+ |
PRKCA |
phosphorylation
|
PLCB1 |
0.703 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249081 |
Ser887 |
HSQPAPGsVKAPAKT |
Mus musculus |
Swiss-3T3 Cell |
pmid |
sentence |
11278470 |
. Two-dimensional phosphopeptide mapping and site-directed mutagenesis demonstrated that PKC promoted phosphorylation of PLC beta1 at serine 887 in the nucleus of IGF-I-treated cells. Overexpression of either a PLC beta1 mutant in which the PKC phosphorylation site Ser(887) was replaced by alanine, or a dominant-negative PKC alpha, resulted in a sustained activation of nuclear PLC following IGF-I stimulation. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
Pathways: | Thyroid Hormone Metabolism |
+ |
MAPK1 | up-regulates activity
phosphorylation
|
PLCB1 |
0.406 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-106561 |
Ser982 |
KKKSEPSsPDHGSST |
in vitro |
|
pmid |
sentence |
11287604 |
coimmunoprecipitation detected a specific association between the activated erk and plc beta1 within the nucleus. In vitro studies revealed that recombinant plc beta1 could be efficiently phosphorylated by activated mitogen-activated protein kinase but not by pka. The erk phosphorylation site was mapped to serine 982 this result suggests that erk-evoked phosphorylation of plc beta1 at serine 982 plays a critical role in the activation of the nuclear pi cycle and is also crucial to the mitogenic action of igf-i. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
MAPK3 | up-regulates activity
phosphorylation
|
PLCB1 |
0.422 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-106565 |
Ser982 |
KKKSEPSsPDHGSST |
in vitro |
|
pmid |
sentence |
11287604 |
Plc beta1 could be efficiently phosphorylated by activated mitogen-activated protein kinase but not by pka. The erk phosphorylation site was mapped to serine 982 |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
PLCB1 | up-regulates quantity
chemical modification
|
1,2-diacyl-sn-glycerol |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-256496 |
|
|
in vitro |
|
pmid |
sentence |
23880553 |
Phospholipase C (PLC) enzymes convert phosphatidylinositol-4,5-bisphosphate into the second messengers diacylglycerol and inositol-1,4,5-triphosphate. |
|
Publications: |
1 |
Organism: |
In Vitro |
Pathways: | Oxytocin signaling, Thyroid Hormone Metabolism |
+ |
DVL1 | up-regulates activity
|
PLCB1 |
0.278 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-258978 |
|
|
Homo sapiens |
|
pmid |
sentence |
19279717 |
Dsh through PLC activates IP3, which leads to release of intracellular Ca2+, which in turn activates CamK11 and calcineurin |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GNAQ | up-regulates
binding
|
PLCB1 |
0.76 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-37149 |
|
|
Homo sapiens |
|
pmid |
sentence |
8245028 |
The beta- but not the gamma- and delta-type isozymes of inositol phospholipid-specific phospholipase c (plc) are activated by g protein alpha q and beta gamma subunits. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Dopaminergic Synapse, Oxytocin signaling, Thyroid Hormone Metabolism |
+ |
GNA11 | up-regulates activity
binding
|
PLCB1 |
0.607 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267203 |
|
|
Homo sapiens |
|
pmid |
sentence |
27515033 |
TRH-R1 receptor, which is coupled to Gq/11 protein, activates phospholipase C, mobilizes calcium and activates protein kinase C. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Thyroid Hormone Metabolism |
+ |
GNB1 | down-regulates
binding
|
PLCB1 |
0.461 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-44369 |
|
|
Homo sapiens |
|
pmid |
sentence |
8870665 |
These results indicate that g-protein beta gamma subunits constitute a mechanism by which g-protein mediate a rapid and transient plc- beta 1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GNAS | up-regulates activity
binding
|
PLCB1 |
0.33 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265066 |
|
|
Homo sapiens |
|
pmid |
sentence |
8245028 |
The beta- but not the gamma- and delta-type isozymes of inositol phospholipid-specific phospholipase c (plc) are activated by g protein alpha q and beta gamma subunits. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Glutamatergic synapse, Thyroid Hormone Metabolism |
+ |
DVL2 | up-regulates activity
|
PLCB1 |
0.271 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-258979 |
|
|
Homo sapiens |
|
pmid |
sentence |
19279717 |
Dsh through PLC activates IP3, which leads to release of intracellular Ca2+, which in turn activates CamK11 and calcineurin |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PLCB1 | up-regulates
binding
|
GNA11 |
0.607 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-17239 |
|
|
Homo sapiens |
|
pmid |
sentence |
1322796 |
Plc-_1 stimulates hydrolysis of gq/11-bound gtp and acts as a gtpase-activating protein (gap) for its physiologic regulator, gq/11 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Thyroid Hormone Metabolism |
+ |
ERK1/2 | up-regulates activity
phosphorylation
|
PLCB1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270200 |
|
|
in vitro |
|
pmid |
sentence |
11287604 |
Plc beta1 could be efficiently phosphorylated by activated mitogen-activated protein kinase but not by pka. The erk phosphorylation site was mapped to serine 982 |
|
Publications: |
1 |
Organism: |
In Vitro |
Pathways: | Oxytocin signaling |
+ |
PLCB1 | up-regulates quantity
chemical modification
|
1D-myo-inositol 1,4,5-trisphosphate |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-256497 |
|
|
in vitro |
|
pmid |
sentence |
23880553 |
Phospholipase C (PLC) enzymes convert phosphatidylinositol-4,5-bisphosphate into the second messengers diacylglycerol and inositol-1,4,5-triphosphate. |
|
Publications: |
1 |
Organism: |
In Vitro |
Pathways: | Dopaminergic Synapse, Glutamatergic synapse, Oxytocin signaling, Thyroid Hormone Metabolism |
+ |
DVL3 | up-regulates activity
|
PLCB1 |
0.355 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-258980 |
|
|
Homo sapiens |
|
pmid |
sentence |
19279717 |
Dsh through PLC activates IP3, which leads to release of intracellular Ca2+, which in turn activates CamK11 and calcineurin |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Gbeta | up-regulates activity
phosphorylation
|
PLCB1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270109 |
|
|
in vitro |
|
pmid |
sentence |
11287604 |
Plc beta1 could be efficiently phosphorylated by activated mitogen-activated protein kinase but not by pka. The erk phosphorylation site was mapped to serine 982 |
|
Publications: |
1 |
Organism: |
In Vitro |