| + |
PIP2(16:0/18:1(9Z)) | up-regulates activity 
chemical activation
|
AKT1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252432 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18249092 |
Furthermore, overall PKB activity, primarily consisting of cytosolic enzyme, was dependent upon levels of PI(3,4)P2, while only membrane-associated PKB activity was dependent upon PI(3,4,5)P3 levels. We conclude that PI(3,4,5)P3 and PI(3,4)P2 have distinct roles in determining PKB phosphorylation and activity. Thus, when investigating PI3K-PKB pathways, the importance of both lipids must be considered |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIP2(16:0/18:1(9Z)) | down-regulates activity 
chemical inhibition
|
GSN |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261841 |
|
|
Homo sapiens |
Blood Platelet |
| pmid |
sentence |
| 12788695 |
We further measured the ability of ppIs phosphorylated in positions D-3 and D-4 to release the F-actin capping proteins CapZ and gelsolin from OG-permeabilized platelets (Fig. 7A). Ten percent of platelet CapZ and gelsolin is found in the OG-insoluble fraction (4). PI3,4,5P3 and PI3,4P2 release both CapZ and gelsolin from these preparations. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
INPP5D | up-regulates quantity
chemical modification
|
PIP2(16:0/18:1(9Z)) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252427 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23650141 |
PtdIns(3,4)P2 is commonly reported as a product of the SH2 domain-containing inositol 5-phosphatases 1/2 (SHIP1 and SHIP2) that dephosphorylate PtdIns(3,4,5)P3 at the 5-position |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIP2(16:0/18:1(9Z)) | up-regulates activity
chemical activation
|
CADPS2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264335 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 24363652 |
CAPS exhibits low affinity but functionally significant interactions with plasma membrane PIP2 via its central PH (pleckstrin homology) domain (82, 111). PIP2 enhanced CAPS stimulation of SNARE-dependent liposome fusion with wild-type but not with mutant PH domain CAPS proteins |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIP2(16:0/18:1(9Z)) | down-regulates activity
chemical inhibition
|
CAPZA1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261843 |
|
|
Homo sapiens |
Blood Platelet |
| pmid |
sentence |
| 12788695 |
We further measured the ability of ppIs phosphorylated in positions D-3 and D-4 to release the F-actin capping proteins CapZ and gelsolin from OG-permeabilized platelets (Fig. 7A). Ten percent of platelet CapZ and gelsolin is found in the OG-insoluble fraction (4). PI3,4,5P3 and PI3,4P2 release both CapZ and gelsolin from these preparations. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIP2(16:0/18:1(9Z)) | up-regulates activity
chemical activation
|
WASL |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261870 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10219243 |
In the presence of Cdc42 and PI(4,5)P2, the potency of N-WASP was increased to a level approaching that of GST-VCA, suggesting that N-WASP was fully activated by the two molecules. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
INPP4B | down-regulates quantity
chemical modification
|
PIP2(16:0/18:1(9Z)) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252433 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21127264 |
Collectively this data indicates INPP4B is the only PtdIns(3,4)P2 4-phosphatase expressed in breast cancer cells and suggests a correlation between INPP4B and hormone receptor status in human breast cancer |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIP2(16:0/18:1(9Z)) | up-regulates activity
chemical activation
|
CADPS |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264334 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 24363652 |
CAPS exhibits low affinity but functionally significant interactions with plasma membrane PIP2 via its central PH (pleckstrin homology) domain (82, 111). PIP2 enhanced CAPS stimulation of SNARE-dependent liposome fusion with wild-type but not with mutant PH domain CAPS proteins |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PIP2(16:0/18:1(9Z))
