| + |
SYP | up-regulates quantity 
binding
|
VAMP2 |
0.625 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264102 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17331077 |
Synaptophysin I interacts with VAMP2 and controls its subcellular distribution. On the SV membrane, VAMP2 is engaged in a complex with synaptophysin I, which is mutually exclusive with the formation of fusogenic SNARE complexes. This model implicates synaptophysin I in escorting VAMP2 to the sites where exocytosis must take place exclusively after the arrival of the appropriate stimulus. We show that, at early stages along the secretory pathway, synaptophysin I directs sorting of VAMP2 to vesicles exhibiting limited availability for constitutive exocytosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264117 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26903854 |
Recent studies have revealed that sybII and synaptotagmin-1 interact with other SV cargoes to ensure a high fidelity of retrieval. These cargoes are synaptophysin (for sybII) and SV2A (for synaptotagmin-1). SV2A Acts as an iTRAP to Direct Synaptotagmin-1 Retrieval to SVs. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Neurotransmitters release |
| + |
VAMP2 | form complex 
binding
|
SNARE_complex |
0.931 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263966 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30267828 |
The best-studied SNARE-complex is the one formed between three proteins, VAMP2/synaptobrevin-2, syntaxin-1, and SNAP-25, that mediate fast exocytosis in neuronal cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Neurotransmitters release |
| + |
MYO5A | up-regulates activity
binding
|
VAMP2 |
0.459 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269281 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21077886 |
Another potential role of myosin Va in LDCV exocytosis lies in facilitating the formation of the SNARE complex, which is needed for fusion of the vesicle with the plasma membrane. Notably, myosin Va binds to at least two SNARE proteins in a Ca2+-dependent manner: at micromolar Ca2+-levels, it binds to VAMP2 located in the membrane of the cargo vesicle via its globular tail domain |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
VAMP2 | up-regulates 
|
Synaptic_vesicle_exocytosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264103 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 17331077 |
Synaptobrevin 2/VAMP2 (vesicle-associated membrane protein 2), a critical component of the synaptic vesicle-fusion machinery. On the SV membrane, VAMP2 is engaged in a complex with synaptophysin I, which is mutually exclusive with the formation of fusogenic SNARE complexes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Neurotransmitters release |
| + |
CADPS2 | up-regulates activity
binding
|
VAMP2 |
0.257 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264341 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 24363652 |
CAPS interactions with N-terminal regions of the SNARE motif of VAMP2 were also detected, which suggests that CAPS might recruit VAMP2 into syntaxin-1/SNAP-25 heterodimers for RQaQbc-SNARE complex assembly. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SNCA | down-regulates quantity 
binding
|
VAMP2 |
0.413 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264104 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 31110017 |
The normal function of the small presynaptic protein α-synuclein (α-syn) is of exceptional interest, not only in the context of neurodegeneration, but also as a cytosolic regulator of neurotransmission. we show that α-syn-VAMP2 interactions are necessary for α-syn-induced synaptic attenuation. Our data connect divergent views and suggest a unified model of α-syn function. the data indicate that α-syn–VAMP2 binding is essential for α-syn function and advocate an “interlocking model” where α-syn multimers on the SV surface interact with VAMP2 on adjacent SVs, helping to maintain physiologic SV clustering. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Neurotransmitters release |
| + |
SNAP91 | up-regulates quantity
binding
|
VAMP2 |
0.614 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264112 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 26903854 |
the monomeric adaptor proteins AP180/CALM and stonin-2 are required for the efficient retrieval of synaptobrevin II (sybII) and synaptotagmin-1 respectively. Furthermore, recent studies have revealed that sybII and synaptotagmin-1 interact with other SV cargoes to ensure a high fidelity of retrieval. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CADPS | up-regulates activity
binding
|
VAMP2 |
0.445 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264340 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 24363652 |
CAPS interactions with N-terminal regions of the SNARE motif of VAMP2 were also detected, which suggests that CAPS might recruit VAMP2 into syntaxin-1/SNAP-25 heterodimers for RQaQbc-SNARE complex assembly. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STON2 | up-regulates quantity
binding
|
VAMP2 |
0.544 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264113 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26903854 |
the monomeric adaptor proteins AP180/CALM and stonin-2 are required for the efficient retrieval of synaptobrevin II (sybII) and synaptotagmin-1 respectively. Furthermore, recent studies have revealed that sybII and synaptotagmin-1 interact with other SV cargoes to ensure a high fidelity of retrieval. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Neurotransmitters release |
3.0
VAMP2
- 
- 