Gene interactions and pathways from curated databases and text-mining

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STAT1 — TYK2

Pathways - manually collected, often from reviews:

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

Text-mined interactions from Literome

Aoki et al., Exp Hematol 2003 : Phosphorylation of Stat1 by limitin is partially dependent on Tyk2
Kasper et al., J Interferon Cytokine Res 2007 : However, GM-CSF induced downregulation of Tyk2 and Jak1 tyrosine phosphorylation as well as Tyk2 protein levels likely contributed to the reduced Stat1 tyrosine phosphorylation
Prchal-Murphy et al., PloS one 2012 (Genetic Predisposition to Disease...) : We show that kinase-active TYK2 is required for full fledged type I interferon- ( IFN ) induced activation of the transcription factors STAT1-4 and for the in vivo antiviral defence against viruses primarily controlled through type I IFN actions
Herzig et al., Shock 2012 (Bacteremia...) : TYK2 is essential for type I, but not type II, IFN induced STAT1 activation
Bhattacharjee et al., Free Radic Biol Med 2013 : We further show that Jak2 is upstream of Stat3 activation and Tyk2 controls Stat1 and Stat6 activation in response to IL-13 stimulation
Haque et al., J Biol Chem 1995 : Interestingly, ligand independent Stat1 alpha activation by peroxo-derivatives of these transition metals does not require Jak1, Jak2, or Tyk2 kinase activity, suggesting that other kinases can phosphorylate Stat1 alpha on tyrosine 701
Quelle et al., J Biol Chem 1995 : Co-expression of Stat1 with Tyk2 , Jak1, or Jak2 resulted in the specific tyrosine phosphorylation of Stat1 at Tyr701, the residue phosphorylated in mammalian cells stimulated with interferon gamma
Eilers et al., Cell Growth Differ 1996 : TYK2 activity led to an IFN-alpha independent appearance of tyrosine phosphorylated STAT1 but not STAT2 or JAK1 proteins
Gatsios et al., J Biol Chem 1998 : In this study, we demonstrate that in different cell lines a particular stress, namely hyperosmolarity, results in tyrosine phosphorylation of the Janus kinases Jak1, Jak2, and Tyk2 and in the activation of STAT1 and/or STAT3