| + |
RAB32 | up-regulates activity 
relocalization
|
AP-1 complex |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260700 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23247405 |
Rab32 and Rab38 interact physically and colocalize with BLOC-2, AP-1 and AP-3|These results indicate that Rab32 and Rab38 operate in the same pathways previously defined for AP-1, AP-3 and BLOC-2 and suggest they are the specific proteins that divert AP-1, AP-3 and BLOC-2-dependent cargoes to maturing melanosomes and away from lysosomes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AP1M1 | form complex 
binding
|
AP-1 complex |
0.885 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260686 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21097499 |
Key components of this system are the heterotetrameric adaptor protein (AP)4 complexes, AP-1 (gamma-beta1-mi1-sigma1), AP-2 (α-beta2-mi2-sigma2), AP-3 (delta-beta3-mi3-sigma3), and AP-4 (epsilon-beta4-mi4-sigma4) (subunit composition shown in parentheses) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AP-1 complex | form complex
binding
|
AP-1/clathrin vescicle |
0.542 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260674 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23103167 |
Clathrin-coated pits and vesicles are diffraction-limited objects with typical diameters ranging between 75 and 130 nm. The smaller ∼75 nm coats contain at least 36 copies of clathrin, a heterohexameric protein of three heavy chains and three light chains, and about half that number of copies of the heterotetrameric AP adaptor complex | Intracellular clathrin-coated vesicles contain AP1 or AP3 adaptors |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AP-1 complex | up-regulates quantity
binding
|
SORT1 |
0.433 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273720 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 31767632 |
The short intracellular domain of sortilin binds several cytoplasmic adaptor proteins (e.g., the AP-1 complex and GGA1 to -3), most of which target two well-defined motifs: a C-terminal acidic cluster dileucine motif and a YXXΦ motif in the proximal third of the domain. Both motifs contribute to endocytosis as well as Golgi-endosome trafficking of sortilin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AP1B1 | form complex
binding
|
AP-1 complex |
0.809 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260685 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21097499 |
Key components of this system are the heterotetrameric adaptor protein (AP)4 complexes, AP-1 (gamma-beta1-mi1-sigma1), AP-2 (α-beta2-mi2-sigma2), AP-3 (delta-beta3-mi3-sigma3), and AP-4 (epsilon-beta4-mi4-sigma4) (subunit composition shown in parentheses) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AP1S1 | form complex
binding
|
AP-1 complex |
0.859 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260684 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21097499 |
Key components of this system are the heterotetrameric adaptor protein (AP)4 complexes, AP-1 (gamma-beta1-mi1-sigma1), AP-2 (α-beta2-mi2-sigma2), AP-3 (delta-beta3-mi3-sigma3), and AP-4 (epsilon-beta4-mi4-sigma4) (subunit composition shown in parentheses) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AP1G1 | form complex
binding
|
AP-1 complex |
0.81 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260687 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21097499 |
Key components of this system are the heterotetrameric adaptor protein (AP)4 complexes, AP-1 (gamma-beta1-mi1-sigma1), AP-2 (α-beta2-mi2-sigma2), AP-3 (delta-beta3-mi3-sigma3), and AP-4 (epsilon-beta4-mi4-sigma4) (subunit composition shown in parentheses) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RAB38 | up-regulates activity
relocalization
|
AP-1 complex |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260701 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23247405 |
Rab32 and Rab38 interact physically and colocalize with BLOC-2, AP-1 and AP-3|These results indicate that Rab32 and Rab38 operate in the same pathways previously defined for AP-1, AP-3 and BLOC-2 and suggest they are the specific proteins that divert AP-1, AP-3 and BLOC-2-dependent cargoes to maturing melanosomes and away from lysosomes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
AP-1 complex
CPX-5047