IndraLab

Statements

JAK2 phosphorylates JAK2 on Y1007. 15 / 15
3 2 3 1 | 1 5
biopax:netpath
No evidence text available
18718905
reach
"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."
33731692
hprd
No evidence text available
9111318
hprd
No evidence text available
15143187
biopax:netpath
No evidence text available
17565041
rlimsp
"Moreover, transient expression studies showed that Jak2 is polyubiquitinated when co-expressed with EpoR and autophosphorylated on Y1007 (Fig. 3B)."
22087308
phosphoelm
No evidence text available
9111318
rlimsp
"Moreover, transient expression studies showed that Jak2 is polyubiquitinated when co-expressed with EpoR and autophosphorylated on Y1007 (Fig. 3B). This is in agreement with the previous report that Jak2 becomes polyubiquitinated when autophosphorylated on Y1007 [19]."
22087308
rlimsp
"In accordance with this, it was reported that autophosphorylation of Jak2 on Y1007 creates a binding site for the SOCS1 complex, resulting in ubiquitination and proteasomal degradation of Jak2 [19]."
22087308
rlimsp
"In this study, we employed MALDI-TOF/TOF and triple quadrupole mass spectrometers to analyze qualitatively and quantitatively the dephosphorylation process by using synthetic peptides derived from the tandem autophosphorylation sites (Y1007 and Y1008) of human JAK2."
25354842
biopax:netpath
No evidence text available
11585385
signor
"Multiple autophosphorylation sites on Jak2, including Y1007 and Y1008. Activation of Jak2 catalytic activity requires phosphorylation of Y1007 in the kinase activation loop."
9111318
hprd
No evidence text available
11593427
rlimsp
"In accordance with our previous report, Jak2 becomes activated and autophosphorylated on Y1007 in the activation loop without Epo stimulation when overexpressed with EpoR [18]."
22087308
signor
"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"
9111318