Gene interactions and pathways from curated databases and text-mining

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DOK1 — INS

Pathways - manually collected, often from reviews:

Text-mined interactions from Literome

Noguchi et al., EMBO J 1999 : The maximal insulin induced tyrosine phosphorylation of Dok required a Src family kinase ... Insulin promoted the association of tyrosine phosphorylated Dok with the adapter protein NCK and rasGAP
Wick et al., J Biol Chem 2001 (MAP Kinase Signaling System) : However, mutations at Tyr ( 362 ) and Tyr ( 398 ) only partially blocked insulin stimulated p62(dok) tyrosine phosphorylation in cells, indicating that p62(dok) is also a target for other cellular tyrosine kinase ( s ) in addition to the IR
Sánchez-Margalet et al., Cell Mol Life Sci 2003 : In summary, these results demonstrate that Sam68 works as a cytoplasmic docking protein which is recruited by IR signaling and whose expression is induced by insulin stimulation, suggesting a putative role for Sam68 in insulin signal transduction
Csermely et al., Biochemistry 1992 : Insulin induced the phosphorylation of seven DNA binding proteins : pp34, pp40, pp48, pp62 , pp64, pp66, and pp72