NRG2
Gene Ontology Biological Process
- Fc-epsilon receptor signaling pathway [TAS]
- epidermal growth factor receptor signaling pathway [TAS]
- fibroblast growth factor receptor signaling pathway [TAS]
- innate immune response [TAS]
- intracellular signal transduction [IBA]
- neurotrophin TRK receptor signaling pathway [TAS]
- organ development [IBA]
- phosphatidylinositol-mediated signaling [TAS]
- signal transduction [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
ERBB4
Gene Ontology Biological Process
- Fc-epsilon receptor signaling pathway [TAS]
- cardiac muscle tissue regeneration [ISS]
- cell migration [IDA]
- cell proliferation [TAS]
- central nervous system morphogenesis [ISS]
- embryonic pattern specification [ISS]
- epidermal growth factor receptor signaling pathway [TAS]
- fibroblast growth factor receptor signaling pathway [TAS]
- heart development [ISS]
- innate immune response [TAS]
- lactation [IMP]
- mammary gland alveolus development [ISS]
- mammary gland epithelial cell differentiation [ISS]
- mitochondrial fragmentation involved in apoptotic process [IMP]
- negative regulation of apoptotic process [IMP]
- negative regulation of cell proliferation [IMP]
- nervous system development [ISS]
- neural crest cell migration [ISS]
- neurotrophin TRK receptor signaling pathway [TAS]
- olfactory bulb interneuron differentiation [ISS]
- peptidyl-tyrosine phosphorylation [IDA]
- phosphatidylinositol-mediated signaling [TAS]
- positive regulation of ERK1 and ERK2 cascade [IMP]
- positive regulation of STAT protein import into nucleus [IMP]
- positive regulation of cardiac muscle cell proliferation [ISS]
- positive regulation of cell proliferation [IMP]
- positive regulation of phosphatidylinositol 3-kinase activity [IDA]
- positive regulation of protein phosphorylation [TAS]
- positive regulation of transcription, DNA-templated [IMP]
- positive regulation of tyrosine phosphorylation of Stat5 protein [IMP]
- protein autophosphorylation [IDA]
- regulation of cell migration [ISS]
- signal transduction [IDA]
- transmembrane receptor protein tyrosine kinase signaling pathway [IDA]
Gene Ontology Molecular Function
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
Neuregulin-2, a new ligand of ErbB3/ErbB4-receptor tyrosine kinases.
The neuregulins (NRGs) are a family of multipotent epidermal-growth-factor-like (EGF-like) factors that arise from splice variants of a single gene. They influence the growth, differentiation, survival and fate of several cell types. We have now discovered a set of new neuregulin-like growth factors, which we call neuregulin-2 (NRG-2): these are encoded by their own gene and exhibit a distinct expression ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| ERBB4 NRG2 | 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