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
ABL1
Gene Ontology Biological Process
- DNA damage induced protein phosphorylation [IDA]
- Fc-gamma receptor signaling pathway involved in phagocytosis [TAS]
- actin cytoskeleton organization [ISS]
- axon guidance [TAS]
- blood coagulation [TAS]
- cell cycle arrest [TAS]
- cell differentiation [IBA]
- cell migration [IBA]
- cellular protein modification process [NAS]
- cellular response to DNA damage stimulus [IDA]
- cellular response to dopamine [TAS]
- cellular response to oxidative stress [TAS]
- epidermal growth factor receptor signaling pathway [IBA]
- innate immune response [IBA, TAS]
- intrinsic apoptotic signaling pathway in response to DNA damage [TAS]
- mismatch repair [TAS]
- mitochondrial depolarization [TAS]
- mitotic nuclear division [TAS]
- muscle cell differentiation [TAS]
- negative regulation of phospholipase C activity [IMP]
- negative regulation of protein serine/threonine kinase activity [IDA]
- negative regulation of ubiquitin-protein transferase activity [IDA, TAS]
- peptidyl-tyrosine autophosphorylation [IBA]
- peptidyl-tyrosine phosphorylation [IDA, TAS]
- platelet-derived growth factor receptor signaling pathway [IBA]
- positive regulation of apoptotic process [IDA]
- positive regulation of cytosolic calcium ion concentration [IMP]
- positive regulation of muscle cell differentiation [TAS]
- positive regulation of oxidoreductase activity [IDA]
- positive regulation of peptidyl-tyrosine phosphorylation [IDA]
- regulation of actin cytoskeleton reorganization [TAS]
- regulation of autophagy [TAS]
- regulation of cell adhesion [TAS]
- regulation of cell motility [TAS]
- regulation of cell proliferation [IBA]
- regulation of endocytosis [TAS]
- regulation of response to DNA damage stimulus [IDA]
- regulation of transcription, DNA-templated [TAS]
- response to oxidative stress [IGI]
- signal transduction in response to DNA damage [IDA]
Gene Ontology Molecular Function- ATP binding [IDA]
- DNA binding [NAS]
- SH3 domain binding [IPI]
- actin monomer binding [TAS]
- magnesium ion binding [IDA]
- manganese ion binding [IDA]
- mitogen-activated protein kinase binding [IPI]
- nicotinate-nucleotide adenylyltransferase activity [TAS]
- non-membrane spanning protein tyrosine kinase activity [IDA]
- proline-rich region binding [IDA, IPI]
- protein C-terminus binding [IPI]
- protein binding [IPI]
- protein kinase activity [IDA]
- protein tyrosine kinase activity [IDA]
- receptor binding [IBA]
- syntaxin binding [IPI]
- ATP binding [IDA]
- DNA binding [NAS]
- SH3 domain binding [IPI]
- actin monomer binding [TAS]
- magnesium ion binding [IDA]
- manganese ion binding [IDA]
- mitogen-activated protein kinase binding [IPI]
- nicotinate-nucleotide adenylyltransferase activity [TAS]
- non-membrane spanning protein tyrosine kinase activity [IDA]
- proline-rich region binding [IDA, IPI]
- protein C-terminus binding [IPI]
- protein binding [IPI]
- protein kinase activity [IDA]
- protein tyrosine kinase activity [IDA]
- receptor binding [IBA]
- syntaxin binding [IPI]
Gene Ontology Cellular Component
Far Western
An interaction is detected between a protein immobilized on a membrane and a purified protein probe.
Publication
Reciprocal regulation of Abl and receptor tyrosine kinases.
Previously, we showed that Abl kinases (c-Abl, Arg) are activated downstream of PDGF in a manner dependent on Src kinases and PLC-gamma1, and promote PDGF-mediated proliferation and migration of fibroblasts. We additionally demonstrated that Abl kinases bind directly to PDGFR-beta via their SH2 domains.In this study, we extend these findings by demonstrating that Abl kinases also are activated downstream of ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| ERBB2 ABL1 | Biochemical Activity Biochemical Activity An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation. | Low | - | BioGRID | 2526429 | |
| ABL1 ERBB2 | Protein-peptide Protein-peptide An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments. | High | - | BioGRID | 833462 | |
| ERBB2 ABL1 | 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 | 5.35 | BioGRID | 2846929 | |
| ABL1 ERBB2 | 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 | - |
Curated By
- BioGRID