| + |
PRKACA |
phosphorylation
|
VASP |
0.487 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250064 |
Ser157 |
EHIERRVsNAGGPPA |
Homo sapiens |
|
| pmid |
sentence |
| 12576312 |
Three phosphorylation sites have been identified in VASP: Ser157, Ser239, and Thr278, all of which can be phosphorylated by either PKA or PKG in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-140841 |
Ser157 |
EHIERRVsNAGGPPA |
Homo sapiens |
|
| pmid |
sentence |
| 16197368 |
We show that, in human platelets, vasp is phosphorylated by pkc on ser157, but not ser239, in response to phorbol ester stimulation, in a manner blocked by the pkc inhibitor bim i (bisindolylmaleimide i). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250063 |
Ser239 |
GAKLRKVsKQEEASG |
Homo sapiens |
|
| pmid |
sentence |
| 12576312 |
Three phosphorylation sites have been identified in VASP: Ser157, Ser239, and Thr278, all of which can be phosphorylated by either PKA or PKG in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250065 |
Thr278 |
LARRRKAtQVGEKTP |
in vitro |
|
| pmid |
sentence |
| 8182057 |
The vasodilator-stimulated phosphoprotein (VASP) is a major substrate for cAMP-dependent- (cAK) and cGMP-dependent protein kinase (cGK) in human platelets and other cardiovascular cells.‚ three VASP phosphorylation sites are phosphorylated by cAK and cGK. Thr, Ser I, and Ser 2 correspond to Thr278, Ser157, Ser239 of the VASP protein, respectively |
|
| Publications: |
4 |
Organism: |
Homo Sapiens, In Vitro |
| + |
PRKG1 |
phosphorylation
|
VASP |
0.729 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120347 |
Ser157 |
EHIERRVsNAGGPPA |
Homo sapiens |
|
| pmid |
sentence |
| 14679200 |
Three phosphorylation sites have been identified in VASP: Ser157, Ser239, and Thr278, all of which can be phosphorylated by either PKA or PKG in vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120351 |
Ser239 |
GAKLRKVsKQEEASG |
Homo sapiens |
|
| pmid |
sentence |
| 14679200 |
Three phosphorylation sites have been identified in VASP: Ser157, Ser239, and Thr278, all of which can be phosphorylated by either PKA or PKG in vitro |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Axon guidance |
| + |
AMPK | down-regulates 
phosphorylation
|
VASP |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216568 |
Ser322 |
TTLPRMKsSSSVTTS |
Homo sapiens |
|
| pmid |
sentence |
| 21945940 |
Here we show that phosphorylation of vasp by ampk occurs at a novel site, serine 322, and that phosphorylation at this site alters actin filament binding. We also show that inhibition of ampk activity results in the accumulation of vasp at cell-cell adhesions and a concomitant increase in cell-cell adhesion. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216515 |
Thr278 |
LARRRKAtQVGEKTP |
Homo sapiens |
|
| pmid |
sentence |
| 17082196 |
Pharmacological ampk inhibitors and activators and ampk mutants revealed that the kinase specifically targets residue thr-278 but not ser-157 or ser-239. Quantitative fluorescence-activated cell sorter analysis and serum response factor transcriptional reporter assays, which quantify the cellular f-/g-actin equilibrium, indicated that ampk-mediated vasp phosphorylation impaired actin stress fiber formation and altered cell morphology. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKAA2 | down-regulates
phosphorylation
|
VASP |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176642 |
Ser322 |
TTLPRMKsSSSVTTS |
Homo sapiens |
|
| pmid |
sentence |
| 21945940 |
Here we show that phosphorylation of vasp by ampk occurs at a novel site, serine 322, and that phosphorylation at this site alters actin filament binding. We also show that inhibition of ampk activity results in the accumulation of vasp at cell-cell adhesions and a concomitant increase in cell-cell adhesion. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-150462 |
Thr278 |
LARRRKAtQVGEKTP |
Homo sapiens |
|
| pmid |
sentence |
| 17082196 |
Pharmacological ampk inhibitors and activators and ampk mutants revealed that the kinase specifically targets residue thr-278 but not ser-157 or ser-239. Quantitative fluorescence-activated cell sorter analysis and serum response factor transcriptional reporter assays, which quantify the cellular f-/g-actin equilibrium, indicated that ampk-mediated vasp phosphorylation impaired actin stress fiber formation and altered cell morphology. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKG1 | down-regulates
phosphorylation
|
VASP |
0.729 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-98139 |
Thr278 |
LARRRKAtQVGEKTP |
Homo sapiens |
|
| pmid |
sentence |
| 12576312 |
Vasodilator-stimulated phosphoprotein activation of serum-response element-dependent transcription occurs downstream of rhoa and is inhibited by cgmp-dependent protein kinase phosphorylation. Three phosphorylation sites have been identified in vasp: ser157, ser239, and thr278, all of which can be phosphorylated by either pka or pkg in vitro |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Axon guidance |
| + |
RPS6K | down-regulates
phosphorylation
|
VASP |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252802 |
Thr278 |
LARRRKAtQVGEKTP |
Homo sapiens |
Lung Cancer Cell |
| pmid |
sentence |
| 21423205 |
Rsk1 phosphorylated vasp on t278, a site regulating its binding to actin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KA1 | down-regulates
phosphorylation
|
VASP |
0.462 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-172899 |
Thr278 |
LARRRKAtQVGEKTP |
Homo sapiens |
Lung Cancer Cell |
| pmid |
sentence |
| 21423205 |
Rsk1 phosphorylated vasp on t278, a site regulating its binding to actin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
VASP | up-regulates activity 
phosphorylation
|
ATIC |
0.35 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276172 |
Tyr104 |
RVVACNLyPFVKTVA |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 18845790 |
ATIC and VASP phosphorylation is dependent on NPM-ALK kinase activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKG1 | down-regulates activity
phosphorylation
|
VASP |
0.729 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268289 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15066263 |
Vertebrate Ena/VASP proteins are phosphorylated by PKA, as well as PKG, and the phosphorylation is required for full function in a number of cellular contexts |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Axon guidance |
| + |
VASP | up-regulates 
|
Axonal_growth_cone_formation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268390 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18508258 |
Here we review recent findings into Ena/VASP function in neurite initiation, axon outgrowth and guidance. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Axon guidance |
| + |
VASP | up-regulates
|
Neurite_outgrowth |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268393 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18508258 |
Here we review recent findings into Ena/VASP function in neurite initiation, axon outgrowth and guidance. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RAPH1 | up-regulates activity
binding
|
VASP |
0.597 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268426 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20417104 |
Here we show that Lpd is a substrate of Abl kinases and binds to the Abl SH2 domain. Phosphorylation of Lpd positively regulates the interaction between Lpd and Ena/VASP proteins. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Axon guidance |
| + |
PKA | up-regulates activity
phosphorylation
|
VASP |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268286 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15066263 |
Vertebrate Ena/VASP proteins are phosphorylated by PKA, as well as PKG, and the phosphorylation is required for full function in a number of cellular contexts |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Axon guidance |
3.0
VASP
- 
- 