a receptor tyrosine kinase of the PDGFR family that binds members of the platelet-derived growth factor family. The identity of the growth factor bound determines whether the functional receptor is a homodimer or a heterodimer, composed of both PDGFR-alpha and -beta. Ligand binding induces receptor dimerization and autophosphorylation, thereby recruiting SH2-containing proteins including Grb2, Src, GAP, PTPN11, PI3 kinase, PLC-gamma and Nck. Regulates cell growth, actin reorganization, migration and differentiation. A variety of myeloproliferative disorders and cancers result from translocations that activate PDGFRbeta by fusion with proteins such as TEL/ETV6, H2, CEV14/TRP11, rabaptin 5, and huntington interacting protein 1. Gleevec treatment of TEL fusions has been successful. Overexpressed in metastatic medulloblastoma. Inhibitors: Gleevec, Sutent. Note: This description may include information from UniProtKB.
Protein type: Kinase, protein; Oncoprotein; Membrane protein, integral; EC 188.8.131.52; Protein kinase, tyrosine (receptor); Protein kinase, TK; TK group; PDGFR family
LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.