Bone morphogenetic protein receptor type-2 (IPR015770)

Short name: BMPR2

Overlapping homologous superfamilies

Family relationships


Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity [PMID: 3291115]:

  • Serine/threonine-protein kinases
  • Tyrosine-protein kinases
  • Dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)

Protein kinase function is evolutionarily conserved from Escherichia coli to human [PMID: 12471243]. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation [PMID: 12368087]. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [PMID: 15078142], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [PMID: 15320712].

Bone morphogenetic proteins (BMPs) regulate a wide range of cellular functions that contribute to embryonic development from mesoderm formation to organogenesis [PMID: 15736264]. BMP type II receptor (BMPR2) transduces BMP signals from all BMPs by forming heteromeric complexes with and phosphorylating BMP type I receptors. Heterozygous germline mutations of BMPR-II gene in mice [PMID: 15286002] complement the finding of BMPR-II mutations in patients with familial and sporadic primary pulmonary hypertension, indicating that BMPR-II may contribute to the maintenance of normal pulmonary vascular structure and function [PMID: 15358693, PMID: 14985116].

Mice with a smooth muscle-specific transgenic mouse expressing a dominant-negative BMPR-II under control of the tetracycline develop pulmonary hypertension [PMID: 15031260]. Knockout studies have demonstrated that BMPR-II is essential for epiblast differentiation and mesoderm induction during early mouse development [PMID: 10772805]. In contrast, knockout mice that express a BMPR-II lacking half of the ligand-binding domain die at midgestation with cardiovascular and skeletal defects [PMID: 12441304].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.