+ |
JAK3 | up-regulates activity
phosphorylation
|
JAK1 |
0.515 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251363 |
Tyr1034 |
AIETDKEyYTVKDDR |
in vitro |
|
pmid |
sentence |
12559972 |
Phosphorylation by recombinant JAK3 of a peptide substrate corresponding to the JAK1 activation loop (KAIETDKEYYTVKD) |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251364 |
Tyr1035 |
IETDKEYyTVKDDRD |
in vitro |
|
pmid |
sentence |
12559972 |
Phosphorylation by recombinant JAK3 of a peptide substrate corresponding to the JAK1 activation loop (KAIETDKEYYTVKD) |
|
Publications: |
2 |
Organism: |
In Vitro |
+ |
JAK3 | up-regulates activity
phosphorylation
|
NFATC1 |
0.391 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276435 |
Tyr371 |
ADFAPEDySSFQHIR |
Homo sapiens |
Thymocyte |
pmid |
sentence |
23263556 |
Here we found that IL-7-Jak3 signals activated the transcription factor NFATc1 in DN thymocytes by phosphorylating Tyr371 in the regulatory region of NFATc1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
JAK3 | up-regulates
phosphorylation
|
PLD2 |
0.418 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-163858 |
Tyr415 |
ALGINSGySKRALML |
Homo sapiens |
|
pmid |
sentence |
20176813 |
We identified three kinases capable of phosphorylating pld2 in vitro-epidermal growth factor receptor (egfr), jak3, and src (with jak3 reported for the first time in this study)-that phosphorylate an inhibitory, an activator, and an ambivalent (one that can yield either effect) site, respectively. Mass spectrometry analyses indicated the target of each of these kinases as y(296) for egfr, y(415) for jak3, and y(511) for src. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
JAK3 | up-regulates
phosphorylation
|
SIGLEC10 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-112479 |
Tyr597 |
RHSTILDyINVVPTA |
Homo sapiens |
|
pmid |
sentence |
11733002 |
These results suggest that the tyrosines at positions 597 and 667, contained within itim-like motifs, are likely targets of phosphorylation by several classes of signaling molecules, including lck, jak3, and emt. The tyrosine located at position y691 was also contributing to the phosphorylation of the wild-type siglec tail by lck and jak3 kinases. Y597 and y667 are likely involved in intracellular signaling |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-112483 |
Tyr667 |
ESQEELHyATLNFPG |
Homo sapiens |
|
pmid |
sentence |
11733002 |
These results suggest that the tyrosines at positions 597 and 667, contained within itim-like motifs, are likely targets of phosphorylation by several classes of signaling molecules, including lck, jak3, and emt. The tyrosine located at position y691 was also contributing to the phosphorylation of the wild-type siglec tail by lck and jak3 kinases. Phosphorylation of the tyrosine located at position 667 in an itim motif appears to be necessary for the recruitment of shp-1 and partial recruitment of shp-2 |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
JAK3 |
phosphorylation
|
SIGLEC10 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-112487 |
Tyr691 |
PKGTQADyAEVKFQ |
Homo sapiens |
|
pmid |
sentence |
11733002 |
These results suggest that the tyrosines at positions 597 and 667, contained within itim-like motifs, are likely targets of phosphorylation by several classes of signaling molecules, including lck, jak3, and emt. The tyrosine located at position y691 was also contributing to the phosphorylation of the wild-type siglec tail by lck and jak3 kinases. however, it is not clear whether y691 is capable of binding sap or a similar protein. Future studies will attempt to elucidate the signaling activities associated with y691 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
JAK3 | up-regulates
phosphorylation
|
STAT5A |
0.85 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-160672 |
Tyr694 |
LAKAVDGyVKPQIKQ |
Homo sapiens |
|
pmid |
sentence |
18250158 |
For these assays, coexpression of wt jak3 with stat5a was found to result in tyrosine phosphorylation of stat5a (lane 2) mediated by jak3, since stat5a coexpressed with the kinase-inactive k855a mutant form of jak3 was not tyrosine phosphorylated. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-182817 |
Tyr694 |
LAKAVDGyVKPQIKQ |
Homo sapiens |
|
pmid |
sentence |
19088846 |
For these assays, coexpression of wt jak3 with stat5a was found to result in tyrosine phosphorylation of stat5a (lane 2) mediated by jak3, since stat5a coexpressed with the kinase-inactive k855a mutant form of jak3 was not tyrosine phosphorylated. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
JAK3 | up-regulates
phosphorylation
|
JAK3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-160660 |
Tyr785 |
NSLISSDyELLSDPT |
Homo sapiens |
|
pmid |
sentence |
18250158 |
The phosphorylation of wt jak3 and y980f/y981f/y785f mutant jak3 is presumably mediated through autophosphorylation at distinct jak3 sites within this model systemhosphorylation of jak3 on y785 has been reported to create a binding site for the adaptor protein sh2b-beta |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-160664 |
Tyr904 |
SLRLVMEyLPSGCLR |
Homo sapiens |
|
pmid |
sentence |
18250158 |
Y904 and y939 are required for optimal jak3 autophosphorylation and kinase activity in vitro |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-160668 |
Tyr939 |
QICKGMEyLGSRRCV |
Homo sapiens |
|
pmid |
sentence |
18250158 |
Y904 and y939 are required for optimal jak3 autophosphorylation and kinase activity in vitro |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-53590 |
Tyr980 |
LLPLDKDyYVVREPG |
Homo sapiens |
|
pmid |
sentence |
9391116 |
We found that jak3 is autophosphorylated on multiple sites including y980 and y981. Compared with the activity of wild-type (wt) jak3, mutant y980f demonstrated markedly decreased kinase activity, and optimal phosphorylation of jak3 on other sites was dependent on y980 phosphorylation. The mutant y980f also exhibited reduced phosphorylation of its substrates, gammac and stat5a. In contrast, mutant y981f had greatly increased kinase activity, whereas the double mutant, yy980/981ff, had intermediate activity. |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
+ |
JAK3 | down-regulates
phosphorylation
|
JAK3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-53594 |
Tyr981 |
LPLDKDYyVVREPGQ |
Homo sapiens |
|
pmid |
sentence |
9391116 |
We found that jak3 is autophosphorylated on multiple sites including y980 and y981. Compared with the activity of wild-type (wt) jak3, mutant y980f demonstrated markedly decreased kinase activity, and optimal phosphorylation of jak3 on other sites was dependent on y980 phosphorylation. The mutant y980f also exhibited reduced phosphorylation of its substrates, gammac and stat5a. In contrast, mutant y981f had greatly increased kinase activity, whereas the double mutant, yy980/981ff, had intermediate activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
IL2RG | up-regulates
binding
|
JAK3 |
0.736 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-178491 |
|
|
Homo sapiens |
B-lymphocyte |
pmid |
sentence |
18445337 |
Jak3 is associated with the ?c20,21. Cytokine binding mediates the trans-phosphorylation of receptor associated jak kinases, which in turn phosphorylate tyrosine residues on the receptors themselves. The receptor phosphotyrosines serve as docking sites for sh2 domain proteins including the stat family of transcription factors which are activated by jak-mediated phosphorylation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
IL4R | up-regulates
|
JAK3 |
0.662 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-28399 |
|
|
Homo sapiens |
B-lymphocyte |
pmid |
sentence |
7538655 |
The overlapping and distinct protein tyrosine phosphorylation and activation of the same jak1 kinase in t lymphocytes strongly suggests that il-4 and il-9 share the common signal transduction pathways. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
tofacitinib citrate | down-regulates
chemical inhibition
|
JAK3 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-207311 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
JAK1 | up-regulates
|
JAK3 |
0.515 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-77551 |
|
|
Homo sapiens |
|
pmid |
sentence |
10825200 |
Syk activation required jak3, probably indirectly via activation of jak1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ruxolitinib | down-regulates activity
chemical inhibition
|
JAK3 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-258278 |
|
|
in vitro |
|
pmid |
sentence |
22037378 |
Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. | The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
IL21R | up-regulates
binding
|
JAK3 |
0.54 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-90269 |
|
|
Homo sapiens |
B-lymphocyte |
pmid |
sentence |
12093291 |
Retroviral-mediated transduction of wild-type gamma c into xscid jt cells restored function to the il-21r, as shown by il-21-induced tyrosine phosphorylation of jak1 and jak3, and downstream activation of stat5 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
9-(1-Methyl-4-pyrazolyl)-1-[1-(1-oxoprop-2-enyl)-2,3-dihydroindol-6-yl]-2-benzo[h][1,6]naphthyridinone | down-regulates activity
chemical inhibition
|
JAK3 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262234 |
|
|
in vitro |
|
pmid |
sentence |
24556163 |
This analysis revealed that QL47 also potently inhibits BMX with an IC50 of 6.7 nM but impressively displays more than 100-fold selectivity against EGFR, HER2, JAK3, BLK, TEC, and ITK that possess an equivalently placed cysteine |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
TG101209 | down-regulates
chemical inhibition
|
JAK3 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-207266 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PTPRC | down-regulates activity
dephosphorylation
|
JAK3 |
0.468 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248359 |
|
|
Mus musculus |
|
pmid |
sentence |
11201744 |
CD45 is a JAK phosphatase and negatively regulates cytokine receptor signalling |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
SOCS3 | down-regulates activity
binding
|
JAK3 |
0.687 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-238645 |
|
|
Homo sapiens |
|
pmid |
sentence |
21508344 |
SOCS proteins bind to janus kinase and to certain cytokine receptors and signaling molecules, thereby suppressing further signaling events. Studies have shown that SOCS proteins are key physiological regulators of inflammation. Recent studies have also demonstrated that SOCS1 and SOCS3 are important regulators of adaptive immunity.Both SOCS1 and SOCS3 can inhibit JAK tyrosine kinase activity directly through their kinase inhibitory regions (KIR). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
JAK1 | up-regulates
phosphorylation
|
JAK3 |
0.515 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-152914 |
|
|
Homo sapiens |
T-lymphocyte |
pmid |
sentence |
17259970 |
Il-7r signalling is initiated when il-7 crosslinks the extracellular domains of il-7ralpha and gammac, bringing together jak1 and jak3, which mutually phosphorylate each other, increasing their kinase activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PTPRC | up-regulates
dephosphorylation
|
JAK3 |
0.468 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-87157 |
|
|
Homo sapiens |
B-lymphocyte, RAMOS Cell |
pmid |
sentence |
11994288 |
These negative regulatory effects on ig class switching were concomitant with the ability of cd45 to dephosphorylate the induced phosphorylation of jak1, jak3, |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ruxolitinib | down-regulates
chemical inhibition
|
JAK3 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-206673 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
JAK3 | up-regulates
phosphorylation
|
STAT3 |
0.785 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-256254 |
|
|
Homo sapiens |
|
pmid |
sentence |
30029643 |
Since Jak-STAT pathway primarily activated in IL-15-me- diated cell proliferation, we tested whether it is also participates in IL-15-mediated proliferation of FAPs. Interestingly, we found the expression of phospho-Jak3 and phospho-Tyk2, as well as their downstream, phospho- STAT3 and phospho-STAT5, was significantly upregulated |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
IL15RA | up-regulates
, phosphorylation
|
JAK3 |
0.481 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-256226 |
|
|
Homo sapiens |
|
pmid |
sentence |
30029643 |
Since Jak-STAT pathway primarily activated in IL-15-me- diated cell proliferation, we tested whether it is also participates in IL-15-mediated proliferation of FAPs. Interestingly, we found the expression of phospho-Jak3 and phospho-Tyk2, as well as their downstream, phospho- STAT3 and phospho-STAT5, was significantly upregulated |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-256225 |
|
|
Homo sapiens |
|
pmid |
sentence |
30029643 |
Since Jak-STAT pathway primarily activated in IL-15-me- diated cell proliferation, we tested whether it is also participates in IL-15-mediated proliferation of FAPs. Interestingly, we found the expression of phospho-Jak3 and phospho-Tyk2, as well as their downstream, phospho- STAT3 and phospho-STAT5, was significantly upregulated |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
SOCS1 | down-regulates activity
binding
|
JAK3 |
0.697 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-238642 |
|
|
Homo sapiens |
|
pmid |
sentence |
21508344 |
SOCS proteins bind to janus kinase and to certain cytokine receptors and signaling molecules, thereby suppressing further signaling events. Studies have shown that SOCS proteins are key physiological regulators of inflammation. Recent studies have also demonstrated that SOCS1 and SOCS3 are important regulators of adaptive immunity.Both SOCS1 and SOCS3 can inhibit JAK tyrosine kinase activity directly through their kinase inhibitory regions (KIR). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AT9283 | down-regulates
chemical inhibition
|
JAK3 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-190020 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
tofacitinib | down-regulates activity
chemical inhibition
|
JAK3 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-258302 |
|
|
in vitro |
|
pmid |
sentence |
22037378 |
Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. | The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
PTPN2 | down-regulates activity
dephosphorylation
|
JAK3 |
0.684 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-133078 |
|
|
Homo sapiens |
|
pmid |
sentence |
15780598 |
Upon ligand binding, IL-2R , IL-6R or LeptinR , IFN-_R , IFN-_R and PRLR or growth hormone (GH) receptor associated JAKs become activated. These JAKs mediate phosphorylation of specific tyrosine residues and recruit STATs. Activated STATs are released from the receptor and translocate to the nucleus. PTP1B dephosphorylates JAK2, TYK2 and STAT5 . The 45-kDa form of TC-PTP was shown to dephosphorylate JAK1 and JAK3 as well as STAT1, STAT3 and STAT5. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PTPN6 | up-regulates
dephosphorylation
|
JAK3 |
0.675 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-82764 |
|
|
Homo sapiens |
|
pmid |
sentence |
11021818 |
The expression of shp-1 protein was associated with dephosphorylation of the jak3 kinase. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
JAK3 | up-regulates
phosphorylation
|
JAK1 |
0.515 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-152917 |
|
|
Homo sapiens |
T-lymphocyte |
pmid |
sentence |
17259970 |
Il-7r signalling is initiated when il-7 crosslinks the extracellular domains of il-7ralpha and gammac, bringing together jak1 and jak3, which mutually phosphorylate each other, increasing their kinase activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |