| + |
Neuronal AP-3 | up-regulates 
|
Platelet_dense_granule_formation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268523 |
|
|
Homo sapiens |
Blood Platelet |
| pmid |
sentence |
| 12019270 |
BLOC-1, a novel complex containing the pallidin and muted proteins involved in the biogenesis of melanosomes and platelet-dense granules|Interestingly, immunofluorescence and in vitro binding experiments demonstrated that pallidin/BLOC-1 is able to associate with actin filaments. We propose that BLOC-1 mediates the biogenesis of lysosome-related organelles by a mechanism that may involve self-assembly and interaction with the actin cytoskeleton. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AP3M2 | form complex 
binding
|
Neuronal AP-3 |
0.738 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268520 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 19497727 |
Mammals contain more than one AP-3 complex owing to the existence of pairs of genes encoding β3, μ3, and σ3 subunits (A and B isoforms). While both σ3A and σ3B are expressed ubiquitously and seem to be functionally equivalent, the B isoforms of β3 and μ3 display rather restricted expression patterns, mostly in cells of neuronal origin. This has led to the notion of the existence of two types of mammalian AP-3 complexes: a ubiquitous AP-3 comprising δ, β3A, μ3A, and σ3(A or B) subunits, and a brain-specific AP-3 complex containing δ, β3B, μ3B, and σ3(A or B) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Neuronal AP-3 | form complex
binding
|
AP-3/clathrin vescicle |
0.386 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268525 |
|
|
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 |
| + |
AP3S2 | form complex
binding
|
Neuronal AP-3 |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268518 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 19497727 |
Mammals contain more than one AP-3 complex owing to the existence of pairs of genes encoding β3, μ3, and σ3 subunits (A and B isoforms). While both σ3A and σ3B are expressed ubiquitously and seem to be functionally equivalent, the B isoforms of β3 and μ3 display rather restricted expression patterns, mostly in cells of neuronal origin. This has led to the notion of the existence of two types of mammalian AP-3 complexes: a ubiquitous AP-3 comprising δ, β3A, μ3A, and σ3(A or B) subunits, and a brain-specific AP-3 complex containing δ, β3B, μ3B, and σ3(A or B) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RAB32 | up-regulates activity 
relocalization
|
Neuronal AP-3 |
0.277 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268524 |
|
|
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 |
| + |
RAB38 | up-regulates activity
relocalization
|
Neuronal AP-3 |
0.282 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268526 |
|
|
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 |
| + |
AP3D1 | form complex
binding
|
Neuronal AP-3 |
0.809 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268519 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 19497727 |
Mammals contain more than one AP-3 complex owing to the existence of pairs of genes encoding β3, μ3, and σ3 subunits (A and B isoforms). While both σ3A and σ3B are expressed ubiquitously and seem to be functionally equivalent, the B isoforms of β3 and μ3 display rather restricted expression patterns, mostly in cells of neuronal origin. This has led to the notion of the existence of two types of mammalian AP-3 complexes: a ubiquitous AP-3 comprising δ, β3A, μ3A, and σ3(A or B) subunits, and a brain-specific AP-3 complex containing δ, β3B, μ3B, and σ3(A or B) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Neuronal AP-3 | up-regulates
|
Melanosome_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268522 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22203680 |
Lysosome-related organelles (LROs) 6 are present in a range of cells in multicellular eukaryotes and include lytic granules, lung lamellar bodies, platelet-dense granules, and melanosomes (1.). The melanosome of the pigment cells in the skin and eye is the best studied of the LROs (1., 2.). The biogenesis of the melanosome and other LROs requires the AP-3 adaptor complex, the class C Vps complex, and three BLOC (biogenesis of lysosome-related organelles complex) complexes |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AP3B2 | form complex
binding
|
Neuronal AP-3 |
0.648 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268521 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 19497727 |
Mammals contain more than one AP-3 complex owing to the existence of pairs of genes encoding β3, μ3, and σ3 subunits (A and B isoforms). While both σ3A and σ3B are expressed ubiquitously and seem to be functionally equivalent, the B isoforms of β3 and μ3 display rather restricted expression patterns, mostly in cells of neuronal origin. This has led to the notion of the existence of two types of mammalian AP-3 complexes: a ubiquitous AP-3 comprising δ, β3A, μ3A, and σ3(A or B) subunits, and a brain-specific AP-3 complex containing δ, β3B, μ3B, and σ3(A or B) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
Neuronal AP-3
CPX-5053