| + |
Caspase 3 complex | down-regulates activity 
cleavage
|
GSN |
0.641 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256433 |
Asp403 |
WRDPDQTdGLGLSYL |
Homo sapiens |
|
| pmid |
sentence |
| 9671712 |
We showed that human gelsolin was cleaved during Fas-mediated apoptosis in vivo and that the caspase-3 cleavage site of human gelsolin was at D352 of DQTD352G. gelsolin seems to have dual functions, i.e., it both prevents and, once cleaved, induces cell death. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CASP3 | down-regulates activity
cleavage
|
GSN |
0.641 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256357 |
Asp403 |
WRDPDQTdGLGLSYL |
Homo sapiens |
|
| pmid |
sentence |
| 9671712 |
We showed that human gelsolin was cleaved during Fas-mediated apoptosis in vivo and that the caspase-3 cleavage site of human gelsolin was at D352 of DQTD352G. gelsolin seems to have dual functions, i.e., it both prevents and, once cleaved, induces cell death. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SRC |
phosphorylation
|
GSN |
0.573 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250780 |
Tyr409 |
TDGLGLSyLSSHIAN |
in vitro |
|
| pmid |
sentence |
| 10210201 |
Gelsolin phosphorylation by c-Src in the presence of lysophosphatidic acid also revealed Tyr438 as the most prominent site. Additional minor sites were found using the anti-phosphotyrosine bead immunoprecipitation method followed by MALDI-MS and PSD analysis. These sites, representing approximately 5% of the total phosphate incorporation, were identified as Tyr59, Tyr382, Tyr576, and Tyr624. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250784 |
Tyr465 |
VPVPTNLyGDFFTGD |
in vitro |
|
| pmid |
sentence |
| 10210201 |
Gelsolin phosphorylation by c-Src in the presence of lysophosphatidic acid also revealed Tyr438 as the most prominent site. Additional minor sites were found using the anti-phosphotyrosine bead immunoprecipitation method followed by MALDI-MS and PSD analysis. These sites, representing approximately 5% of the total phosphate incorporation, were identified as Tyr59, Tyr382, Tyr576, and Tyr624. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250782 |
Tyr603 |
LKTPSAAyLWVGTGA |
in vitro |
|
| pmid |
sentence |
| 10210201 |
Gelsolin phosphorylation by c-Src in the presence of lysophosphatidic acid also revealed Tyr438 as the most prominent site. Additional minor sites were found using the anti-phosphotyrosine bead immunoprecipitation method followed by MALDI-MS and PSD analysis. These sites, representing approximately 5% of the total phosphate incorporation, were identified as Tyr59, Tyr382, Tyr576, and Tyr624. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250783 |
Tyr651 |
ALGGKAAyRTSPRLK |
in vitro |
|
| pmid |
sentence |
| 10210201 |
Gelsolin phosphorylation by c-Src in the presence of lysophosphatidic acid also revealed Tyr438 as the most prominent site. Additional minor sites were found using the anti-phosphotyrosine bead immunoprecipitation method followed by MALDI-MS and PSD analysis. These sites, representing approximately 5% of the total phosphate incorporation, were identified as Tyr59, Tyr382, Tyr576, and Tyr624. |
|
| Publications: |
4 |
Organism: |
In Vitro |
| + |
SRC | up-regulates 
phosphorylation
|
GSN |
0.573 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-67014 |
Tyr465 |
VPVDPATyGQFYGGD |
Homo sapiens |
|
| pmid |
sentence |
| 10210201 |
Identification of tyr438 as the major in vitro c-src phosphorylation site in human gelsolin recently |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TNIK | up-regulates activity
phosphorylation
|
GSN |
0.499 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280154 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18701680 |
In vitro , TNIK can phosphorylate and activate the F-actin-fragmenting enzyme gelsolin, and in cultured cells, TNIK induces actin fiber disassembly ( xref ).|In vitro, TNIK can phosphorylate and activate the F-actin-fragmenting enzyme gelsolin, and in cultured cells, TNIK induces actin fiber disassembly. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Caspase 3 complex | down-regulates
cleavage
|
GSN |
0.641 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256461 |
|
|
Homo sapiens |
Neutrophil |
| pmid |
sentence |
| 9323209 |
Caspase-3 mediates cleavage of gelsolin, generating a fragment that severs actin filaments in an unregulated fashion. The cleavage of gelsolin causes cells to round up, detach and undergo nuclear fragmentation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
calcium(2+) | up-regulates activity
chemical activation
|
GSN |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261844 |
|
|
Homo sapiens |
Blood Platelet |
| pmid |
sentence |
| 27871158 |
Gelsolin is an actin binding protein that severs and caps the barbed-end actin filaments to prevent actin monomer exchange upon intracellular calcium increase in the initial step. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
phosphatidylinositol bisphosphate | 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 |
| + |
1D-myo-inositol 1,4,5-trisphosphate | down-regulates activity
chemical inhibition
|
GSN |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261840 |
|
|
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 |
| + |
CASP3 | down-regulates
cleavage
|
GSN |
0.641 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-51652 |
|
|
Homo sapiens |
Neutrophil |
| pmid |
sentence |
| 9323209 |
Caspase-3 mediates cleavage of gelsolin, generating a fragment that severs actin filaments in an unregulated fashion. The cleavage of gelsolin causes cells to round up, detach and undergo nuclear fragmentation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GSN | down-regulates quantity
binding
|
F-actin_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261835 |
|
|
Homo sapiens |
Blood Platelet |
| pmid |
sentence |
| 27871158 |
Gelsolin is an actin binding protein that severs and caps the barbed-end actin filaments to prevent actin monomer exchange upon intracellular calcium increase in the initial step. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTK2B | down-regulates activity
phosphorylation
|
GSN |
0.527 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278325 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12578912 |
Our results demonstrate that PYK2 inhibits this EGTA stable gelsolin-actin monomer association.|PYK2 phosphorylates gelsolin at tyrosine residues and regulates gelsolin bioactivity, including decreasing gelsolin binding to actin monomer and increasing gelsolin binding to phosphatidylinositol lipids. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
GSN
- 
- 