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]
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
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.
Publication
The crystal structure of the BMP-2:BMPR-IA complex and the generation of BMP-2 antagonists.
BACKGROUND: Bone morphogenetic proteins (BMPs) and growth and differentiation factors (GDFs) belong to the large transforming growth factor-beta (TGF-beta) superfamily of multifunctional cytokines. Signaling of the BMPs requires the binding of the BMP to the BMP cell surface receptors BMPR-IA, BMPR-IB, and BMPR-II. Similar to other cytokines, members of the TGF-beta superfamily exhibit stringent specificity in their ligand-receptor interactions, which ... [more]
Throughput
- Low Throughput
Additional Notes
- The wrist epitope identified in the homodimeric BMP-2 molecule encompasses a large area that correlates with the high affinity for BMPR-IA binding; BMPR-II binding residues in the knuckle epitope of BMP-2 are provided by only one monomer and are located i
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| 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 | - | |
| 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