FOG00756
EOG8VMD1D
sce:COX5B;COX5A
Genes: 34
Protein descriptionCOX.05B
SGD DescriptionSubunit Vb of cytochrome c oxidase; cytochrome c oxidase is the terminal member of the mitochondrial inner membrane electron transport chain; Cox5Bp is predominantly expressed during anaerobic growth while its isoform Va (Cox5Ap) is expressed during aerobic growth; COX5B has a paralog, COX5A, that arose from the whole genome duplication|Subunit Va of cytochrome c oxidase; cytochrome c oxidase is the terminal member of the mitochondrial inner membrane electron transport chain; Cox5Ap is predominantly expressed during aerobic growth while its isoform Vb (Cox5Bp) is expressed during anaerobic growth; COX5A has a paralog, COX5B, that arose from the whole genome duplication
PomBase Descriptioncytochrome c oxidase subunit V (predicted)
AspGD DescriptionCytochrome c oxidase subunit
References
Cerletti N, et al. (1983 Apr 25). Import of proteins into mitochondria. Isolated yeast mitochondria and a solubilized matrix protease correctly process cytochrome c oxidase subunit V precursor at the NH2 terminus.
Power SD, et al. (1984 May 25). The nuclear-coded subunits of yeast cytochrome c oxidase. III. Identification of homologous subunits in yeast, bovine heart, and Neurospora crassa cytochrome c oxidases.
Séraphin B, et al. (1985). Primary structure of a gene for subunit V of the cytochrome c oxidase from Saccharomyces cerevisiae.
Cumsky MG, et al. (1985 Apr). Two nonidentical forms of subunit V are functional in yeast cytochrome c oxidase.
Koerner TJ, et al. (1985 Aug 15). Cloning and characterization of the yeast nuclear gene for subunit 5 of cytochrome oxidase.
Cumsky MG, et al. (1987 Oct). Structural analysis of two genes encoding divergent forms of yeast cytochrome c oxidase subunit V.
Hodge MR, et al. (1989 Jun). Splicing of a yeast intron containing an unusual 5' junction sequence.
Geier BM, et al. (1995 Jan 15). Kinetic properties and ligand binding of the eleven-subunit cytochrome-c oxidase from Saccharomyces cerevisiae isolated with a novel large-scale purification method.