PIK3R2
Gene Ontology Biological Process
- Fc-epsilon receptor signaling pathway [TAS]
- Fc-gamma receptor signaling pathway involved in phagocytosis [TAS]
- T cell receptor signaling pathway [TAS]
- blood coagulation [TAS]
- cellular glucose homeostasis [ISS]
- cellular response to insulin stimulus [ISS]
- epidermal growth factor receptor signaling pathway [TAS]
- fibroblast growth factor receptor signaling pathway [TAS]
- innate immune response [TAS]
- insulin receptor signaling pathway [TAS]
- leukocyte migration [TAS]
- neurotrophin TRK receptor signaling pathway [TAS]
- phosphatidylinositol 3-kinase signaling [IDA]
- phosphatidylinositol biosynthetic process [TAS]
- phosphatidylinositol-3-phosphate biosynthetic process [ISS]
- phosphatidylinositol-mediated signaling [TAS]
- phospholipid metabolic process [TAS]
- positive regulation of transcription factor import into nucleus [ISS]
- positive regulation of transcription from RNA polymerase II promoter [ISS]
- regulation of autophagy [IMP]
- regulation of small GTPase mediated signal transduction [TAS]
- response to endoplasmic reticulum stress [ISS]
- small GTPase mediated signal transduction [TAS]
- small molecule metabolic process [TAS]
Gene Ontology Molecular Function
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
Protein-peptide
An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments.
Publication
A quantitative protein interaction network for the ErbB receptors using protein microarrays.
Although epidermal growth factor receptor (EGFR; also called ErbB1) and its relatives initiate one of the most well-studied signalling networks, there is not yet a genome-wide view of even the earliest step in this pathway: recruitment of proteins to the activated receptors. Here we use protein microarrays comprising virtually every Src homology 2 (SH2) and phosphotyrosine binding (PTB) domain encoded ... [more]
Throughput
- High Throughput
Additional Notes
- interaction detected by probing protein array with labeled peptides
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| ERBB2 PIK3R2 | Affinity Capture-MS 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. | High | 0 | BioGRID | 3509692 | |
| ERBB2 PIK3R2 | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | - | |
| ERBB2 PIK3R2 | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | High | 1.73 | BioGRID | 2846953 |
Curated By
- BioGRID