Gene content    
PDGFRB ( by HUGO)
Platelet-Derived Growth Factor Receptor, Beta Polypeptide
Oncogene
Platelet-Derived Growth Factor Receptor
Beta Polypeptide
PDGFR
Beta-Type Platelet-Derived Growth Factor Receptor
Platelet-Derived Growth Factor Receptor 1
PDGF-R-beta
PDGFR-1
PDGFR-beta
PDGFR1
CD140 Antigen-Like Family Member B
EC 2.7.10.1
IBGC4
IMF1
CD140B
JTK12
Platelet-Derived Growth Factor Receptor Beta
Beta Platelet-Derived Growth Factor Receptor
CD140b Antigen
EC 2.7.10
NCBI: 5q33.1    Ensembl: 5q32
PGFRB_HUMANSize: 1106 amino acidsMass: 123968 Da

  • Subunit: Interacts with homodimeric PDGFB and PDGFD, and with heterodimers formed by PDGFA and PDGFB. May also interact with homodimeric PDGFC. Monomer in the absence of bound ligand. Interaction with homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFD, leads to receptor dimerization, where both PDGFRA homodimers and heterodimers with PDGFRB are observed. Interacts with SH2B2/APS. Interacts directly (tyrosine phosphorylated) with SHB. Interacts (tyrosine phosphorylated) with PIK3R1. Interacts (tyrosine phosphorylated) with CBL. Interacts (tyrosine phosphorylated) with SRC and SRC family kinases. Interacts (tyrosine phosphorylated) with PIK3C2B, maybe indirectly. Interacts (tyrosine phosphorylated) with SHC1, GRB7, GRB10 and NCK1. Interaction with GRB2 is mediated by SHC1. Interacts (via C-terminus) with SLC9A3R1 Selected PDB 3D structures from [IMAGE] and Proteopedia [IMAGE] for PDGFRB (see all 7): 1GQ5 (3D) [IMAGE] 1H9O (3D) [IMAGE] 1LWP (3D) [IMAGE] 2L6W (3D) [IMAGE] 2PLD (3D) [IMAGE] 2PLE (3D) [IMAGE]
  • Function:
    Tyrosine-protein kinase that acts as cell-surface receptor for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA and PDGFB, and plays an essential role in the regulation of embryonic development, cell proliferation, survival, differentiation, chemotaxis and migration. Plays an essential role in blood vessel development by promoting proliferation, migration and recruitment of pericytes and smooth muscle cells to endothelial cells. Plays a role in the migration of vascular smooth muscle cells and the formation of neointima at vascular injury sites. Required for normal development of the cardiovascular system. Required for normal recruitment of pericytes (mesangial cells) in the kidney glomerulus, and for normal formation of a branched network of capillaries in kidney glomeruli. Promotes rearrangement of the actin cytoskeleton and the formation of membrane ruffles. Binding of its cognate ligands - homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFD -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PLCG1, PIK3R1, PTPN11, RASA1/GAP, CBL, SHC1 and NCK1. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca(2+) and the activation of protein kinase C. Phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leads to the activation of the AKT1 signaling pathway. Phosphorylation of SHC1, or of the C-terminus of PTPN11, creates a binding site for GRB2, resulting in the activation of HRAS, RAF1 and down-stream MAP kinases, including MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation and activation of SRC family kinases. Promotes phosphorylation of PDCD6IP/ALIX and STAM. Receptor signaling is down-regulated by protein phosphatases that dephosphorylate the receptor and its down-stream effectors, and by rapid internalization of the activated receptor
                          
    Tyrosine-protein kinase that acts as cell-surface receptor for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA and PDGFB, and plays an essential role in the regulation of embryonic development, cell proliferation, survival, differentiation, chemotaxis and migration. Plays an essential role in blood vessel development by promoting proliferation, migration and recruitment of pericytes and smooth muscle cells to endothelial cells. Plays a role in the migration of vascular smooth muscle cells and the formation of neointima at vascular injury sites. Required for normal development of the cardiovascular system. Required for normal recruitment of pericytes (mesangial cells) in the kidney glomerulus, and for normal formation of a branched network of capillaries in kidney glomeruli. Promotes rearrangement of the actin cytoskeleton and the formation of membrane ruffles. Binding of its cognate ligands - homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFD -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PLCG1, PIK3R1, PTPN11, RASA1/GAP, CBL, SHC1 and NCK1. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca(2+) and the activation of protein kinase C. Phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leads to the activation of the AKT1 signaling pathway. Phosphorylation of SHC1, or of the C-terminus of PTPN11, creates a binding site for GRB2, resulting in the activation of HRAS, RAF1 and down-stream MAP kinases, including MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation and activation of SRC family kinases. Promotes phosphorylation of PDCD6IP/ALIX and STAM. Receptor signaling is down-regulated by protein phosphatases that dephosphorylate the receptor and its down-stream effectors, and by rapid internalization of the activated receptor
  • Catalytic activity:
    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
  • Similarity:
    Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily
                          
    Contains 5 Ig-like C2-type (immunoglobulin-like) domains
                          
    Contains 1 protein kinase domain [IMAGE]
  • Protein Domain/Family    
    Source ID Domain Name Type
    InterProIPR000719Prot_kinase_domProtein kinaseDomain
    IPR001245Ser-Thr/Tyr_kinase_cat_domTyrosine protein kinaseDomain
    IPR001824Tyr_kinase_rcpt_3_CSReceptor tyrosine kinase, class IIIFamily
    IPR003598Ig_sub2Immunoglobulin C2 typeDomain
    IPR003599Ig_subImmunoglobulin subtypeDomain
    IPR007110Ig-like_domImmunoglobulin-likeDomain
    IPR008266Tyr_kinase_ASTyrosine protein kinase, active siteActive Sites
    IPR011009Kinase-like_domProtein kinase-likeDomain
    IPR013098Ig_I-setImmunoglobulin I-setDomain
    IPR013151ImmunoglobulinImmunoglobulinDomain
    BlocksIPB001824Receptor tyrosine kinaseReceptor tyrosine kinase, class III
    IPB003598Immunoglobulin C-2 typeImmunoglobulin C-2 type
    IPB008266Tyrosine protein kinaseTyrosine protein kinase, active site
    IPB009134Vascular endothelial growth factor receptor signatureVascular endothelial growth factor receptor signature

    Gene Ontology    
    Type Term Evidence Source Pub
    Biological Process cell chemotaxis IDA GOA 17991872
    cell migration IMP GOA 2554309
    G-protein coupled receptor signaling pathway TAS GOA 2536956
    peptidyl-tyrosine phosphorylation IDA GOA 1653029
    phosphatidylinositol metabolic process IMP GOA 1653029
    phosphatidylinositol-mediated signaling IMP GOA 2554309
    platelet-derived growth factor receptor signaling pathway IDA GOA 1314164
    positive regulation of cell migration IDA GOA 17470632
    positive regulation of cell proliferation IMP GOA 2554309
    positive regulation of phosphatidylinositol 3-kinase activity IDA GOA 1314164
    positive regulation of phospholipase C activity IDA GOA 1653029
    positive regulation of phosphoprotein phosphatase activity IDA GOA 7691811
    protein autophosphorylation IDA GOA 1314164
    signal transduction IDA GOA 10821867
    Cellular Component intrinsic component of plasma membrane IDA GOA 2554309
    membrane IDA GOA 16477012
    Molecular Function platelet activating factor receptor activity TAS GOA 2536956
    platelet-derived growth factor beta-receptor activity IMP GOA 2554309
    platelet-derived growth factor beta-receptor activity IDA GOA 1314164
    platelet-derived growth factor binding IPI GOA 2536956
    platelet-derived growth factor binding IDA GOA 2554309
    platelet-derived growth factor receptor binding IPI GOA 2542288
    platelet-derived growth factor-activated receptor activity TAS GOA 2536956
    protein binding IPI GOA 10336465
    protein kinase binding IPI GOA 16479011
    protein tyrosine kinase activity IDA GOA 1653029
    receptor binding IPI GOA 10821867

    Disorder & Mutation    
    Source Disease
    SWISS-PROTNote=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)
    SWISS-PROTMyeloproliferative disorder chronic with eosinophilia (MPE) [MIM:131440]: A hematologic disorder characterized by malignant eosinophils proliferation. Note=The gene represented in this entry may be involved in disease pathogenesis. Chromosomal aberrations involving PDGFRB have been found in many instances of chronic myeloproliferative disorder with eosinophilia. Translocation t(5;12) with ETV6 on chromosome 12 creating an PDGFRB-ETV6 fusion protein (PubMed:12181402). Translocation t(5;15)(q33;q22) with TP53BP1 creating a PDGFRB-TP53BP1 fusion protein (PubMed:15492236). Translocation t(1;5)(q23;q33) that forms a PDE4DIP-PDGFRB fusion protein (PubMed:12907457). Translocation t(5;6)(q33-34;q23) with CEP85L that fuses the 5'-end of CEP85L (isoform 4) to the 3'-end of PDGFRB (PubMed:21938754)
    SWISS-PROTLeukemia, acute myelogenous (AML) [MIM:601626]: A subtype of acute leukemia, a cancer of the white blood cells. AML is a malignant disease of bone marrow characterized by maturational arrest of hematopoietic precursors at an early stage of development. Clonal expansion of myeloid blasts occurs in bone marrow, blood, and other tissue. Myelogenous leukemias develop from changes in cells that normally produce neutrophils, basophils, eosinophils and monocytes. Note=The gene represented in this entry may be involved in disease pathogenesis. A chromosomal aberration involving PDGFRB has been found in a patient with AML. Translocation t(5;14)(q33;q32) with TRIP11 (PubMed:9373237)
    SWISS-PROTLeukemia, juvenile myelomonocytic (JMML) [MIM:607785]: An aggressive pediatric myelodysplastic syndrome/myeloproliferative disorder characterized by malignant transformation in the hematopoietic stem cell compartment with proliferation of differentiated progeny. Patients have splenomegaly, enlarged lymph nodes, rashes, and hemorrhages. Note=The gene represented in this entry may be involved in disease pathogenesis. A chromosomal aberration involving PDGFRB has been found in a patient with JMML. Translocation t(5;17)(q33;p11.2) with SPECC1 (PubMed:15087372)
    SWISS-PROTBasal ganglia calcification, idiopathic, 4 (IBGC4) [MIM:615007]: A form of basal ganglia calcification, an autosomal dominant condition characterized by symmetric calcification in the basal ganglia and other brain regions. Affected individuals can either be asymptomatic or show a wide spectrum of neuropsychiatric symptoms, including parkinsonism, dystonia, tremor, ataxia, dementia, psychosis, seizures, and chronic headache. Serum levels of calcium, phosphate, alkaline phosphatase and parathyroid hormone are normal. The neuropathological hallmark of the disease is vascular and pericapillary calcification, mainly of calcium phosphate, in the affected brain areas. Note=The disease is caused by mutations affecting the gene represented in this entry

    PDGFRB cross reference    
    PubMed OMIM Entrez Gene NCKU SNP Nucleotide UniProt Genome Data Viewer HomoloGene