| + |
AP-4 Adaptor complex | up-regulates 
|
Vesicle_transport |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280855 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23167973 |
The adaptor proteins (APs) are a family of five heterotetrameric complexes with important functions in vesicle trafficking. The predominant steady-state localization of a sorting adaptor usually indicates the donor compartment of the mediated transport step, suggesting that AP-4 is involved in sorting at the TGN. The simplest model that emerges from these findings suggests that AP-4 mediates anterograde trafficking between the TGN and an endosomal compartment (Figure 1). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AP4M1 | form complex 
binding
|
AP-4 Adaptor complex |
0.807 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280850 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23167973 |
The adaptor proteins (APs) are a family of five heterotetrameric complexes with important functions in vesicle trafficking. While the roles of APs 1–3 are broadly established, comparatively little is known about AP-4 and AP-5. Five independent studies have reported patients with mutations in AP-4 genes, covering all four AP-4 subunits (Table 1): 15 (AP-4 μ); 16 (AP-4 β, AP-4 ϵ, AP-4 σ); 17 (AP-4 ϵ); 18 (AP-4 ϵ, AP-4 μ) and 19 (AP-4 β). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AP4E1 | form complex
binding
|
AP-4 Adaptor complex |
0.864 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280851 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23167973 |
The adaptor proteins (APs) are a family of five heterotetrameric complexes with important functions in vesicle trafficking. While the roles of APs 1–3 are broadly established, comparatively little is known about AP-4 and AP-5. Five independent studies have reported patients with mutations in AP-4 genes, covering all four AP-4 subunits (Table 1): 15 (AP-4 μ); 16 (AP-4 β, AP-4 ϵ, AP-4 σ); 17 (AP-4 ϵ); 18 (AP-4 ϵ, AP-4 μ) and 19 (AP-4 β). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AP4S1 | form complex
binding
|
AP-4 Adaptor complex |
0.862 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280852 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23167973 |
The adaptor proteins (APs) are a family of five heterotetrameric complexes with important functions in vesicle trafficking. While the roles of APs 1–3 are broadly established, comparatively little is known about AP-4 and AP-5. Five independent studies have reported patients with mutations in AP-4 genes, covering all four AP-4 subunits (Table 1): 15 (AP-4 μ); 16 (AP-4 β, AP-4 ϵ, AP-4 σ); 17 (AP-4 ϵ); 18 (AP-4 ϵ, AP-4 μ) and 19 (AP-4 β). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AP4B1 | form complex
binding
|
AP-4 Adaptor complex |
0.862 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280853 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23167973 |
The adaptor proteins (APs) are a family of five heterotetrameric complexes with important functions in vesicle trafficking. While the roles of APs 1–3 are broadly established, comparatively little is known about AP-4 and AP-5. Five independent studies have reported patients with mutations in AP-4 genes, covering all four AP-4 subunits (Table 1): 15 (AP-4 μ); 16 (AP-4 β, AP-4 ϵ, AP-4 σ); 17 (AP-4 ϵ); 18 (AP-4 ϵ, AP-4 μ) and 19 (AP-4 β). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ARF1 | up-regulates quantity 
binding
|
AP-4 Adaptor complex |
0.607 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280854 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23167973 |
The adaptor proteins (APs) are a family of five heterotetrameric complexes with important functions in vesicle trafficking. Whereas AP-1 and AP-2 are components of clathrin-coated vesicles, AP-4 and AP-5 are thought to act independently of clathrin. Like other AP-complexes, AP-4 probably interacts with further cytosolic proteins. In addition to ARF1, only one such protein, named Tepsin, has been identified to date, through proteomic analysis of an AP-4 enriched vesicle fraction |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
AP-4 Adaptor complex
CPX-5151