IndraLab

Statements


JAK2 phosphorylates JAK2 on Y1007. 11 / 11
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"65 JAK2 dimerization induces the trans‐phosphorylation of each JAK2 protein at Y1007 and Y1008 in the activation loop of the tyrosine kinase (TK) domain leading to TK activation."

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"Multiple autophosphorylation sites on Jak2, including Y1007 and Y1008. Activation of Jak2 catalytic activity requires phosphorylation of Y1007 in the kinase activation loop."

"Within the Jak2 kinase domain, there is a region that has considerable sequence homology to the regulatory region of the insulin receptor and contains two tyrosines, Y1007 and Y1008, that are potential regulatory sites. Y1007 and Y1008 are sites of trans- or autophosphorylation in vivo and in in vitro kinase reactions. Mutation of Y1007, or both Y1007 and Y1008, to phenylalanine essentially eliminated kinase activity, whereas mutation of Y1008 to phenylalanine had no detectable effect on kinase activity"

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"JAK2 and STAT1 signaling was activated by IFNgamma, resulting in phosphorylation of JAK2 (Tyr 1007/1008), and STAT1 (Tyr 701) at 1h and 6h, whereas IL-1beta had no effect."