Post Translational Modifications | The soluble form (GHBP) is produced by phorbol ester-promoted proteolytic cleavage at the cell surface (shedding) by ADAM17/TACE. Shedding is inhibited by growth hormone (GH) binding to the receptor probably due to a conformational change in GHR rendering the receptor inaccessible to ADAM17. On GH binding, phosphorylated on tyrosine residues in the cytoplasmic domain by JAK2. Ubiquitinated by the ECS(SOCS2) complex following ligand-binding and phosphorylation by JAK2, leading to its degradation by the proteasome. Regulation by the ECS(SOCS2) complex acts as a negative feedback loop of growth hormone receptor signaling. Ubiquitination is not sufficient for GHR internalization. |
Function | Receptor for pituitary gland growth hormone (GH1) involved in regulating postnatal body growth. On ligand binding, couples to the JAK2/STAT5 pathway. Growth hormone-binding protein: The soluble form (GHBP) acts as a reservoir of growth hormone in plasma and may be a modulator/inhibitor of GH signaling. Isoform 2: Up-regulates the production of the soluble Growth hormone-binding protein form (GHBP) and acts as a negative inhibitor of growth hormone signaling. |
Protein Name | Growth Hormone ReceptorGh ReceptorSomatotropin Receptor Cleaved Into - Growth Hormone-Binding ProteinGh-Binding ProteinGhbpSerum-Binding Protein |
Database Links | Reactome: R-HSA-1170546Reactome: R-HSA-982772 |
Cellular Localisation | Cell MembraneSingle-Pass Type I Membrane ProteinOn Growth Hormone BindingGhr Is UbiquitinatedInternalizedDown-Regulated And Transported Into A Degradative Or Non-Degradative PathwayIsoform 2: Cell MembraneRemains Fixed To The Cell Membrane And Is Not InternalizedGrowth Hormone-Binding Protein: SecretedComplexed To A Substantial Fraction Of Circulating Gh |
Alternative Protein Names | Growth Hormone Receptor proteinGh Receptor proteinSomatotropin Receptor Cleaved Into - Growth Hormone-Binding Protein proteinGh-Binding Protein proteinGhbp proteinSerum-Binding Protein proteinGHR protein |
Information sourced from Uniprot.org