| + |
BTK | up-regulates 
phosphorylation
|
ITK |
0.469 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-98036 |
Tyr180 |
ETVVIALyDYQTNDP |
Homo sapiens |
|
| pmid |
sentence |
| 12573241 |
Tec family protein tyrosine kinases (tfks) play a central role in hematopoietic cellular signaling. Initial activation takes place through specific tyrosine phosphorylation situated in the activation loop. Further activation occurs within the sh3 domain via a transphosphorylation mechanismthe major phosphorylation sites were identified as conserved tyrosines, for itk y180 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ITK | up-regulates activity
phosphorylation
|
ITK |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-103170 |
Tyr180 |
ETVVIALyDYQTNDP |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 12842872 |
In this study, we present evidence for another mode of regulation for itk, the autophosphorylation of tyr-180 in the src homology 3 (sh3) domain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ITK | up-regulates
phosphorylation
|
CD28 |
0.675 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-45512 |
Tyr191 |
SRLLHSDyMNMTPRR |
Homo sapiens |
T-lymphocyte, Leukemia Cell |
| pmid |
sentence |
| 8992971 |
We demonstrate that emt can phosphorylate all four tyrosines of the cd28 tail, in contrast to lck, which phosphorylates only tyrosine 173. Together with evidence that in vivo, tyrosines other than tyrosine 173 become phosphorylated following cd28 stimulation, this finding suggests that, like lck, one function of emt during cd28 signaling is phosphorylation of the receptor |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-198747 |
Tyr191 |
SRLLHSDyMNMTPRR |
Homo sapiens |
|
| pmid |
sentence |
| 22936936 |
We demonstrate that emt can phosphorylate all four tyrosines of the cd28 tail, in contrast to lck, which phosphorylates only tyrosine 173. Together with evidence that in vivo, tyrosines other than tyrosine 173 become phosphorylated following cd28 stimulation, this finding suggests that, like lck, one function of emt during cd28 signaling is phosphorylation of the receptor |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-198751 |
Tyr209 |
TRKHYQPyAPPRDFA |
Homo sapiens |
JURKAT Cell |
| pmid |
sentence |
| 22936936 |
We demonstrate that emt can phosphorylate all four tyrosines of the cd28 tailother studies demonstrated that tyr191 within the p190yap motif is one of two major phosphorylation sites in cd28-stimulated jurkat t cells, and the only tyrosine residue within the cd28 cytoplasmic tail that is essential for delivery of costimulatory signals |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-45516 |
Tyr209 |
TRKHYQPyAPPRDFA |
Homo sapiens |
T-lymphocyte, Leukemia Cell |
| pmid |
sentence |
| 8992971 |
We demonstrate that emt can phosphorylate all four tyrosines of the cd28 tailother studies demonstrated that tyr191 within the p190yap motif is one of two major phosphorylation sites in cd28-stimulated jurkat t cells, and the only tyrosine residue within the cd28 cytoplasmic tail that is essential for delivery of costimulatory signals |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-45520 |
Tyr218 |
PPRDFAAyRS |
Homo sapiens |
T-lymphocyte, Leukemia Cell |
| pmid |
sentence |
| 8992971 |
We demonstrate that emt can phosphorylate all four tyrosines of the cd28 tail |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| + |
ITK | up-regulates activity
phosphorylation
|
CD28 |
0.675 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251336 |
Tyr191 |
SRLLHSDyMNMTPRR |
|
|
| pmid |
sentence |
| 8992971 |
EMT can phosphorylate all four tyrosines of the CD28 tail. in vivo, tyrosines other than tyrosine 173 become phosphorylated following CD28 stimulation, this finding suggests that, like LCK, one function of EMT during CD28 signaling is phosphorylation of the receptor. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251334 |
Tyr206 |
PGPTRKHyQPYAPPR |
|
|
| pmid |
sentence |
| 8992971 |
EMT can phosphorylate all four tyrosines of the CD28 tail. in vivo, tyrosines other than tyrosine 173 become phosphorylated following CD28 stimulation, this finding suggests that, like LCK, one function of EMT during CD28 signaling is phosphorylation of the receptor. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251337 |
Tyr218 |
PPRDFAAyRS |
|
|
| pmid |
sentence |
| 8992971 |
EMT can phosphorylate all four tyrosines of the CD28 tail. in vivo, tyrosines other than tyrosine 173 become phosphorylated following CD28 stimulation, this finding suggests that, like LCK, one function of EMT during CD28 signaling is phosphorylation of the receptor. |
|
| Publications: |
3 |
| + |
ITK | up-regulates
phosphorylation
|
TEC |
0.376 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-98090 |
Tyr206 |
RLERGQEyLILEKND |
Homo sapiens |
|
| pmid |
sentence |
| 12573241 |
Tec family protein tyrosine kinases (tfks) play a central role in hematopoietic cellular signaling. Initial activation takes place through specific tyrosine phosphorylation situated in the activation loop. Further activation occurs within the sh3 domain via a transphosphorylation mechanism. Here, we could confirm that y223 is the only site in the btk-sh3 domain being detectably phosphorylated |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ITK | up-regulates activity
phosphorylation
|
BMX |
0.339 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251331 |
Tyr216 |
SSTSLAQyDSNSKKI |
in vitro |
|
| pmid |
sentence |
| 12573241 |
Itk phosphorylated Bmx-SH3 to a low extent. pY positions correspond to the residues Y215 and Y223 in Bmx. Tec family protein tyrosine kinases (TFKs) play a central role in hematopoietic cellular signaling. Initial activation takes place through specific tyrosine phosphorylation situated in the activation loop. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251332 |
Tyr224 |
DSNSKKIyGSQPNFN |
in vitro |
|
| pmid |
sentence |
| 12573241 |
Itk phosphorylated Bmx-SH3 to a low extent. pY positions correspond to the residues Y215 and Y223 in Bmx. Tec family protein tyrosine kinases (TFKs) play a central role in hematopoietic cellular signaling. Initial activation takes place through specific tyrosine phosphorylation situated in the activation loop. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
ITK | down-regulates activity 
phosphorylation
|
BTK |
0.469 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251333 |
Tyr223 |
LKKVVALyDYMPMNA |
in vitro |
|
| pmid |
sentence |
| 12573241 |
Btk-SH3 mutant Y223A was not phosphorylated by Itk. Tec family protein tyrosine kinases (TFKs) play a central role in hematopoietic cellular signaling. Initial activation takes place through specific tyrosine phosphorylation situated in the activation loop.|In Btk, the SH3 domain mutation Y223F results in enhanced fibroblast transformation, implying that the SH3 domain may play a negative regulatory role |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ITK | up-regulates activity
phosphorylation
|
HAVCR2 |
0.318 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273644 |
Tyr265 |
IRSEENIyTIEENVY |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 17069754 |
When we tested the effect of ITK on the Y265 mutant, we found a pronounced reduction of ITK-mediated tyrosine phosphorylation, suggesting that Y265 is specifically phosphorylated by ITK (Fig. 3B). Our results demonstrate that specific phosphorylation of Y265 of Tim-3 occurs in the presence of galectin-9, probably through a receptor-ligand interaction. Phosphorylation of Y265, which is situated in a highly conserved SH2 binding domain, could result in the recruitment of SH2 containing adaptor proteins and trigger downstream signalling events regulating the fate of Tim-3 expressing T-cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LCK | up-regulates
phosphorylation
|
ITK |
0.529 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251380 |
Tyr512 |
RFVLDDQyTSSTGTK |
in vitro |
|
| pmid |
sentence |
| 9312162 |
Lck phosphorylates the activation loop tyrosine of the Itk kinase domain and activates Itk kinase activity. The major site of Lck phosphorylation on Itk was mapped to the conserved tyrosine (Tyr511) in the activation loop of the Itk kinase domain. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ITK | up-regulates
phosphorylation
|
SIGLEC10 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-112471 |
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-112475 |
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 |
| + |
pazopanib hydrochloride | down-regulates activity
chemical inhibition
|
ITK |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259164 |
|
|
in vitro |
|
| pmid |
sentence |
| 17620431 |
Pazopanib inhibition of a number of kinases outside of the VEGFR family was also determined. These included Abl1; Akt3; activin-like kinase 6; cyclin-dependent kinase 1/cyclin A; cyclin-dependent kinase 2/cyclin A; c-fms; c-Kit; epidermal growth factor receptor; ErbB2; ErbB4; EphB4; focal adhesion kinase; FGF receptors (FGFR) 1, 2, and 3; Flt-3; glycogen synthase kinase 3; insulin-like growth factor type I receptor; insulin receptor; interleukin-2–inducible T-cell kinase; c-jun NH2-terminal kinases 1, 2, and 3; lymphocyte-specific protein tyrosine kinase (murine); Met; p38α; PDGFRα and PDGFRβ; protein kinase C-β1 and -β2; polo-like kinases 1 and 3; Ret; Src; Syk; Tie-2; and Wee1. All assays were conducted using purified, recombinantly expressed catalytic domains of the kinases. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ITK | up-regulates
phosphorylation
|
PLCG1 |
0.617 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-165803 |
|
|
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 20519342 |
In t cells, the predominant tec kinase is itk, which functions downstream of the t-cell receptor to regulate phospholipase c-gamma. |
|
| 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
|
ITK |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262236 |
|
|
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 |
3.0
ITK
- 
- 