ERBB2
Gene Ontology Biological Process
- Fc-epsilon receptor signaling pathway [TAS]
- axon guidance [TAS]
- cell proliferation [TAS]
- cell surface receptor signaling pathway [IDA]
- enzyme linked receptor protein signaling pathway [TAS]
- epidermal growth factor receptor signaling pathway [TAS]
- fibroblast growth factor receptor signaling pathway [TAS]
- innate immune response [TAS]
- neurotrophin TRK receptor signaling pathway [TAS]
- peptidyl-tyrosine phosphorylation [IDA, IGI, TAS]
- phosphatidylinositol 3-kinase signaling [IDA]
- phosphatidylinositol-mediated signaling [TAS]
- positive regulation of MAP kinase activity [IDA]
- positive regulation of Rho GTPase activity [ISS]
- positive regulation of cell adhesion [IDA]
- positive regulation of cell growth [IMP]
- positive regulation of epithelial cell proliferation [IDA]
- positive regulation of protein phosphorylation [ISS]
- positive regulation of transcription from RNA polymerase I promoter [IMP]
- positive regulation of transcription from RNA polymerase III promoter [IDA]
- positive regulation of translation [IMP]
- protein autophosphorylation [IDA]
- protein phosphorylation [TAS]
- regulation of ERK1 and ERK2 cascade [IMP]
- regulation of angiogenesis [NAS]
- regulation of microtubule-based process [IDA]
- signal transduction [IDA]
- signal transduction by phosphorylation [TAS]
- transmembrane receptor protein tyrosine kinase signaling pathway [IDA, TAS]
- wound healing [IDA]
Gene Ontology Molecular Function- ErbB-3 class receptor binding [TAS]
- RNA polymerase I core binding [IDA]
- growth factor binding [IDA]
- identical protein binding [IPI]
- protein C-terminus binding [IPI]
- protein binding [IPI]
- protein dimerization activity [NAS]
- protein heterodimerization activity [IDA, IPI]
- protein phosphatase binding [IPI]
- protein tyrosine kinase activity [IDA, IGI, TAS]
- transmembrane receptor protein tyrosine kinase activity [IDA]
- transmembrane signaling receptor activity [IDA]
- ErbB-3 class receptor binding [TAS]
- RNA polymerase I core binding [IDA]
- growth factor binding [IDA]
- identical protein binding [IPI]
- protein C-terminus binding [IPI]
- protein binding [IPI]
- protein dimerization activity [NAS]
- protein heterodimerization activity [IDA, IPI]
- protein phosphatase binding [IPI]
- protein tyrosine kinase activity [IDA, IGI, TAS]
- transmembrane receptor protein tyrosine kinase activity [IDA]
- transmembrane signaling receptor activity [IDA]
Gene Ontology Cellular Component
PTK7
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Affinity Capture-MS
An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.
Publication
Physical and functional interactome atlas of human receptor tyrosine kinases.
Much cell-to-cell communication is facilitated by cell surface receptor tyrosine kinases (RTKs). These proteins phosphorylate their downstream cytoplasmic substrates in response to stimuli such as growth factors. Despite their central roles, the functions of many RTKs are still poorly understood. To resolve the lack of systematic knowledge, we apply three complementary methods to map the molecular context and substrate profiles ... [more]
Quantitative Score
- 0.0 [BFDR Score]
Throughput
- High Throughput
Additional Notes
- Affinity Capture-MS was carried out to identify high confidence protein interactors with a BFDR of less than or equal to 0.05 (BFDR score reported)
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| ERBB2 PTK7 | PCA PCA A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay. | High | - | BioGRID | 2575056 |
Curated By
- BioGRID