Difference between revisions of "Phosphatase Family OCA"
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| − | [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Superfamily_CC1|Superfamily CC1]: [[Phosphatase_Family_OCA|OCA]] | + | [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_OCA|OCA]] |
OCA family is named after the five member genes in yeast. OCA stands for Oxidant-induced Cell-cycle Arrest. The physiological substrates of OCAs are still unclear. But, [[Gene_OCA3|OCA3]] has been shown to control intracellular localization of Gln3 (a phosphorylated transcriptional activator), in cooperation with Npr1 kinase <cite>Harashima08</cite>. OCAs also have been shown to be involved in telomere capping and uncapping <cite>lydall08</cite>. | OCA family is named after the five member genes in yeast. OCA stands for Oxidant-induced Cell-cycle Arrest. The physiological substrates of OCAs are still unclear. But, [[Gene_OCA3|OCA3]] has been shown to control intracellular localization of Gln3 (a phosphorylated transcriptional activator), in cooperation with Npr1 kinase <cite>Harashima08</cite>. OCAs also have been shown to be involved in telomere capping and uncapping <cite>lydall08</cite>. | ||
Revision as of 20:21, 6 December 2014
Phosphatase Classification: Superfamily CC1: OCA
OCA family is named after the five member genes in yeast. OCA stands for Oxidant-induced Cell-cycle Arrest. The physiological substrates of OCAs are still unclear. But, OCA3 has been shown to control intracellular localization of Gln3 (a phosphorylated transcriptional activator), in cooperation with Npr1 kinase [1]. OCAs also have been shown to be involved in telomere capping and uncapping [2].
It is found in most if not all of eukaryotes except eumetazoan (i.e. fungi, plants, protists, monosiga, and sponge).
The family is also called as plant and fungi atypical (PFA)-DSPs [3, 4].
Reference
- Hirasaki M, Kaneko Y, and Harashima S. Protein phosphatase Siw14 controls intracellular localization of Gln3 in cooperation with Npr1 kinase in Saccharomyces cerevisiae. Gene. 2008 Feb 15;409(1-2):34-43. DOI:10.1016/j.gene.2007.11.005 |
- Addinall SG, Downey M, Yu M, Zubko MK, Dewar J, Leake A, Hallinan J, Shaw O, James K, Wilkinson DJ, Wipat A, Durocher D, and Lydall D. A genomewide suppressor and enhancer analysis of cdc13-1 reveals varied cellular processes influencing telomere capping in Saccharomyces cerevisiae. Genetics. 2008 Dec;180(4):2251-66. DOI:10.1534/genetics.108.092577 |
- Romá-Mateo C, Ríos P, Tabernero L, Attwood TK, and Pulido R. A novel phosphatase family, structurally related to dual-specificity phosphatases, that displays unique amino acid sequence and substrate specificity. J Mol Biol. 2007 Dec 7;374(4):899-909. DOI:10.1016/j.jmb.2007.10.008 |
- Romá-Mateo C, Sacristán-Reviriego A, Beresford NJ, Caparrós-Martín JA, Culiáñez-Macià FA, Martín H, Molina M, Tabernero L, and Pulido R. Phylogenetic and genetic linkage between novel atypical dual-specificity phosphatases from non-metazoan organisms. Mol Genet Genomics. 2011 Apr;285(4):341-54. DOI:10.1007/s00438-011-0611-6 |
