Difference between revisions of "Phosphatase Family OCA"

From PhosphataseWiki
Jump to: navigation, search
Line 1: Line 1:
 
[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Superfamily_Cys-based_I|Superfamily Cys-based I]]:  [[Phosphatase_Family_OCA|OCA]]
 
[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Superfamily_Cys-based_I|Superfamily Cys-based I]]:  [[Phosphatase_Family_OCA|OCA]]
  
OCA is found in most if not all of fungi, plants, protists (chromalveolata, excavata), as well as monosiga and sponge. The family is named after yeast phosphatases OCA1, OCA2, [[Gene_OCA3|OCA3]], OCA4, OCA6. OCA is short for Oxidant-induced Cell-cycle Arrest. They have been shown involved in telomere capping and uncapping <cite>lydall08</cite>. It is also called as plant and fungi atypical (PFA)-DSPs <cite>Pulido07 Pulido11</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>.  
  
 +
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 <cite>Pulido07 Pulido11</cite>.
 +
 +
===== Reference =====
 +
<biblio>
 +
#Harashima08 pmid=18166280
 +
</biblio>
 
=== Reference ===
 
=== Reference ===
 
<biblio>
 
<biblio>
Line 8: Line 16:
 
#Pulido11 pmid=21409566
 
#Pulido11 pmid=21409566
 
#lydall08 pmid=18845848
 
#lydall08 pmid=18845848
 +
#Harashima08 pmid=18166280
 
</biblio>
 
</biblio>

Revision as of 21:28, 28 May 2014

Phosphatase Classification: Superfamily Cys-based I: 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
  1. 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 | PubMed ID:18166280 | HubMed [Harashima08]

Reference

  1. 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 | PubMed ID:18166280 | HubMed [Harashima08]
  2. 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 | PubMed ID:18845848 | HubMed [lydall08]
  3. 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 | PubMed ID:17976645 | HubMed [Pulido07]
  4. 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 | PubMed ID:21409566 | HubMed [Pulido11]
All Medline abstracts: PubMed | HubMed