Difference between revisions of "Phosphatase Subfamily eak"

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(Created page with "Phosphatase Classification: Fold CC1: Superfamily CC1: Phosphatase_Family_PTP|Family ...")
 
 
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__NOTOC__
 
[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]: [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_PTP|Family PTP]]: [[Phosphatase_Subfamily_eak|Subfamily Eak]]
 
[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]: [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_PTP|Family PTP]]: [[Phosphatase_Subfamily_eak|Subfamily Eak]]
  
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=== Function ===
 
=== Function ===
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In ''C. elegant'', both members, eak-6 and sdf-9, potentiate AKT-1/PKB signaling. Eak-6 and sdf-9 mutants have similar [http://www.wormbook.org/chapters/www_dauer/dauer.html dauer] formation phenotypes. The function seems independent of phosphatase activity, because sdf-9 is predicted to be catalytically inactive given the replacement of cysteine by serine at the Cx5R motif <cite>Hu06</cite>.
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=== References ===
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<biblio>
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#Hu06 pmid=16839187
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</biblio>

Latest revision as of 17:12, 29 May 2015

Phosphatase Classification: Fold CC1: Superfamily CC1: Family PTP: Subfamily Eak

Evolution

The eak subfamily is nematode specific. C. elegans has two members eak-6 and sdf-9 (eak-5).

Domain

The eak subfamily has a single structural domain: the phosphatase domain of CC1 fold.

Function

In C. elegant, both members, eak-6 and sdf-9, potentiate AKT-1/PKB signaling. Eak-6 and sdf-9 mutants have similar dauer formation phenotypes. The function seems independent of phosphatase activity, because sdf-9 is predicted to be catalytically inactive given the replacement of cysteine by serine at the Cx5R motif [1].

References

  1. Hu PJ, Xu J, and Ruvkun G. Two membrane-associated tyrosine phosphatase homologs potentiate C. elegans AKT-1/PKB signaling. PLoS Genet. 2006 Jul;2(7):e99. DOI:10.1371/journal.pgen.0020099 | PubMed ID:16839187 | HubMed [Hu06]