ERBB3
Gene Ontology Biological Process
- Fc-epsilon receptor signaling pathway [TAS]
- Schwann cell differentiation [ISS]
- cranial nerve development [ISS]
- epidermal growth factor receptor signaling pathway [TAS]
- extrinsic apoptotic signaling pathway in absence of ligand [IMP]
- fibroblast growth factor receptor signaling pathway [TAS]
- heart development [ISS]
- innate immune response [TAS]
- negative regulation of cell adhesion [IDA]
- negative regulation of neuron apoptotic process [ISS]
- negative regulation of secretion [IDA]
- negative regulation of signal transduction [IDA]
- neuron apoptotic process [IMP]
- neurotrophin TRK receptor signaling pathway [TAS]
- peripheral nervous system development [ISS]
- phosphatidylinositol 3-kinase signaling [IDA]
- phosphatidylinositol-mediated signaling [TAS]
- positive regulation of phosphatidylinositol 3-kinase signaling [TAS]
- positive regulation of protein tyrosine kinase activity [IMP]
- regulation of cell proliferation [IDA]
- signal transduction [IDA]
- transmembrane receptor protein tyrosine kinase signaling pathway [ISS]
- wound healing [NAS]
Gene Ontology Molecular Function- growth factor binding [IPI, ISS]
- identical protein binding [IPI]
- protein binding [IPI]
- protein heterodimerization activity [IDA, IPI]
- protein homodimerization activity [NAS]
- protein tyrosine kinase activator activity [IDA]
- protein tyrosine kinase activity [IDA]
- transmembrane signaling receptor activity [ISS]
- growth factor binding [IPI, ISS]
- identical protein binding [IPI]
- protein binding [IPI]
- protein heterodimerization activity [IDA, IPI]
- protein homodimerization activity [NAS]
- protein tyrosine kinase activator activity [IDA]
- protein tyrosine kinase activity [IDA]
- transmembrane signaling receptor activity [ISS]
Gene Ontology Cellular Component
NRG1
Gene Ontology Biological Process
- ERBB signaling pathway [IDA]
- Fc-epsilon receptor signaling pathway [TAS]
- activation of transmembrane receptor protein tyrosine kinase activity [IDA, NAS]
- cardiac muscle cell differentiation [ISS]
- cardiac muscle cell myoblast differentiation [IDA]
- cell communication [TAS]
- cell proliferation [IDA]
- cellular protein complex disassembly [IGI]
- endocardial cell differentiation [IDA]
- epidermal growth factor receptor signaling pathway [TAS]
- fibroblast growth factor receptor signaling pathway [TAS]
- innate immune response [TAS]
- intracellular signal transduction [IBA]
- mammary gland development [TAS]
- negative regulation of cardiac muscle cell apoptotic process [IDA]
- negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [IDA]
- negative regulation of secretion [IDA]
- negative regulation of transcription, DNA-templated [IDA]
- nervous system development [TAS]
- neural crest cell development [TAS]
- neurotrophin TRK receptor signaling pathway [TAS]
- phosphatidylinositol-mediated signaling [TAS]
- positive regulation of cardiac muscle cell proliferation [IDA]
- positive regulation of cell adhesion [IDA]
- positive regulation of cell growth [IDA]
- positive regulation of protein tyrosine kinase activity [IDA]
- positive regulation of striated muscle cell differentiation [ISS]
- regulation of protein heterodimerization activity [IDA]
- regulation of protein homodimerization activity [TAS]
- transmembrane receptor protein tyrosine kinase signaling pathway [IDA]
- ventricular cardiac muscle cell differentiation [IDA]
- ventricular trabecula myocardium morphogenesis [IDA]
- wound healing [IDA, TAS]
Gene Ontology Molecular Function- ErbB-3 class receptor binding [IDA, IPI]
- cytokine activity [TAS]
- growth factor activity [IDA, NAS]
- protein binding [IPI]
- protein tyrosine kinase activator activity [IDA]
- receptor binding [IPI]
- receptor tyrosine kinase binding [NAS]
- transcription cofactor activity [IDA]
- transmembrane receptor protein tyrosine kinase activator activity [IC, NAS]
- ErbB-3 class receptor binding [IDA, IPI]
- cytokine activity [TAS]
- growth factor activity [IDA, NAS]
- protein binding [IPI]
- protein tyrosine kinase activator activity [IDA]
- receptor binding [IPI]
- receptor tyrosine kinase binding [NAS]
- transcription cofactor activity [IDA]
- transmembrane receptor protein tyrosine kinase activator activity [IC, NAS]
Gene Ontology Cellular Component
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.
Publication
Identification of a heregulin binding site in HER3 extracellular domain.
HER3 (also known as c-Erb-b3) is a type I receptor tyrosine kinase similar in sequence to the epidermal growth factor (EGF) receptor. The extracellular segment of this transmembrane receptor contains four domains. Domains I and II are similar in sequence to domains III and IV, respectively, and domains II and IV are cysteine-rich. We show that the EGF-like domain of ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| NRG1 ERBB3 | 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 | 1 | BioGRID | 3181663 | |
| NRG1 ERBB3 | 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 | - | |
| NRG1 ERBB3 | 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 | - | |
| ERBB3 NRG1 | 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 | - | |
| ERBB3 NRG1 | 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 | - | |
| NRG1 ERBB3 | 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 | - | |
| ERBB3 NRG1 | 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