| Post Translational Modifications | Autophosphorylated. Binding of FGF family members together with heparan sulfate proteoglycan or heparin promotes receptor dimerization and autophosphorylation on tyrosine residues. Autophosphorylation occurs in trans between the two FGFR molecules present in the dimer. Phosphorylation at Tyr-724 is essential for stimulation of cell proliferation and activation of PIK3R1, STAT1 and MAP kinase signaling. Phosphorylation at Tyr-760 is required for interaction with PIK3R1 and PLCG1. Ubiquitinated. Is rapidly ubiquitinated after ligand binding and autophosphorylation, leading to receptor internalization and degradation. Subject to both proteasomal and lysosomal degradation. N-glycosylated in the endoplasmic reticulum. The N-glycan chains undergo further maturation to an Endo H-resistant form in the Golgi apparatus. |
| Function | Tyrosine-protein kinase that acts as a cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation and apoptosis. Plays an essential role in the regulation of chondrocyte differentiation, proliferation and apoptosis, and is required for normal skeleton development. Regulates both osteogenesis and postnatal bone mineralization by osteoblasts. Promotes apoptosis in chondrocytes, but can also promote cancer cell proliferation. Required for normal development of the inner ear. Phosphorylates PLCG1, CBL and FRS2. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Plays a role in the regulation of vitamin D metabolism. Mutations that lead to constitutive kinase activation or impair normal FGFR3 maturation, internalization and degradation lead to aberrant signaling. Over-expressed or constitutively activated FGFR3 promotes activation of PTPN11/SHP2, STAT1, STAT5A and STAT5B. Secreted isoform 3 retains its capacity to bind FGF1 and FGF2 and hence may interfere with FGF signaling. |
| Protein Name | Fibroblast Growth Factor Receptor 3Fgfr-3Cd Antigen Cd333 |
| Database Links | Reactome: R-HSA-109704Reactome: R-HSA-1257604Reactome: R-HSA-1839130Reactome: R-HSA-190371 P22607-2Reactome: R-HSA-190372 P22607-1Reactome: R-HSA-2033515Reactome: R-HSA-2219530Reactome: R-HSA-5654227Reactome: R-HSA-5654704Reactome: R-HSA-5654706Reactome: R-HSA-5654710Reactome: R-HSA-5654732Reactome: R-HSA-5655332Reactome: R-HSA-5673001Reactome: R-HSA-6811558Reactome: R-HSA-8853334 |
| Cellular Localisation | Isoform 1: Cell MembraneSingle-Pass Type I Membrane ProteinCytoplasmic VesicleEndoplasmic ReticulumThe Activated Receptor Is Rapidly Internalized And DegradedDetected In Intracellular Vesicles After Internalization Of The Autophosphorylated ReceptorIsoform 2: Cell MembraneIsoform 3: SecretedIsoform 4: Cell Membrane |
| Alternative Protein Names | Fibroblast Growth Factor Receptor 3 proteinFgfr-3 proteinCd Antigen Cd333 proteinFGFR3 proteinJTK4 protein |
Information sourced from Uniprot.org
