| + |
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 |
| + |
STX1A | form complex 
binding
|
SNARE_complex |
0.931 |
| 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 |
| + |
HOPS tethering complex | up-regulates activity 
binding
|
SNARE_complex |
0.32 |
| 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 |
| + |
Exocyst_EXOC6 variant | up-regulates activity
binding
|
SNARE_complex |
0.441 |
| 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 |
| + |
SNAP25 | form complex
binding
|
SNARE_complex |
0.958 |
| 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 |
| + |
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 |
| + |
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 |
| + |
UNC13A | up-regulates activity
transcriptional regulation
|
SNARE_complex |
0.452 |
| 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 |
| + |
COG tethering complex | up-regulates activity
binding
|
SNARE_complex |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280766 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23378023 |
Multisubunit tethering complexes (MTCs) positively regulate vesicular fusion by as yet unclear mechanism. In this study we provide evidence that the MTC COG enhances the assembly of fusogenic Golgi SNARE complexes and concomitantly prevents nonfusogenic tSNARE interactions. This capability is possibly mediated by multiple direct interactions of COG subunits and specific Golgi SNAREs and SM (Sec1/Munc18) proteins. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Exocyst_EXOC6B variant | up-regulates activity
binding
|
SNARE_complex |
0.425 |
| 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 |
| + |
UNC13B | up-regulates activity
transcriptional regulation
|
SNARE_complex |
0.715 |
| 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 |
| + |
STXBP1 | up-regulates activity
transcriptional regulation
|
SNARE_complex |
0.84 |
| 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 |
| + |
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 |
| + |
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 |
4.0
SNARE_complex