| + |
AP-2 complex | down-regulates quantity 
relocalization
|
GABA-A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264990 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 25600368 |
The endocytosis of GABAARs is regulated by the interaction of the AP2 complex with β and γ2 subunits. Phosphorylation of β3 (S408/S409) and γ2 (Y365/Y367) by PKA/PKC and Src/Fyn, respectively, prevents binding to AP2 and thus stabilizes these receptors at the cell surface. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | GABAergic synapse |
| + |
ATP6V1H | up-regulates activity 
binding
|
AP-2 complex |
0.229 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266887 |
|
|
Mus musculus |
Bone Marrow Stromal Cell |
| pmid |
sentence |
| 29782852 |
ATP6V1H interacts with TGF-β receptor I and AP-2 complex to regulate the proliferation and differentiation of BMSCs. Lack of ATP6V1H function decreases bone formation in vivo |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
AP-2 complex | up-regulates activity
binding
|
EPS15 |
0.651 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260394 |
|
|
Rattus norvegicus |
Brain |
| pmid |
sentence |
| 15496985 |
Some of the more minor interactors are very strongly enriched (AAK, auxilin, Dab2, eps15, epsin1 and synaptojanin170). All these enriched proteins have multiple copies of short alpha‐appendage interaction motifs |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
NECAP1 | up-regulates activity
binding
|
AP-2 complex |
0.458 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260710 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24130457 |
Knockdown and functional rescue studies demonstrate that through these interactions, NECAP 1 and AP-2 cooperate to increase the probability of clathrin-coated vesicle formation and to control the number, size, and cargo content of the vesicles. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AP2M1 | form complex 
binding
|
AP-2 complex |
0.913 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260420 |
|
|
|
|
| pmid |
sentence |
| 31671891 |
The most important endocytic adaptor is the heterotetrameric AP-2 complex made up of the large alpha- and beta2-adaptin subunits, the medium-sized mu2-subunit and a small sigma2-subunit |
|
| Publications: |
1 |
| + |
AP-2 complex | up-regulates activity
binding
|
AAK1 |
0.634 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260393 |
|
|
Rattus norvegicus |
Brain |
| pmid |
sentence |
| 15496985 |
We therefore characterised protein ligands using liquid chromatography tandem mass spectrometry (LC‐MS/MS) and confirmed this using Western blotting to recognise both major and minor bands. Some of the more minor interactors are very strongly enriched (AAK, auxilin, Dab2, eps15, epsin1 and synaptojanin170). All these enriched proteins have multiple copies of short alpha‐appendage interaction motifs |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
AP-2 complex | up-regulates activity
binding
|
DAB2 |
0.485 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260391 |
|
|
Homo sapiens |
HFF-1 Cell, HeLa Cell |
| pmid |
sentence |
| 11247302 |
Dab2 is alternatively spliced and its localization depends on a region of the protein that contains two DPF motifs that are present in the p96 Dab2 protein and absent in the p67 splice variant. This region is sufficient to confer Dab2 binding to the alpha‐adaptin subunit of the clathrin adaptor protein, AP‐2.|These findings suggest that in addition to previously reported signal-transduction functions, Dab2 could also act as an adaptor protein that may regulate protein trafficking. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AP-2 complex | up-regulates activity
binding
|
HIP1 |
0.424 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260392 |
|
|
Rattus norvegicus |
|
| pmid |
sentence |
| 11517213 |
HIP1 functions in clathrin-mediated endocytosis through binding to clathrin and adaptor protein 2.|Here we demonstrate that HIP1 colocalizes with markers of clathrin-mediated endocytosis in neuronal cells and is highly enriched on clathrin-coated vesicles (CCVs) purified from brain homogenates. HIP1 binds to the clathrin adaptor protein 2 (AP2) and the terminal domain of the clathrin heavy chain, predominantly through a small fragment encompassing amino acids 276–335 |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
AP2S1 | form complex
binding
|
AP-2 complex |
0.911 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260421 |
|
|
|
|
| pmid |
sentence |
| 31671891 |
The most important endocytic adaptor is the heterotetrameric AP-2 complex made up of the large alpha- and beta2-adaptin subunits, the medium-sized mu2-subunit and a small sigma2-subunit |
|
| Publications: |
1 |
| + |
AP-2 complex | up-regulates activity
binding
|
ITSN1 |
0.637 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260397 |
|
|
Rattus norvegicus |
Brain |
| pmid |
sentence |
| 15496985 |
Intersectins 1 and 2, epsin2, NECAP and sorting nexin9 were identified as α‐appendage ligands in mass spectrometry of these samples |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
AP2B1 | form complex
binding
|
AP-2 complex |
0.851 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260422 |
|
|
|
|
| pmid |
sentence |
| 31671891 |
The most important endocytic adaptor is the heterotetrameric AP-2 complex made up of the large alpha- and beta2-adaptin subunits, the medium-sized mu2-subunit and a small sigma2-subunit |
|
| Publications: |
1 |
| + |
AP-2 complex | up-regulates activity
binding
|
EPN1 |
0.545 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260395 |
|
|
Rattus norvegicus |
Brain |
| pmid |
sentence |
| 15496985 |
Some of the more minor interactors are very strongly enriched (AAK, auxilin, Dab2, eps15, epsin1 and synaptojanin170). All these enriched proteins have multiple copies of short alpha‐appendage interaction motifs |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
AP-2 complex | form complex
binding
|
AP-2/clathrin vescicle |
0.627 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260663 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24789820 |
AP2 adaptor complexes, associated at the membrane with PtdIns(4,5)P2 (PIP2), recruit clathin triskelions to initiate lattice assembly. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AP2A2 | form complex
binding
|
AP-2 complex |
0.847 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260423 |
|
|
|
|
| pmid |
sentence |
| 31671891 |
The most important endocytic adaptor is the heterotetrameric AP-2 complex made up of the large alpha- and beta2-adaptin subunits, the medium-sized mu2-subunit and a small sigma2-subunit |
|
| Publications: |
1 |
| + |
AP-2 complex | up-regulates activity
binding
|
SYNJ1 |
0.495 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260396 |
|
|
Rattus norvegicus |
|
| pmid |
sentence |
| 15496985 |
Some of the more minor interactors are very strongly enriched (AAK, auxilin, Dab2, eps15, epsin1 and synaptojanin170). All these enriched proteins have multiple copies of short alpha‐appendage interaction motifs |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
AP-2 complex | up-regulates 
|
Endocytosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260416 |
|
|
Rattus norvegicus |
Brain |
| pmid |
sentence |
| 15496985 |
Intersectins 1 and 2, epsin2, NECAP and sorting nexin9 were identified as α‐appendage ligands in mass spectrometry of these samples |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
3.0
AP-2 complex
CPX-5150