| + |
PRKCA | up-regulates activity 
phosphorylation
|
JAK2 |
0.262 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277261 |
Ser518 |
VFRTNGVsDVPTSPT |
in vitro |
|
| pmid |
sentence |
| 27368100 |
These results suggest that PKC activates JAK2 and thereby STAT3 by directly phosphorylating T174 and S518. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277262 |
Thr174 |
KVPVTHEtQEECLGM |
in vitro |
|
| pmid |
sentence |
| 27368100 |
These results suggest that PKC activates JAK2 and thereby STAT3 by directly phosphorylating T174 and S518. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
JAK2 | down-regulates activity 
phosphorylation
|
JAK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176054 |
Ser523 |
GVSDVPTsPTLQRPT |
Homo sapiens |
|
| pmid |
sentence |
| 21841788 |
The jak2 jh2 domain functions as a negative regulator and is presumed to be a catalytically inactive pseudokinase, but the mechanism(s) for its inhibition of jak2 remains unknown. Here we show that jh2 is a dual-specificity protein kinase that phosphorylates two negative regulatory sites in jak2: ser523 and tyr570. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251359 |
Tyr570 |
VRREVGDyGQLHETE |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15143187 |
JAK2 is autophosphorylated on tyrosines 221 and 1007. tyrosines 221 and 570 in JAK2 may serve as regulatory sites in JAK2, with phosphorylation of tyrosine 221 increasing kinase activity and phosphorylation of tyrosine 570 decreasing kinase activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176058 |
Tyr570 |
VRREVGDyGQLHETE |
Homo sapiens |
|
| pmid |
sentence |
| 21841788 |
The jak2 jh2 domain functions as a negative regulator and is presumed to be a catalytically inactive pseudokinase, but the mechanism(s) for its inhibition of jak2 remains unknown. Here we show that jh2 is a dual-specificity protein kinase that phosphorylates two negative regulatory sites in jak2: ser523 and tyr570. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, AML1-ETO in AML, BCR-ABL in AML, FLT3 in AML, Onco-fusion proteins in AML, KIT in AML, EGFR Signaling, EBV infection, Leptin Signaling, Macrophage polarization |
| + |
ERK1/2 | down-regulates
phosphorylation
|
JAK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244553 |
Ser523 |
GVSDVPTsPTLQRPT |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 16705159 |
We hypothesize that phosphorylation of ser523 in jak2 by erks 1 and/or 2 or other as-yet-unidentified kinases acts in a negative feedback manner |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| Pathways: | Acute Myeloid Leukemia, BCR-ABL in AML, FLT3 in AML, KIT in AML, EGFR Signaling, Leptin Signaling |
| + |
MAPK3 | down-regulates
phosphorylation
|
JAK2 |
0.502 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-146747 |
Ser523 |
GVSDVPTsPTLQRPT |
Homo sapiens |
|
| pmid |
sentence |
| 16705159 |
We hypothesize that phosphorylation of ser523 in jak2 by erks 1 and/or 2 or other as-yet-unidentified kinases acts in a negative feedback manner |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK1 | down-regulates
phosphorylation
|
JAK2 |
0.492 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236331 |
Ser523 |
GVSDVPTsPTLQRPT |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 16705159 |
We hypothesize that phosphorylation of ser523 in jak2 by erks 1 and/or 2 or other as-yet-unidentified kinases acts in a negative feedback manner |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
ABL1 | up-regulates activity
phosphorylation
|
JAK2 |
0.42 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-245365 |
Tyr1007 |
VLPQDKEyYKVKEPG |
in vitro |
|
| pmid |
sentence |
| 11593427 |
Jak2 peptide substrate studies indicated that the Bcr-Abl and Abl tyrosine kinases specifically phosphorylated Y1007 of Jak2 but only poorly phosphorylated Y1008. Phosphorylation of Y1007 of Jak2 is known to be critical for its tyrosine kinase activation. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
BCR-ABL | up-regulates activity
phosphorylation
|
JAK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255812 |
Tyr1007 |
VLPQDKEyYKVKEPG |
Mus musculus |
|
| pmid |
sentence |
| 11593427 |
In this report, we show that Bcr–Abl forms a complex with Jak2, and induces tyrosine phosphorylation of Jak2; full phosphorylation requires the SH2 domain of Bcr–Abl. We found that Y1007 of Jak2 was phosphorylated in Bcr–Abl positive cells; phosphorylation of Jak2 Y1007 is known to be required for Jak2 kinase activation. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Acute Myeloid Leukemia, BCR-ABL in AML, Onco-fusion proteins in AML |
| + |
JAK2 |
phosphorylation
|
JAK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251358 |
Tyr1007 |
VLPQDKEyYKVKEPG |
in vitro |
|
| pmid |
sentence |
| 9111318 |
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 |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | Acute Myeloid Leukemia, AML1-ETO in AML, BCR-ABL in AML, FLT3 in AML, Onco-fusion proteins in AML, KIT in AML, EGFR Signaling, EBV infection, Leptin Signaling, Macrophage polarization |
| + |
PTPN1 | down-regulates activity
dephosphorylation
|
JAK2 |
0.789 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248404 |
Tyr1007 |
VLPQDKEyYKVKEPG |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11970898 |
Immunoblots with phospho-specific antibodies confirmed that PTP1B suppresses phosphorylation of the Jak2 activation site tyrosines (Y1007/Y1008) and Stat3 in a dose-dependent manner |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248405 |
Tyr1008 |
LPQDKEYyKVKEPGE |
Homo sapiens |
|
| pmid |
sentence |
| 11970898 |
Immunoblots with phospho-specific antibodies confirmed that PTP1B suppresses phosphorylation of the Jak2 activation site tyrosines (Y1007/Y1008) and Stat3 in a dose-dependent manner |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPRG | down-regulates activity
dephosphorylation
|
JAK2 |
0.291 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254689 |
Tyr1007 |
VLPQDKEyYKVKEPG |
Homo sapiens |
Monocyte |
| pmid |
sentence |
| 25624455 |
Deeper examination shows that JAKs are critically involved in integrin-mediated monocyte adhesion and that PTPRG activation leads to JAK2 dephosphorylation on the critical 1007–1008 phosphotyrosine residues, implying JAK2 inhibition and thus explaining the antiadhesive role of PTPRG. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254690 |
Tyr1008 |
LPQDKEYyKVKEPGE |
Homo sapiens |
Monocyte |
| pmid |
sentence |
| 25624455 |
Deeper examination shows that JAKs are critically involved in integrin-mediated monocyte adhesion and that PTPRG activation leads to JAK2 dephosphorylation on the critical 1007–1008 phosphotyrosine residues, implying JAK2 inhibition and thus explaining the antiadhesive role of PTPRG. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
JAK2 | up-regulates activity
phosphorylation
|
JAK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251357 |
Tyr1007 |
VLPQDKEyYKVKEPG |
in vitro |
|
| pmid |
sentence |
| 9111318 |
Multiple autophosphorylation sites on Jak2, including Y1007 and Y1008. Activation of Jak2 catalytic activity requires phosphorylation of Y1007 in the kinase activation loop. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251360 |
Tyr201 |
DQTPLAIyNSISYKT |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 17027227 |
Site of Jak2 tyrosine autophosphorylation; namely, tyrosine 201. Jak2 tyrosine residue 201 was the principal mediator of SHP-2 binding as conversion of this tyrosine residue to phenylalanine abolished this interaction |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251356 |
Tyr221 |
IRAKIQDyHILTRKR |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15143187 |
JAK2 is autophosphorylated on tyrosines 221 and 1007. tyrosines 221 and 570 in JAK2 may serve as regulatory sites in JAK2, with phosphorylation of tyrosine 221 increasing kinase activity and phosphorylation of tyrosine 570 decreasing kinase activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235885 |
Tyr637 |
KFGSLDTyLKKNKNC |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19364823 |
Analysis of in vitro autophosphorylated jak2while cytokine receptor stimulation mediates the phosphorylation of both tyr317 and tyr637, these residues oppositely regulate jak2-dependent signaling: the mutation of tyr317 enhances jak2 function, suggesting a role for the phosphorylation of tyr317 in the inhibition of jak2. Conversely, mutation of tyr637 reduces jak2 signaling, suggesting a role for the phosphorylation of this residue in the activation of jak2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235910 |
Tyr813 |
NSLFTPDyELLTEND |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15121872 |
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236294 |
Tyr972 |
EYLGTKRyIHRDLAT |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 20304997 |
Tyrosines 868, 966, and 972 in the kinase domain of jak2 are autophosphorylated and required for maximal jak2 kinase activity |
|
| Publications: |
6 |
Organism: |
In Vitro, Chlorocebus Aethiops, Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, AML1-ETO in AML, BCR-ABL in AML, FLT3 in AML, Onco-fusion proteins in AML, KIT in AML, EGFR Signaling, EBV infection, Leptin Signaling, Macrophage polarization |
| + |
PTPN12 | down-regulates activity
dephosphorylation
|
JAK2 |
0.385 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248657 |
Tyr1007 |
VLPQDKEyYKVKEPG |
Homo sapiens |
HC-11 Cell |
| pmid |
sentence |
| 11731619 |
PTP-PEST-Containing Lysates from EGF-Treated HC11 Cells Dephosphorylate JAK2 More Efficiently than Lysates from Control Cells|phospho-JAK2-specific rabbit polyclonal antiserum (44-426, BioSource Technologies, Inc., Camarillo, CA) which recognizes Tyr1007/1008 in the activation site |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248658 |
Tyr1008 |
LPQDKEYyKVKEPGE |
Homo sapiens |
HC-11 Cell |
| pmid |
sentence |
| 11731619 |
PTP-PEST-Containing Lysates from EGF-Treated HC11 Cells Dephosphorylate JAK2 More Efficiently than Lysates from Control Cells|phospho-JAK2-specific rabbit polyclonal antiserum (44-426, BioSource Technologies, Inc., Camarillo, CA) which recognizes Tyr1007/1008 in the activation site |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPN1 | down-regulates
dephosphorylation
|
JAK2 |
0.789 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134955 |
Tyr1007 |
VLPQDKEyYKVKEPG |
Homo sapiens |
|
| pmid |
sentence |
| 15821101 |
Ptp1b has been shown to regulate the activation of cytokine receptors through the dephosphorylation of specific members of the jak family, namely jak2 and tyk2 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-133852 |
Tyr1008 |
LPQDKEYyKVKEPGE |
Homo sapiens |
|
| pmid |
sentence |
| 15780598 |
JAK2 and STAT3 are dephosphorylated by PTP1B in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-135207 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15821101 |
Ptp1b has been shown to regulate the activation of cytokine receptors through the dephosphorylation of specific members of the jak family, namely jak2 and tyk2 |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
IL6ST | up-regulates activity
phosphorylation
|
JAK2 |
0.624 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-238630 |
Tyr1007 |
VLPQDKEyYKVKEPG |
Homo sapiens |
|
| pmid |
sentence |
| 9716487 |
All IL-6-type cytokines recruit gp130to their receptot complexes They either signal via gp130 alone [8] or in combination with LIFR [9] or the recently cloned OSMR [10], which are all able to activate Jaks proteins. Two tyrosine residues at the corresponding positions of Jak2 (tyrosine-1007 and tyrosine-1008) were found to be phosphorylated, and a single mutation of tyrosine-1007 eliminated essentially all tyrosine kinase activity [59]. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-238634 |
Tyr1008 |
LPQDKEYyKVKEPGE |
Homo sapiens |
|
| pmid |
sentence |
| 9716487 |
All IL-6-type cytokines recruit gp130to their receptot complexes They either signal via gp130 alone [8] or in combination with LIFR [9] or the recently cloned OSMR [10], which are all able to activate Jaks proteins. Two tyrosine residues at the corresponding positions of Jak2 (tyrosine-1007 and tyrosine-1008) were found to be phosphorylated, and a single mutation of tyrosine-1007 eliminated essentially all tyrosine kinase activity [59]. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPN11 | up-regulates quantity by stabilization
dephosphorylation
|
JAK2 |
0.786 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248665 |
Tyr1007 |
VLPQDKEyYKVKEPG |
Homo sapiens |
|
| pmid |
sentence |
| 14522994 |
We report that SHP-2 dephosphorylates tyrosine (Tyr-1007) of Jak2 kinase, a critical recruitment site for the ubiquitin ligase-associated inhibitory protein suppressor of cytokine signaling-1 (SOCS-1), thereby contributing to Jak2 stability. Inactivation of SHP-2 function by blocking receptor/SHP-2 association or by using a catalytically inactive mutant of SHP-2 led to a marked increase in Jak2 ubiquitination/degradation, Jak2 phosphorylation on Tyr-1007, and Jak2/SOCS-1 association |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, FLT3 in AML, KIT in AML, EGFR Signaling, Leptin Signaling |
| + |
PTPRC | down-regulates activity
dephosphorylation
|
JAK2 |
0.484 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248348 |
Tyr1007 |
VLPQDKEyYKVKEPG |
Mus musculus |
|
| pmid |
sentence |
| 11201744 |
CD45 is a JAK phosphatase and negatively regulates cytokine receptor signalling|these results show that CD45 dephosphorylates functionally important tyrosine residues. It should be noted that, as with our phosphatase assays in vitro, Tyr 1022 and Tyr 1023 of JAK1, Tyr 1007 and Tyr 1008 of JAK2, and Tyr 1054 and Tyr 1055 of Tyk2 are indeed hyperphosphorylated in cd45-deficient cells |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248349 |
Tyr1008 |
LPQDKEYyKVKEPGE |
Mus musculus |
|
| pmid |
sentence |
| 11201744 |
CD45 is a JAK phosphatase and negatively regulates cytokine receptor signalling|these results show that CD45 dephosphorylates functionally important tyrosine residues. It should be noted that, as with our phosphatase assays in vitro, Tyr 1022 and Tyr 1023 of JAK1, Tyr 1007 and Tyr 1008 of JAK2, and Tyr 1054 and Tyr 1055 of Tyk2 are indeed hyperphosphorylated in cd45-deficient cells |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248347 |
|
|
Mus musculus |
BMMC Cell |
| pmid |
sentence |
| 11201744 |
CD45 is a JAK phosphatase and negatively regulates cytokine receptor signalling |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255679 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24252238 |
Src homology-2 (SH2) containing tyrosine phosphatase and CD45 tyrosine phosphatase play a major role in modulating JAK-STAT pathway. SH2 containing tyrosine phosphatases include SHP1 and SHP2 (shatterproof 1 & 2). Their SH2 domains allow attachment to the phospho-tyrosine residues present on activated receptors, JAKs or STAT proteins, leading to dephosphorylation of the substrates. |
|
| Publications: |
4 |
Organism: |
Mus Musculus, Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, AML1-ETO in AML |
| + |
JAK2 | up-regulates activity
phosphorylation
|
EGFR |
0.599 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251347 |
Tyr1069 |
EDSFLQRySSDPTGA |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 9363897 |
Tyrosine at residue 1,068 of the EGFR is proposed to be one of the principal phosphorylation sites and Grb2-binding sites stimulated by growth hormone via Jak2. Our results indicate that the role of EGFR in signalling by growth hormone is to be phosphorylated by Jak2, thereby providing docking sites for Grb2 and activating MAP kinases and gene expression, independently of the intrinsic tyrosine kinase activity of EGFR.  |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| Pathways: | Acute Myeloid Leukemia, EGFR Signaling |
| + |
JAK2 | up-regulates activity
phosphorylation
|
LEPR |
0.765 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263494 |
Tyr1141 |
SKKTFASyMPQFQTC |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11018044 |
LRb signaling is initiated by leptin binding to the extracellular domain of the LRb dimer, leading to Jak2 transphosphorylation and activation. Activated Jak2 mediates the tyrosine phosphorylation of Tyr985 and Tyr1138of LRb. These phosphotyrosine residues immediately function as binding sites (double-ended lines) for SHP-2 and STAT3, both of which quickly become tyrosine-phosphorylated by Jak2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263493 |
Tyr986 |
QRQPFVKyATLISNS |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11018044 |
LRb signaling is initiated by leptin binding to the extracellular domain of the LRb dimer, leading to Jak2 transphosphorylation and activation. Activated Jak2 mediates the tyrosine phosphorylation of Tyr985 and Tyr1138of LRb. These phosphotyrosine residues immediately function as binding sites (double-ended lines) for SHP-2 and STAT3, both of which quickly become tyrosine-phosphorylated by Jak2. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Leptin Signaling |
| + |
JAK2 | up-regulates activity
phosphorylation
|
CCR2 |
0.601 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251345 |
Tyr139 |
ILLTIDRyLAIVHAV |
Homo sapiens |
|
| pmid |
sentence |
| 9670957 |
JAK2 phosphorylates CCR2 at the Tyr139 position and promotes JAK2/STAT3 complex association to the receptor. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
JAK2 | up-regulates activity
phosphorylation
|
FGF14 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275747 |
Tyr158 |
Y-->S |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 32599005 |
JAK2 regulates Nav1.6 channel function via FGF14Y158 phosphorylation|Patch-clamp electrophysiology revealed that through Y158, JAK2 controls FGF14-dependent modulation of Nav1.6 channels. In hippocampal CA1 pyramidal neurons, the JAK2 inhibitor Fedratinib reduced firing by a mechanism that is dependent upon expression of FGF14. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
JAK2 | up-regulates activity
phosphorylation
|
TET2 |
0.43 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277290 |
Tyr1939 |
CEKYGPDyVPQKSHG |
in vitro |
|
| pmid |
sentence |
| 30944118 |
Specifically, cytokine receptor-associated JAK2 phosphorylates TET2 at tyrosines 1939 and 1964. Phosphorylated TET2 interacts with the erythroid transcription factor KLF1, and this interaction with TET2 is increased upon exposure to erythropoietin. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277289 |
Tyr1964 |
HETSEPTyLRFIKSL |
in vitro |
|
| pmid |
sentence |
| 30944118 |
Specifically, cytokine receptor-associated JAK2 phosphorylates TET2 at tyrosines 1939 and 1964. Phosphorylated TET2 interacts with the erythroid transcription factor KLF1, and this interaction with TET2 is increased upon exposure to erythropoietin. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| Pathways: | Acute Myeloid Leukemia |
| + |
JAK2 | up-regulates quantity by stabilization
phosphorylation
|
CTLA4 |
0.456 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251346 |
Tyr201 |
SPLTTGVyVKMPPTE |
Homo sapiens |
|
| pmid |
sentence |
| 10842319 |
Janus Kinase 2 (Jak2) was directly associated with a box 1-like motif in the cytoplasmic tail of CTLA-4 molecule. Jak2 phosphorylated Y-165 residue in the cytoplasmic region of CTLA-4. It has been reported that phosphorylation and dephosphorylation of tyrosine residue Y-165 in the cytoplasmic region of CTLA-4 play an important role in its negative signaling and cell surface expression. Some signaling molecules such as Src homology 2 protein tyrosine phosphatase 2 (SHP-2) and the p85 subunit of phosphatidylinositol 3 kinase (PI3 kinase) associate with phosphorylated tyrosine residue Y-165, through Src homology 2 (SH2) domains. On the other hand, the adapter complex proteins, AP-2 and AP-50 interact with the same tyrosine residue when unphosphorylated, resulting in clathrin-mediated endocytosis of CTLA-4 molecules. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
JAK2 | up-regulates
phosphorylation
|
JAK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236506 |
Tyr221 |
IRAKIQDyHILTRKR |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15143187 |
Autophosphorylation of jak2 on tyrosines 221 and 570 regulates its activity with phosphorylation of tyrosine 221 increasing kinase activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236298 |
Tyr868 |
GSVEMCRyDPLQDNT |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 20304997 |
Tyrosines 868, 966, and 972 in the kinase domain of jak2 are autophosphorylated and required for maximal jak2 kinase activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236290 |
Tyr966 |
QICKGMEyLGTKRYI |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 20304997 |
Tyrosines 868, 966, and 972 in the kinase domain of jak2 are autophosphorylated and required for maximal jak2 kinase activity |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, AML1-ETO in AML, BCR-ABL in AML, FLT3 in AML, Onco-fusion proteins in AML, KIT in AML, EGFR Signaling, EBV infection, Leptin Signaling, Macrophage polarization |
| + |
JAK2 | up-regulates activity
phosphorylation
|
GTF2I |
0.333 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235313 |
Tyr248 |
EESEDPDyYQYNIQA |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 11313464 |
Jak2 activates tfii-i and regulates its interaction with extracellular signal-regulated kinase the interaction between tfii-i and erk, which is essential for its activity, can be regulated by jak2 through phosphorylation of tfii-i at tyrosine 248 |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
JAK2 | up-regulates activity
phosphorylation
|
STAP2 |
0.349 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249371 |
Tyr250 |
PFLLDEDyEKVLGYV |
|
HEK-293 Cell |
| pmid |
sentence |
| 12540842 |
To examine this possibility, STAP-2 was co-transfected with constitutively active tyrosine kinases in HEK-293 cells. STAP-2 was strongly phosphorylated by various tyrosine kinases, including v-Src (Fig.2 A-a), a JAK2 tyrosine kinase |On the other hand, the phosphorylation levels of Y22F, Y310F, and Y322F by GST-JH1 were reduced to 8060% of the levels of wild-type STAP-2, which suggests that these three are potential phosphorylation sites by activated JAK2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249372 |
Tyr310 |
LPNQEENyVTPIGDG |
|
HEK-293 Cell |
| pmid |
sentence |
| 12540842 |
To examine this possibility, STAP-2 was co-transfected with constitutively active tyrosine kinases in HEK-293 cells. STAP-2 was strongly phosphorylated by various tyrosine kinases, including v-Src (Fig.2 A-a), a JAK2 tyrosine kinase |On the other hand, the phosphorylation levels of Y22F, Y310F, and Y322F by GST-JH1 were reduced to 8060% of the levels of wild-type STAP-2, which suggests that these three are potential phosphorylation sites by activated JAK2. |
|
| Publications: |
2 |
| + |
JAK2 | down-regulates
phosphorylation
|
PRMT5 |
0.68 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-171994 |
Tyr297 |
NRPPPNAyELFAKGY |
Homo sapiens |
|
| pmid |
sentence |
| 21316606 |
Oncogenic jak2 kinases phosphorylate prmt5 in_vivo phosphorylation of prmt5 by jak2v617f greatly impairs its methyltransferase activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
JAK2 | up-regulates activity
phosphorylation
|
PTPN11 |
0.786 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236266 |
Tyr304 |
PNEPVSDyINANIIM |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 8995399 |
Tyrosine residues 304 and 327 in shp-2 are phosphorylated by jaks, and phosphorylated shp-2 can associate with the downstream adapter protein grb2 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236270 |
Tyr327 |
NSKPKKSyIATQGCL |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 8995399 |
Tyrosine residues 304 and 327 in shp-2 are phosphorylated by jaks, and phosphorylated shp-2 can associate with the downstream adapter protein grb2 |
|
| Publications: |
2 |
Organism: |
Chlorocebus Aethiops |
| Pathways: | Acute Myeloid Leukemia, FLT3 in AML, KIT in AML, EGFR Signaling, Leptin Signaling |
| + |
JAK2 | down-regulates
phosphorylation
|
JAK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236502 |
Tyr317 |
TEQDLQLyCDFPNII |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19364823 |
Analysis of in vitro autophosphorylated jak2while cytokine receptor stimulation mediates the phosphorylation of both tyr317 and tyr637, these residues oppositely regulate jak2-dependent signaling: the mutation of tyr317 enhances jak2 function, suggesting a role for the phosphorylation of tyr317 in the inhibition of jak2. Conversely, mutation of tyr637 reduces jak2 signaling, suggesting a role for the phosphorylation of this residue in the activation of jak2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, AML1-ETO in AML, BCR-ABL in AML, FLT3 in AML, Onco-fusion proteins in AML, KIT in AML, EGFR Signaling, EBV infection, Leptin Signaling, Macrophage polarization |
| + |
JAK2 | up-regulates activity
phosphorylation
|
BECN1 |
0.302 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277567 |
Tyr333 |
QRYRLVPyGNHSYLE |
Homo sapiens |
SW-48 Cell |
| pmid |
sentence |
| 34131122 |
Mechanistically, IL-6 triggers the interaction between JAK2 and BECN1, where JAK2 phosphorylates BECN1 at Y333. We demonstrate that BECN1 Y333 phosphorylation is crucial for BECN1 activation and IL-6-induced autophagy by regulating PI3KC3 complex formation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
JAK2 | up-regulates activity
phosphorylation
|
RAF1 |
0.6 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251361 |
Tyr340 |
RGQRDSSyYWEIEAS |
Mus musculus |
CTLL-2 Cell |
| pmid |
sentence |
| 8876196 |
JAK2 phosphorylated Raf-1. e sites at 340/341 are indeed phosphorylated by JAK2 and that this phosphorylation represents a major component of the activation process. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251362 |
Tyr341 |
GQRDSSYyWEIEASE |
Mus musculus |
CTLL-2 Cell |
| pmid |
sentence |
| 8876196 |
JAK2 phosphorylated Raf-1. e sites at 340/341 are indeed phosphorylated by JAK2 and that this phosphorylation represents a major component of the activation process. |
|
| Publications: |
2 |
Organism: |
Mus Musculus |
| + |
JAK2 | up-regulates activity
phosphorylation
|
EPOR |
0.805 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251348 |
Tyr368 |
SEHAQDTyLVLDKWL |
|
|
| pmid |
sentence |
| 12441334 |
JAK2 in turn phosphorylates several tyrosine residues on the EpoR-cytosolic domain and probably on JAK2 itself that serve as docking sites for SH2 or protein tyrosine binding domains of downstream signal transduction proteins such as STAT5, phosphatidylinositol 3-kinase, Shc, and tyrosine phosphatases SHP1 and SHP2 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251349 |
Tyr426 |
ASAASFEyTILDPSS |
|
|
| pmid |
sentence |
| 12441334 |
JAK2 in turn phosphorylates several tyrosine residues on the EpoR-cytosolic domain and probably on JAK2 itself that serve as docking sites for SH2 or protein tyrosine binding domains of downstream signal transduction proteins such as STAT5, phosphatidylinositol 3-kinase, Shc, and tyrosine phosphatases SHP1 and SHP2 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251350 |
Tyr454 |
PTPPHLKyLYLVVSD |
|
|
| pmid |
sentence |
| 12441334 |
JAK2 in turn phosphorylates several tyrosine residues on the EpoR-cytosolic domain and probably on JAK2 itself that serve as docking sites for SH2 or protein tyrosine binding domains of downstream signal transduction proteins such as STAT5, phosphatidylinositol 3-kinase, Shc, and tyrosine phosphatases SHP1 and SHP2 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251351 |
Tyr456 |
PPHLKYLyLVVSDSG |
|
|
| pmid |
sentence |
| 12441334 |
JAK2 in turn phosphorylates several tyrosine residues on the EpoR-cytosolic domain and probably on JAK2 itself that serve as docking sites for SH2 or protein tyrosine binding domains of downstream signal transduction proteins such as STAT5, phosphatidylinositol 3-kinase, Shc, and tyrosine phosphatases SHP1 and SHP2 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251352 |
Tyr468 |
DSGISTDySSGDSQG |
|
|
| pmid |
sentence |
| 12441334 |
JAK2 in turn phosphorylates several tyrosine residues on the EpoR-cytosolic domain and probably on JAK2 itself that serve as docking sites for SH2 or protein tyrosine binding domains of downstream signal transduction proteins such as STAT5, phosphatidylinositol 3-kinase, Shc, and tyrosine phosphatases SHP1 and SHP2 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251353 |
Tyr485 |
GGLSDGPySNPYENS |
|
|
| pmid |
sentence |
| 12441334 |
JAK2 in turn phosphorylates several tyrosine residues on the EpoR-cytosolic domain and probably on JAK2 itself that serve as docking sites for SH2 or protein tyrosine binding domains of downstream signal transduction proteins such as STAT5, phosphatidylinositol 3-kinase, Shc, and tyrosine phosphatases SHP1 and SHP2 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251354 |
Tyr489 |
DGPYSNPyENSLIPA |
|
|
| pmid |
sentence |
| 12441334 |
JAK2 in turn phosphorylates several tyrosine residues on the EpoR-cytosolic domain and probably on JAK2 itself that serve as docking sites for SH2 or protein tyrosine binding domains of downstream signal transduction proteins such as STAT5, phosphatidylinositol 3-kinase, Shc, and tyrosine phosphatases SHP1 and SHP2 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251355 |
Tyr504 |
AEPLPPSyVACS |
|
|
| pmid |
sentence |
| 12441334 |
JAK2 in turn phosphorylates several tyrosine residues on the EpoR-cytosolic domain and probably on JAK2 itself that serve as docking sites for SH2 or protein tyrosine binding domains of downstream signal transduction proteins such as STAT5, phosphatidylinositol 3-kinase, Shc, and tyrosine phosphatases SHP1 and SHP2 |
|
| Publications: |
8 |
| + |
PTPN11 | up-regulates activity
dephosphorylation
|
JAK2 |
0.786 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277037 |
Tyr570 |
VRREVGDyGQLHETE |
Homo sapiens |
|
| pmid |
sentence |
| 30108215 |
Consistently, JAK2/STAT3 signaling was enhanced by overexpression of SHP2 with decreased levels of pJAK2 and increased levels of pJAK2 and pSTAT3 , while it was found suppressed by overexpression of SHP2 (Fig.\u00a06b).|We demonstrate that SHP2 can dephosphorylate JAK2 at Y570 to promote TGF\u03b2-dependent activation of JAK2 and its downstream mediator STAT3 (Supplementary Fig.\u00a04a). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, FLT3 in AML, KIT in AML, EGFR Signaling, Leptin Signaling |
| + |
JAK2 | down-regulates
phosphorylation
|
EZH2 |
0.55 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-202711 |
Tyr641 |
KNEFISEyCGEIISQ |
Homo sapiens |
|
| pmid |
sentence |
| 24469040 |
Oncogenic y641 mutations in ezh2 prevent jak2/beta-trcp-mediated degradationbeta-trcp ubiquitinates ezh2 and jak2-mediated phosphorylation on y641 directs beta-trcp-mediated ezh2 degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia |
| + |
JAK2 | up-regulates
phosphorylation
|
GAB2 |
0.494 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179488 |
Tyr643 |
TSDEKVDyVQVDKEK |
Homo sapiens |
Neutrophil |
| pmid |
sentence |
| 18644434 |
In vitro, activated jak2 directly phosphorylated specific gab2 tyrosine residues. Mutagenesis studies revealed that gab2 tyrosine 643 (y643) was a major target of jak2 in vitro, and a key residue for jak2-dependent phosphorylation in intact cells. Mutation of gab2 y643 inhibited g-csf-stimulated erk1/2 activation and shp2 binding to gab2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
JAK2 | up-regulates
phosphorylation
|
STAT4 |
0.664 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-142736 |
Tyr693 |
TERGDKGyVPSVFIP |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 16324152 |
Janus family tyrosine kinases jak2 and tyk2, which in turn phosphorylate stat4 on tyrosine 693. The p38 mitogen-activated protein kinase (mapk) signaling pathway is also activated in response to il-12, followed by phosphorylation of stat4 on serine 721, which is required for stat4 full transcriptional activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
JAK2 | up-regulates
phosphorylation
|
STAT5A |
0.862 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-56827 |
Tyr694 |
LAKAVDGyVKPQIKQ |
Saccharomyces cerevisiae |
|
| pmid |
sentence |
| 9575217 |
Our mutational analysis suggests that the Stat5 SH2 domain is essential for the interaction with Jak2 and that the kinase domain of Jak2 is sufficient for Jak2-Stat5 interaction. Therefore, the Jak kinase domain may be all that is needed to cause Stat phosphorylation in situations where receptor docking is dispensable. [...] Most obviously, mutation of Tyr694 (Stat5a) or Tyr699 (Stat5b) to phenylalanine abolishes phosphorylation |
|
| Publications: |
1 |
Organism: |
Saccharomyces Cerevisiae |
| Pathways: | Acute Myeloid Leukemia, AML1-ETO in AML, BCR-ABL in AML, FLT3 in AML, Onco-fusion proteins in AML, KIT in AML, Leptin Signaling |
| + |
JAK2 | up-regulates
phosphorylation
|
STAT1 |
0.799 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235709 |
Tyr701 |
DGPKGTGyIKTELIS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 15322115 |
Phosphorylation at tyr701 by the janus family of tyrosine kinases (jak) leads to stat1 dimerization via its src homology 2 domains, exposure of a dimer-specific nuclear localization signal, and subsequent nuclear translocation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256248 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21576360 |
When IFN-γ binds to its receptor, the receptor-associated protein tyrosine kinases Janus kinase I (JAK1) and JAK2 are activated (37). This leads to the phosphorylation of STAT1, which then dimerizes, translocates to the nucleus, and activates its target promoters, including the pIV promoter of Ciita |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255071 |
|
|
|
|
| pmid |
sentence |
| 7888666 |
We found that IL-5 induced two GAS-binding proteins in the nuclear extract from eosinophils. One of them was identified as STAT1 (p91). |
|
| Publications: |
3 |
Organism: |
Homo Sapiens, |
| Tissue: |
Skeletal Muscle |
| Pathways: | EGFR Signaling, EBV infection |
| + |
JAK2 | up-regulates activity
phosphorylation
|
STAT3 |
0.812 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-238638 |
Tyr705 |
DPGSAAPyLKTKFIC |
Homo sapiens |
Hep-G2 Cell |
| pmid |
sentence |
| 9575217 |
Inactive cytoplasmic STATs are recruited to the activated receptor by docking of the STAT SH2 domain to selected receptor tyrosine phosphopeptides, where they are in turn phosphorylated on a single tyrosine by Jak kinases. Has been identified tyrosine 705 of Stat3 as the likely site of phosphorylation by Jak kinases during signal transduction. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236463 |
Tyr705 |
DPGSAAPyLKTKFIC |
Homo sapiens |
Hep-G2 Cell |
| pmid |
sentence |
| 9575217 |
Activation of wild type stat3: il-6 treatment causes stat3 recruitment to receptor tyrosine phosphopeptides (gp130) where it is phosphorylated on tyrosine 705 (y) by jak kinase |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, KIT in AML, EGFR Signaling, EBV infection, Leptin Signaling, Macrophage polarization |
| + |
JAK2 | down-regulates
phosphorylation
|
MAP3K5 |
0.374 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-184600 |
Tyr718 |
IPERDSRySQPLHEE |
Homo sapiens |
|
| pmid |
sentence |
| 19287004 |
Previously we have shown that tyrosine 718 of ask1 when phosphorylated is critical for socs1 binding and socs1-mediated degradation of ask1we identified jak2 and shp2 as a tyr-718-specific kinase and phosphatase, respectively. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
JAK2 | down-regulates quantity by destabilization
phosphorylation
|
MAP3K5 |
0.374 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276145 |
Tyr718 |
IPERDSRySQPLHEE |
Homo sapiens |
Aorta Cell Line |
| pmid |
sentence |
| 19287004 |
Furthermore, JAK2, but not JAK1, directly bound to and phosphorylated ASK1 at Tyr-718, leading to an enhanced association of ASK1 with SOCS1 and subsequent ASK1 degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
JAK2 | up-regulates
phosphorylation
|
ARHGEF1 |
0.332 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163557 |
Tyr738 |
WDQEAQIyELVAQTV |
Homo sapiens |
|
| pmid |
sentence |
| 20098430 |
We found that angiotensin ii activates arhgef1 through a previously undescribed mechanism in which jak2 phosphorylates tyr738 of arhgef1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
JAK2 | up-regulates quantity
phosphorylation
|
ATOH1 |
0.346 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262201 |
Tyr80 |
CTARAAQyLLHSPEL |
Homo sapiens |
DAOY Cell |
| pmid |
sentence |
| 29168692 |
We discovered tyrosine 78 of Atoh1 is phosphorylated by a Jak2-mediated pathway only in tumor-initiating cells and in human SHH-type medulloblastoma. Phosphorylation of tyrosine 78 stabilizes Atoh1, increases Atoh1’s transcriptional activity, and is independent of canonical Jak2 signaling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRJ | down-regulates activity
dephosphorylation
|
JAK2 |
0.329 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277093 |
Tyr813 |
NSLFTPDyELLTEND |
Homo sapiens |
|
| pmid |
sentence |
| 28912580 |
These results support PTPRJ preferentially dephosphorylating Y813 and Y868 in JAK2.|We revealed that PTPRJ negatively regulates leptin signaling by dephosphorylating specific tyrosine residues (Y813 and Y868) in JAK2, the simultaneous phosphorylation of which plays a pivotal role in JAK2 activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277094 |
Tyr868 |
GSVEMCRyDPLQDNT |
Homo sapiens |
|
| pmid |
sentence |
| 28912580 |
These results support PTPRJ preferentially dephosphorylating Y813 and Y868 in JAK2.|We revealed that PTPRJ negatively regulates leptin signaling by dephosphorylating specific tyrosine residues (Y813 and Y868) in JAK2, the simultaneous phosphorylation of which plays a pivotal role in JAK2 activation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia |
| + |
JAK2 | down-regulates activity
phosphorylation
|
PDP1 |
0.267 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276642 |
Tyr94 |
SILKANEySFKVPEF |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 24962578 |
Here we report that phosphorylation at another tyrosine residue, Tyr-94, inhibits PDP1 by reducing the binding ability of PDP1 to lipoic acid, which is covalently attached to the L2 domain of dihydrolipoyl acetyltransferase (E2) to recruit PDP1 to PDC. We found that multiple oncogenic tyrosine kinases directly phosphorylated PDP1 at Tyr-94, and Tyr-94 phosphorylation of PDP1 was common in diverse human cancer cells and primary leukemia cells from patients. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
JAK2 | up-regulates quantity by stabilization
phosphorylation
|
BRD4 |
0.33 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277313 |
Tyr97 |
VKLNLPDyYKIIKTP |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 34290255 |
JAK2 induces tyrosine phosphorylation of BRD4 at Y97/Y98, resulting in BRD4 stabilization. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277312 |
Tyr98 |
KLNLPDYyKIIKTPM |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 34290255 |
JAK2 induces tyrosine phosphorylation of BRD4 at Y97/Y98, resulting in BRD4 stabilization. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
JAK2 | up-regulates activity
phosphorylation
|
IFNGR1 |
0.702 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249490 |
|
|
Homo sapiens |
Macrophage |
| pmid |
sentence |
| 23898330 |
In the classical model of IFNgamma signaling, dimeric IFNgamma cross-links the IFNGR1 receptor subunit that results in allosteric changes in receptor cytoplasmic domain. This results in movement of JAK2 from receptor subunit IFNGR2 to IFNGR1. The JAKs autophosphorylate and then phosphorylate IFNGR1 cytoplasmic domain. This results in binding, phosphorylation, and dimer formation of STAT1_. The dimeric STAT1_ dissociates from receptor and undergoes nuclear translocation via an intrinsic NLS for specific gene activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IL5RA | up-regulates activity
phosphorylation
|
JAK2 |
0.585 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254352 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 7602114 |
Jak 2 is physically associated with the IL-5b receptor. The binding of IL-5 to its receptor results in tyrosine phosphorylation and activation of Jak 2 tyrosine kinase within 1 to 3 min. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
JAK2 | up-regulates activity
phosphorylation
|
ITGAL |
0.272 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254739 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25624455 |
PTKs of the JAK and SRC families have a regulatory role in LFA-1 affinity triggering, with JAKs showing a positive role (3), whereas SRCs possibly have a negative role. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LY2784544 | down-regulates
chemical inhibition
|
JAK2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-193796 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NIN | down-regulates
binding
|
JAK2 |
0.244 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-205581 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25332239 |
We showed that jak2 directly phosphorylates the n-terminus ofnineinwhile the c-terminus ofnineininhibits jak2 kinase activity in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IL23R | up-regulates
binding
|
JAK2 |
0.689 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-87808 |
|
|
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 12023369 |
Il-23 activates the same jak-stat signaling molecules as il-12: jak2, tyk2, and stat1, -3, -4, and -5, but stat4 activation is substantially weaker and different dna-binding stat complexes form in response to il-23 compared with il-12. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSF2RA | up-regulates activity
binding
|
JAK2 |
0.513 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249502 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8977526 |
JAK2 is a primary kinase regulating all the known activities of GM-CSF. JAK2 mediates GM-CSF induced c-fos activation through receptor phosphorylation and Shc/PTP 1D activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN6 | down-regulates activity
dephosphorylation
|
JAK2 |
0.718 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248466 |
|
|
Chlorocebus aethiops |
|
| pmid |
sentence |
| 8943354 |
Direct association with and dephosphorylation of Jak2 kinase by the SH2-domain-containing protein tyrosine phosphatase SHP-1 |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| Pathways: | Acute Myeloid Leukemia, FLT3 in AML |
| + |
ruxolitinib | down-regulates
chemical inhibition
|
JAK2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-206670 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IFNGR1 | up-regulates
binding
|
JAK2 |
0.702 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-135955 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15864272 |
The only type ii ifn, ifn-, binds a distinct cell-surface receptor, which is known as the type ii ifn receptor. This receptor is also composed of two subunits, ifngr1 and ifngr2, which are associated with jak1 and jak2, respectively. Activation of the jaks that are associated with the type i ifn receptor results in tyrosine phosphorylation of stat2 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-150197 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17063185 |
Interferon- (ifn;type ii ifn) induces reorganization of the ifn-receptor subunits, ifngr1 and ifngr2, activating the janus kinases jak1 and jak2, which are constitutively associated with each subunit, respectively |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
JAK2 | up-regulates activity
phosphorylation
|
STAT6 |
0.658 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-62585 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9852261 |
Stat6 activation is mediated through jak1 and jak2 tyrosine kinases. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249532 |
|
|
Homo sapiens |
Macrophage |
| pmid |
sentence |
| 18852293 |
Downstream intracellular signaling from the IL-4IL-4Rc complex involves activation of the Jak1 and Jak3 kinases, phosphorylation of the Stat6 transcription factor, and activation of the insulin receptor substrate (IRS)-2 and Dok2-signaling intermediates. IL-13 initially binds to IL-13R1 with intermediate affinity, and then heterodimerizes with IL-4R. The IL-13IL-13R1IL-4R complex activates the Tyk2, Jak2, and Jak1 kinases and Stat6. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Macrophage polarization |
| + |
tyrphostin B42 | down-regulates activity
chemical inhibition,
|
JAK2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-238542 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11368440 |
The Janus kinase inhibitor, tyrphostine AG490, inhibits STAT3 activation, STAT3 DNA binding, and IL-2Ralpha mRNA and protein expression in parallel |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-238293 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11368440 |
The Janus kinase inhibitor, tyrphostine AG490, inhibits STAT3 activation, STAT3 DNA binding, and IL-2Ralpha mRNA and protein expression in parallel |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
2-[1-ethylsulfonyl-3-[4-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)-1-pyrazolyl]-3-azetidinyl]acetonitrile | down-regulates activity
chemical inhibition
|
JAK2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257832 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20363976 |
INCB028050 is a selective orally bioavailable JAK1/JAK2 inhibitor with nanomolar potency against JAK1 (5.9 nM) and JAK2 (5.7 nM). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SOCS3 | down-regulates activity
binding
|
JAK2 |
0.789 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255329 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24600449 |
The ability of SOCS3 to simultaneously bind to JAK and to the cytokine receptor explains the specificity of the suppression. SOCS3 binds JAK and gp130 receptor simultaneously, using two opposing surfaces: while the phosphotyrosine-binding groove on the SOCS3 SH2 domain is occupied by the gp130 receptor, a subdomain in the SH2 domain of SOCS3 is also required for inhibition of JAK, binding in a phospho-independent manner to a non-canonical surface of JAK2 (58, 59). The KIR of SOCS3 occludes the substrate-binding groove on JAK2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Leptin Signaling |
| + |
JAK2 | up-regulates activity
binding
|
IFNGR2 |
0.688 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249489 |
|
|
Homo sapiens |
Macrophage |
| pmid |
sentence |
| 23898330 |
In the classical model of IFNgamma signaling, dimeric IFNgamma cross-links the IFNGR1 receptor subunit that results in allosteric changes in receptor cytoplasmic domain. This results in movement of JAK2 from receptor subunit IFNGR2 to IFNGR1. The JAKs autophosphorylate and then phosphorylate IFNGR1 cytoplasmic domain. This results in binding, phosphorylation, and dimer formation of STAT1_. The dimeric STAT1_ dissociates from receptor and undergoes nuclear translocation via an intrinsic NLS for specific gene activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
JAK2 | up-regulates
phosphorylation
|
STAT5B |
0.861 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-56894 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9575217 |
Jak2 kinase induces tyrosine phosphorylation, dimerization, nuclear translocation, and dna binding of a concomitantly expressed stat5 protein |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
JAK2 | up-regulates activity
phosphorylation
|
CSF2RA/CSF2RB |
0.568 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255584 |
|
|
Homo sapiens |
Monocyte |
| pmid |
sentence |
| 19436055 |
The GM-CSF receptor does not have intrinsic tyrosine kinase activity, but associates with the tyrosine kinase Jak2 that is required for βc transphosphorylation and the initiation of signaling and biological activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256001 |
|
|
Homo sapiens |
Macrophage |
| pmid |
sentence |
| 8977526 |
JAK2 is a primary kinase regulating all the known activities of GM-CSF. JAK2 mediates GM-CSF induced c-fos activation through receptor phosphorylation and Shc/PTP 1D activation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Skeletal Muscle |
| Pathways: | Acute Myeloid Leukemia, BCR-ABL in AML |
| + |
AZ 960 | down-regulates
chemical inhibition
|
JAK2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-190128 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ruxolitinib phosphate | down-regulates activity
chemical inhibition
|
JAK2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259171 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23061804 |
Ruxolitinib is a selective inhibitor of Janus kinases (JAK) 1 and 2, which are involved in the signalling pathway of various cytokines and growth factors essential to haematopoiesis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
JAK2 | up-regulates activity
phosphorylation
|
ITGB2 |
0.268 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254738 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25624455 |
PTKs of the JAK and SRC families have a regulatory role in LFA-1 affinity triggering, with JAKs showing a positive role (3), whereas SRCs possibly have a negative role. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IFNGR2 | up-regulates activity
binding
|
JAK2 |
0.688 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249504 |
|
|
Homo sapiens |
Macrophage |
| pmid |
sentence |
| 23898330 |
In the classical model of IFNgamma signaling, dimeric IFNgamma cross-links the IFNGR1 receptor subunit that results in allosteric changes in receptor cytoplasmic domain. This results in movement of JAK2 from receptor subunit IFNGR2 to IFNGR1. The JAKs autophosphorylate and then phosphorylate IFNGR1 cytoplasmic domain. This results in binding, phosphorylation, and dimer formation of STAT1_. The dimeric STAT1_ dissociates from receptor and undergoes nuclear translocation via an intrinsic NLS for specific gene activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EGFR | up-regulates activity 
|
JAK2 |
0.599 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235870 |
|
|
Mus musculus |
Keratinocyte |
| pmid |
sentence |
| 15284024 |
Two possibilities for STAT activation exist: a janus kinase (JAK)-dependent and a JAK-independent mechanism. Herein, we demonstrate that EGFR overexpression in primary esophageal keratinocytes activates STAT in a JAK-dependent fashion |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Acute Myeloid Leukemia, EGFR Signaling |
| + |
AT9283 | down-regulates
chemical inhibition
|
JAK2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-190017 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSF2RA | up-regulates
|
JAK2 |
0.513 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-46334 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9028317 |
We show that the amount of jak2 physically associated with gm-csfr beta chain is increased after gm-csf stimulation and that gm-csf triggers both beta chain and jak2 tyrosine phosphorylation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
JAK2 | up-regulates activity
phosphorylation
|
IFNGR2/INFGR1 |
0.695 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249493 |
|
|
Homo sapiens |
Macrophage |
| pmid |
sentence |
| 23898330 |
In the classical model of IFNgamma signaling, dimeric IFNgamma cross-links the IFNGR1 receptor subunit that results in allosteric changes in receptor cytoplasmic domain. This results in movement of JAK2 from receptor subunit IFNGR2 to IFNGR1. The JAKs autophosphorylate and then phosphorylate IFNGR1 cytoplasmic domain. This results in binding, phosphorylation, and dimer formation of STAT1_. The dimeric STAT1_ dissociates from receptor and undergoes nuclear translocation via an intrinsic NLS for specific gene activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EBV infection, Macrophage polarization |
| + |
N-tert-butyl-3-[[5-methyl-2-[4-[2-(1-pyrrolidinyl)ethoxy]anilino]-4-pyrimidinyl]amino]benzenesulfonamide | down-regulates activity
chemical inhibition
|
JAK2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258301 |
|
|
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 |
| + |
LEPR | up-regulates activity
binding
|
JAK2 |
0.765 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263491 |
|
|
Homo sapiens |
HT-1080 Cell |
| pmid |
sentence |
| 18718905 |
Janus kinase 2 (JAK2) is associated with LEPRb and autophosphorylates in response to leptin. JAK2 also phosphorylates LEPRb, STAT3, and multiple other downstream molecules. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Leptin Signaling |
| + |
JAK2 | up-regulates activity
|
APOA1 |
0.303 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252107 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14668333 |
ApoA-I interactions with ABCA1 and lipid efflux to apoA-I were substantially impaired by inhibiting or abolishing JAK2, whereas ABCA1 protein levels were unaffected, and ABCA1 cholesterol translocase activity was only slightly reduced. The most likely explanation for these findings is that JAK2 promotes apolipoprotein interactions with ABCA1 or a closely proximal site, and this facilitates the removal of cellular lipids. the interaction of apolipoproteins with ABCA1-expressing cells activates JAK2, which in turn activates a process that enhances apolipoprotein interactions with ABCA1 and lipid removal from cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
APOA1 | up-regulates activity
|
JAK2 |
0.303 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252108 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14668333 |
ApoA-I Stimulates JAK2 Autophosphorylation. the interaction of apolipoproteins with ABCA1-expressing cells activates JAK2, which in turn activates a process that enhances apolipoprotein interactions with ABCA1 and lipid removal from cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SOCS1 | down-regulates quantity by destabilization
ubiquitination
|
JAK2 |
0.787 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-118407 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14522994 |
Shp-2 regulates socs-1-mediated janus kinase-2 ubiquitination/degradation downstream of the prolactin receptor |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Macrophage polarization |
| + |
IFNGR1 | up-regulates activity
binding
|
JAK2 |
0.702 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249505 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23898330 |
In the classical model of IFNgamma signaling, dimeric IFNgamma cross-links the IFNGR1 receptor subunit that results in allosteric changes in receptor cytoplasmic domain. This results in movement of JAK2 from receptor subunit IFNGR2 to IFNGR1. The JAKs autophosphorylate and then phosphorylate IFNGR1 cytoplasmic domain. This results in binding, phosphorylation, and dimer formation of STAT1_. The dimeric STAT1_ dissociates from receptor and undergoes nuclear translocation via an intrinsic NLS for specific gene activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
KIT | up-regulates activity
binding
|
JAK2 |
0.597 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254954 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15526160 |
C-Kit stimulates rapid and transient tyrosine phosphorylation of JAK2. JAK2 was found to be constitutively associated with c-Kit, with increased association after ligand stimulation of c-Kit |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, Onco-fusion proteins in AML, KIT in AML |
| + |
PTPN12 | down-regulates
dephosphorylation
|
JAK2 |
0.385 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-112383 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11731619 |
In intact hc11 cells, ptp-pest was constitutively associated with jak2, and in response to egf treatment there was an increased level of ptp-pest in jak2 complexes. An in vitro phosphatase assay, using prl-activated jak2 as the substrate and lysates from hc11 cells as the source of ptp-pest, revealed that jak2 could serve as a ptp-pest substrate. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SH2B3 | down-regulates activity
binding
|
JAK2 |
0.63 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260075 |
|
|
Mus musculus |
32D Cell |
| pmid |
sentence |
| 18618018 |
we identified Lnk as a physiological negative regulator of JAK2 in stem cells and TPO/Mpl/JAK2/Lnk as a major regulatory pathway in controlling stem cell self-renewal and quiescence. we identify a direct interaction between Lnk and the Mpl/JAK2 complex that regulates various HSC functions. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Acute Myeloid Leukemia, KIT in AML |
| + |
IL3RA | up-regulates
binding
|
JAK2 |
0.598 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134859 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15795318 |
Indeed, only upon fibronectin adhesion is janus kinase 2 (jak2) recruited to the beta1 integrin-il-3r complex and triggers il-3r beta common phosphorylation, leading to the formation of docking sites for activated stat5a. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
JAK2 | up-regulates activity
phosphorylation
|
STAT5A |
0.862 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249507 |
|
|
Homo sapiens |
Macrophage |
| pmid |
sentence |
| 9575217 |
Jak2 kinase induces tyrosine phosphorylation, dimerization, nuclear translocation, and dna binding of a concomitantly expressed stat5 protein |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, AML1-ETO in AML, BCR-ABL in AML, FLT3 in AML, Onco-fusion proteins in AML, KIT in AML, Leptin Signaling |
| + |
N-(cyanomethyl)-4-[2-[4-(4-morpholinyl)anilino]-4-pyrimidinyl]benzamide | down-regulates
chemical inhibition
|
JAK2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-191247 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IL10RA | up-regulates activity
phosphorylation
|
JAK2 |
0.419 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249545 |
|
|
Homo sapiens |
Macrophage |
| pmid |
sentence |
| 26260587 |
IL10R2 recruits cytoplasmic protein Jak1 followed by phosphorylation of tyrosine at position 705 in the STAT3 (705Y-STAT3) molecule. Phosphorylated STAT3 forms a homodimer, which is then translocated to the nucleus to facilitate transcriptional regulation of target genes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Macrophage polarization |
| + |
TG101209 | down-regulates
chemical inhibition
|
JAK2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-207263 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IL31RA | up-regulates
binding
|
JAK2 |
0.39 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161430 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18926762 |
Il-31 can activate janus kinase (jak) 1 and jak2 signaling molecules after binding to its receptor complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IFNGR2/INFGR1 | up-regulates activity
binding
|
JAK2 |
0.695 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249506 |
|
|
Homo sapiens |
Macrophage |
| pmid |
sentence |
| 23898330 |
In the classical model of IFNgamma signaling, dimeric IFNgamma cross-links the IFNGR1 receptor subunit that results in allosteric changes in receptor cytoplasmic domain. This results in movement of JAK2 from receptor subunit IFNGR2 to IFNGR1. The JAKs autophosphorylate and then phosphorylate IFNGR1 cytoplasmic domain. This results in binding, phosphorylation, and dimer formation of STAT1_. The dimeric STAT1_ dissociates from receptor and undergoes nuclear translocation via an intrinsic NLS for specific gene activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EBV infection, Macrophage polarization |
| + |
LSM-1231 | down-regulates activity
chemical inhibition
|
JAK2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258237 |
|
|
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 |
| + |
JAK2 | down-regulates activity
relocalization
|
SLC6A8 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265807 |
|
|
Xenopus laevis laevis |
Oocyte |
| pmid |
sentence |
| 22407360 |
Janus-activated kinase-2 (JAK2) participates in the regulation of the Na⁺-coupled glucose transporter SGLT1 and the Na⁺-coupled amino acid transporter SLC6A19. JAK2 is a novel regulator of the creatine transporter SLC6A8, which downregulates the carrier, presumably by interference with carrier protein insertion into the cell membrane. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265781 |
|
|
Xenopus laevis laevis |
Oocyte |
| pmid |
sentence |
| 22407360 |
Janus-activated kinase-2 (JAK2) participates in the regulation of the Na⁺-coupled glucose transporter SGLT1 and the Na⁺-coupled amino acid transporter SLC6A19. JAK2 is a novel regulator of the creatine transporter SLC6A8, which downregulates the carrier, presumably by interference with carrier protein insertion into the cell membrane. |
|
| Publications: |
2 |
Organism: |
Xenopus Laevis Laevis |
| + |
IL6R | up-regulates activity
phosphorylation
|
JAK2 |
0.552 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254405 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23869758 |
On binding of IL-6 to its receptor IL-6R, JAK2 is phosphorylated, then STAT3 is phosphorylated by JAK2 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IL4R | up-regulates activity
phosphorylation
|
JAK2 |
0.608 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249530 |
|
|
Homo sapiens |
Macrophage |
| pmid |
sentence |
| 18852293 |
Downstream intracellular signaling from the IL-4IL-4Rc complex involves activation of the Jak1 and Jak3 kinases, phosphorylation of the Stat6 transcription factor, and activation of the insulin receptor substrate (IRS)-2 and Dok2-signaling intermediates. IL-13 initially binds to IL-13R1 with intermediate affinity, and then heterodimerizes with IL-4R. The IL-13IL-13R1IL-4R complex activates the Tyk2, Jak2, and Jak1 kinases and Stat6. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Macrophage polarization |
| + |
JAK2 | up-regulates quantity by expression
transcriptional regulation
|
MYC |
0.464 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255811 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 12370803 |
In this study, we show that Jak2 is involved in c-Myc induction by inducing c-MYC mRNA and protecting c-Myc protein from 26S proteasome-dependent degradation. These results indicate that c-Myc is a downstream target of activated Jak2 in Bcr-Abl positive cells. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Acute Myeloid Leukemia, AML1-ETO in AML, BCR-ABL in AML, FLT3 in AML, KIT in AML, EGFR Signaling |
| + |
JAK2 | up-regulates
phosphorylation
|
STAM |
0.604 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-47834 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9133424 |
Stam is associated with jak3 and jak2 tyrosine kinases via its itam region and phosphorylated by jak3 and jak2 upon stimulation with il-2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DAB2IP | down-regulates activity
binding
|
JAK2 |
0.357 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254760 |
|
|
Homo sapiens |
Vascular Smooth Muscle Cell Line |
| pmid |
sentence |
| 27858941 |
In vascular smooth muscle cells (VSMCs) treated with IFN-γ, DAB2IP directly binds to JAK2 and inhibits its kinase activity, limiting JAK-dependent STAT1/3 and PI3K–AKT phosphorylation and activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
JAK2 | up-regulates quantity by stabilization
binding
|
MYC |
0.464 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255810 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 12370803 |
In this study, we show that Jak2 is involved in c-Myc induction by inducing c-MYC mRNA and protecting c-Myc protein from 26S proteasome-dependent degradation. These results indicate that c-Myc is a downstream target of activated Jak2 in Bcr-Abl positive cells. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Acute Myeloid Leukemia, AML1-ETO in AML, BCR-ABL in AML, FLT3 in AML, KIT in AML, EGFR Signaling |
| + |
JAK2 | up-regulates activity
phosphorylation
|
CSF2RA |
0.513 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249503 |
|
|
Homo sapiens |
Macrophage |
| pmid |
sentence |
| 8977526 |
JAK2 is a primary kinase regulating all the known activities of GM-CSF. JAK2 mediates GM-CSF induced c-fos activation through receptor phosphorylation and Shc/PTP 1D activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Gbeta | down-regulates
phosphorylation
|
JAK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270046 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16705159 |
We hypothesize that phosphorylation of ser523 in jak2 by erks 1 and/or 2 or other as-yet-unidentified kinases acts in a negative feedback manner |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SH2B1 | up-regulates activity
binding
|
JAK2 |
0.679 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253078 |
|
|
|
|
| pmid |
sentence |
| 27154742 |
The SH2B adaptor protein 1 (SH2B1) is a key regulator of leptin, as it enhances leptin signalling by both stimulating Janus kinase 2 (JAK2) activity and assembling a JAK2/IRS1/2 signalling complex |
|
| Publications: |
1 |
| Pathways: | Leptin Signaling |
| + |
NVP-BSK805 dihydrochloride | down-regulates
chemical inhibition
|
JAK2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-194934 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
JAK2 | up-regulates activity
phosphorylation
|
STAT1/STAT3 |
0.806 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254999 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15526160 |
Downstream of JAKs are the signal transducers and activators of transcription (STATs), which are phosphorylated by JAKs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
N-tert-butyl-3-[[5-methyl-2-[4-[2-(1-pyrrolidinyl)ethoxy]anilino]-4-pyrimidinyl]amino]benzenesulfonamide | down-regulates
chemical inhibition
|
JAK2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-207239 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ruxolitinib | down-regulates activity
chemical inhibition
|
JAK2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258277 |
|
|
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 |
| + |
erlotinib hydrochloride | down-regulates
chemical inhibition
|
JAK2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-151274 |
|
|
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 17178722 |
This study shows that the anti-cancer drug erlotinib (tarceva) is a potent inhibitor of jak2(v617f) activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DENR | up-regulates quantity by expression
transcriptional regulation
|
JAK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269675 |
|
|
Mus musculus |
MC-38 Cell |
| pmid |
sentence |
| 35440133 |
DENR directly regulates JAK2 expression. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
AZD1480 | down-regulates
chemical inhibition
|
JAK2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-190167 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AML1-ETO | down-regulates quantity by repression 
transcriptional regulation
|
JAK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260120 |
|
|
Mus musculus |
Leukemia Cell |
| pmid |
sentence |
| 22740448 |
Chromosome translocation 8q22;21q22 [t(8;21)] is commonly associated with acute myeloid leukemia (AML), and the resulting AML1-ETO fusion proteins are involved in the pathogenesis of AML. To identify novel molecular and therapeutic targets, we performed combined gene expression microarray and promoter occupancy (ChIP-chip) profiling using Lin(-)/Sca1(-)/cKit(+) cells, the major leukemia cell population, from an AML mouse model induced by AML1-ETO9a (AE9a).CD45, a protein tyrosine phosphatase and a negative regulator of cytokine/growth factor receptor and JAK/STAT signaling, is among those targets. Its expression is substantially down-regulated in leukemia cells. Consequently, JAK/STAT signaling is enhanced. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Acute Myeloid Leukemia, AML1-ETO in AML, Onco-fusion proteins in AML |
3.0
JAK2
- 
- 