Gene content    
PDGFRA ( by HUGO)
Platelet-Derived Growth Factor Receptor, Alpha Polypeptide
Oncogene
Platelet-Derived Growth Factor Receptor
Alpha Polypeptide
Alpha-Type Platelet-Derived Growth Factor Receptor
Platelet-Derived Growth Factor Receptor 2
PDGF-R-alpha
PDGFR-2
PDGFR2
RHEPDGFRA
CD140 Antigen-Like Family Member A
CD140a Antigen
EC 2.7.10.1
CD140A
PDGFRA/BCR Fusion
Platelet-Derived Growth Factor Receptor Alpha
Rearranged-In-Hypereosinophilia-Platelet Derived Growth Factor Receptor Alpha Fusion Protein
PDGFR-alpha
Alpha Platelet-Derived Growth Factor Receptor
Platelet-Derived Growth Factor Alpha Receptor
EC 2.7.10
NCBI: 4q12    Ensembl: 4q12
PGFRA_HUMANSize: 1089 amino acidsMass: 122670 Da

  • Subunit: Interacts with homodimeric PDGFA, PDGFB and PDGFC, and with heterodimers formed by PDGFA and PDGFB. Monomer in the absence of bound ligand. Interaction with dimeric PDGFA, PDGFB and/or PDGFC leads to receptor dimerization, where both PDGFRA homodimers and heterodimers with PDGFRB are observed. Interacts (tyrosine phosphorylated) with SHB (via SH2 domain) (By similarity). Interacts (tyrosine phosphorylated) with SHF (via SH2 domain). Interacts (tyrosine phosphorylated) with SRC (via SH2 domain). Interacts (tyrosine phosphorylated) with PIK3R1. Interacts (tyrosine phosphorylated) with PLCG1 (via SH2 domain). Interacts (tyrosine phosphorylated) with CRK, GRB2 and GRB7. Interacts with human cytomegalovirus/HHV-5 envelop glycoprotein B/gB Sequence caution: Sequence=AAP69563.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; 1 PDB 3D structure from [IMAGE] and Proteopedia [IMAGE] for PDGFRA: 1GQ5 (3D) [IMAGE]
  • Tissue specificity: Detected in platelets (at protein level). Widely expressed. Detected in brain, fibroblasts, smooth muscle, heart, and embryo. Expressed in primary and metastatic colon tumors and in normal colon tissue [IMAGE] Pathway & Disease-focused RT2 Profiler PCR Ar
  • Function:
    Tyrosine-protein kinase that acts as a cell-surface receptor for PDGFA, PDGFB and PDGFC and plays an essential role in the regulation of embryonic development, cell proliferation, survival and chemotaxis. Depending on the context, promotes or inhibits cell proliferation and cell migration. Plays an important role in the differentiation of bone marrow-derived mesenchymal stem cells. Required for normal skeleton development and cephalic closure during embryonic development. Required for normal development of the mucosa lining the gastrointestinal tract, and for recruitment of mesenchymal cells and normal development of intestinal villi. Plays a role in cell migration and chemotaxis in wound healing. Plays a role in platelet activation, secretion of agonists from platelet granules, and in thrombin-induced platelet aggregation. Binding of its cognate ligands - homodimeric PDGFA, homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFC -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 PIK3R1, PLCG1, and PTPN11. 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. Phosphorylates PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and thereby mediates activation of the AKT1 signaling pathway. Mediates activation of HRAS and of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3 and STAT5A and/or STAT5B. 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 a cell-surface receptor for PDGFA, PDGFB and PDGFC and plays an essential role in the regulation of embryonic development, cell proliferation, survival and chemotaxis. Depending on the context, promotes or inhibits cell proliferation and cell migration. Plays an important role in the differentiation of bone marrow-derived mesenchymal stem cells. Required for normal skeleton development and cephalic closure during embryonic development. Required for normal development of the mucosa lining the gastrointestinal tract, and for recruitment of mesenchymal cells and normal development of intestinal villi. Plays a role in cell migration and chemotaxis in wound healing. Plays a role in platelet activation, secretion of agonists from platelet granules, and in thrombin-induced platelet aggregation. Binding of its cognate ligands - homodimeric PDGFA, homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFC -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 PIK3R1, PLCG1, and PTPN11. 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. Phosphorylates PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and thereby mediates activation of the AKT1 signaling pathway. Mediates activation of HRAS and of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3 and STAT5A and/or STAT5B. 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
    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 activation TAS GOA 10508235
    cell chemotaxis IMP GOA 1646396
    negative regulation of platelet activation IDA GOA 8188664
    peptidyl-tyrosine phosphorylation IDA GOA 1646396
    phosphatidylinositol-mediated signaling IMP GOA 2554309
    platelet aggregation IMP GOA 8188664
    platelet-derived growth factor receptor signaling pathway IDA GOA 10806482
    positive regulation of cell migration IMP GOA 1646396
    positive regulation of cell migration IDA GOA 17470632
    positive regulation of cell proliferation IMP GOA 2554309
    positive regulation of cytosolic calcium ion concentration IMP GOA 2554309
    positive regulation of DNA replication IDA GOA 10806482
    positive regulation of ERK1 and ERK2 cascade IMP GOA 10734113
    positive regulation of fibroblast proliferation IDA GOA 10806482
    positive regulation of phosphatidylinositol 3-kinase activity IMP GOA 1646396
    positive regulation of phosphatidylinositol 3-kinase signaling TAS GOA 10734113
    positive regulation of phospholipase C activity IMP GOA 1646396
    protein autophosphorylation IDA GOA 1646396
    regulation of chemotaxis IMP GOA 2554309
    Cellular Component integral component of plasma membrane IDA GOA 2536956
    intrinsic component of plasma membrane IDA GOA 2554309
    membrane IDA GOA 19946888
    Molecular Function platelet-derived growth factor alpha-receptor activity IMP GOA 2554309
    platelet-derived growth factor alpha-receptor activity IDA GOA 10806482
    platelet-derived growth factor binding IPI GOA 10806482
    platelet-derived growth factor binding IDA GOA 2554309
    platelet-derived growth factor receptor binding IPI GOA 2542288
    protein binding IPI GOA 10733900
    protein homodimerization activity IDA GOA 2542288
    transmembrane receptor protein tyrosine kinase activity IDA GOA 1646396
    vascular endothelial growth factor-activated receptor activity IDA GOA 17470632

    Disorder & Mutation    
    Source Disease
    SWISS-PROTNote=A chromosomal aberration involving PDGFRA is found in some cases of hypereosinophilic syndrome. Interstitial chromosomal deletion del(4)(q12q12) causes the fusion of FIP1L1 and PDGFRA (FIP1L1-PDGFRA). Mutations that cause overexpression and/or constitutive activation of PDGFRA may be a cause of hypereosinophilic syndrome

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