IndraLab

Statements


JAK2 phosphorylates JAK2 on Y813. 10 / 10
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rlimsp
"This alternative mechanism might also complement the bipolar clamp function of SH2-Bβ, but only in cells where Jak2 in J(RLR)J complexes (without SH2-Bβ bound) tends to be dephosphorylated, at least on certain sites (it is important to bear in mind that Tyr813 must be autophosphorylated in order for SH2-Bβ to bind; see Figure S2B, Supporting Information)."

rlimsp
"Tyrosine 813 is a site of JAK2 autophosphorylation critical for activation of JAK2 by SH2-B beta."

No evidence text available

No evidence text available

rlimsp
"Using two-dimensional phosphopeptide mapping and a phosphospecific antibody, we identified tyrosine 813 as a site of JAK2 autophosphorylation of overexpressed JAK2 and endogenous JAK2 activated by growth hormone."

No evidence text available

No evidence text available

"Tyrosine 813 is a site of jak2 autophosphorylation critical for activation of jak2 by sh2-b betawe show that phosphorylation of tyrosine 813 is required for the sh2 domain-containing adapter protein sh2-b beta to bind jak2 and to enhance the activity of jak2 and stat5b."

rlimsp
"This is because Jak2 must already be autophosphorylated, at least on Tyr813, for SH2-Bβ to bind."

rlimsp
"Taken together these data strongly suggest that tyrosine 813 is a site of autophosphorylation in JAK2 and is the SH2-B beta-binding site within JAK2 that is required for SH2-B beta to enhance activation of JAK2."