| + |
BTK | up-regulates activity 
phosphorylation
|
PLCG2 |
0.55 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109746 |
Tyr1197 |
LESEEELySSCRQLR |
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 11507089 |
These findings indicate that the phosphorylations of the tyrosine residues 753, 759, 1197, and 1217, which have been identified as btk-dependent phosphorylation sites in vitro, coordinately contribute to bcr-induced activation of plcgamma2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109750 |
Tyr1217 |
LNNQLFLyDTHQNLR |
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 11507089 |
These findings indicate that the phosphorylations of the tyrosine residues 753, 759, 1197, and 1217, which have been identified as btk-dependent phosphorylation sites in vitro, coordinately contribute to bcr-induced activation of plcgamma2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109754 |
Tyr753 |
ERDINSLyDVSRMYV |
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 11507089 |
These findings indicate that the phosphorylations of the tyrosine residues 753, 759, 1197, and 1217, which have been identified as btk-dependent phosphorylation sites in vitro, coordinately contribute to bcr-induced activation of plcgamma2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109758 |
Tyr759 |
LYDVSRMyVDPSEIN |
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 11507089 |
These findings indicate that the phosphorylations of the tyrosine residues 753, 759, 1197, and 1217, which have been identified as btk-dependent phosphorylation sites in vitro, coordinately contribute to bcr-induced activation of plcgamma2. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
FYN | up-regulates activity
phosphorylation
|
PLCG2 |
0.14 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249339 |
Tyr753 |
ERDINSLyDVSRMYV |
in vitro |
|
| pmid |
sentence |
| 7682059 |
The phosphorylation of purified phospholipase C-gamma 1 (PLC-gamma 1) and PLC-gamma 2 by src-family-protein tyrosine kinases (PTKs) P56lck, p53/56lyn, p59hck, p59fyn, and p60src was studied in vitro. All five PTKs phosphorylated PLC-gamma 1 and PLC-gamma 2, suggesting that both PLC-gamma isozymes can be phosphorylated in cells by any of the src-family PTKs in response to the activation of cell surface receptors. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249340 |
Tyr759 |
LYDVSRMyVDPSEIN |
in vitro |
|
| pmid |
sentence |
| 7682059 |
The phosphorylation of purified phospholipase C-gamma 1 (PLC-gamma 1) and PLC-gamma 2 by src-family-protein tyrosine kinases (PTKs) P56lck, p53/56lyn, p59hck, p59fyn, and p60src was studied in vitro. All five PTKs phosphorylated PLC-gamma 1 and PLC-gamma 2, suggesting that both PLC-gamma isozymes can be phosphorylated in cells by any of the src-family PTKs in response to the activation of cell surface receptors. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
HCK | up-regulates activity
phosphorylation
|
PLCG2 |
0.14 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249363 |
Tyr753 |
ERDINSLyDVSRMYV |
in vitro |
|
| pmid |
sentence |
| 7682059 |
The phosphorylation of purified phospholipase C-gamma 1 (PLC-gamma 1) and PLC-gamma 2 by src-family-protein tyrosine kinases (PTKs) P56lck, p53/56lyn, p59hck, p59fyn, and p60src was studied in vitro. All five PTKs phosphorylated PLC-gamma 1 and PLC-gamma 2, suggesting that both PLC-gamma isozymes can be phosphorylated in cells by any of the src-family PTKs in response to the activation of cell surface receptors. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249364 |
Tyr759 |
LYDVSRMyVDPSEIN |
in vitro |
|
| pmid |
sentence |
| 7682059 |
The phosphorylation of purified phospholipase C-gamma 1 (PLC-gamma 1) and PLC-gamma 2 by src-family-protein tyrosine kinases (PTKs) P56lck, p53/56lyn, p59hck, p59fyn, and p60src was studied in vitro. All five PTKs phosphorylated PLC-gamma 1 and PLC-gamma 2, suggesting that both PLC-gamma isozymes can be phosphorylated in cells by any of the src-family PTKs in response to the activation of cell surface receptors. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
BTK | up-regulates
phosphorylation
|
PLCG2 |
0.55 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-111069 |
Tyr753 |
ERDINSLyDVSRMYV |
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 11606584 |
By measuring the ability of human plcgamma2 to restore calcium responses to the b-cell receptor stimulation or oxidative stress in a b-cell line (dt40) deficient in plcgamma2, we have demonstrated that two tyrosine residues, tyr(753) and tyr(759), were important for the plcgamma2 signaling function.Of the two kinases that previously have been proposed to phosphorylate plcgamma2, btk, and syk, purified btk had much greater ability to phosphorylate recombinant plcgamma2 in vitro, whereas syk efficiently phosphorylated adapter protein blnk. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-111073 |
Tyr759 |
LYDVSRMyVDPSEIN |
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 11606584 |
By measuring the ability of human plcgamma2 to restore calcium responses to the b-cell receptor stimulation or oxidative stress in a b-cell line (dt40) deficient in plcgamma2, we have demonstrated that two tyrosine residues, tyr(753) and tyr(759), were important for the plcgamma2 signaling function.Of the two kinases that previously have been proposed to phosphorylate plcgamma2, btk, and syk, purified btk had much greater ability to phosphorylate recombinant plcgamma2 in vitro, whereas syk efficiently phosphorylated adapter protein blnk. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
LYN | up-regulates activity
phosphorylation
|
PLCG2 |
0.31 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249383 |
Tyr753 |
ERDINSLyDVSRMYV |
in vitro |
|
| pmid |
sentence |
| 7682059 |
The phosphorylation of purified phospholipase C-gamma 1 (PLC-gamma 1) and PLC-gamma 2 by src-family-protein tyrosine kinases (PTKs) P56lck, p53/56lyn, p59hck, p59fyn, and p60src was studied in vitro. All five PTKs phosphorylated PLC-gamma 1 and PLC-gamma 2, suggesting that both PLC-gamma isozymes can be phosphorylated in cells by any of the src-family PTKs in response to the activation of cell surface receptors. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249384 |
Tyr759 |
LYDVSRMyVDPSEIN |
in vitro |
|
| pmid |
sentence |
| 7682059 |
The phosphorylation of purified phospholipase C-gamma 1 (PLC-gamma 1) and PLC-gamma 2 by src-family-protein tyrosine kinases (PTKs) P56lck, p53/56lyn, p59hck, p59fyn, and p60src was studied in vitro. All five PTKs phosphorylated PLC-gamma 1 and PLC-gamma 2, suggesting that both PLC-gamma isozymes can be phosphorylated in cells by any of the src-family PTKs in response to the activation of cell surface receptors. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
LCK | up-regulates
phosphorylation
|
PLCG2 |
0.31 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-91473 |
Tyr753 |
ERDINSLyDVSRMYV |
Homo sapiens |
|
| pmid |
sentence |
| 12181444 |
In vitro phosphorylation experiments with recombinant plcgamma2 and recombinant lck, fyn, and lyn tyrosine kinases showed that phosphorylation of plcgamma2 led to activation of the recombinant enzyme. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-91477 |
Tyr759 |
LYDVSRMyVDPSEIN |
Homo sapiens |
|
| pmid |
sentence |
| 12181444 |
In vitro phosphorylation experiments with recombinant plcgamma2 and recombinant lck, fyn, and lyn tyrosine kinases showed that phosphorylation of plcgamma2 led to activation of the recombinant enzyme. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PLCG2 | up-regulates 
|
Macrophage_differentiation |
0.14 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255571 |
|
|
Homo sapiens |
Monocyte |
| pmid |
sentence |
| 24890514 |
Studies with multipotent precursor cell lines (Fig. 4A) indicate that CSF-1R Tyr-807 and Tyr-721 promote macrophage differentiation via the PLC-γ2 pathway |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Skeletal Muscle |
| + |
CSF1R | up-regulates
|
PLCG2 |
0.34 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255570 |
|
|
Homo sapiens |
Monocyte |
| pmid |
sentence |
| 24890514 |
Studies with multipotent precursor cell lines (Fig. 4A) indicate that CSF-1R Tyr-807 and Tyr-721 promote macrophage differentiation via the PLC-γ2 pathway |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Skeletal Muscle |
PLCG2
- 
- 