BAIT
EPS8
DFNB102
epidermal growth factor receptor pathway substrate 8
GO Process (13)
GO Function (4)
GO Component (5)
Gene Ontology Biological Process
- Rac protein signal transduction [ISS]
- actin crosslink formation [ISS]
- actin filament bundle assembly [ISS]
- actin polymerization-dependent cell motility [ISS]
- barbed-end actin filament capping [ISS]
- cell proliferation [TAS]
- dendritic cell migration [ISS]
- epidermal growth factor receptor signaling pathway [TAS]
- exit from mitosis [ISS]
- positive regulation of signal transduction [TAS]
- regulation of actin filament length [ISS]
- regulation of cell shape [ISS]
- signal transduction [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
SERPINA5
PAI-3, PAI3, PCI, PCI-B, PLANH3, PROCI
serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 5
GO Process (4)
GO Function (7)
GO Component (19)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- acrosomal membrane [IDA]
- external side of plasma membrane [IDA]
- extracellular region [IBA, NAS, TAS]
- extracellular space [IDA]
- extracellular vesicular exosome [IDA]
- membrane [IDA]
- platelet alpha granule [IDA]
- platelet dense tubular network [IDA]
- protein C inhibitor-KLK3 complex [IDA]
- protein C inhibitor-PLAT complex [IDA]
- protein C inhibitor-PLAU complex [IDA]
- protein C inhibitor-TMPRSS11E complex [IDA]
- protein C inhibitor-TMPRSS7 complex [IDA]
- protein C inhibitor-coagulation factor V complex [IDA]
- protein C inhibitor-coagulation factor XI complex [IDA]
- protein C inhibitor-coagulation factor Xa complex [IDA]
- protein C inhibitor-plasma kallikrein complex [IDA]
- protein C inhibitor-thrombin complex [IDA]
- protein complex [IDA]
Homo sapiens
Two-hybrid
Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.
Publication
Phospho-tyrosine dependent protein-protein interaction network.
Post-translational protein modifications, such as tyrosine phosphorylation, regulate protein-protein interactions (PPIs) critical for signal processing and cellular phenotypes. We extended an established yeast two-hybrid system employing human protein kinases for the analyses of phospho-tyrosine (pY)-dependent PPIs in a direct experimental, large-scale approach. We identified 292 mostly novel pY-dependent PPIs which showed high specificity with respect to kinases and interacting proteins ... [more]
Mol. Syst. Biol. Mar. 01, 2015; 11(3);794 [Pubmed: 25814554]
Throughput
- High Throughput
Curated By
- BioGRID