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P09619 (PGFRB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 183. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Platelet-derived growth factor receptor beta

Short name=PDGF-R-beta
Short name=PDGFR-beta
EC=2.7.10.1
Alternative name(s):
Beta platelet-derived growth factor receptor
Beta-type platelet-derived growth factor receptor
CD140 antigen-like family member B
Platelet-derived growth factor receptor 1
Short name=PDGFR-1
CD_antigen=CD140b
Gene names
Name:PDGFRB
Synonyms:PDGFR, PDGFR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1106 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 Ca2+ 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. Ref.1 Ref.2 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.18 Ref.20 Ref.21 Ref.29 Ref.30 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.43

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.13 Ref.18 Ref.39

Enzyme regulation

Present in an inactive conformation in the absence of bound ligand. Binding of PDGFB and/or PDGFD leads to dimerization and activation by autophosphorylation on tyrosine residues. Inhibited by imatinib. Ref.34

Subunit structure

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 and RASA1. 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. Ref.1 Ref.2 Ref.12 Ref.14 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.25 Ref.26 Ref.28 Ref.29 Ref.37 Ref.42 Ref.49 Ref.50

Subcellular location

Cell membrane; Single-pass type I membrane protein. Cytoplasmic vesicle. Lysosome lumen. Note: After ligand binding, the autophosphorylated receptor is ubiquitinated and internalized, leading to its degradation. Ref.1 Ref.2 Ref.10 Ref.13 Ref.37 Ref.39

Post-translational modification

Autophosphorylated on tyrosine residues upon ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation at Tyr-579, and to a lesser degree, at Tyr-581, is important for interaction with SRC family kinases. Phosphorylation at Tyr-740 and Tyr-751 is important for interaction with PIK3R1. Phosphorylation at Tyr-751 is important for interaction with NCK1. Phosphorylation at Tyr-771 and Tyr-857 is important for interaction with RASA1/GAP. Phosphorylation at Tyr-857 is important for efficient phosphorylation of PLCG1 and PTPN11, resulting in increased phosphorylation of AKT1, MAPK1/ERK2 and/or MAPK3/ERK1, PDCD6IP/ALIX and STAM, and in increased cell proliferation. Phosphorylation at Tyr-1009 is important for interaction with PTPN11. Phosphorylation at Tyr-1009 and Tyr-1021 is important for interaction with PLCG1. Phosphorylation at Tyr-1021 is important for interaction with CBL; PLCG1 and CBL compete for the same binding site. Dephosphorylated by PTPRJ at Tyr-751, Tyr-857, Tyr-1009 and Tyr-1021. Dephosphorylated by PTPN2 at Tyr-579 and Tyr-1021. Ref.1 Ref.2 Ref.9 Ref.12 Ref.14 Ref.15 Ref.18 Ref.27 Ref.35 Ref.36 Ref.39

N-glycosylated. Ref.2 Ref.50

Ubiquitinated. After autophosphorylation, the receptor is polyubiquitinated, leading to its degradation. Ref.16 Ref.37

Involvement in 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).

Myeloproliferative 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 (Ref.31). Translocation t(5;15)(q33;q22) with TP53BP1 creating a PDGFRB-TP53BP1 fusion protein (Ref.34). Translocation t(1;5)(q23;q33) that forms a PDE4DIP-PDGFRB fusion protein (Ref.32). Translocation t(5;6)(q33-34;q23) with CEP85L that fuses the 5'-end of CEP85L (isoform 4)to the 3'-end of PDGFRB (Ref.6).

Leukemia, 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 (Ref.24).

Leukemia, 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 (Ref.33).

Basal 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. Ref.54

Myofibromatosis, infantile 1 (IMF1) [MIM:228550]: A rare mesenchymal disorder characterized by the development of benign tumors in the skin, striated muscles, bones, and, more rarely, visceral organs. Subcutaneous or soft tissue nodules commonly involve the skin of the head, neck, and trunk. Skeletal and muscular lesions occur in about half of the patients. Lesions may be solitary or multicentric, and they may be present at birth or become apparent in early infancy or occasionally in adult life. Visceral lesions are associated with high morbidity and mortality.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.52 Ref.53

Sequence similarities

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.

Ontologies

Keywords
   Biological processChemotaxis
   Cellular componentCell membrane
Cytoplasmic vesicle
Lysosome
Membrane
   Coding sequence diversityChromosomal rearrangement
Polymorphism
   DiseaseDisease mutation
Proto-oncogene
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

G-protein coupled receptor signaling pathway

Traceable author statement PubMed 2536956. Source: GOC

adrenal gland development

Inferred from electronic annotation. Source: Ensembl

aorta morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

cardiac myofibril assembly

Inferred from sequence or structural similarity. Source: UniProtKB

cell chemotaxis

Inferred from direct assay Ref.10. Source: UniProtKB

cell migration

Inferred from mutant phenotype Ref.10. Source: UniProtKB

cell migration involved in coronary angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

cell migration involved in vasculogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to platelet-derived growth factor stimulus

Traceable author statement PubMed 2536956. Source: GOC

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

glycosaminoglycan biosynthetic process

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

inner ear development

Inferred from electronic annotation. Source: Ensembl

metanephric S-shaped body morphogenesis

Inferred from electronic annotation. Source: Ensembl

metanephric comma-shaped body morphogenesis

Inferred from electronic annotation. Source: Ensembl

metanephric glomerular capillary formation

Inferred from sequence or structural similarity. Source: UniProtKB

metanephric glomerular mesangial cell proliferation involved in metanephros development

Inferred from sequence or structural similarity. Source: UniProtKB

metanephric mesenchymal cell migration

Inferred from electronic annotation. Source: Ensembl

metanephric mesenchyme development

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

peptidyl-tyrosine phosphorylation

Inferred from direct assay Ref.11Ref.2. Source: UniProtKB

phosphatidylinositol metabolic process

Inferred from mutant phenotype Ref.11. Source: UniProtKB

phosphatidylinositol-mediated signaling

Inferred from mutant phenotype Ref.10. Source: UniProtKB

platelet-derived growth factor receptor signaling pathway

Inferred from direct assay Ref.14. Source: UniProtKB

platelet-derived growth factor receptor-beta signaling pathway

Inferred from mutant phenotype Ref.10. Source: UniProtKB

positive regulation of DNA biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of ERK1 and ERK2 cascade

Inferred from mutant phenotype Ref.43. Source: UniProtKB

positive regulation of MAP kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of calcium ion import

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell migration

Inferred from direct assay PubMed 17470632. Source: BHF-UCL

positive regulation of cell proliferation

Inferred from mutant phenotype Ref.10. Source: UniProtKB

positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway

Inferred from direct assay PubMed 17470632. Source: BHF-UCL

positive regulation of chemotaxis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of collagen biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of mitosis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of phosphatidylinositol 3-kinase activity

Inferred from direct assay Ref.14. Source: UniProtKB

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of phospholipase C activity

Inferred from direct assay Ref.11. Source: UniProtKB

positive regulation of phosphoprotein phosphatase activity

Inferred from direct assay Ref.20. Source: UniProtKB

positive regulation of reactive oxygen species metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of smooth muscle cell migration

Inferred from mutant phenotype Ref.43. Source: UniProtKB

positive regulation of smooth muscle cell proliferation

Inferred from mutant phenotype Ref.43. Source: UniProtKB

protein autophosphorylation

Inferred from direct assay Ref.14Ref.2. Source: UniProtKB

regulation of actin cytoskeleton organization

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to fluid shear stress

Inferred from electronic annotation. Source: Ensembl

response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

response to hyperoxia

Inferred from electronic annotation. Source: Ensembl

response to retinoic acid

Inferred from electronic annotation. Source: Ensembl

response to toxic substance

Inferred from electronic annotation. Source: Ensembl

retina vasculature development in camera-type eye

Inferred from sequence or structural similarity. Source: UniProtKB

signal transduction

Inferred from direct assay Ref.27. Source: UniProtKB

skeletal system morphogenesis

Inferred from electronic annotation. Source: Ensembl

smooth muscle cell chemotaxis

Inferred from sequence or structural similarity. Source: BHF-UCL

smooth muscle tissue development

Inferred from electronic annotation. Source: Ensembl

tissue homeostasis

Inferred from electronic annotation. Source: Ensembl

transforming growth factor beta receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

wound healing

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentapical plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intrinsic component of plasma membrane

Inferred from direct assay Ref.10. Source: UniProtKB

lysosomal lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from direct assay PubMed 16477012. Source: BHF-UCL

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

platelet activating factor receptor activity

Traceable author statement PubMed 2536956. Source: ProtInc

platelet-derived growth factor beta-receptor activity

Inferred from direct assay Ref.14Ref.2. Source: UniProtKB

platelet-derived growth factor binding

Inferred from direct assay Ref.10Ref.2. Source: UniProtKB

platelet-derived growth factor receptor binding

Inferred from physical interaction PubMed 2542288. Source: BHF-UCL

platelet-derived growth factor-activated receptor activity

Traceable author statement PubMed 2536956. Source: ProtInc

protein binding

Inferred from physical interaction PubMed 16456542PubMed 17242191PubMed 17470632PubMed 2157284. Source: UniProtKB

protein kinase binding

Inferred from physical interaction PubMed 16479011. Source: UniProtKB

protein tyrosine kinase activity

Inferred from direct assay Ref.11. Source: UniProtKB

receptor binding

Inferred from physical interaction Ref.27. Source: UniProtKB

vascular endothelial growth factor binding

Inferred from physical interaction PubMed 17470632. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 Ref.8
Chain33 – 11061074Platelet-derived growth factor receptor beta
PRO_0000016757

Regions

Topological domain33 – 532500Extracellular Potential
Transmembrane533 – 55321Helical; Potential
Topological domain554 – 1106553Cytoplasmic Potential
Domain33 – 12088Ig-like C2-type 1
Domain129 – 21082Ig-like C2-type 2
Domain214 – 30996Ig-like C2-type 3
Domain331 – 40373Ig-like C2-type 4
Domain416 – 524109Ig-like C2-type 5
Domain600 – 962363Protein kinase
Nucleotide binding606 – 6149ATP By similarity

Sites

Active site8261Proton acceptor By similarity
Binding site6341ATP Probable
Site527 – 5282Breakpoint for insertion to form PDE4DIP-PDGFRB fusion protein
Site527 – 5282Breakpoint for translocation to form TRIP11-PDGFRB
Site558 – 5592Breakpoint for translocation to form the CEP85L-PDGFRB fusion protein

Amino acid modifications

Modified residue5621Phosphotyrosine; by autocatalysis Ref.27
Modified residue5791Phosphotyrosine; by autocatalysis Ref.18 Ref.35 Ref.36
Modified residue5811Phosphotyrosine; by autocatalysis Ref.18 Ref.36
Modified residue5891Phosphotyrosine; by autocatalysis
Modified residue6861Phosphotyrosine; by ABL1 and ABL2 By similarity
Modified residue7161Phosphotyrosine; by autocatalysis Ref.36
Modified residue7401Phosphotyrosine; by autocatalysis Ref.14 Ref.36
Modified residue7511Phosphotyrosine; by autocatalysis Ref.9 Ref.12 Ref.14 Ref.27 Ref.35
Modified residue7631Phosphotyrosine; by autocatalysis Ref.27
Modified residue7711Phosphotyrosine; by autocatalysis Ref.14 Ref.27 Ref.35 Ref.36
Modified residue7751Phosphotyrosine; by autocatalysis Ref.27
Modified residue7781Phosphotyrosine; by autocatalysis Ref.27
Modified residue8571Phosphotyrosine; by autocatalysis Ref.9 Ref.12 Ref.14 Ref.27 Ref.36
Modified residue9341Phosphotyrosine; by ABL1 and ABL2 By similarity
Modified residue9701Phosphotyrosine; by ABL1 and ABL2 By similarity
Modified residue10091Phosphotyrosine; by autocatalysis Ref.15 Ref.27 Ref.36
Modified residue10211Phosphotyrosine; by autocatalysis Ref.15 Ref.27 Ref.35 Ref.36
Glycosylation451N-linked (GlcNAc...) Potential
Glycosylation891N-linked (GlcNAc...) Ref.50
Glycosylation1031N-linked (GlcNAc...) Ref.50
Glycosylation2151N-linked (GlcNAc...) Ref.50
Glycosylation2301N-linked (GlcNAc...) Ref.50
Glycosylation2921N-linked (GlcNAc...) Ref.50
Glycosylation3071N-linked (GlcNAc...) Ref.50
Glycosylation3541N-linked (GlcNAc...) Potential
Glycosylation3711N-linked (GlcNAc...) Potential
Glycosylation4681N-linked (GlcNAc...) Potential
Glycosylation4791N-linked (GlcNAc...) Potential
Disulfide bond54 ↔ 100 Ref.50
Disulfide bond149 ↔ 190 Ref.50
Disulfide bond235 ↔ 291 Ref.50
Disulfide bond436 ↔ 508 By similarity

Natural variations

Natural variant291I → F. Ref.51
Corresponds to variant rs17110944 [ dbSNP | Ensembl ].
VAR_034377
Natural variant1801S → F. Ref.4
Corresponds to variant rs17853027 [ dbSNP | Ensembl ].
VAR_035125
Natural variant2821E → K. Ref.51
Corresponds to variant rs34586048 [ dbSNP | Ensembl ].
VAR_042027
Natural variant3451P → S.
Corresponds to variant rs2229558 [ dbSNP | Ensembl ].
VAR_049717
Natural variant4851E → K. Ref.51
Corresponds to variant rs41287110 [ dbSNP | Ensembl ].
VAR_042028
Natural variant5611R → C in IMF1. Ref.53
VAR_069925
Natural variant5891Y → H in a gastric adenocarcinoma sample; somatic mutation. Ref.51
VAR_042029
Natural variant6581L → P in IBGC4. Ref.54
VAR_069320
Natural variant6601P → T in IMF1. Ref.52
Corresponds to variant rs144050370 [ dbSNP | Ensembl ].
VAR_069926
Natural variant7181N → Y. Ref.51
Corresponds to variant rs35322465 [ dbSNP | Ensembl ].
VAR_042030
Natural variant8821T → I in a breast infiltrating ductal carcinoma sample; somatic mutation. Ref.51
VAR_042031
Natural variant9871R → W in IBGC4. Ref.54
VAR_069321

Experimental info

Mutagenesis5791Y → F: Loss of kinase activity; when associated with F-581. Strongly reduces interaction with SRC family kinases. No effect on interaction with GRB10. Ref.18 Ref.25
Mutagenesis5811Y → F: Loss of kinase activity; when associated with F-579. No effect on interaction with GRB10. Ref.18 Ref.25
Mutagenesis6341K → A or R: Loss of kinase activity. Abolishes interaction with RASA1. No effect on phosphatidylinositol 3-kinase activity. Ref.13 Ref.14 Ref.39
Mutagenesis7161Y → F: No effect neither on interaction with GRB10 and RASA1 nor on phosphatidylinositol 3-kinase activity. Ref.14 Ref.25
Mutagenesis7401Y → F: Strongly reduces up-regulation of cell proliferation; when associated with F-751. Strongly decreases phosphatidylinositol 3-kinase activity. No effect on interaction with GRB10 and RASA1. Ref.14 Ref.17 Ref.25 Ref.43
Mutagenesis7511Y → F: Strongly reduces up-regulation of cell proliferation; when associated with F-740. Abolishes phosphatidylinositol 3-kinase activity and interaction wit NCK1, and slightly reduces interaction with RASA1. No effect on interaction with GRB10. Ref.11 Ref.14 Ref.17 Ref.21 Ref.25 Ref.43
Mutagenesis7631Y → F: No effect on interaction with RASA1 and on phosphatidylinositol 3-kinase activity. Ref.14
Mutagenesis7711Y → F: Loss of interaction with GRB10. Abolishes interaction with RASA1. No effect on phosphatidylinositol 3-kinase activity. Ref.14 Ref.17 Ref.25
Mutagenesis7751Y → F: No effect on interaction with RASA1 and on phosphatidylinositol 3-kinase activity. Ref.14
Mutagenesis7781Y → F: Strongly reduces expression levels. Ref.14
Mutagenesis8571Y → F: Reduces kinase activity. No effect on interaction with GRB10. Abolishes interaction with RASA1. No effect on phosphatidylinositol 3-kinase activity. Ref.11 Ref.14 Ref.25 Ref.39
Mutagenesis10091Y → F: No effect on interaction with GRB10. Abolishes interaction with PLCG1; when associated with F-1021. Ref.15 Ref.20 Ref.25
Mutagenesis10211Y → F: Strongly reduces up-regulation of cell proliferation. Abolishes interaction with PLCG1; when associated with F-1009. No effect on interaction with GRB10. Ref.15 Ref.25 Ref.37 Ref.43
Sequence conflict2411E → D in AAA36427. Ref.2

Secondary structure

...................................................... 1106
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09619 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 038C15E531D6E89D

FASTA1,106123,968
        10         20         30         40         50         60 
MRLPGAMPAL ALKGELLLLS LLLLLEPQIS QGLVVTPPGP ELVLNVSSTF VLTCSGSAPV 

        70         80         90        100        110        120 
VWERMSQEPP QEMAKAQDGT FSSVLTLTNL TGLDTGEYFC THNDSRGLET DERKRLYIFV 

       130        140        150        160        170        180 
PDPTVGFLPN DAEELFIFLT EITEITIPCR VTDPQLVVTL HEKKGDVALP VPYDHQRGFS 

       190        200        210        220        230        240 
GIFEDRSYIC KTTIGDREVD SDAYYVYRLQ VSSINVSVNA VQTVVRQGEN ITLMCIVIGN 

       250        260        270        280        290        300 
EVVNFEWTYP RKESGRLVEP VTDFLLDMPY HIRSILHIPS AELEDSGTYT CNVTESVNDH 

       310        320        330        340        350        360 
QDEKAINITV VESGYVRLLG EVGTLQFAEL HRSRTLQVVF EAYPPPTVLW FKDNRTLGDS 

       370        380        390        400        410        420 
SAGEIALSTR NVSETRYVSE LTLVRVKVAE AGHYTMRAFH EDAEVQLSFQ LQINVPVRVL 

       430        440        450        460        470        480 
ELSESHPDSG EQTVRCRGRG MPQPNIIWSA CRDLKRCPRE LPPTLLGNSS EEESQLETNV 

       490        500        510        520        530        540 
TYWEEEQEFE VVSTLRLQHV DRPLSVRCTL RNAVGQDTQE VIVVPHSLPF KVVVISAILA 

       550        560        570        580        590        600 
LVVLTIISLI ILIMLWQKKP RYEIRWKVIE SVSSDGHEYI YVDPMQLPYD STWELPRDQL 

       610        620        630        640        650        660 
VLGRTLGSGA FGQVVEATAH GLSHSQATMK VAVKMLKSTA RSSEKQALMS ELKIMSHLGP 

       670        680        690        700        710        720 
HLNVVNLLGA CTKGGPIYII TEYCRYGDLV DYLHRNKHTF LQHHSDKRRP PSAELYSNAL 

       730        740        750        760        770        780 
PVGLPLPSHV SLTGESDGGY MDMSKDESVD YVPMLDMKGD VKYADIESSN YMAPYDNYVP 

       790        800        810        820        830        840 
SAPERTCRAT LINESPVLSY MDLVGFSYQV ANGMEFLASK NCVHRDLAAR NVLICEGKLV 

       850        860        870        880        890        900 
KICDFGLARD IMRDSNYISK GSTFLPLKWM APESIFNSLY TTLSDVWSFG ILLWEIFTLG 

       910        920        930        940        950        960 
GTPYPELPMN EQFYNAIKRG YRMAQPAHAS DEIYEIMQKC WEEKFEIRPP FSQLVLLLER 

       970        980        990       1000       1010       1020 
LLGEGYKKKY QQVDEEFLRS DHPAILRSQA RLPGFHGLRS PLDTSSVLYT AVQPNEGDND 

      1030       1040       1050       1060       1070       1080 
YIIPLPDPKP EVADEGPLEG SPSLASSTLN EVNTSSTISC DSPLEPQDEP EPEPQLELQV 

      1090       1100 
EPEPELEQLP DSGCPAPRAE AEDSFL 

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References

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[1]"Cloning and expression of a cDNA coding for the human platelet-derived growth factor receptor: evidence for more than one receptor class."
Gronwald R.G.K., Grant F.J., Haldeman B.A., Hart C.E., O'Hara P.J., Hagen F.S., Ross R., Bowen-Pope D.F., Murray M.J.
Proc. Natl. Acad. Sci. U.S.A. 85:3435-3439(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION AS PDGFB RECEPTOR, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, INTERACTION WITH PDGFB.
[2]"cDNA cloning and expression of a human platelet-derived growth factor (PDGF) receptor specific for B-chain-containing PDGF molecules."
Claesson-Welsh L., Eriksson A., Moren A., Severinsson L., Ek B., Oestman A., Betsholtz C., Heldin C.-H.
Mol. Cell. Biol. 8:3476-3486(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION AS PDGFB RECEPTOR, SUBCELLULAR LOCATION, GLYCOSYLATION, AUTOPHOSPHORYLATION, INTERACTION WITH PDGFA AND PDGFB.
[3]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT PHE-180.
Tissue: Brain.
[5]"Integration of proviral DNA into the PDGF beta-receptor gene in HTLV-I-infected T-cells results in a novel tyrosine kinase product with transforming activity."
Chi K.D., McPhee R.A., Wagner A.S., Dietz J.J., Pantazis P., Goustin A.S.
Oncogene 15:1051-1057(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 548-569.
[6]"Systematic screen for tyrosine kinase rearrangements identifies a novel C6orf204-PDGFRB fusion in a patient with recurrent T-ALL and an associated myeloproliferative neoplasm."
Chmielecki J., Peifer M., Viale A., Hutchinson K., Giltnane J., Socci N.D., Hollis C.J., Dean R.S., Yenamandra A., Jagasia M., Kim A.S., Dave U.P., Thomas R.K., Pao W.
Genes Chromosomes Cancer 51:54-65(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 559-1106, CHROMOSOMAL TRANSLOCATION WITH CEP85L.
[7]"Tandem linkage of human CSF-1 receptor (c-fms) and PDGF receptor genes."
Roberts W.M., Look A.T., Roussel M.F., Sherr C.J.
Cell 55:655-661(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1046-1106.
[8]"Signal peptide prediction based on analysis of experimentally verified cleavage sites."
Zhang Z., Henzel W.J.
Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 33-47.
[9]"Autophosphorylation of the PDGF receptor in the kinase insert region regulates interactions with cell proteins."
Kazlauskas A., Cooper J.A.
Cell 58:1121-1133(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-751 AND TYR-857.
[10]"Independent expression of human alpha or beta platelet-derived growth factor receptor cDNAs in a naive hematopoietic cell leads to functional coupling with mitogenic and chemotactic signaling pathways."
Matsui T., Pierce J.H., Fleming T.P., Greenberger J.S., LaRochelle W.J., Ruggiero M., Aaronson S.A.
Proc. Natl. Acad. Sci. U.S.A. 86:8314-8318(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS PDGFB RECEPTOR IN CELL PROLIFERATION AND CHEMOTAXIS, SUBCELLULAR LOCATION.
[11]"Functions of the major tyrosine phosphorylation site of the PDGF receptor beta subunit."
Kazlauskas A., Durden D.L., Cooper J.A.
Cell Regul. 2:413-425(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL PROLIFERATION; ACTIVATION OF PLCG1 AND IN PHOSPHORYLATION OF PLCG1 AND RASA1/GAP, MUTAGENESIS OF TYR-751 AND TYR-857.
[12]"Platelet-derived growth factor (PDGF) stimulates PDGF receptor subunit dimerization and intersubunit trans-phosphorylation."
Kelly J.D., Haldeman B.A., Grant F.J., Murray M.J., Seifert R.A., Bowen-Pope D.F., Cooper J.A., Kazlauskas A.
J. Biol. Chem. 266:8987-8992(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDGFRA; PDGFA AND PDGFB, FUNCTION AS RECEPTOR FOR PDGFA AND PDGFB, PHOSPHORYLATION AT TYR-857 AND TYR-751.
[13]"Effect of receptor kinase inactivation on the rate of internalization and degradation of PDGF and the PDGF beta-receptor."
Sorkin A., Westermark B., Heldin C.H., Claesson-Welsh L.
J. Cell Biol. 112:469-478(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS RECEPTOR FOR PDGFA AND PDGFB, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-634.
[14]"Phosphorylation sites in the PDGF receptor with different specificities for binding GAP and PI3 kinase in vivo."
Kashishian A., Kazlauskas A., Cooper J.A.
EMBO J. 11:1373-1382(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ACTIVATION OF PHOSPHATIDYLINOSITOL 3-KINASE ACTIVITY, INTERACTION WITH PIK3R1 AND RASA1, PHOSPHORYLATION AT TYR-740; TYR-751; TYR-771 AND TYR-857, MUTAGENESIS OF LYS-634; TYR-716; TYR-740; TYR-751; TYR-763; TYR-771; TYR-775; TYR-778 AND TYR-857.
[15]"Identification of two C-terminal autophosphorylation sites in the PDGF beta-receptor: involvement in the interaction with phospholipase C-gamma."
Ronnstrand L., Mori S., Arridsson A.K., Eriksson A., Wernstedt C., Hellman U., Claesson-Welsh L., Heldin C.H.
EMBO J. 11:3911-3919(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS PDGFB RECEPTOR IN CELL PROLIFERATION AND PHOSPHORYLATION OF PLCG1, INTERACTION WITH PLCG1, PHOSPHORYLATION AT TYR-1009 AND TYR-1021, MUTAGENESIS OF TYR-1009 AND TYR-1021.
[16]"Ligand-induced polyubiquitination of the platelet-derived growth factor beta-receptor."
Mori S., Heldin C.H., Claesson-Welsh L.
J. Biol. Chem. 267:6429-6434(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, DEGRADATION.
[17]"GTPase-activating protein and phosphatidylinositol 3-kinase bind to distinct regions of the platelet-derived growth factor receptor beta subunit."
Kazlauskas A., Kashishian A., Cooper J.A., Valius M.
Mol. Cell. Biol. 12:2534-2544(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PIK3R1 AND RASA1, MUTAGENESIS OF TYR-740; TYR-751 AND TYR-771.
[18]"Identification of two juxtamembrane autophosphorylation sites in the PDGF beta-receptor; involvement in the interaction with Src family tyrosine kinases."
Mori S., Ronnstrand L., Yokote K., Engstrom A., Courtneidge S.A., Claesson-Welsh L., Heldin C.H.
EMBO J. 12:2257-2264(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS PDGFB RECEPTOR IN CELL PROLIFERATION, PHOSPHORYLATION AT TYR-579 AND TYR-581; INTERACTION WITH SRC, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-579 AND TYR-581.
[19]"Mechanism of platelet-derived growth factor (PDGF) AA, AB, and BB binding to alpha and beta PDGF receptor."
Fretto L.J., Snape A.J., Tomlinson J.E., Seroogy J.J., Wolf D.L., LaRochelle W.J., Giese N.A.
J. Biol. Chem. 268:3625-3631(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DGFA AND PDGFB.
[20]"Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor."
Lechleider R.J., Sugimoto S., Bennett A.M., Kashishian A.S., Cooper J.A., Shoelson S.E., Walsh C.T., Neel B.G.
J. Biol. Chem. 268:21478-21481(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION AND ACTIVATION OF PTPN11, INTERACTION WITH PTPN11; PIK3R1; PLCG1 AND RASA1, MUTAGENESIS OF TYR-1009.
[21]"Two signaling molecules share a phosphotyrosine-containing binding site in the platelet-derived growth factor receptor."
Nishimura R., Li W., Kashishian A., Mondino A., Zhou M., Cooper J., Schlessinger J.
Mol. Cell. Biol. 13:6889-6896(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NCK1 AND PIK3R1, FUNCTION IN PHOSPHORYLATION OF NCK1, MUTAGENESIS OF TYR-751.
[22]"Shb is a ubiquitously expressed Src homology 2 protein."
Welsh M., Mares J., Karlsson T., Lavergne C., Breant B., Claesson-Welsh L.
Oncogene 9:19-27(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SHB.
[23]"Grb7 is a downstream signaling component of platelet-derived growth factor alpha- and beta-receptors."
Yokote K., Margolis B., Heldin C.H., Claesson-Welsh L.
J. Biol. Chem. 271:30942-30949(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GRB7.
[24]"Fusion of the platelet-derived growth factor receptor beta to a novel gene CEV14 in acute myelogenous leukemia after clonal evolution."
Abe A., Emi N., Tanimoto M., Terasaki H., Marunouchi T., Saito H.
Blood 90:4271-4277(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH TRIP11.
[25]"Grb10, a positive, stimulatory signaling adapter in platelet-derived growth factor BB-, insulin-like growth factor I-, and insulin-mediated mitogenesis."
Wang J., Dai H., Yousaf N., Moussaif M., Deng Y., Boufelliga A., Swamy O.R., Leone M.E., Riedel H.
Mol. Cell. Biol. 19:6217-6228(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GRB10, MUTAGENESIS OF TYR-579; TYR-581; TYR-716; TYR-740; TYR-751; TYR-771; TYR-857; TYR-1009 AND TYR-1021.
[26]"APS, an adaptor protein containing PH and SH2 domains, is associated with the PDGF receptor and c-Cbl and inhibits PDGF-induced mitogenesis."
Yokouchi M., Wakioka T., Sakamoto H., Yasukawa H., Ohtsuka S., Sasaki A., Ohtsubo M., Valius M., Inoue A., Komiya S., Yoshimura A.
Oncogene 18:759-767(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SH2B2/APS.
[27]"Site-selective dephosphorylation of the platelet-derived growth factor beta-receptor by the receptor-like protein-tyrosine phosphatase DEP-1."
Kovalenko M., Denner K., Sandstrom J., Persson C., Gross S., Jandt E., Vilella R., Bohmer F., Ostman A.
J. Biol. Chem. 275:16219-16226(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: AUTOPHOSPHORYLATION AT TYR-562; TYR-751; TYR-763; TYR-771; TYR-775; TYR-778; TYR-857; TYR-1009 AND TYR-1021, DEPHOSPHORYLATION BY PTPRJ AT TYR-751; TYR-857; TYR-1009 AND TYR-1021.
[28]"Class II phosphoinositide 3-kinases are downstream targets of activated polypeptide growth factor receptors."
Arcaro A., Zvelebil M.J., Wallasch C., Ullrich A., Waterfield M.D., Domin J.
Mol. Cell. Biol. 20:3817-3830(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PIK3C2B.
[29]"Platelet-derived growth factor C (PDGF-C), a novel growth factor that binds to PDGF alpha and beta receptor."
Gilbertson D.G., Duff M.E., West J.W., Kelly J.D., Sheppard P.O., Hofstrand P.D., Gao Z., Shoemaker K., Bukowski T.R., Moore M., Feldhaus A.L., Humes J.M., Palmer T.E., Hart C.E.
J. Biol. Chem. 276:27406-27414(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A RECEPTOR FOR PDGFC, INTERACTION WITH PDGFC.
[30]"PDGF-D is a specific, protease-activated ligand for the PDGF beta-receptor."
Bergsten E., Uutela M., Li X., Pietras K., Oestman A., Heldin C.-H., Alitalo K., Eriksson U.
Nat. Cell Biol. 3:512-516(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A RECEPTOR FOR PDGFD.
[31]"Response to imatinib mesylate in patients with chronic myeloproliferative diseases with rearrangements of the platelet-derived growth factor receptor beta."
Apperley J.F., Gardembas M., Melo J.V., Russell-Jones R., Bain B.J., Baxter E.J., Chase A., Chessells J.M., Colombat M., Dearden C.E., Dimitrijevic S., Mahon F.-X., Marin D., Nikolova Z., Olavarria E., Silberman S., Schultheis B., Cross N.C.P., Goldman J.M.
N. Engl. J. Med. 347:481-487(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH ETV6.
[32]"Cloning of the t(1;5)(q23;q33) in a myeloproliferative disorder associated with eosinophilia: involvement of PDGFRB and response to imatinib."
Wilkinson K., Velloso E.R.P., Lopes L.F., Lee C., Aster J.C., Shipp M.A., Aguiar R.C.T.
Blood 102:4187-4190(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH PDE4DIP.
[33]"HCMOGT-1 is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with t(5;17)(q33;p11.2)."
Morerio C., Acquila M., Rosanda C., Rapella A., Dufour C., Locatelli F., Maserati E., Pasquali F., Panarello C.
Cancer Res. 64:2649-2651(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH SPECC1.
[34]"p53-Binding protein 1 is fused to the platelet-derived growth factor receptor beta in a patient with a t(5;15)(q33;q22) and an imatinib-responsive eosinophilic myeloproliferative disorder."
Grand F.H., Burgstaller S., Kuhr T., Baxter E.J., Webersinke G., Thaler J., Chase A.J., Cross N.C.
Cancer Res. 64:7216-7219(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH TP53BP1, ENZYME REGULATION.
[35]"Site-selective regulation of platelet-derived growth factor beta receptor tyrosine phosphorylation by T-cell protein tyrosine phosphatase."
Persson C., Saevenhed C., Bourdeau A., Tremblay M.L., Markova B., Boehmer F.D., Haj F.G., Neel B.G., Elson A., Heldin C.H., Roennstrand L., Ostman A., Hellberg C.
Mol. Cell. Biol. 24:2190-2201(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-579; TYR-751; TYR-771 AND TYR-1021, DEPHOSPHORYLATION AT TYR-579 AND TYR-1021 BY PTPN2.
[36]"Regulation of PDGF signalling and vascular remodelling by peroxiredoxin II."
Choi M.H., Lee I.K., Kim G.W., Kim B.U., Han Y.H., Yu D.Y., Park H.S., Kim K.Y., Lee J.S., Choi C., Bae Y.S., Lee B.I., Rhee S.G., Kang S.W.
Nature 435:347-353(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: AUTOPHOSPHORYLATION AT TYR-579; TYR-581; TYR-716; TYR-740; TYR-771; TYR-857; TYR-1009 AND TYR-1021.
[37]"Binding of Cbl to a phospholipase Cgamma1-docking site on platelet-derived growth factor receptor beta provides a dual mechanism of negative regulation."
Reddi A.L., Ying G., Duan L., Chen G., Dimri M., Douillard P., Druker B.J., Naramura M., Band V., Band H.
J. Biol. Chem. 282:29336-29347(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CBL, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-1021, UBIQUITINATION.
[38]"A novel signaling axis of matriptase/PDGF-D/ss-PDGFR in human prostate cancer."
Ustach C.V., Huang W., Conley-LaComb M.K., Lin C.Y., Che M., Abrams J., Kim H.R.
Cancer Res. 70:9631-9640(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS PDGFD RECEPTOR.
[39]"Mutation of tyrosine residue 857 in the PDGF beta-receptor affects cell proliferation but not migration."
Wardega P., Heldin C.H., Lennartsson J.
Cell. Signal. 22:1363-1368(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF CBL; STAM; PDCD6IP/ALIX; PLCG1 AND PTPN11, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-634 AND TYR-857.
[40]"Stimulation of platelet-derived growth factor receptor beta (PDGFRbeta) activates ADAM17 and promotes metalloproteinase-dependent cross-talk between the PDGFRbeta and epidermal growth factor receptor (EGFR) signaling pathways."
Mendelson K., Swendeman S., Saftig P., Blobel C.P.
J. Biol. Chem. 285:25024-25032(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[41]"Glyceollins inhibit platelet-derived growth factor-mediated human arterial smooth muscle cell proliferation and migration."
Kim H.J., Cha B.Y., Choi B., Lim J.S., Woo J.T., Kim J.S.
Br. J. Nutr. 107:24-35(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN SMOOTH MUSCLE CELL PROLIFERATION AND MIGRATION.
[42]"Direct interaction between Shc and the platelet-derived growth factor beta-receptor."
Yokote K., Mori S., Hansen K., McGlade J., Pawson T., Heldin C.H., Claesson-Welsh L.
J. Biol. Chem. 269:15337-15343(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SHC1 AND GRB2, FUNCTION IN PHOSPHORYLATION OF SHC1.
[43]"Disruption of platelet-derived growth factor-dependent phosphatidylinositol 3-kinase and phospholipase Cgamma 1 activity abolishes vascular smooth muscle cell proliferation and migration and attenuates neointima formation in vivo."
Caglayan E., Vantler M., Leppanen O., Gerhardt F., Mustafov L., Ten Freyhaus H., Kappert K., Odenthal M., Zimmermann W.H., Tallquist M.D., Rosenkranz S.
J. Am. Coll. Cardiol. 57:2527-2538(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN SMOOTH MUSCLE CELL MIGRATION AND NEOINTIMA FORMATION AFTER BLOOD VESSEL INJURY, MUTAGENESIS OF TYR-740; TYR-751 AND TYR-1021.
[44]"Signal transduction via platelet-derived growth factor receptors."
Heldin C.H., Ostman A., Ronnstrand L.
Biochim. Biophys. Acta 1378:F79-113(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON SIGNALING AND AUTOPHOSPHORYLATION.
[45]"PDGF receptors-mediators of autocrine tumor growth and regulators of tumor vasculature and stroma."
Ostman A.
Cytokine Growth Factor Rev. 15:275-286(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[46]"PDGF receptors as targets in tumor treatment."
Ostman A., Heldin C.H.
Adv. Cancer Res. 97:247-274(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[47]"Role of platelet-derived growth factors in physiology and medicine."
Andrae J., Gallini R., Betsholtz C.
Genes Dev. 22:1276-1312(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION; LIGANDS; ROLE IN DEVELOPMENT AND DISEASE AND ACTIVATION OF SIGNALING PATHWAYS.
[48]"NMR trial models: experiences with the colicin immunity protein Im7 and the p85alpha C-terminal SH2-peptide complex."
Pauptit R.A., Dennis C.A., Derbyshire D.J., Breeze A.L., Weston S.A., Rowsell S., Murshudov G.N.
Acta Crystallogr. D 57:1397-1404(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 751-755 IN COMPLEX WITH PIK3R1, COMPARISON WITH NMR ANALYSIS.
[49]"Structural determinants of the Na+/H+ exchanger regulatory factor interaction with the beta 2 adrenergic and platelet-derived growth factor receptors."
Karthikeyan S., Leung T., Ladias J.A.A.
J. Biol. Chem. 277:18973-18978(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1102-1106 IN COMPLEX WITH SLC9A3R1, INTERACTION WITH SLC9A3R1.
[50]"Structures of a platelet-derived growth factor/propeptide complex and a platelet-derived growth factor/receptor complex."
Shim A.H., Liu H., Focia P.J., Chen X., Lin P.C., He X.
Proc. Natl. Acad. Sci. U.S.A. 107:11307-11312(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 33-314 IN COMPLEX WITH PDGFB, SUBUNIT, GLYCOSYLATION AT ASN-45; ASN-89; ASN-103; ASN-215; ASN-230; ASN-292 AND ASN-307, DISULFIDE BONDS.
[51]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] PHE-29; LYS-282; LYS-485; HIS-589; TYR-718 AND ILE-882.
[52]"Mutations in PDGFRB cause autosomal-dominant infantile myofibromatosis."
Martignetti J.A., Tian L., Li D., Ramirez M.C., Camacho-Vanegas O., Camacho S.C., Guo Y., Zand D.J., Bernstein A.M., Masur S.K., Kim C.E., Otieno F.G., Hou C., Abdel-Magid N., Tweddale B., Metry D., Fournet J.C., Papp E. expand/collapse author list , McPherson E.W., Zabel C., Vaksmann G., Morisot C., Keating B., Sleiman P.M., Cleveland J.A., Everman D.B., Zackai E., Hakonarson H.
Am. J. Hum. Genet. 92:1001-1007(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT IMF1 THR-660.
[53]"A recurrent PDGFRB mutation causes familial infantile myofibromatosis."
Cheung Y.H., Gayden T., Campeau P.M., Leduc C.A., Russo D., Nguyen V.H., Guo J., Qi M., Guan Y., Albrecht S., Moroz B., Eldin K.W., Lu J.T., Schwartzentruber J., Malkin D., Berghuis A.M., Emil S., Gibbs R.A. expand/collapse author list , Burk D.L., Vanstone M., Lee B.H., Orchard D., Boycott K.M., Chung W.K., Jabado N.
Am. J. Hum. Genet. 92:996-1000(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT IMF1 CYS-561.
[54]"Mutation of the PDGFRB gene as a cause of idiopathic basal ganglia calcification."
Nicolas G., Pottier C., Maltete D., Coutant S., Rovelet-Lecrux A., Legallic S., Rousseau S., Vaschalde Y., Guyant-Marechal L., Augustin J., Martinaud O., Defebvre L., Krystkowiak P., Pariente J., Clanet M., Labauge P., Ayrignac X., Lefaucheur R. expand/collapse author list , Le Ber I., Frebourg T., Hannequin D., Campion D.
Neurology 80:181-187(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS IBGC4 PRO-658 AND TRP-987.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03278 mRNA. Translation: AAA60049.1.
M21616 mRNA. Translation: AAA36427.1.
AC005895 Genomic DNA. No translation available.
AC011382 Genomic DNA. No translation available.
BC032224 mRNA. Translation: AAH32224.1.
U33172 Genomic DNA. Translation: AAC51675.1.
CCDSCCDS4303.1.
PIRPFHUGB. A28206.
RefSeqNP_002600.1. NM_002609.3.
UniGeneHs.509067.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GQ5X-ray2.20A1102-1106[»]
1H9OX-ray1.79B751-755[»]
1LWPmodel-A600-962[»]
1SHAX-ray1.50B751-755[»]
2L6WNMR-A/B526-563[»]
2PLDNMR-B1018-1029[»]
2PLENMR-B1018-1029[»]
3MJGX-ray2.30X/Y33-314[»]
ProteinModelPortalP09619.
SMRP09619. Positions 33-463, 526-563, 576-1006.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111185. 43 interactions.
DIPDIP-558N.
IntActP09619. 53 interactions.
MINTMINT-148093.
STRING9606.ENSP00000261799.

Chemistry

BindingDBP09619.
ChEMBLCHEMBL1913.
DrugBankDB00102. Becaplermin.
DB01254. Dasatinib.
DB00619. Imatinib.
DB00398. Sorafenib.
DB01268. Sunitinib.
GuidetoPHARMACOLOGY1804.

PTM databases

PhosphoSiteP09619.

Polymorphism databases

DMDM129890.

Proteomic databases

MaxQBP09619.
PaxDbP09619.
PRIDEP09619.

Protocols and materials databases

DNASU5159.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261799; ENSP00000261799; ENSG00000113721.
GeneID5159.
KEGGhsa:5159.
UCSCuc003lro.3. human.

Organism-specific databases

CTD5159.
GeneCardsGC05M149473.
GeneReviewsPDGFRB.
HGNCHGNC:8804. PDGFRB.
HPACAB003842.
CAB018144.
HPA028499.
MIM131440. phenotype.
173410. gene.
228550. phenotype.
601626. phenotype.
607785. phenotype.
615007. phenotype.
neXtProtNX_P09619.
Orphanet1980. Bilateral striopallidodentate calcinosis.
98823. Chronic myelomonocytic leukemia.
3260. Idiopathic hypereosinophilic syndrome.
2591. Infantile myofibromatosis.
168950. Myeloid neoplasm associated with PDGFRB rearrangement.
86830. Unclassified chronic myeloproliferative disease.
PharmGKBPA33148.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000112009.
HOVERGENHBG004335.
InParanoidP09619.
KOK05089.
OMAAPYDNYV.
OrthoDBEOG7GXP9Q.
PhylomeDBP09619.
TreeFamTF325768.

Enzyme and pathway databases

BRENDA2.7.10.1. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.
SignaLinkP09619.

Gene expression databases

ArrayExpressP09619.
BgeeP09619.
CleanExHS_PDGFRB.
GenevestigatorP09619.

Family and domain databases

Gene3D2.60.40.10. 4 hits.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
IPR011009. Kinase-like_dom.
IPR027288. PGFRB.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016243. Tyr_kinase_CSF1/PDGF_rcpt.
IPR001824. Tyr_kinase_rcpt_3_CS.
[Graphical view]
PANTHERPTHR24416:SF53. PTHR24416:SF53. 1 hit.
PfamPF07679. I-set. 1 hit.
PF00047. ig. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFPIRSF500948. Beta-PDGF_receptor. 1 hit.
PIRSF000615. TyrPK_CSF1-R. 1 hit.
SMARTSM00409. IG. 2 hits.
SM00408. IGc2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 2 hits.
PROSITEPS50835. IG_LIKE. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPDGFRB. human.
EvolutionaryTraceP09619.
GeneWikiPDGFRB.
GenomeRNAi5159.
NextBio19958.
PROP09619.
SOURCESearch...

Entry information

Entry namePGFRB_HUMAN
AccessionPrimary (citable) accession number: P09619
Secondary accession number(s): Q8N5L4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: July 9, 2014
This is version 183 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries