| + |
PRKACA | down-regulates activity 
phosphorylation
|
SYN2 |
0.331 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250059 |
Ser10 |
NFLRRRLsDSSFIAN |
in vitro |
|
| pmid |
sentence |
| 10571231 |
Synapsin phosphorylation in the A domain, at the only phosphorylation site shared by all synapsins, dissociates synapsins from synaptic vesicles.This site is located in the N-terminal A domain and is a substrate for both PKA and CaM Kinase I |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PKA | down-regulates activity
phosphorylation
|
SYN2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264109 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 10571231 |
Synapsins are exclusively localized to synaptic vesicles, which they coat as peripheral membrane proteins; they probably constitute one of the most abundant neuronal PKA substrates. Our study reveals an unexpectedly dynamic state of synapsins in nerve terminals: any changes in PKA or CaM Kinase I activity will modulate the amount of synapsin on synaptic vesicles. PKA Activation Triggers Synapsin Dissociation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SYN2 | down-regulates 
|
Synaptic_vesicle_exocytosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264106 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 33809712 |
Synapsins are a family of peripheral proteins that bind to the SV membrane. Synapsins Maintain the SV Reserve Pool. Synapsins serve as a key protein for maintaining SVs within this reserve pool, but the mechanism that allows synapsins to do this is unclear. This mechanism is likely to involve synapsins either cross-linking SVs, thereby anchoring SVs to each other, or creating a liquid phase that allows SVs to float within a synapsin droplet. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SYN2 | up-regulates activity 
binding
|
ACTB |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269182 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 15265865 |
Synapsins, a family of neuron-specific phosphoproteins, have been demonstrated to regulate the availability of synaptic vesicles for exocytosis by binding to both synaptic vesicles and the actin cytoskeleton in a phosphorylation-dependent manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SYN2 | up-regulates activity
binding
|
Actin_cytoskeleton_reorganization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269185 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 15265865 |
Synapsins, a family of neuron-specific phosphoproteins, have been demonstrated to regulate the availability of synaptic vesicles for exocytosis by binding to both synaptic vesicles and the actin cytoskeleton in a phosphorylation-dependent manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
SYN2
- 
- 