+ |
CDK5 | down-regulates activity
phosphorylation
|
PLD2 |
0.377 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276168 |
Ser134 |
ARFAVAYsPARDAGN |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
18625302 |
In this study, we suggest that the phosphorylation and activation of PLD2 by cyclin-dependent kinase 5 (Cdk5) is critical for EGF-dependent insulin secretion. We determined that the phosphorylation site of PLD2 was located at Ser(134). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKCA | up-regulates
phosphorylation
|
PLD2 |
0.679 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-138351 |
Ser243 |
RWLVVKDsFLLYMCL |
Homo sapiens |
|
pmid |
sentence |
15979581 |
The phosphorylation sites in phospholipase d2 (pld2) induced by activation of protein kinase calpha (pkcalpha) in cos 7 cells were analyzed by mass spectrometry. Ser134, 146, and 243, and thr72, 99/100, and 252 were identified. These sites were mutated to ala and the double mutation of ser243 and thr252 eliminated the phosphorylation. / the s243/t252a mutant showed a partial decrease in pld2 activity |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-138355 |
Thr252 |
LLYMCLEtGAISFVQ |
Homo sapiens |
|
pmid |
sentence |
15979581 |
The phosphorylation sites in phospholipase d2 (pld2) induced by activation of protein kinase calpha (pkcalpha) in cos 7 cells were analyzed by mass spectrometry. Ser134, 146, and 243, and thr72, 99/100, and 252 were identified. These sites were mutated to ala and the double mutation of ser243 and thr252 eliminated the phosphorylation. / the s243/t252a mutant showed a partial decrease in pld2 activity |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
PRKCD | up-regulates
phosphorylation
|
PLD2 |
0.476 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-167577 |
Thr566 |
FIQRWNFtKTTKAKY |
Homo sapiens |
|
pmid |
sentence |
20733000 |
Finally, we show that thr566 of pld2 is directly phosphorylated by pkc and that pld2 mutation in this region prevents pld2 activation, pld2 translocation to the edge of lamellipodia, rac translocation, and cell spreading after integrin activation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
EGFR | up-regulates activity
phosphorylation
|
PLD2 |
0.532 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251095 |
Tyr179 |
RLLTMSFyRNYHAMT |
Homo sapiens |
|
pmid |
sentence |
9837959 |
Using transiently transfected human embryonic kidney fibroblasts (HEK293), we demonstrate here that PLD1 activity, and to a lesser extent PLD2 activity, is stimulated in response to epidermal growth factor (EGF). PLD2, but not PLD1, associates with the EGF receptor in a ligand-independent manner and becomes tyrosine-phosphorylated upon EGF receptor activation. Tyrosine 11 (Tyr-11) of PLD2 was identified as the specific phosphorylation site. Mutation of this residue to phenylalanine enhanced basal activity almost 2-fold |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
JAK3 | up-regulates
phosphorylation
|
PLD2 |
0.418 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-163858 |
Tyr415 |
ALGINSGySKRALML |
Homo sapiens |
|
pmid |
sentence |
20176813 |
We identified three kinases capable of phosphorylating pld2 in vitro-epidermal growth factor receptor (egfr), jak3, and src (with jak3 reported for the first time in this study)-that phosphorylate an inhibitory, an activator, and an ambivalent (one that can yield either effect) site, respectively. Mass spectrometry analyses indicated the target of each of these kinases as y(296) for egfr, y(415) for jak3, and y(511) for src. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PLD2 | up-regulates
|
ERK1/2 |
0.57 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-254983 |
|
|
Homo sapiens |
|
pmid |
sentence |
18423386 |
Altogether, these data suggest that PLD acting upstream of the MAP kinases ERK1/2 may play a key role in the regulation of IL-2 production by stimulated Jurkat cells. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GNAI1 | down-regulates
binding
|
PLD2 |
0.312 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-48256 |
|
|
Homo sapiens |
|
pmid |
sentence |
9148895 |
The results of this study suggest that membrane phospholipase d activity can be negatively regulated via gi |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
P2RX7 | up-regulates
|
PLD2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-254966 |
|
|
Homo sapiens |
|
pmid |
sentence |
8573088 |
This study shows that extracellular ATP, acting through the P2Z purinoceptor, stimulated PLD activity in human lymphocytes. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |