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Any process that modulates the activity of the enzyme lipoprotein lipase. Any process that activates or increases the frequency, rate or extent of myosin-light-chain-phosphatase activity. Any process that activates or increases the frequency, rate or extent of hydrolase activity, the catalysis of the hydrolysis of various bonds. Any process that modulates the frequency, rate or extent of lipase activity, the hydrolysis of a lipid or phospholipid. Any process that activates or increases the activity of the enzyme protein phosphatase type 2B. Any process that increases the rate or frequency of phosphatase activity. Phosphatases catalyze the hydrolysis of phosphoric monoesters, releasing inorganic phosphate. Any process that modulates the rate or frequency of phosphatase activity. Phosphatases catalyze the hydrolysis of phosphoric monoesters, releasing inorganic phosphate. Any process that activates or increases the activity of a phosphoprotein phosphatase. Any process that modulates the frequency, rate or extent of phosphoprotein phosphatase activity, the catalysis of the hydrolysis of phosphate from a phosphoprotein. Any process that activates or increases the activity of the enzyme protein phosphatase type 2A.

View Gene Ontology (GO) Term

GO TERM SUMMARY
Name: positive regulation of phosphoprotein phosphatase activity
Acc: GO:0032516
Aspect: Biological Process
Desc: Any process that activates or increases the activity of a phosphoprotein phosphatase.
Synonyms:
  • up regulation of phosphoprotein phosphatase activity
  • upregulation of phosphoprotein phosphatase activity
  • activation of phosphoprotein phosphatase activity
  • stimulation of phosphoprotein phosphatase activity
  • up-regulation of phosphoprotein phosphatase activity
Proteins in PDR annotated with:
   This term: 6 [Search]
   Term or descendants: 8 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0032516 - positive regulation of phosphoprotein phosphatase activity (interactive image map)
YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle