Relation Results

Summary

Name AP-2 complex
Primary ID SIGNOR-C245
Links CPX-5150
Type complex
Formed by AP2A2, AP2B1, AP2M1, AP2S1
Relations 16
Pathways GABAergic synapse

Viewer

Type: Score: Layout: SPV 
0.4680.4340.6460.20.70.5040.5880.9130.4950.2280.8550.5530.9150.8510.6570.643NECAP1AP-2 complexHIP1ITSN1GABA-AEndocytosisSYNJ1AP-2/clathrin vescicleAP2S1DAB2ATP6V1HAP2B1EPN1AP2M1AP2A2EPS15AAK1

Search Tools

Refine search:

  • by mechanism


  • by effect
  • by organism:


  • by tissue:


  • by cell-line

Relations
Regulator
Mechanism
target
score ℹ
+ NECAP1up-regulates activity img/direct-activation.png binding AP-2 complex 0.468
Identifier Residue Sequence Organism Cell Line
SIGNOR-260710 Homo sapiens
pmid sentence
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
+ AP-2 complexup-regulates activity img/direct-activation.png binding HIP1 0.434
Identifier Residue Sequence Organism Cell Line
SIGNOR-260392 Rattus norvegicus
pmid sentence
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
+ AP-2 complexup-regulates activity img/direct-activation.png binding ITSN1 0.646
Identifier Residue Sequence Organism Cell Line
SIGNOR-260397 Rattus norvegicus Brain
pmid sentence
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
+ AP-2 complexdown-regulates quantity img/direct_inhibition.png relocalization GABA-A 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-264990 Homo sapiens Neuron
pmid sentence
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
+ AP-2 complexup-regulates img/indirect-activation.png Endocytosis 0.7
Identifier Residue Sequence Organism Cell Line
SIGNOR-260416 Rattus norvegicus Brain
pmid sentence
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
+ AP-2 complexup-regulates activity img/direct-activation.png binding SYNJ1 0.504
Identifier Residue Sequence Organism Cell Line
SIGNOR-260396 Rattus norvegicus
pmid sentence
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 complexform complex img/form-complex.png binding AP-2/clathrin vescicle 0.588
Identifier Residue Sequence Organism Cell Line
SIGNOR-260663 Homo sapiens
pmid sentence
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
+ AP2S1form complex img/form-complex.png binding AP-2 complex 0.913
Identifier Residue Sequence Organism Cell Line
SIGNOR-260421
pmid sentence
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 complexup-regulates activity img/direct-activation.png binding DAB2 0.495
Identifier Residue Sequence Organism Cell Line
SIGNOR-260391 Homo sapiens HFF-1 Cell, HeLa Cell
pmid sentence
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
+ ATP6V1Hup-regulates activity img/direct-activation.png binding AP-2 complex 0.228
Identifier Residue Sequence Organism Cell Line
SIGNOR-266887 Mus musculus Bone Marrow Stromal Cell
pmid sentence
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
+ AP2B1form complex img/form-complex.png binding AP-2 complex 0.855
Identifier Residue Sequence Organism Cell Line
SIGNOR-260422
pmid sentence
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 complexup-regulates activity img/direct-activation.png binding EPN1 0.553
Identifier Residue Sequence Organism Cell Line
SIGNOR-260395 Rattus norvegicus Brain
pmid sentence
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
+ AP2M1form complex img/form-complex.png binding AP-2 complex 0.915
Identifier Residue Sequence Organism Cell Line
SIGNOR-260420
pmid sentence
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
+ AP2A2form complex img/form-complex.png binding AP-2 complex 0.851
Identifier Residue Sequence Organism Cell Line
SIGNOR-260423
pmid sentence
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 complexup-regulates activity img/direct-activation.png binding EPS15 0.657
Identifier Residue Sequence Organism Cell Line
SIGNOR-260394 Rattus norvegicus Brain
pmid sentence
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 complexup-regulates activity img/direct-activation.png binding AAK1 0.643
Identifier Residue Sequence Organism Cell Line
SIGNOR-260393 Rattus norvegicus Brain
pmid sentence
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
a simple tooltip