| + |
COG7 | form complex 
binding
|
COG tethering complex |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280758 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31381138 |
The conserved oligomeric Golgi (COG) complex, a multisubunit tethering complex of the CATCHR (complexes associated with tethering containing helical rods) family, controls membrane trafficking and ensures Golgi homeostasis by orchestrating retrograde vesicle targeting within the Golgi. In humans, COG defects lead to severe multisystemic diseases known as COG-congenital disorders of glycosylation (COG-CDG). The COG complex both physically and functionally interacts with all classes of molecules maintaining intra-Golgi trafficking, namely SNAREs, SNARE-interacting proteins, Rabs, coiled-coil tethers, and vesicular coats. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
COG2 | form complex
binding
|
COG tethering complex |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280759 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31381138 |
The conserved oligomeric Golgi (COG) complex, a multisubunit tethering complex of the CATCHR (complexes associated with tethering containing helical rods) family, controls membrane trafficking and ensures Golgi homeostasis by orchestrating retrograde vesicle targeting within the Golgi. In humans, COG defects lead to severe multisystemic diseases known as COG-congenital disorders of glycosylation (COG-CDG). The COG complex both physically and functionally interacts with all classes of molecules maintaining intra-Golgi trafficking, namely SNAREs, SNARE-interacting proteins, Rabs, coiled-coil tethers, and vesicular coats. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
COG1 | form complex
binding
|
COG tethering complex |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280760 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31381138 |
The conserved oligomeric Golgi (COG) complex, a multisubunit tethering complex of the CATCHR (complexes associated with tethering containing helical rods) family, controls membrane trafficking and ensures Golgi homeostasis by orchestrating retrograde vesicle targeting within the Golgi. In humans, COG defects lead to severe multisystemic diseases known as COG-congenital disorders of glycosylation (COG-CDG). The COG complex both physically and functionally interacts with all classes of molecules maintaining intra-Golgi trafficking, namely SNAREs, SNARE-interacting proteins, Rabs, coiled-coil tethers, and vesicular coats. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
COG3 | form complex
binding
|
COG tethering complex |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280761 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31381138 |
The conserved oligomeric Golgi (COG) complex, a multisubunit tethering complex of the CATCHR (complexes associated with tethering containing helical rods) family, controls membrane trafficking and ensures Golgi homeostasis by orchestrating retrograde vesicle targeting within the Golgi. In humans, COG defects lead to severe multisystemic diseases known as COG-congenital disorders of glycosylation (COG-CDG). The COG complex both physically and functionally interacts with all classes of molecules maintaining intra-Golgi trafficking, namely SNAREs, SNARE-interacting proteins, Rabs, coiled-coil tethers, and vesicular coats. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
COG8 | form complex
binding
|
COG tethering complex |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280762 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31381138 |
The conserved oligomeric Golgi (COG) complex, a multisubunit tethering complex of the CATCHR (complexes associated with tethering containing helical rods) family, controls membrane trafficking and ensures Golgi homeostasis by orchestrating retrograde vesicle targeting within the Golgi. In humans, COG defects lead to severe multisystemic diseases known as COG-congenital disorders of glycosylation (COG-CDG). The COG complex both physically and functionally interacts with all classes of molecules maintaining intra-Golgi trafficking, namely SNAREs, SNARE-interacting proteins, Rabs, coiled-coil tethers, and vesicular coats. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
COG4 | form complex
binding
|
COG tethering complex |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280763 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31381138 |
The conserved oligomeric Golgi (COG) complex, a multisubunit tethering complex of the CATCHR (complexes associated with tethering containing helical rods) family, controls membrane trafficking and ensures Golgi homeostasis by orchestrating retrograde vesicle targeting within the Golgi. In humans, COG defects lead to severe multisystemic diseases known as COG-congenital disorders of glycosylation (COG-CDG). The COG complex both physically and functionally interacts with all classes of molecules maintaining intra-Golgi trafficking, namely SNAREs, SNARE-interacting proteins, Rabs, coiled-coil tethers, and vesicular coats. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
COG5 | form complex
binding
|
COG tethering complex |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280764 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31381138 |
The conserved oligomeric Golgi (COG) complex, a multisubunit tethering complex of the CATCHR (complexes associated with tethering containing helical rods) family, controls membrane trafficking and ensures Golgi homeostasis by orchestrating retrograde vesicle targeting within the Golgi. In humans, COG defects lead to severe multisystemic diseases known as COG-congenital disorders of glycosylation (COG-CDG). The COG complex both physically and functionally interacts with all classes of molecules maintaining intra-Golgi trafficking, namely SNAREs, SNARE-interacting proteins, Rabs, coiled-coil tethers, and vesicular coats. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
COG6 | form complex
binding
|
COG tethering complex |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280765 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31381138 |
The conserved oligomeric Golgi (COG) complex, a multisubunit tethering complex of the CATCHR (complexes associated with tethering containing helical rods) family, controls membrane trafficking and ensures Golgi homeostasis by orchestrating retrograde vesicle targeting within the Golgi. In humans, COG defects lead to severe multisystemic diseases known as COG-congenital disorders of glycosylation (COG-CDG). The COG complex both physically and functionally interacts with all classes of molecules maintaining intra-Golgi trafficking, namely SNAREs, SNARE-interacting proteins, Rabs, coiled-coil tethers, and vesicular coats. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
COG tethering complex | up-regulates activity 
binding
|
SNARE_complex |
|
| 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 |
| + |
COG tethering complex | up-regulates activity
binding
|
STX11-SNAP23 SNARE complex |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280767 |
|
|
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 |
| + |
COG tethering complex | up-regulates activity
binding
|
STX11-VAMP8 SNARE complex |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280768 |
|
|
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 |
| + |
COG tethering complex | up-regulates activity
binding
|
STX17-VAMP8 SNARE complex |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280769 |
|
|
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 |
4.0
COG tethering complex
CPX-6199