| + |
MAPK3 | down-regulates 
phosphorylation
|
LAT |
0.305 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-125770 |
Thr184 |
PSAPALStPGIRDSA |
Homo sapiens |
|
| pmid |
sentence |
| 15192708 |
Lat, an adapter protein essential for t-cell signaling, is phosphorylated at its thr 155 by erk in response to t-cell receptor stimulation. Thr 155 phosphorylation reduces the ability of lat to recruit plcgamma1 and slp76, leading to attenuation of subsequent downstream events such as [ca2+]i mobilization and activation of the erk pathway. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK8 | down-regulates
phosphorylation
|
LAT |
0.309 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-125774 |
Thr184 |
PSAPALStPGIRDSA |
Homo sapiens |
|
| pmid |
sentence |
| 15192708 |
Lat, an adapter protein essential for t-cell signaling, is phosphorylated at its thr 155 by erk in response to t-cell receptor stimulation. Thr 155 phosphorylation reduces the ability of lat to recruit plcgamma1 and slp76, leading to attenuation of subsequent downstream events such as [ca2+]i mobilization and activation of the erk pathway.Mutational analysis revealed that t155 but not t94 or t140 is the site of jnk-mediated phosphorylation (figure 2b). Erk also phosphorylated lat at t155 (figure 2c), whereas p38, which was able to phosphorylate atf2, failed to induce threonine phosphorylation of lat (figure 2d). These results indicate that lat is directly phosphorylated by erk and jnk at the same site, t155. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ZAP70 | up-regulates activity 
phosphorylation
|
LAT |
0.775 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274561 |
Tyr 132 |
DYHNPGyLVVLPD |
Homo sapiens |
|
| pmid |
sentence |
| 29915297 |
In the presence of the catalytically inactive LckK273R, the phosphorylation of LAT Y132 and Y191 residues by Zap70K362E were considerably increased |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247018 |
Tyr156 |
ADEDEDDyHNPGYLV |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 11368773 |
In the present study we reconstituted the LAT signalling pathway by demonstrating that a direct tyrosine phosphorylation of LAT with activated protein-tyrosine kinase Zap70 is necessary and sufficient for the association and activation of signalling proteins. Zap-70 efficiently phosphorylates LAT on tyrosine residues at positions 226, 191, 171, 132 and 127. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247022 |
Tyr161 |
DDYHNPGyLVVLPDS |
Homo sapiens |
|
| pmid |
sentence |
| 11368773 |
In the present study we reconstituted the LAT signalling pathway by demonstrating that a direct tyrosine phosphorylation of LAT with activated protein-tyrosine kinase Zap70 is necessary and sufficient for the association and activation of signalling proteins. Zap-70 efficiently phosphorylates LAT on tyrosine residues at positions 226, 191, 171, 132 and 127. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274562 |
Tyr191 |
LDGSREyVNVSQE |
Homo sapiens |
|
| pmid |
sentence |
| 29915297 |
In the presence of the catalytically inactive LckK273R, the phosphorylation of LAT Y132 and Y191 residues by Zap70K362E were considerably increased |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247026 |
Tyr200 |
SMESIDDyVNVPESG |
Homo sapiens |
|
| pmid |
sentence |
| 11368773 |
In the present study we reconstituted the LAT signalling pathway by demonstrating that a direct tyrosine phosphorylation of LAT with activated protein-tyrosine kinase Zap70 is necessary and sufficient for the association and activation of signalling proteins. Zap-70 efficiently phosphorylates LAT on tyrosine residues at positions 226, 191, 171, 132 and 127. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247030 |
Tyr220 |
SLDGSREyVNVSQEL |
Homo sapiens |
|
| pmid |
sentence |
| 11368773 |
In the present study we reconstituted the LAT signalling pathway by demonstrating that a direct tyrosine phosphorylation of LAT with activated protein-tyrosine kinase Zap70 is necessary and sufficient for the association and activation of signalling proteins. Zap-70 efficiently phosphorylates LAT on tyrosine residues at positions 226, 191, 171, 132 and 127. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247034 |
Tyr255 |
EEEGAPDyENLQELN |
Homo sapiens |
|
| pmid |
sentence |
| 11368773 |
In the present study we reconstituted the LAT signalling pathway by demonstrating that a direct tyrosine phosphorylation of LAT with activated protein-tyrosine kinase Zap70 is necessary and sufficient for the association and activation of signalling proteins. Zap-70 efficiently phosphorylates LAT on tyrosine residues at positions 226, 191, 171, 132 and 127. |
|
| Publications: |
7 |
Organism: |
Homo Sapiens |
| Pathways: | T cell activation |
| + |
LCK | up-regulates
phosphorylation
|
LAT |
0.762 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149182 |
Tyr200 |
SMESIDDyVNVPESG |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 16938345 |
Evidence of lat as a dual substrate for lck and syk in t lymphocytes.Lat is a linker protein essential for activation of t lymphocytes. Its rapid tyrosine-phosphorylation upon t cell receptor (tcr) stimulation recruits downstream signaling molecules for membrane targeting and activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149186 |
Tyr220 |
SLDGSREyVNVSQEL |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 16938345 |
Evidence of lat as a dual substrate for lck and syk in t lymphocytes.Lat is a linker protein essential for activation of t lymphocytes. Its rapid tyrosine-phosphorylation upon t cell receptor (tcr) stimulation recruits downstream signaling molecules for membrane targeting and activation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | T cell activation |
| + |
FYN | up-regulates
phosphorylation
|
LAT |
0.751 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149174 |
Tyr200 |
SMESIDDyVNVPESG |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 16938345 |
Both lck and syk, phosphorylate the itam-like motifs on lat at y171y191, which is essential for induction of the interaction of lat with downstream signaling molecules such as grb2, plc-gamma1 and c-cbl, and for activation of mapk-erk. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-148931 |
Tyr220 |
SLDGSREyVNVSQEL |
Homo sapiens |
|
| pmid |
sentence |
| 16938345 |
Both lck and syk, phosphorylate the itam-like motifs on lat at y171y191, which is essential for induction of the interaction of lat with downstream signaling molecules such as grb2, plc-gamma1 and c-cbl, and for activation of mapk-erk. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation, T cell activation |
| + |
PTPN1 | down-regulates activity
dephosphorylation
|
LAT |
0.506 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248403 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12857726 |
Using a pharmacological inhibitor, we provide evidence that PTP1B activation and LAT dephosphorylation processes were required for irreversible platelet aggregation.|In collagen-stimulated platelets, the signaling complexes recruited by tyrosine-phosphorylated LAT are essential for PLCgamma2 activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LAT | up-regulates activity
binding
|
PI3K |
0.412 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252734 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11368773 |
By substituting these tyrosine residues in LAT with phenylalanine and by utilizing phosphorylated peptides derived from these sites, we mapped the tyrosine residues in LAT required for the direct interaction and activation of Vav, p85/p110alpha and phospholipase Cgamma1 (PLCgamma1). Our results indicate that Tyr(226) and Tyr(191) are required for Vav binding, whereas Tyr(171) and Tyr(132) are necessary for association and activation of phosphoinositide 3-kinase activity and PLCgamma1 respectively. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation, T cell activation |
| + |
PTPRJ | down-regulates
dephosphorylation
|
LAT |
0.35 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-105787 |
|
|
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 11259588 |
We propose that cd148 negatively regulates tcr signaling by interfering with the phosphorylation and function of plcgamma1 and lat |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LAT | up-regulates activity
binding
|
VAV1 |
0.755 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246045 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11368773 |
By substituting these tyrosine residues in LAT with phenylalanine and by utilizing phosphorylated peptides derived from these sites, we mapped the tyrosine residues in LAT required for the direct interaction and activation of Vav, p85/p110alpha and phospholipase Cgamma1 (PLCgamma1). Our results indicate that Tyr(226) and Tyr(191) are required for Vav binding, whereas Tyr(171) and Tyr(132) are necessary for association and activation of phosphoinositide 3-kinase activity and PLCgamma1 respectively. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STK25 | up-regulates activity
phosphorylation
|
LAT |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279294 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30948712 |
In sum, these data reveal that STK25 activates LATS kinases through a mechanism that is distinct from what has been characterized for the MAP4K/MST kinases (Fig.\u00a0 xref ).|Mechanistically, we demonstrate that STK25 promotes LATS phosphorylation at the activation loop in the absence of hydrophobic motif phosphorylation, which distinguishes it from all of the other known LATS-activating kinases discovered to date. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LAT | up-regulates activity
binding
|
PIK3R1 |
0.405 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246050 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11368773 |
By substituting these tyrosine residues in LAT with phenylalanine and by utilizing phosphorylated peptides derived from these sites, we mapped the tyrosine residues in LAT required for the direct interaction and activation of Vav, p85/p110alpha and phospholipase Cgamma1 (PLCgamma1). Our results indicate that Tyr(226) and Tyr(191) are required for Vav binding, whereas Tyr(171) and Tyr(132) are necessary for association and activation of phosphoinositide 3-kinase activity and PLCgamma1 respectively. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | T cell activation |
| + |
LAT | up-regulates activity
binding
|
PIK3CA |
0.419 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246065 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11368773 |
By substituting these tyrosine residues in LAT with phenylalanine and by utilizing phosphorylated peptides derived from these sites, we mapped the tyrosine residues in LAT required for the direct interaction and activation of Vav, p85/p110alpha and phospholipase Cgamma1 (PLCgamma1). Our results indicate that Tyr(226) and Tyr(191) are required for Vav binding, whereas Tyr(171) and Tyr(132) are necessary for association and activation of phosphoinositide 3-kinase activity and PLCgamma1 respectively. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN1 | down-regulates
dephosphorylation
|
LAT |
0.506 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-103599 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12857726 |
Our results demonstrate that ptp1b plays an important role in the integrin-mediated dephosphorylation of lat in human platelets and is involved in the control of irreversible aggregation upon fcgammariia stimulation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LAT | up-regulates activity
binding
|
PLCG1 |
0.811 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246060 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11368773 |
By substituting these tyrosine residues in LAT with phenylalanine and by utilizing phosphorylated peptides derived from these sites, we mapped the tyrosine residues in LAT required for the direct interaction and activation of Vav, p85/p110alpha and phospholipase Cgamma1 (PLCgamma1). Our results indicate that Tyr(226) and Tyr(191) are required for Vav binding, whereas Tyr(171) and Tyr(132) are necessary for association and activation of phosphoinositide 3-kinase activity and PLCgamma1 respectively. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation, T cell activation |
| + |
LAT | up-regulates activity
binding
|
PIK3R2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246055 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11368773 |
By substituting these tyrosine residues in LAT with phenylalanine and by utilizing phosphorylated peptides derived from these sites, we mapped the tyrosine residues in LAT required for the direct interaction and activation of Vav, p85/p110alpha and phospholipase Cgamma1 (PLCgamma1). Our results indicate that Tyr(226) and Tyr(191) are required for Vav binding, whereas Tyr(171) and Tyr(132) are necessary for association and activation of phosphoinositide 3-kinase activity and PLCgamma1 respectively. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LAT | up-regulates
binding
|
GRB2 |
0.807 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251521 |
|
|
Homo sapiens |
JURKAT Cell |
| pmid |
sentence |
| 10811803 |
Our results showed that three distal tyrosines, Tyr(171), Tyr(191), and Tyr(226), are responsible for Grb2-binding; |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251520 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23150273 |
Phosphorylated tyrosines 171, 191, and 226 [in LAT] bind to the SH2 domains of the Grb2 family of adaptor proteins and must be present for optimal signalling |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation, T cell activation |
| + |
PTPRJ | down-regulates activity
dephosphorylation
|
LAT |
0.35 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248696 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11259588 |
Protein tyrosine phosphatase CD148-mediated inhibition of T-cell receptor signal transduction is associated with reduced LAT and phospholipase Cgamma1 phosphorylation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STK4 | up-regulates activity
phosphorylation
|
LAT |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279661 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26456820 |
MST kinase phosphorylates and activates LATS kinase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TRAF6 | up-regulates activity
ubiquitination
|
LAT |
0.342 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278675 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23514740 |
Interestingly, this study has demonstrated that the membrane-proximal region of linker for activation of T cells preceding tyrosine-132 mediates its association with TRAF6, which promotes the ubiquitination of linker for activation of T cells and, in turn, the phosphorylation of tyrosine residues on linker for activation of T cells.|Moreover, LAT was ubiquitinated at Lysine 88 by TRAF6 via K63 linked chain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NUAK2 | down-regulates activity
phosphorylation
|
LAT |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280052 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30158528 |
Analysis by an in vitro kinase assay revealed that NUAK2 could phosphorylate immunoprecipitated LATS and that this phosphorylation was lost in the LATS double mutant (DM), T246A/S613A (Fig.\u00a0 xref ).|We showed that phosphorylation of Ser613, located upstream of the KD, adjacent to the MOB binding site and to a lesser extent the N-terminal localized T246, are required for NUAK2 to inhibit LATS. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
LAT
- 
- 