| + |
PRKACA | down-regulates 
phosphorylation
|
PLCG1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-17901 |
Ser1248 |
HGRAREGsFESRYQQ |
Homo sapiens |
T-lymphocyte, JURKAT Cell |
| pmid |
sentence |
| 1370476 |
The observation that pka also phosphorylates plc-yl on serine 1248 suggests that phosphorylation of this residue may be a common mechanism by which pkc and pka inhibit plc-yl. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCA | down-regulates
phosphorylation
|
PLCG1 |
0.535 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-17905 |
Ser1248 |
HGRAREGsFESRYQQ |
Homo sapiens |
T-lymphocyte, JURKAT Cell |
| pmid |
sentence |
| 1370476 |
The observation that pka also phosphorylates plc-yl on serine 1248 suggests that phosphorylation of this residue may be a common mechanism by which pkc and pka inhibit plc-yl. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation, T cell activation, VEGF Signaling |
| + |
PRKD1 | down-regulates activity
phosphorylation
|
PLCG1 |
0.414 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248846 |
Ser1248 |
HGRAREGsFESRYQQ |
Homo sapiens |
JURKAT Cell |
| pmid |
sentence |
| 1370476 |
Thus, phosphorylation of PLC-gamma 1 by PKC or PKA at serine 1248 may modulate the interaction of PLC-gamma 1 with the protein tyrosine kinase or the protein tyrosine phosphatase; this altered interaction may, at least in part, be responsible for the decreased tyrosine phosphorylation of PLC-gamma 1 seen in PMA- and forskolin-treated Jurkat cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLCG1 | up-regulates quantity by stabilization 
phosphorylation
|
CDKN1A |
0.267 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262962 |
Ser146 |
GRKRRQTsMTDFYHS |
Homo sapiens |
|
| pmid |
sentence |
| 31575057 |
Phosphorylation at Ser-146 by PKCδ increases p21 stability |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ABL1 | down-regulates activity
phosphorylation
|
PLCG1 |
0.567 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276002 |
Tyr1003 |
KGKKFLQyNRLQLSR |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 12652307 |
C-Abl induces Tyr phosphorylation of PLC-γ1 in vivo. These findings demonstrate that c-Abl phosphorylates PLC-γ1 in vivo predominantly at Tyr 771 and Tyr 1003.c-Abl phosphorylation of PLC-γ1 causes downregulation of PLC activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276001 |
Tyr771 |
IGTAEPDyGALYEGR |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 12652307 |
C-Abl induces Tyr phosphorylation of PLC-γ1 in vivo. These findings demonstrate that c-Abl phosphorylates PLC-γ1 in vivo predominantly at Tyr 771 and Tyr 1003.c-Abl phosphorylation of PLC-γ1 causes downregulation of PLC activity. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
HCK | up-regulates activity
phosphorylation
|
PLCG1 |
0.661 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249360 |
Tyr1253 |
EGSFESRyQQPFEDF |
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-249361 |
Tyr771 |
IGTAEPDyGALYEGR |
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-249362 |
Tyr783 |
EGRNPGFyVEANPMP |
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: |
3 |
Organism: |
In Vitro |
| + |
EGFR | up-regulates
phosphorylation
|
PLCG1 |
0.833 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-20976 |
Tyr1253 |
EGSFESRyQQPFEDF |
Homo sapiens |
|
| pmid |
sentence |
| 1689310 |
We have identified the sites phosphorylated in vitro by epidermal growth factor (egf) receptor kinase in bovine brain phospholipase c-gamma (plc-gamma). They are tyrosine residues 472, 771, 783, and 1254. we propose, therefore, that the phosphorylation of plc-gamma by egf receptor kinase alters its interaction with putative inhibitory proteins and leads to its activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-20980 |
Tyr472 |
KLAEGSAyEEVPTSM |
Homo sapiens |
|
| pmid |
sentence |
| 1689310 |
We have identified the sites phosphorylated in vitro by epidermal growth factor (egf) receptor kinase in bovine brain phospholipase c-gamma (plc-gamma). They are tyrosine residues 472, 771, 783, and 1254. we propose, therefore, that the phosphorylation of plc-gamma by egf receptor kinase alters its interaction with putative inhibitory proteins and leads to its activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-20984 |
Tyr771 |
IGTAEPDyGALYEGR |
Homo sapiens |
|
| pmid |
sentence |
| 1689310 |
We have identified the sites phosphorylated in vitro by epidermal growth factor (egf) receptor kinase in bovine brain phospholipase c-gamma (plc-gamma). They are tyrosine residues 472, 771, 783, and 1254. we propose, therefore, that the phosphorylation of plc-gamma by egf receptor kinase alters its interaction with putative inhibitory proteins and leads to its activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-48872 |
Tyr783 |
EGRNPGFyVEANPMP |
Homo sapiens |
|
| pmid |
sentence |
| 9176240 |
In contrast, egf-induced tyrosine phosphorylation of plc-gamma 1 was rather small, indicating that tyrosine phosphorylation of plc-gamma 1 is not proportional to changes in plc activity. These results suggest that autophosphorylation of theegfr may induce a conformational change of its kinase domain which enhances its kinase activity with exogenous substrates and may induce association with phospholipase c-gamma by increasing its affinity to a domain containing tyr-771. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
LYN | up-regulates activity
phosphorylation
|
PLCG1 |
0.639 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249381 |
Tyr771 |
IGTAEPDyGALYEGR |
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-249382 |
Tyr783 |
EGRNPGFyVEANPMP |
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 |
| Pathways: | B-cell activation |
| + |
SYK | up-regulates activity
phosphorylation
|
PLCG1 |
0.759 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246572 |
Tyr771 |
IGTAEPDyGALYEGR |
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 8657103 |
Syk isolated from antigen receptor-activated B cells phosphorylated PLC-gamma1 on Tyr-771 and the key regulatory residue Tyr-783 in vitro, whereas Lyn from the same B cells phosphorylated PLC-gamma1 only on Tyr-771. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246576 |
Tyr783 |
EGRNPGFyVEANPMP |
Homo sapiens |
|
| pmid |
sentence |
| 8657103 |
Syk isolated from antigen receptor-activated B cells phosphorylated PLC-gamma1 on Tyr-771 and the key regulatory residue Tyr-783 in vitro, whereas Lyn from the same B cells phosphorylated PLC-gamma1 only on Tyr-771. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
| + |
SRC | up-regulates activity
phosphorylation
|
PLCG1 |
0.616 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247316 |
Tyr783 |
EGRNPGFyVEANPMP |
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: |
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 |
| + |
PLCG1 | up-regulates
chemical modification
|
1D-myo-inositol 1,4,5-trisphosphate |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176609 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21918248 |
Phospholypase c is an enzyme which catalyzes the hydrolysis of phosphatidylinositol-4,5-biphosphate (p(4,5)p(2)) into second messangers inositol-1,4,5-triphosphate (ins(1,4,5)p3) and dag. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation, VEGF Signaling |
| + |
PLCG1 | up-regulates
phosphorylation
|
PRKCA |
0.535 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-99310 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12645577 |
Tnf-alfa binds to tnfr1 and activates pc-plc to induce pkcalfa and c-src activation, leading to tyrosine phosphorylation of ikkbeta at tyr188 and tyr199. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation, T cell activation, VEGF Signaling |
| + |
ALK | up-regulates
binding
|
PLCG1 |
0.525 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-122082 |
|
|
Homo sapiens |
Lymphoma Cell |
| pmid |
sentence |
| 14968112 |
Proteins that interact with alk tyrosine kinase play important roles in mediating downstream cellular signals. Previously reported proteins in the alk signal pathway were identified including pi3-k, jak2, jak3, stat3, grb2, irs, and plcgamma1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GNG3 | up-regulates
binding
|
PLCG1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-199141 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23074268 |
Furthermore, this work suggested that the gbetagamma subunits released upon gi activation activated phospholipase c-gamma (plc-gamma) to produce inositol 3 phosphate (ip3) which would subsequently increase intracellular ca2+ abundance. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FLT1 | up-regulates
binding
|
PLCG1 |
0.659 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-53743 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9398617 |
We conclude that both flt-1 and kdr have the potential to signal through plc gamma via phosphotyrosine residues located in juxta-membrane and carboxyl tail regions |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GNG2 | up-regulates
binding
|
PLCG1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-199138 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23074268 |
Furthermore, this work suggested that the gbetagamma subunits released upon gi activation activated phospholipase c-gamma (plc-gamma) to produce inositol 3 phosphate (ip3) which would subsequently increase intracellular ca2+ abundance. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PDGFRA | up-regulates
phosphorylation
|
PLCG1 |
0.628 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-28176 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 7535778 |
Tyrosine phosphorylation has been shown to increase the enzymatic activity of plc-? / we show that the human pdgf ?- And ?-Receptors differ quantitatively in their abilities to associate with and phosphorylate plc-? And to stimulate inositol phosphate production. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STOML2 | up-regulates activity
binding
|
PLCG1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260378 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18641330 |
In these studies, we also found that SLP-2 interacted with Lck, ZAP70, LAT, and PLC-gamma1 during the 30-min period following stimulation in vitro|The SLP-2-associated pool of these molecules became phosphorylated/activated in a sequential manner, a profile compatible with their temporal involvement in early TCR signalling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GIT1 | up-regulates
binding
|
PLCG1 |
0.532 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-118454 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14523024 |
Git1 interaction with plcgamma is required for plcgamma activation based on inhibition of tyrosine phosphorylation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Smooth Muscle |
| + |
GNB2 | up-regulates 
|
PLCG1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-199132 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23074268 |
Furthermore, this work suggested that the gbetagamma subunits released upon gi activation activated phospholipase c-gamma (plc-gamma) to produce inositol 3 phosphate (ip3) which would subsequently increase intracellular ca2+ abundance. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LAT | up-regulates activity
binding
|
PLCG1 |
0.801 |
| 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 |
| + |
TNK1 | up-regulates quantity
binding
|
PLCG1 |
0.345 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273864 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10873601 |
GST-protein precipitations from cell lysates confirmed that GST-PLC-gamma1(SH3) associated with endogenously expressed Tnk1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLCG1 | up-regulates
|
ITPRIPL1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-172500 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 21368195 |
Recruitment of g protein also can activate phospholipase c (plc) that in turn increases inositol triphosphate (ip3) levels and induces ca2+ release from internal stores |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GNB3 | up-regulates
binding
|
PLCG1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-199135 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23074268 |
Furthermore, this work suggested that the g subunits released upon gi activation activated phospholipase c (plc- ) to produce inositol 3-phosphate (ip3), which would subsequently increase intracellular ca2+ abundance. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
KDR | up-regulates
binding
|
PLCG1 |
0.657 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-147870 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16835467 |
(vegfr) phosphorylated y1175 creates a binding site for phospholipase cgamma1 (plc-gamma1) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | VEGF Signaling |
| + |
PTPRJ | down-regulates
dephosphorylation
|
PLCG1 |
0.377 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-105790 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11259588 |
Cd148 can dephosphorylate lat and plc?1 In vitro. / plc?1 Undergoes inducible tyrosine phosphorylation following tcr stimulation (46), and this phosphorylation is required to stimulate its catalytic activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GNB1 | up-regulates
|
PLCG1 |
0.377 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-199129 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23074268 |
Furthermore, this work suggested that the gbetagamma subunits released upon gi activation activated phospholipase c-gamma (plc-gamma) to produce inositol 3 phosphate (ip3) which would subsequently increase intracellular ca2+ abundance. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRF | down-regulates
dephosphorylation
|
PLCG1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-85166 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11121408 |
Here we show that lar reduces the constitutive tyrosine autophosphorylation and kinase activity of ret-men2a but not ret-men2b, accompanying a significant decrease of phosphorylation of phospholipase cgamma, akt, and erk1/2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PDGFRB | up-regulates
phosphorylation
|
PLCG1 |
0.85 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-28179 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 7535778 |
Tyrosine phosphorylation has been shown to increase the enzymatic activity of plc-? / we show that the human pdgf ?- And ?-Receptors differ quantitatively in their abilities to associate with and phosphorylate plc-? And to stimulate inositol phosphate production. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRJ |
dephosphorylation
|
PLCG1 |
0.377 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248706 |
|
|
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 |
| + |
GNGT1 | up-regulates
binding
|
PLCG1 |
0.378 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-199144 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23074268 |
Furthermore, this work suggested that the gbetagamma subunits released upon gi activation activated phospholipase c-gamma (plc-gamma) to produce inositol 3 phosphate (ip3) which would subsequently increase intracellular ca2+ abundance. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLCG1 | up-regulates
|
RAC1 |
0.513 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-155747 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17562871 |
We propose that the association of plcgamma1 with complexes containing git1 and beta-pix is essential for its role in integrin-mediated cell spreading and motility. As a component of this complex, plcgamma1 is also involved in the activation of cdc42 and rac1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NTRK3 | up-regulates
binding
|
PLCG1 |
0.598 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-67404 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 10235685 |
Unglycosylated trka core protein is phosphorylated even in the absence of ligand stimulation and displays constitutive kinase activity as well as constitutive interaction with the signaling molecules shc and plc-gamma. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLCG1 | up-regulates
binding
|
SOS1 |
0.629 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-80024 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10913276 |
We provide evidence that sos1, a p21ras-specific guanine nucleotide exchange factor, directly binds to the sh3 domain of plc-gamma1, and that the sh3 domain of plc-gamma1 is involved in sos1-mediated p21ras activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | T cell activation, VEGF Signaling |
| + |
NTRK1 | up-regulates
phosphorylation, binding
|
PLCG1 |
0.634 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-38538 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8384556 |
The nerve growth factor (ngf) receptor/trk associated with and phosphorylated phospholipase c gamma (plc gamma) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-75405 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 10708759 |
Autophosphorylated trka binds directly to plc?, Abl, and shc. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PLCG1 | up-regulates
chemical modification
|
1,2-diacyl-sn-glycerol |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176606 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21918248 |
Phospholypase c is an enzyme which catalyzes the hydrolysis of phosphatidylinositol-4,5-biphosphate (p(4,5)p(2)) into second messangers inositol-1,4,5-triphosphate (ins(1,4,5)p3) and dag. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation, T cell activation, VEGF Signaling |
| + |
PIK3C2A | up-regulates
|
PLCG1 |
0.378 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-54707 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9430633 |
Activation of pi 3-kinase causes plc gamma ph domain-mediated membrane targeting and plc gamma activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
KAT2A | down-regulates activity
acetylation
|
PLCG1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275498 |
|
|
|
|
| pmid |
sentence |
| 24870244 |
The histone acetyltransferase GCN5 (general control non-repressed protein 5) acetylates PGC-1alpha and suppresses its transcriptional activity, whereas sirtuin 1 deacetylates and activates PGC-1alpha. |
|
| Publications: |
1 |
| + |
SIRT1 | up-regulates activity
deacetylation
|
PLCG1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275499 |
|
|
|
|
| pmid |
sentence |
| 24870244 |
The histone acetyltransferase GCN5 (general control non-repressed protein 5) acetylates PGC-1alpha and suppresses its transcriptional activity, whereas sirtuin 1 deacetylates and activates PGC-1alpha. |
|
| Publications: |
1 |
| + |
PLCG1 | up-regulates quantity
chemical modification
|
1,2-diacyl-sn-glycerol |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251558 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23140367 |
Phospholipase C (PLC) converts phosphatidylinositol 4,5-bisphosphate (PIP2) to inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DAG). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation, T cell activation, VEGF Signaling |
| + |
ERBB2 | up-regulates
binding
|
PLCG1 |
0.63 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-20815 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 1676673 |
Activated egfr binds the sh2 domain of phospholipase c-gamma (plc-gamma), activating plc-gamma-mediated downstream signaling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PLCG1
- 
- 