| + |
UNC13B | up-regulates activity 
transcriptional regulation
|
SNARE_complex |
0.71 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263972 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 30267828 |
In neuronal exocytosis, Munc18-1 (aSM-protein) and Munc13-1/2 (similar to CATCHRs) arethe relevant proteins responsible for SNARE-complex formation. Munc18-1 associates with syntaxin-1 in its‘closed’ conformation, i.e. with the regulatory Habc-domain folded against the SNARE (H3-)-domain. Opening-up of syntaxin is catalyzed by the Mun-domainwithin Munc13-1/2 and allows assembly with the partnerSNARE SNAP-25 and possibly VAMP2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Neurotransmitters release |
| + |
SNAP25 | form complex 
binding
|
SNARE_complex |
0.957 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263967 |
|
|
Homo sapiens |
Neuron |
| 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 |
| + |
SNARE_complex | up-regulates 
|
Synaptic_vesicle_exocytosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265065 |
|
|
Homo sapiens |
Neuron |
| 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 |
| + |
CORVET tethering complex | up-regulates activity
binding
|
SNARE_complex |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273699 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23351085 |
The two Vps-C complexes CORVET (class C core vacuole/endosome tethering) and HOPS (homotypic fusion and vacuole protein sorting) perform diverse biochemical functions in endocytosis: they tether membranes, interact with Rab GTPases, activate and proof-read SNARE assembly to drive membrane fusion, and possibly attach endosomes to the cytoskeleton. The core subunits Vps11, Vps16 and Vps18 present the SNARE-interacting Vps33 subunit on one side and bind the Rab GTPase interaction module through Vps3/Vps8 (in CORVET) or Vps39/Vps41 (in HOPS) on the other side (Fig. 3A) The core subunits Vps11, Vps16 and Vps18 present the SNARE-interacting Vps33 subunit on one side and bind the Rab GTPase interaction module through Vps3/Vps8 (in CORVET) or Vps39/Vps41 (in HOPS) on the other side (Fig. 3A) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HOPS tethering complex | up-regulates activity
binding
|
SNARE_complex |
0.324 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273692 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23351085 |
The two Vps-C complexes CORVET (class C core vacuole/endosome tethering) and HOPS (homotypic fusion and vacuole protein sorting) perform diverse biochemical functions in endocytosis: they tether membranes, interact with Rab GTPases, activate and proof-read SNARE assembly to drive membrane fusion, and possibly attach endosomes to the cytoskeleton. The core subunits Vps11, Vps16 and Vps18 present the SNARE-interacting Vps33 subunit on one side and bind the Rab GTPase interaction module through Vps3/Vps8 (in CORVET) or Vps39/Vps41 (in HOPS) on the other side (Fig. 3A) The core subunits Vps11, Vps16 and Vps18 present the SNARE-interacting Vps33 subunit on one side and bind the Rab GTPase interaction module through Vps3/Vps8 (in CORVET) or Vps39/Vps41 (in HOPS) on the other side (Fig. 3A) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STX1A | form complex
binding
|
SNARE_complex |
0.93 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263968 |
|
|
Homo sapiens |
Neuron |
| 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 |
| + |
Exocyst_EXOC6 variant | up-regulates activity
binding
|
SNARE_complex |
0.443 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270793 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30205058 |
The exocyst is a multisubunit protein complex that was first identified and characterized in budding yeast. This complex mediates the tethering of secretory vesicles to the plasma membrane prior to fusion mediated by soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs). Sec3 interacts with PI(4,5)P2 (red dots) in the plasma membrane. Its interaction with the t-SNARE protein Sso promotes the assembly of the Sso–Sec9 binary t-SNARE complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SNARE_complex | up-regulates
|
Membrane_fusion |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263973 |
|
|
Homo sapiens |
Neuron |
| 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. The event directly leading to membrane fusion is theassembly of the C-terminal end of the SNARE-complex,and the linker domains, which couples the releasedenergy directly to the fusion of the membranes |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SNARE_complex | up-regulates
|
Exocytosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263969 |
|
|
Homo sapiens |
Neuron |
| 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 |
| + |
VAMP2 | form complex
binding
|
SNARE_complex |
0.932 |
| 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 |
| + |
UNC13A | up-regulates activity
transcriptional regulation
|
SNARE_complex |
0.467 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263971 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 30267828 |
In neuronal exocytosis, Munc18-1 (aSM-protein) and Munc13-1/2 (similar to CATCHRs) arethe relevant proteins responsible for SNARE-complex formation. Munc18-1 associates with syntaxin-1 in its‘closed’ conformation, i.e. with the regulatory Habc-domain folded against the SNARE (H3-)-domain. Opening-up of syntaxin is catalyzed by the Mun-domainwithin Munc13-1/2 and allows assembly with the partnerSNARE SNAP-25 and possibly VAMP2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Exocyst_EXOC6B variant | up-regulates activity
binding
|
SNARE_complex |
0.427 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270792 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30205058 |
The exocyst is a multisubunit protein complex that was first identified and characterized in budding yeast. This complex mediates the tethering of secretory vesicles to the plasma membrane prior to fusion mediated by soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs). Sec3 interacts with PI(4,5)P2 (red dots) in the plasma membrane. Its interaction with the t-SNARE protein Sso promotes the assembly of the Sso–Sec9 binary t-SNARE complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STXBP1 | up-regulates activity
transcriptional regulation
|
SNARE_complex |
0.837 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263970 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 30267828 |
In neuronal exocytosis, Munc18-1 (aSM-protein) and Munc13-1/2 (similar to CATCHRs) arethe relevant proteins responsible for SNARE-complex formation. Munc18-1 associates with syntaxin-1 in its‘closed’ conformation, i.e. with the regulatory Habc-domain folded against the SNARE (H3-)-domain. Opening-up of syntaxin is catalyzed by the Mun-domainwithin Munc13-1/2 and allows assembly with the partnerSNARE SNAP-25 and possibly VAMP2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Neurotransmitters release |
3.0
SNARE_complex