Gene interactions and pathways from curated databases and text-mining

◀ Back to JAK2

JAK2 — TYR

Text-mined interactions from Literome

Suzuki et al., Exp Neurol 2001 (Brain Ischemia...) : JAK-STAT is the major downstream signal pathway of interleukin-6 (IL-6) cytokine family and is regulated by Tyr705 phosphorylation of Stat3
Mazière et al., Free Radic Biol Med 2001 : We provide evidence that cupric-ion oxidized LDL ( CuLDL ) or endothelial cell oxidized LDL ( ELDL ) induced the activation by Tyr-phosphorylation of JAK2 , one of the Janus kinase involved upstream of STATs in the JAK/STAT pathway of cytokine transduction
Stross et al., J Biol Chem 2006 (Carcinoma, Hepatocellular...) : Binding of SOCS3 to the phosphorylated Tyr ( 759 ) in the cytoplasmic region of gp130, the common signal transducing receptor chain of all IL-6-type cytokines, is necessary for inhibition of Janus kinase mediated signaling
Liu et al., J Biol Chem 2006 : Induction of STAT3 Tyr705 and Ser727 phosphorylations by Galpha ( s ) QL was suppressed by inhibition of protein kinase A, Janus kinase 2/3 , Rac1, c-Jun N-terminal kinase (JNK), or phosphatidylinositol 3-kinase, and a similar profile was observed in response to beta2-adrenergic receptor stimulation
Jiang et al., J Biol Chem 2008 : Tyr1138 in LEPRb was required for leptin stimulated phosphorylation of STAT3 but not JAK2 ( K882E )
Robertson et al., Mol Cell Biol 2009 : Mutation of Tyr ( 317 ) promotes increased Jak2 activity, and the phosphorylation of Tyr ( 317 ) during cytokine signaling requires prior activation loop phosphorylation, which is consistent with a role for Tyr ( 317 ) in the feedback inhibition of Jak2 kinase activity after receptor stimulation
Shi et al., J Recept Signal Transduct Res 2012 (MAP Kinase Signaling System) : In contrast, we found that PKCd inhibition affected p-SRC and p-JAK2 resulting in decreased p-Tyr and p-Ser STAT3 levels
Andrés et al., Exp Dermatol 2013 (MAP Kinase Signaling System...) : Tyr705 phosphorylation was induced by IL-6 and IL-20 in a Jak2 dependent manner, and moreover, phosphorylation of Tyr705 produced a strong increase in STAT3 transcriptional activity