PDGFRB PDGFR PDGFR1

PDGFRB ;
PDGFR ;
PDGFR1 ;
Platelet-derived growth factor receptor beta ;
PDGF-R-beta ;
PDGFR-beta ;
Beta platelet-derived growth factor receptor ;
Beta-type platelet-derived growth factor receptor ;
CD140 antigen-like family member B ;
Platelet-deri

catalytic activity:ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. ,disease:A chromosomal aberration involving PDGFRB is a cause in many instances of chronic myeloproliferative disorder with eosinophilia (MPE) [MIM:131440]. Translocation t (5;12) with ETV6 on chromosome 12 creating an PDGFRB-ETV6 fusion protein. ,disease:A chromosomal aberration involving PDGFRB is found in a form of chronic myelomonocytic leukemia (CMML) . Translocation t (5;12) (q33;p13) with EVT6/TEL. It is characterized by abnormal clonal myeloid proliferation and by progression to acute myelogenous leukemia (AML) . ,disease:A chromosomal aberration involving PDGFRB may be a cause of acute myelogenous leukemia. Translocation t (5;14) (q33;q32) with TRIP11. The fusion protein may be involved in clonal evolution of leukemia and eosinophilia. ,disease:A chromosomal aberration involving PDGFRB may be a cause of juvenile myelomonocytic leukemia. Translocation t (5;17) (q33;p11.2) with SPECC1. ,disease:A chromosomal aberration involving PDGFRB may be the cause of a myeloproliferative disorder (MBD) associated with eosinophilia. Translocation t (1;5) (q23;q33) that forms a PDE4DIP-PDGFRB fusion protein. ,function:Receptor that binds specifically to PDGFB and PDGFD and has a tyrosine-protein kinase activity. Phosphorylates Tyr residues at the C-terminus of PTPN11 creating a binding site for the SH2 domain of GRB2. ,similarity:Belongs to the protein kinase superfamily. Tyr protein kinase family. ,similarity:Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily. ,similarity:Contains 1 protein kinase domain. ,similarity:Contains 5 Ig-like C2-type (immunoglobulin-like) domains. ,subunit:Homodimer , and heterodimer with PDGFRA. Interacts with APS. The autophosphorylated form interacts directly with SHB and with PIK3C2B , maybe indirectly. ,

skeletal system development , urogenital system development , in utero embryonic development , kidney development ,tissue homeostasis , regulation of protein amino acid phosphorylation , protein amino acid phosphorylation ,phosphorus metabolic process , phosphate metabolic process , cell motion , chemotaxis , cell surface receptor linked signal transduction , enzyme linked receptor protein signaling pathway , transmembrane receptor protein tyrosine kinase signaling pathway , muscle organ development , behavior , locomotory behavior , positive regulation of cell proliferation , embryonic development ending in birth or egg hatching , phosphorylation , cell migration , peptidyl-tyrosine phosphorylation , peptidyl-tyrosine modification , regulation of phosphate metabolic process , regulation of cell migration , positive regulation of cell migration , regulation of protein modification process , regulation of cellular protein metabolic process , regulation of locomotion , positive regulation of locomotion , regulation of cell proliferation ,regulation of phosphorylation , taxis , homeostatic process , chordate embryonic development , protein amino acid autophosphorylation , platelet-derived growth factor receptor signaling pathway , vascular endothelial growth factor receptor signaling pathway , skeletal system morphogenesis , smooth muscle tissue development , cell motility ,multicellular organismal homeostasis , regulation of peptidyl-tyrosine phosphorylation , regulation of phosphorus metabolic process , regulation of cell motion , positive regulation of cell motion , localization of cell , anatomical structure homeostasis , cell chemotaxis , muscle tissue development ,

Cell membrane; Single-pass type I membrane protein. Cytoplasmic vesicle. Lysosome lumen. After ligand binding , the autophosphorylated receptor is ubiquitinated and internalized , leading to its degradation.