BMP2
Gene Ontology Biological Process
- BMP signaling pathway [IDA, IEP, IMP, TAS]
- BMP signaling pathway involved in heart induction [IDA]
- Notch signaling pathway [ISS]
- SMAD protein signal transduction [IDA]
- activation of MAPK activity [IDA]
- atrioventricular valve morphogenesis [ISS]
- bone mineralization [ISS]
- bone mineralization involved in bone maturation [IDA]
- branching involved in ureteric bud morphogenesis [ISS]
- cardiac epithelial to mesenchymal transition [IDA]
- cardiac muscle cell differentiation [IMP]
- cardiac muscle tissue morphogenesis [ISS]
- cardiocyte differentiation [IDA, IMP]
- cell fate commitment [ISS]
- cell-cell signaling [TAS]
- cellular response to BMP stimulus [IDA]
- chondrocyte differentiation [IDA]
- corticotropin hormone secreting cell differentiation [ISS]
- embryo development [ISS]
- embryonic heart tube anterior/posterior pattern specification [ISS]
- endocardial cushion morphogenesis [ISS]
- epithelial to mesenchymal transition [IDA]
- extracellular matrix organization [TAS]
- heart development [ISS]
- in utero embryonic development [ISS]
- inflammatory response [ISS]
- inner ear development [ISS]
- mesenchymal cell differentiation [IDA]
- mesenchymal cell proliferation involved in ureteric bud development [ISS]
- mesenchyme development [IMP]
- negative regulation of Wnt signaling pathway involved in heart development [IDA]
- negative regulation of aldosterone biosynthetic process [IDA]
- negative regulation of calcium-independent cell-cell adhesion [IDA]
- negative regulation of canonical Wnt signaling pathway [IEP]
- negative regulation of cardiac muscle cell differentiation [IDA]
- negative regulation of cell cycle [IDA]
- negative regulation of cell proliferation [IDA]
- negative regulation of cortisol biosynthetic process [IDA]
- negative regulation of insulin-like growth factor receptor signaling pathway [IDA]
- negative regulation of steroid biosynthetic process [IDA]
- negative regulation of transcription from RNA polymerase II promoter [IDA]
- negative regulation of transcription, DNA-templated [IDA]
- odontogenesis of dentin-containing tooth [ISS]
- organ morphogenesis [ISS]
- osteoblast differentiation [IDA]
- pathway-restricted SMAD protein phosphorylation [IDA]
- pericardium development [ISS]
- positive regulation of ERK1 and ERK2 cascade [IDA, IMP]
- positive regulation of MAPK cascade [IDA]
- positive regulation of Wnt signaling pathway [ISS]
- positive regulation of Wnt signaling pathway by BMP signaling pathway [ISS]
- positive regulation of apoptotic process [IDA]
- positive regulation of astrocyte differentiation [ISS]
- positive regulation of bone mineralization [IDA]
- positive regulation of cartilage development [IDA]
- positive regulation of cell migration [ISS]
- positive regulation of endothelial cell proliferation [IDA]
- positive regulation of epithelial to mesenchymal transition [IDA]
- positive regulation of fat cell differentiation [ISS]
- positive regulation of gene expression [IDA]
- positive regulation of neuron differentiation [ISS]
- positive regulation of odontogenesis [ISS]
- positive regulation of ossification [IDA]
- positive regulation of osteoblast differentiation [IDA]
- positive regulation of osteoblast proliferation [ISS]
- positive regulation of p38MAPK cascade [IDA]
- positive regulation of pathway-restricted SMAD protein phosphorylation [IDA, IMP]
- positive regulation of phosphatase activity [IDA]
- positive regulation of protein phosphorylation [IDA]
- positive regulation of transcription from RNA polymerase II promoter [IDA]
- positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus [IDA]
- positive regulation of transcription, DNA-templated [IDA]
- protein phosphorylation [IDA]
- regulation of transcription, DNA-templated [IDA]
- response to hypoxia [ISS]
- skeletal system development [TAS]
- telencephalon development [IDA]
- telencephalon regionalization [ISS]
- thyroid-stimulating hormone-secreting cell differentiation [ISS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
BMPR1A
Gene Ontology Biological Process
- BMP signaling pathway [IDA, TAS]
- endocardial cushion formation [ISS]
- immune response [IMP]
- positive regulation of SMAD protein import into nucleus [IDA]
- positive regulation of bone mineralization [IMP]
- positive regulation of osteoblast differentiation [IMP]
- positive regulation of pathway-restricted SMAD protein phosphorylation [IDA]
- protein phosphorylation [IDA]
- transforming growth factor beta receptor signaling pathway [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- caveola [IMP]
- plasma membrane [IDA, TAS]
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
Type I receptor binding of bone morphogenetic protein 6 is dependent on N-glycosylation of the ligand.
Bone morphogenetic proteins (BMPs), together with transforming growth factor (TGF)-beta and activins/inhibins, constitute the TGF-beta superfamily of ligands. This superfamily is formed by more than 30 structurally related secreted proteins. The crystal structure of human BMP-6 was determined to a resolution of 2.1 A; the overall structure is similar to that of other TGF-beta superfamily ligands, e.g. BMP-7. The asymmetric ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| BMPR1A BMP2 | Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex. | Low | - | BioGRID | 245047 | |
| BMP2 BMPR1A | 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 | - | |
| BMP2 BMPR1A | 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 | - | |
| BMP2 BMPR1A | 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