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The process of introducing a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein. Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein. Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a Stat2 protein. Any process that modulates the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a STAT (Signal Transducer and Activator of Transcription) protein. Any process that activates or increases the frequency, rate or extent of the phosphorylation of peptidyl-tyrosine. Any process that modulates the frequency, rate or extent of introducing a phosphate group to a tyrosine residue of a Stat2 protein. The process of introducing a phosphate group to a tyrosine residue of a Stat2 protein. Any process that activates or increases the frequency, rate or extent of the JAK-STAT signaling pathway activity.

View Gene Ontology (GO) Term

GO TERM SUMMARY
Name: positive regulation of tyrosine phosphorylation of Stat2 protein
Acc: GO:0042515
Aspect: Biological Process
Desc: Any process that activates or increases the frequency, rate or extent of the introduction of a phosphate group to a tyrosine residue of a Stat2 protein.
Synonyms:
  • activation of tyrosine phosphorylation of Stat2 protein
  • up-regulation of tyrosine phosphorylation of Stat2 protein
  • up regulation of tyrosine phosphorylation of Stat2 protein
  • stimulation of tyrosine phosphorylation of Stat2 protein
  • upregulation of tyrosine phosphorylation of Stat2 protein
Proteins in PDR annotated with:
   This term: 0
   Term or descendants: 0


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0042515 - positive regulation of tyrosine phosphorylation of Stat2 protein (interactive image map)
YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle