| + |
UHMK1 |
phosphorylation
|
SYN1 |
0.373 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-78899 |
Ser438 |
GSHGQTPsPGALPLG |
Homo sapiens |
|
| pmid |
sentence |
| 10880969 |
We also identified a tryptic peptide of synapsin i phosphorylated by kis |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK5 | up-regulates 
phosphorylation
|
SYN1 |
0.564 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-78883 |
Ser551 |
PAARPPAsPSPQRQA |
Homo sapiens |
|
| pmid |
sentence |
| 10880969 |
Synapsin i (syni), a major sv phosphoprotein involved in the regulation of sv trafficking and neurotransmitter release, is one of the presynaptic substrates of cdk5, which phosphorylates it in its c-terminal region at ser(549) (site 6) and ser(551) (site 7). Phosphorylation of syni by cdk5 is physiologically regulated and enhances its binding to f-actin. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-78887 |
Ser553 |
ARPPASPsPQRQAGP |
Homo sapiens |
|
| pmid |
sentence |
| 10880969 |
Synapsin i (syni), a major sv phosphoprotein involved in the regulation of sv trafficking and neurotransmitter release, is one of the presynaptic substrates of cdk5, which phosphorylates it in its c-terminal region at ser(549) (site 6) and ser(551) (site 7). Phosphorylation of syni by cdk5 is physiologically regulated and enhances its binding to f-actin. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CAMK2G |
phosphorylation
|
SYN1 |
0.445 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250707 |
Ser568 |
PQATRQTsVSGPAPP |
|
|
| pmid |
sentence |
| 3118371 |
Sites 2 and 3 are serine residues phosphorylated by calcium/calmodulin-dependent protein kinase II. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250708 |
Ser605 |
AGPTRQAsQAGPVPR |
|
|
| pmid |
sentence |
| 3118371 |
Sites 2 and 3 are serine residues phosphorylated by calcium/calmodulin-dependent protein kinase II. |
|
| Publications: |
2 |
| + |
PAK3 | up-regulates activity
phosphorylation
|
SYN1 |
0.332 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250246 |
Ser605 |
AGPTRQAsQAGPVPR |
Rattus norvegicus |
PC-12 Cell |
| pmid |
sentence |
| 12237306 |
Synapsin I is phosphorylated at Ser603 by p21-activated kinases. the Ser603 residue must be one of the pivotal sites for the release |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PAK1 | up-regulates activity
phosphorylation
|
SYN1 |
0.348 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250235 |
Ser605 |
AGPTRQAsQAGPVPR |
Rattus norvegicus |
PC-12 Cell |
| pmid |
sentence |
| 12237306 |
Synapsin I is phosphorylated at Ser603 by p21-activated kinases. the Ser603 residue must be one of the pivotal sites for the release |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PRKAA1 | down-regulates activity 
phosphorylation
|
SYN1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-78891 |
Ser9 |
NYLRRRLsDSNFMAN |
Homo sapiens |
|
| pmid |
sentence |
| 10880969 |
It has been reported that site 1 of syn i can be phosphorylated by pka. Pka-mediated synapsin i ser9 phosphorylation occurs in response to cgs 21680 treatment. Results show that the adenosine a2a receptor agonist, cgs 21680, increases neurotransmitter release, in particular, glutamate and noradrenaline and such response is mediated by protein kinase a activation, which in turn increased synapsin i phosphorylation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK2 |
phosphorylation
|
SYN1 |
0.325 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250236 |
Ser9 |
NYLRRRLsDSNFMAN |
Rattus norvegicus |
|
| pmid |
sentence |
| 12237306 |
Recombinant PAK2 could also phosphorylate the Ser9 and Ser551 residues. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PRKACA | down-regulates activity
phosphorylation
|
SYN1 |
0.337 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250058 |
Ser9 |
NYLRRRLsDSNFMAN |
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 |
| + |
CAMK1 | down-regulates activity
phosphorylation
|
SYN1 |
0.561 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250615 |
Ser9 |
NYLRRRLsDSNFMAN |
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 |
| + |
SYN1 | up-regulates activity
binding
|
RAB3A |
0.619 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269181 |
|
|
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. The interaction between synapsin I and Rab3A was confirmed by photoaffinity labeling experiments on purified synaptic vesicles and by the formation of a chemically cross-linked complex between synapsin I and Rab3A in intact nerve terminals. The data indicate that synapsin I is a novel Rab3 interactor on synaptic vesicles and suggest that the synapsin-Rab3 interaction may participate in the regulation of synaptic vesicle trafficking within the nerve terminals. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Neurotransmitters release |
| + |
KDM5C | down-regulates quantity by repression 
transcriptional regulation
|
SYN1 |
0.346 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264314 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 31691806 |
The KDM5C decrease was associated with a lack of repression of downstream target genes Scn2a, Syn1 and Bdnf in the embryonic brain of Arx-null mice. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
BHC complex | down-regulates quantity by repression
transcriptional regulation
|
SYN1 |
0.27 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264504 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12032298 |
We show that BHC interacts with the promoter of the synapsin gene and mediates its RE1-dependent repression. BHC is recruited to the endogenous synapsin gene. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SYN1 | up-regulates activity
binding
|
ACTB |
0.3 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269184 |
|
|
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 |
| + |
SYN1 | up-regulates activity
binding
|
Actin_cytoskeleton_reorganization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269187 |
|
|
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 |
| + |
PKA | down-regulates activity
phosphorylation
|
SYN1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264108 |
|
|
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 |
| Pathways: | Neurotransmitters release |
| + |
SYN1 | down-regulates
|
Synaptic_vesicle_exocytosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264105 |
|
|
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 |
| Pathways: | Neurotransmitters release |
| + |
PAK |
phosphorylation
|
SYN1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269974 |
|
|
Rattus norvegicus |
|
| pmid |
sentence |
| 12237306 |
Recombinant PAK2 could also phosphorylate the Ser9 and Ser551 residues. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
4.0
SYN1
- 
- 