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Showing Protein Platelet-derived growth factor receptor beta (HMDBP12105)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP12105
Secondary Accession Numbers None
Name Platelet-derived growth factor receptor beta
Synonyms
  1. PDGF-R-beta
  2. PDGFR-beta
  3. Beta platelet-derived growth factor receptor
  4. Beta-type platelet-derived growth factor receptor
  5. CD140 antigen-like family member B
  6. Platelet-derived growth factor receptor 1
  7. PDGFR-1
Gene Name PDGFRB
Protein Type Unknown
Biological Properties
General Function Not Available
Specific 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 (By similarity).
Pathways
  • Calcium signaling pathway
  • Central carbon metabolism in cancer
  • Choline metabolism in cancer
  • EGFR tyrosine kinase inhibitor resistance
  • Focal adhesion
  • Gap junction
  • Glioma
  • Human papillomavirus infection
  • JAK-STAT signaling pathway
  • MAPK signaling pathway
  • Melanoma
  • MicroRNAs in cancer
  • Phospholipase D signaling pathway
  • PI3K-Akt signaling pathway
  • Prostate cancer
  • Rap1 signaling pathway
  • Ras signaling pathway
  • Regulation of actin cytoskeleton
Reactions Not Available
GO Classification
Biological Process
response to organic cyclic compound
tissue homeostasis
multicellular organismal development
positive regulation of reactive oxygen species metabolic process
positive regulation of cell proliferation
response to retinoic acid
aging
response to hydrogen peroxide
intracellular signal transduction
positive regulation of apoptotic process
male gonad development
blood vessel development
kidney development
response to estradiol stimulus
in utero embryonic development
response to toxin
cellular response to hydrogen peroxide
response to estrogen stimulus
signal transduction
negative regulation of apoptotic process
glycosaminoglycan biosynthetic process
nitrogen compound metabolic process
phosphatidylinositol-mediated signaling
positive regulation of phosphatidylinositol 3-kinase cascade
response to hyperoxia
positive regulation of ERK1 and ERK2 cascade
adrenal gland development
retina vasculature development in camera-type eye
positive regulation of fibroblast proliferation
inner ear development
positive regulation of cell migration
positive regulation of collagen biosynthetic process
aorta morphogenesis
wound healing
cell migration
positive regulation of smooth muscle cell proliferation
skeletal system morphogenesis
ruffle assembly
response to lipid
response to fluid shear stress
platelet-derived growth factor receptor signaling pathway
smooth muscle tissue development
positive regulation of MAP kinase activity
phosphatidylinositol metabolic process
positive regulation of chemotaxis
peptidyl-tyrosine phosphorylation
transmembrane receptor protein tyrosine kinase signaling pathway
protein autophosphorylation
cell migration involved in vasculogenesis
cardiac myofibril assembly
cell chemotaxis
lung growth
metanephric glomerular capillary formation
positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway
positive regulation of kinase activity
positive regulation of phosphatidylinositol 3-kinase activity
positive regulation of phospholipase C activity
cell migration involved in coronary angiogenesis
embryonic organ development
metanephric comma-shaped body morphogenesis
metanephric glomerular mesangial cell proliferation involved in metanephros development
metanephric glomerular mesangium development
metanephric glomerulus morphogenesis
metanephric mesenchymal cell migration
metanephric mesenchyme development
metanephric S-shaped body morphogenesis
platelet-derived growth factor receptor-beta signaling pathway
positive regulation of calcium ion import
positive regulation of DNA biosynthetic process
positive regulation of hepatic stellate cell activation
positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway
positive regulation of mitotic nuclear division
positive regulation of phosphoprotein phosphatase activity
positive regulation of Rho protein signal transduction
positive regulation of smooth muscle cell migration
regulation of actin cytoskeleton organization
regulation of peptidyl-tyrosine phosphorylation
response to ceramide
smooth muscle cell chemotaxis
Cellular Component
cytoplasm
plasma membrane
nucleus
membrane
integral to plasma membrane
cell surface
Golgi apparatus
apical plasma membrane
lysosomal lumen
cytoplasmic vesicle
ruffle
intrinsic component of plasma membrane
receptor complex
Molecular Function
ATP binding
protein kinase binding
receptor binding
protein kinase activity
enzyme binding
kinase activity
platelet-derived growth factor receptor binding
growth factor binding
phosphatidylinositol 3-kinase binding
platelet-derived growth factor binding
transmembrane receptor protein tyrosine kinase activity
vascular endothelial growth factor binding
platelet-derived growth factor beta-receptor activity
platelet-derived growth factor-activated receptor activity
protein tyrosine kinase activity
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 1097
Molecular Weight 122826.68
Theoretical pI 5.161
Pfam Domain Function
Signals
  • 1-31;
Transmembrane Regions
  • 532-552;
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q05030
UniProtKB/Swiss-Prot Entry Name PGFRB_RAT
PDB IDs Not Available
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Herren B, Weyer KA, Rouge M, Lotscher P, Pech M: Conservation in sequence and affinity of human and rodent PDGF ligands and receptors. Biochim Biophys Acta. 1993 Jun 25;1173(3):294-302. doi: 10.1016/0167-4781(93)90127-y. [PubMed:8318539 ]
  2. Okuyama H, Shimahara Y, Kawada N, Seki S, Kristensen DB, Yoshizato K, Uyama N, Yamaoka Y: Regulation of cell growth by redox-mediated extracellular proteolysis of platelet-derived growth factor receptor beta. J Biol Chem. 2001 Jul 27;276(30):28274-80. doi: 10.1074/jbc.M102995200. Epub 2001 May 9. [PubMed:11346654 ]