. Genomics (1999) [Pubmed]
  6. Conservation of the Caenorhabditis elegans timing gene clk-1 from yeast to human: a gene required for ubiquinone biosynthesis with potential implications for aging. Vajo, Z., King, L.M., Jonassen, T., Wilkin, D.J., Ho, N., Munnich, A., Clarke, C.F., Francomano, C.A. Mamm. Genome (1999) [Pubmed]
  7. Mouse coq7/clk-1 orthologue rescued slowed rhythmic behavior and extended life span of clk-1 longevity mutant in Caenorhabditis elegans. Takahashi, M., Asaumi, S., Honda, S., Suzuki , Y., Nakai, D., Kuroyanagi, H., Shimizu, T., Honda, Y., Shirasawa, T. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
  8. Biogenesis of catalase in glyoxysomes and leaf-type peroxisomes of sunflower cotyledons. Eising, R., Trelease, R.N., Ni, W.T. Arch. Biochem. Biophys. (1990) [Pubmed]
  9. CLK-1/Coq7p is a DMQ mono-oxygenase and a new member of the di-iron carboxylate protein family. Rea, S. FEBS Lett. (2001) [Pubmed]
  10. Fenofibrate activates the biochemical pathways and the de novo expression of genes related to lipid handling and uncoupling protein-3 functions in liver of normal rats. Silvestri, E., de Lange, P., Moreno, M., Lombardi, A., Ragni, M., Feola, A., Schiavo, L., Goglia, F., Lanni, A. Biochim. Biophys. Acta (2006) [Pubmed]
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