UniProtKB - P09619 (PGFRB_HUMAN)
Protein
Platelet-derived growth factor receptor beta
Gene
PDGFRB
Organism
Homo sapiens (Human)
Status
Functioni
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.20 Publications
Catalytic activityi
- ATP + L-tyrosyl-[protein] = ADP + H+ + O-phospho-L-tyrosyl-[protein]PROSITE-ProRule annotation3 PublicationsEC:2.7.10.1PROSITE-ProRule annotation3 Publications
Activity regulationi
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.1 Publication
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Sitei | 527 – 528 | Breakpoint for insertion to form PDE4DIP-PDGFRB fusion protein | 2 | |
| Binding sitei | 634 | ATPCurated | 1 | |
| Active sitei | 826 | Proton acceptorPROSITE-ProRule annotation | 1 |
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Nucleotide bindingi | 606 – 614 | ATPPROSITE-ProRule annotation | 9 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- enzyme binding Source: BHF-UCL
- growth factor binding Source: GO_Central
- phosphatidylinositol 3-kinase binding Source: Ensembl
- platelet activating factor receptor activity Source: ProtInc
- platelet-derived growth factor-activated receptor activity Source: GO_Central
- platelet-derived growth factor beta-receptor activity Source: UniProtKB
- platelet-derived growth factor binding Source: UniProtKB
- platelet-derived growth factor receptor binding Source: BHF-UCL
- protein kinase binding Source: UniProtKB
- protein tyrosine kinase activity Source: UniProtKB
- signaling receptor binding Source: UniProtKB
- transmembrane receptor protein tyrosine kinase activity Source: GO_Central
- vascular endothelial growth factor binding Source: BHF-UCL
GO - Biological processi
- adrenal gland development Source: Ensembl
- aging Source: Ensembl
- aorta morphogenesis Source: BHF-UCL
- cardiac myofibril assembly Source: UniProtKB
- cell chemotaxis Source: UniProtKB
- cell migration Source: UniProtKB
- cell migration involved in coronary angiogenesis Source: UniProtKB
- cell migration involved in vasculogenesis Source: UniProtKB
- cellular response to hydrogen peroxide Source: Ensembl
- embryonic organ development Source: Ensembl
- glycosaminoglycan biosynthetic process Source: Ensembl
- inner ear development Source: Ensembl
- in utero embryonic development Source: Ensembl
- lung growth Source: Ensembl
- male gonad development Source: Ensembl
- MAPK cascade Source: Reactome
- metanephric comma-shaped body morphogenesis Source: Ensembl
- metanephric glomerular capillary formation Source: UniProtKB
- metanephric glomerular mesangial cell proliferation involved in metanephros development Source: UniProtKB
- metanephric mesenchymal cell migration Source: Ensembl
- metanephric mesenchyme development Source: Ensembl
- metanephric S-shaped body morphogenesis Source: Ensembl
- multicellular organism development Source: GO_Central
- negative regulation of apoptotic process Source: Ensembl
- peptidyl-tyrosine phosphorylation Source: UniProtKB
- phosphatidylinositol-mediated signaling Source: UniProtKB
- phosphatidylinositol metabolic process Source: UniProtKB
- platelet-derived growth factor receptor-beta signaling pathway Source: UniProtKB
- platelet-derived growth factor receptor signaling pathway Source: UniProtKB
- positive regulation of apoptotic process Source: Ensembl
- positive regulation of calcium ion import Source: UniProtKB
- positive regulation of cell migration Source: BHF-UCL
- positive regulation of cell population proliferation Source: UniProtKB
- positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway Source: BHF-UCL
- positive regulation of chemotaxis Source: UniProtKB
- positive regulation of collagen biosynthetic process Source: Ensembl
- positive regulation of DNA biosynthetic process Source: UniProtKB
- positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
- positive regulation of fibroblast proliferation Source: Ensembl
- positive regulation of hepatic stellate cell activation Source: Ensembl
- positive regulation of kinase activity Source: GO_Central
- positive regulation of MAP kinase activity Source: UniProtKB
- positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway Source: UniProtKB
- positive regulation of mitotic nuclear division Source: UniProtKB
- positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
- positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
- positive regulation of phospholipase C activity Source: UniProtKB
- positive regulation of phosphoprotein phosphatase activity Source: UniProtKB
- positive regulation of protein kinase B signaling Source: Reactome
- positive regulation of reactive oxygen species metabolic process Source: UniProtKB
- positive regulation of Rho protein signal transduction Source: Ensembl
- positive regulation of smooth muscle cell migration Source: UniProtKB
- positive regulation of smooth muscle cell proliferation Source: UniProtKB
- protein autophosphorylation Source: UniProtKB
- regulation of actin cytoskeleton organization Source: BHF-UCL
- regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
- response to ceramide Source: Ensembl
- response to estradiol Source: Ensembl
- response to estrogen Source: Ensembl
- response to fluid shear stress Source: Ensembl
- response to hyperoxia Source: Ensembl
- response to retinoic acid Source: Ensembl
- response to toxic substance Source: Ensembl
- retina vasculature development in camera-type eye Source: UniProtKB
- ruffle assembly Source: Ensembl
- signal transduction Source: UniProtKB
- skeletal system morphogenesis Source: Ensembl
- smooth muscle cell chemotaxis Source: BHF-UCL
- smooth muscle tissue development Source: Ensembl
- tissue homeostasis Source: Ensembl
- transmembrane receptor protein tyrosine kinase signaling pathway Source: GO_Central
- wound healing Source: Ensembl
Keywordsi
| Molecular function | Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase |
| Biological process | Chemotaxis |
| Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
| BRENDAi | 2.7.10.1, 2681 |
| PathwayCommonsi | P09619 |
| Reactomei | R-HSA-1257604, PIP3 activates AKT signaling R-HSA-186763, Downstream signal transduction R-HSA-186797, Signaling by PDGF R-HSA-2219530, Constitutive Signaling by Aberrant PI3K in Cancer R-HSA-5673001, RAF/MAP kinase cascade R-HSA-6811558, PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling |
| SignaLinki | P09619 |
| SIGNORi | P09619 |
Names & Taxonomyi
| Protein namesi | Recommended name: Platelet-derived growth factor receptor beta (EC:2.7.10.1)Short name: PDGF-R-beta Short name: PDGFR-beta 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 namesi | Name:PDGFRB Synonyms:PDGFR, PDGFR1 |
| Organismi | Homo sapiens (Human) |
| Taxonomic identifieri | 9606 [NCBI] |
| Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
| Proteomesi |
|
Organism-specific databases
| EuPathDBi | HostDB:ENSG00000113721.13 |
| HGNCi | HGNC:8804, PDGFRB |
| MIMi | 173410, gene |
| neXtProti | NX_P09619 |
Subcellular locationi
Lysosome
Plasma membrane
Other locations
Note: After ligand binding, the autophosphorylated receptor is ubiquitinated and internalized, leading to its degradation.
Golgi apparatus
- Golgi apparatus Source: HPA
Lysosome
- lysosomal lumen Source: UniProtKB-SubCell
Nucleus
- nucleus Source: UniProtKB
Plasma Membrane
- apical plasma membrane Source: UniProtKB
- integral component of plasma membrane Source: GO_Central
- intrinsic component of plasma membrane Source: UniProtKB
- plasma membrane Source: Reactome
Other locations
- cell surface Source: Ensembl
- cytoplasm Source: UniProtKB
- cytoplasmic vesicle Source: UniProtKB-KW
- focal adhesion Source: UniProtKB
- intracellular membrane-bounded organelle Source: HPA
- membrane Source: BHF-UCL
- receptor complex Source: GO_Central
- ruffle Source: Ensembl
Topology
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Topological domaini | 33 – 532 | ExtracellularSequence analysisAdd BLAST | 500 | |
| Transmembranei | 533 – 553 | HelicalSequence analysisAdd BLAST | 21 | |
| Topological domaini | 554 – 1106 | CytoplasmicSequence analysisAdd BLAST | 553 |
Keywords - Cellular componenti
Cell membrane, Cytoplasmic vesicle, Lysosome, MembranePathology & Biotechi
Involvement in diseasei
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)
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).4 Publications
Disease descriptionA hematologic disorder characterized by malignant eosinophils proliferation.
Related information in OMIMLeukemia, acute myelogenous (AML)
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).1 Publication
Disease descriptionA 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.
Related information in OMIMLeukemia, juvenile myelomonocytic (JMML)
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).1 Publication
Disease descriptionAn 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.
Related information in OMIMBasal ganglia calcification, idiopathic, 4 (IBGC4)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
Related information in OMIM| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Natural variantiVAR_069320 | 658 | L → P in IBGC4; no effect on protein abundance; loss of PDGF beta receptor activity. 3 PublicationsCorresponds to variant dbSNP:rs397509381EnsemblClinVar. | 1 | |
| Natural variantiVAR_069321 | 987 | R → W in IBGC4; decreased protein abundance; no effect on receptor activity; decreased PDGF signaling pathway. 3 PublicationsCorresponds to variant dbSNP:rs397509382EnsemblClinVar. | 1 | |
| Natural variantiVAR_075395 | 1071 | E → V in IBGC4; no effect on protein abundance; no effect on receptor activity; decreased PDGF signaling pathway. 2 Publications | 1 |
Myofibromatosis, infantile 1 (IMF1)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
Related information in OMIM| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Natural variantiVAR_069925 | 561 | R → C in IMF1. 1 PublicationCorresponds to variant dbSNP:rs367543286EnsemblClinVar. | 1 | |
| Natural variantiVAR_069926 | 660 | P → T in IMF1. 1 PublicationCorresponds to variant dbSNP:rs144050370EnsemblClinVar. | 1 |
Kosaki overgrowth syndrome (KOGS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA syndrome characterized by somatic overgrowth, distinctive facial features, hyperelastic and fragile skin, and progressive neurologic deterioration with white matter lesions on brain imaging.
Related information in OMIM| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Natural variantiVAR_075865 | 584 | P → R in KOGS. 1 PublicationCorresponds to variant dbSNP:rs863224946EnsemblClinVar. | 1 |
Premature aging syndrome, Penttinen type (PENTT)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA syndrome characterized by a prematurely aged appearance with lipoatrophy, epidermal and dermal atrophy along with hypertrophic lesions that resemble scars, thin hair, proptosis, underdeveloped cheekbones, and marked acro-osteolysis.
Related information in OMIM| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Natural variantiVAR_075866 | 665 | V → A in PENTT; gain of function in protein tyrosine kinase activity; shows ligand-independent constitutive signaling. 1 PublicationCorresponds to variant dbSNP:rs1554108211EnsemblClinVar. | 1 |
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Mutagenesisi | 579 | Y → F: Loss of kinase activity; when associated with F-581. Strongly reduces interaction with SRC family kinases. No effect on interaction with GRB10. 2 Publications | 1 | |
| Mutagenesisi | 581 | Y → F: Loss of kinase activity; when associated with F-579. No effect on interaction with GRB10. 2 Publications | 1 | |
| Mutagenesisi | 634 | K → A or R: Loss of kinase activity. Abolishes interaction with RASA1. No effect on phosphatidylinositol 3-kinase activity. 3 Publications | 1 | |
| Mutagenesisi | 716 | Y → F: No effect neither on interaction with GRB10 and RASA1 nor on phosphatidylinositol 3-kinase activity. 2 Publications | 1 | |
| Mutagenesisi | 740 | Y → 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. 4 Publications | 1 | |
| Mutagenesisi | 751 | Y → F: Strongly reduces up-regulation of cell proliferation; when associated with F-740. Abolishes phosphatidylinositol 3-kinase activity and interaction with NCK1, and slightly reduces interaction with RASA1. No effect on interaction with GRB10. 6 Publications | 1 | |
| Mutagenesisi | 763 | Y → F: No effect on interaction with RASA1 and on phosphatidylinositol 3-kinase activity. 1 Publication | 1 | |
| Mutagenesisi | 771 | Y → F: Loss of interaction with GRB10. Abolishes interaction with RASA1. No effect on phosphatidylinositol 3-kinase activity. 3 Publications | 1 | |
| Mutagenesisi | 775 | Y → F: No effect on interaction with RASA1 and on phosphatidylinositol 3-kinase activity. 1 Publication | 1 | |
| Mutagenesisi | 778 | Y → F: Strongly reduces expression levels. 1 Publication | 1 | |
| Mutagenesisi | 857 | Y → F: Reduces kinase activity. No effect on interaction with GRB10. Abolishes interaction with RASA1. No effect on phosphatidylinositol 3-kinase activity. 4 Publications | 1 | |
| Mutagenesisi | 1009 | Y → F: No effect on interaction with GRB10. Abolishes interaction with PLCG1; when associated with F-1021. 3 Publications | 1 | |
| Mutagenesisi | 1021 | Y → F: Strongly reduces up-regulation of cell proliferation. Abolishes interaction with PLCG1; when associated with F-1009. No effect on interaction with GRB10. 4 Publications | 1 |
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Sitei | 527 – 528 | Breakpoint for translocation to form TRIP11-PDGFRB | 2 | |
| Sitei | 558 – 559 | Breakpoint for translocation to form the CEP85L-PDGFRB fusion protein | 2 |
Keywords - Diseasei
Disease mutation, Proto-oncogeneOrganism-specific databases
| DisGeNETi | 5159 |
| GeneReviewsi | PDGFRB |
| MalaCardsi | PDGFRB |
| MIMi | 131440, phenotype 228550, phenotype 601626, phenotype 601812, phenotype 607785, phenotype 615007, phenotype 616592, phenotype |
| OpenTargetsi | ENSG00000113721 |
| Orphaneti | 363665, Acroosteolysis-keloid-like lesions-premature aging syndrome 1980, Bilateral striopallidodentate calcinosis 98823, Chronic myelomonocytic leukemia 86830, Chronic myeloproliferative disease, unclassifiable 2591, Infantile myofibromatosis 168950, Myeloid/lymphoid neoplasm associated with PDGFRB rearrangement 314950, Primary hypereosinophilic syndrome 477831, Skeletal overgrowth-craniofacial dysmorphism-hyperelastic skin-white matter lesions syndrome |
| PharmGKBi | PA33148 |
Miscellaneous databases
| Pharosi | P09619, Tclin |
Chemistry databases
| ChEMBLi | CHEMBL1913 |
| DrugBanki | DB00102, Becaplermin DB01254, Dasatinib DB12147, Erdafitinib DB10770, Foreskin fibroblast (neonatal) DB12010, Fostamatinib DB00619, Imatinib DB06595, Midostaurin DB09079, Nintedanib DB06589, Pazopanib DB12978, Pexidartinib DB09221, Polaprezinc DB08896, Regorafenib DB00398, Sorafenib DB01268, Sunitinib DB09283, Trapidil DB05146, XL820 DB05014, XL999 |
| DrugCentrali | P09619 |
| GuidetoPHARMACOLOGYi | 1804 |
Polymorphism and mutation databases
| BioMutai | PDGFRB |
| DMDMi | 129890 |
PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Signal peptidei | 1 – 32 | 1 PublicationAdd BLAST | 32 | |
| ChainiPRO_0000016757 | 33 – 1106 | Platelet-derived growth factor receptor betaAdd BLAST | 1074 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Glycosylationi | 45 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Disulfide bondi | 54 ↔ 100 | PROSITE-ProRule annotation1 Publication | ||
| Glycosylationi | 89 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
| Glycosylationi | 103 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
| Disulfide bondi | 149 ↔ 190 | PROSITE-ProRule annotation1 Publication | ||
| Glycosylationi | 215 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
| Glycosylationi | 230 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
| Disulfide bondi | 235 ↔ 291 | PROSITE-ProRule annotation1 Publication | ||
| Glycosylationi | 292 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
| Glycosylationi | 307 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
| Glycosylationi | 354 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Glycosylationi | 371 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Disulfide bondi | 436 ↔ 508 | PROSITE-ProRule annotation | ||
| Glycosylationi | 468 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Glycosylationi | 479 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Modified residuei | 562 | Phosphotyrosine; by autocatalysis1 Publication | 1 | |
| Modified residuei | 579 | Phosphotyrosine; by autocatalysis3 Publications | 1 | |
| Modified residuei | 581 | Phosphotyrosine; by autocatalysis2 Publications | 1 | |
| Modified residuei | 686 | Phosphotyrosine; by ABL1 and ABL2By similarity | 1 | |
| Modified residuei | 716 | Phosphotyrosine; by autocatalysis1 Publication | 1 | |
| Modified residuei | 740 | Phosphotyrosine; by autocatalysis2 Publications | 1 | |
| Modified residuei | 751 | Phosphotyrosine; by autocatalysis5 Publications | 1 | |
| Modified residuei | 763 | Phosphotyrosine; by autocatalysis1 Publication | 1 | |
| Modified residuei | 771 | Phosphotyrosine; by autocatalysis4 Publications | 1 | |
| Modified residuei | 775 | Phosphotyrosine; by autocatalysis1 Publication | 1 | |
| Modified residuei | 778 | Phosphotyrosine; by autocatalysis1 Publication | 1 | |
| Modified residuei | 857 | Phosphotyrosine; by autocatalysis5 Publications | 1 | |
| Modified residuei | 934 | Phosphotyrosine; by ABL1 and ABL2By similarity | 1 | |
| Modified residuei | 970 | Phosphotyrosine; by ABL1 and ABL2By similarity | 1 | |
| Modified residuei | 1009 | Phosphotyrosine; by autocatalysis3 Publications | 1 | |
| Modified residuei | 1021 | Phosphotyrosine; by autocatalysis4 Publications | 1 |
Post-translational modificationi
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-1021.8 Publications
N-glycosylated.2 Publications
Ubiquitinated. After autophosphorylation, the receptor is polyubiquitinated, leading to its degradation.2 Publications
Keywords - PTMi
Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugationProteomic databases
| CPTACi | CPTAC-1630 |
| EPDi | P09619 |
| jPOSTi | P09619 |
| MassIVEi | P09619 |
| MaxQBi | P09619 |
| PaxDbi | P09619 |
| PeptideAtlasi | P09619 |
| PRIDEi | P09619 |
| ProteomicsDBi | 52253 [P09619-1] |
PTM databases
| GlyConnecti | 1967, 4 N-Linked glycans (3 sites) |
| GlyGeni | P09619, 11 sites |
| iPTMneti | P09619 |
| PhosphoSitePlusi | P09619 |
Expressioni
Gene expression databases
| Bgeei | ENSG00000113721, Expressed in stromal cell of endometrium and 224 other tissues |
| ExpressionAtlasi | P09619, baseline and differential |
| Genevisiblei | P09619, HS |
Organism-specific databases
| HPAi | ENSG00000113721, Low tissue specificity |
Interactioni
Subunit structurei
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.
20 PublicationsBinary interactionsi
Hide detailsP09619
GO - Molecular functioni
- enzyme binding Source: BHF-UCL
- growth factor binding Source: GO_Central
- phosphatidylinositol 3-kinase binding Source: Ensembl
- platelet-derived growth factor binding Source: UniProtKB
- platelet-derived growth factor receptor binding Source: BHF-UCL
- protein kinase binding Source: UniProtKB
- signaling receptor binding Source: UniProtKB
- vascular endothelial growth factor binding Source: BHF-UCL
Protein-protein interaction databases
| BioGRIDi | 111185, 99 interactors |
| ComplexPortali | CPX-2882, PDGF receptor beta - PDGF-BB complex CPX-2883, PDGF receptor alpha-beta - PDGF-BB complex CPX-2886, PDGF receptor beta - PDGF-AB complex CPX-2888, PDGF receptor alpha-beta - PDGF-CC complex CPX-2889, PDGF receptor beta - PDGF-DD complex CPX-2890, PDGF receptor alpha-beta - PDGF-DD complex CPX-2891, PDGF receptor beta - PDGF-CC complex CPX-2892, PDGF receptor alpha-beta - PDGF-AB complex |
| CORUMi | P09619 |
| DIPi | DIP-558N |
| IntActi | P09619, 200 interactors |
| MINTi | P09619 |
| STRINGi | 9606.ENSP00000261799 |
Chemistry databases
| BindingDBi | P09619 |
Miscellaneous databases
| RNActi | P09619, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
| BMRBi | P09619 |
| SMRi | P09619 |
| ModBasei | Search... |
| PDBe-KBi | Search... |
Miscellaneous databases
| EvolutionaryTracei | P09619 |
Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Domaini | 33 – 120 | Ig-like C2-type 1Add BLAST | 88 | |
| Domaini | 129 – 210 | Ig-like C2-type 2Add BLAST | 82 | |
| Domaini | 214 – 309 | Ig-like C2-type 3Add BLAST | 96 | |
| Domaini | 331 – 403 | Ig-like C2-type 4Add BLAST | 73 | |
| Domaini | 416 – 524 | Ig-like C2-type 5Add BLAST | 109 | |
| Domaini | 600 – 962 | Protein kinasePROSITE-ProRule annotationAdd BLAST | 363 |
Sequence similaritiesi
Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily.PROSITE-ProRule annotation
Keywords - Domaini
Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helixPhylogenomic databases
| eggNOGi | KOG0200, Eukaryota |
| GeneTreei | ENSGT00940000157138 |
| HOGENOMi | CLU_000288_49_0_1 |
| InParanoidi | P09619 |
| KOi | K05089 |
| OMAi | TYVCNVS |
| OrthoDBi | 269253at2759 |
| PhylomeDBi | P09619 |
| TreeFami | TF325768 |
Family and domain databases
| Gene3Di | 2.60.40.10, 5 hits |
| InterProi | View protein in InterPro IPR007110, Ig-like_dom IPR036179, Ig-like_dom_sf IPR013783, Ig-like_fold IPR013098, Ig_I-set IPR003599, Ig_sub IPR003598, Ig_sub2 IPR013151, Immunoglobulin IPR011009, Kinase-like_dom_sf 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 IPR001824, Tyr_kinase_rcpt_3_CS |
| Pfami | View protein in Pfam PF07679, I-set, 1 hit PF00047, ig, 1 hit PF07714, PK_Tyr_Ser-Thr, 1 hit |
| PIRSFi | PIRSF500948, Beta-PDGF_receptor, 1 hit |
| SMARTi | View protein in SMART SM00409, IG, 3 hits SM00408, IGc2, 3 hits SM00219, TyrKc, 1 hit |
| SUPFAMi | SSF48726, SSF48726, 3 hits SSF56112, SSF56112, 1 hit |
| PROSITEi | View protein in PROSITE PS50835, 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 |
Sequences (2+)i
Sequence statusi: Complete.
Sequence processingi: The displayed sequence is further processed into a mature form.
This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basketThis entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All
Isoform 1 (identifier: P09619-1) [UniParc]FASTAAdd to basket
This isoform has been chosen as the canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
10 20 30 40 50
MRLPGAMPAL ALKGELLLLS LLLLLEPQIS QGLVVTPPGP ELVLNVSSTF
60 70 80 90 100
VLTCSGSAPV VWERMSQEPP QEMAKAQDGT FSSVLTLTNL TGLDTGEYFC
110 120 130 140 150
THNDSRGLET DERKRLYIFV PDPTVGFLPN DAEELFIFLT EITEITIPCR
160 170 180 190 200
VTDPQLVVTL HEKKGDVALP VPYDHQRGFS GIFEDRSYIC KTTIGDREVD
210 220 230 240 250
SDAYYVYRLQ VSSINVSVNA VQTVVRQGEN ITLMCIVIGN EVVNFEWTYP
260 270 280 290 300
RKESGRLVEP VTDFLLDMPY HIRSILHIPS AELEDSGTYT CNVTESVNDH
310 320 330 340 350
QDEKAINITV VESGYVRLLG EVGTLQFAEL HRSRTLQVVF EAYPPPTVLW
360 370 380 390 400
FKDNRTLGDS SAGEIALSTR NVSETRYVSE LTLVRVKVAE AGHYTMRAFH
410 420 430 440 450
EDAEVQLSFQ LQINVPVRVL ELSESHPDSG EQTVRCRGRG MPQPNIIWSA
460 470 480 490 500
CRDLKRCPRE LPPTLLGNSS EEESQLETNV TYWEEEQEFE VVSTLRLQHV
510 520 530 540 550
DRPLSVRCTL RNAVGQDTQE VIVVPHSLPF KVVVISAILA LVVLTIISLI
560 570 580 590 600
ILIMLWQKKP RYEIRWKVIE SVSSDGHEYI YVDPMQLPYD STWELPRDQL
610 620 630 640 650
VLGRTLGSGA FGQVVEATAH GLSHSQATMK VAVKMLKSTA RSSEKQALMS
660 670 680 690 700
ELKIMSHLGP HLNVVNLLGA CTKGGPIYII TEYCRYGDLV DYLHRNKHTF
710 720 730 740 750
LQHHSDKRRP PSAELYSNAL PVGLPLPSHV SLTGESDGGY MDMSKDESVD
760 770 780 790 800
YVPMLDMKGD VKYADIESSN YMAPYDNYVP SAPERTCRAT LINESPVLSY
810 820 830 840 850
MDLVGFSYQV ANGMEFLASK NCVHRDLAAR NVLICEGKLV KICDFGLARD
860 870 880 890 900
IMRDSNYISK GSTFLPLKWM APESIFNSLY TTLSDVWSFG ILLWEIFTLG
910 920 930 940 950
GTPYPELPMN EQFYNAIKRG YRMAQPAHAS DEIYEIMQKC WEEKFEIRPP
960 970 980 990 1000
FSQLVLLLER LLGEGYKKKY QQVDEEFLRS DHPAILRSQA RLPGFHGLRS
1010 1020 1030 1040 1050
PLDTSSVLYT AVQPNEGDND YIIPLPDPKP EVADEGPLEG SPSLASSTLN
1060 1070 1080 1090 1100
EVNTSSTISC DSPLEPQDEP EPEPQLELQV EPEPELEQLP DSGCPAPRAE
AEDSFL
Computationally mapped potential isoform sequencesi
There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket| E5RII0 | E5RII0_HUMAN | Platelet-derived growth factor rece... | PDGFRB | 174 | Annotation score: | ||
| E5RJ14 | E5RJ14_HUMAN | Platelet-derived growth factor rece... | PDGFRB | 146 | Annotation score: | ||
| E5RH16 | E5RH16_HUMAN | Platelet-derived growth factor rece... | PDGFRB | 239 | Annotation score: |
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Sequence conflicti | 241 | E → D in AAA36427 (PubMed:2850496).Curated | 1 |
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Natural variantiVAR_034377 | 29 | I → F1 PublicationCorresponds to variant dbSNP:rs17110944EnsemblClinVar. | 1 | |
| Natural variantiVAR_035125 | 180 | S → F1 PublicationCorresponds to variant dbSNP:rs17853027Ensembl. | 1 | |
| Natural variantiVAR_042027 | 282 | E → K1 PublicationCorresponds to variant dbSNP:rs34586048Ensembl. | 1 | |
| Natural variantiVAR_049717 | 345 | P → S. Corresponds to variant dbSNP:rs2229558EnsemblClinVar. | 1 | |
| Natural variantiVAR_042028 | 485 | E → K1 PublicationCorresponds to variant dbSNP:rs41287110EnsemblClinVar. | 1 | |
| Natural variantiVAR_069925 | 561 | R → C in IMF1. 1 PublicationCorresponds to variant dbSNP:rs367543286EnsemblClinVar. | 1 | |
| Natural variantiVAR_075865 | 584 | P → R in KOGS. 1 PublicationCorresponds to variant dbSNP:rs863224946EnsemblClinVar. | 1 | |
| Natural variantiVAR_042029 | 589 | Y → H in a gastric adenocarcinoma sample; somatic mutation. 1 Publication | 1 | |
| Natural variantiVAR_069320 | 658 | L → P in IBGC4; no effect on protein abundance; loss of PDGF beta receptor activity. 3 PublicationsCorresponds to variant dbSNP:rs397509381EnsemblClinVar. | 1 | |
| Natural variantiVAR_069926 | 660 | P → T in IMF1. 1 PublicationCorresponds to variant dbSNP:rs144050370EnsemblClinVar. | 1 | |
| Natural variantiVAR_075866 | 665 | V → A in PENTT; gain of function in protein tyrosine kinase activity; shows ligand-independent constitutive signaling. 1 PublicationCorresponds to variant dbSNP:rs1554108211EnsemblClinVar. | 1 | |
| Natural variantiVAR_042030 | 718 | N → Y1 PublicationCorresponds to variant dbSNP:rs35322465Ensembl. | 1 | |
| Natural variantiVAR_042031 | 882 | T → I in a breast infiltrating ductal carcinoma sample; somatic mutation. 1 Publication | 1 | |
| Natural variantiVAR_069321 | 987 | R → W in IBGC4; decreased protein abundance; no effect on receptor activity; decreased PDGF signaling pathway. 3 PublicationsCorresponds to variant dbSNP:rs397509382EnsemblClinVar. | 1 | |
| Natural variantiVAR_075395 | 1071 | E → V in IBGC4; no effect on protein abundance; no effect on receptor activity; decreased PDGF signaling pathway. 2 Publications | 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Alternative sequenceiVSP_056008 | 311 – 336 | VESGY…RSRTL → RAATCGSWERWAHYNLLSCI GAGHCR in isoform 2. 1 PublicationAdd BLAST | 26 | |
| Alternative sequenceiVSP_056009 | 337 – 1106 | Missing in isoform 2. 1 PublicationAdd BLAST | 770 |
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J03278 mRNA Translation: AAA60049.1 M21616 mRNA Translation: AAA36427.1 EU826595 mRNA Translation: ACF47631.1 AC005895 Genomic DNA No translation available. AC011382 Genomic DNA No translation available. BC032224 mRNA Translation: AAH32224.1 U33172 Genomic DNA Translation: AAC51675.1 |
| CCDSi | CCDS4303.1 [P09619-1] |
| PIRi | A28206, PFHUGB |
| RefSeqi | NP_002600.1, NM_002609.3 [P09619-1] XP_011535960.1, XM_011537658.1 XP_011535961.1, XM_011537659.1 |
Genome annotation databases
| Ensembli | ENST00000261799; ENSP00000261799; ENSG00000113721 [P09619-1] |
| GeneIDi | 5159 |
| KEGGi | hsa:5159 |
| UCSCi | uc003lro.4, human [P09619-1] |
Keywords - Coding sequence diversityi
Alternative splicing, Chromosomal rearrangement, PolymorphismSimilar proteinsi
Cross-referencesi
Web resourcesi
| Atlas of Genetics and Cytogenetics in Oncology and Haematology |
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J03278 mRNA Translation: AAA60049.1 M21616 mRNA Translation: AAA36427.1 EU826595 mRNA Translation: ACF47631.1 AC005895 Genomic DNA No translation available. AC011382 Genomic DNA No translation available. BC032224 mRNA Translation: AAH32224.1 U33172 Genomic DNA Translation: AAC51675.1 |
| CCDSi | CCDS4303.1 [P09619-1] |
| PIRi | A28206, PFHUGB |
| RefSeqi | NP_002600.1, NM_002609.3 [P09619-1] XP_011535960.1, XM_011537658.1 XP_011535961.1, XM_011537659.1 |
3D structure databases
| Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1GQ5 | X-ray | 2.20 | A | 1102-1106 | [»] | |
| 1H9O | X-ray | 1.79 | B | 751-755 | [»] | |
| 1LWP | model | - | A | 600-962 | [»] | |
| 1SHA | X-ray | 1.50 | B | 751-755 | [»] | |
| 2IUI | X-ray | 2.40 | C/D | 748-758 | [»] | |
| 2L6W | NMR | - | A/B | 526-563 | [»] | |
| 2PLD | NMR | - | B | 1018-1029 | [»] | |
| 2PLE | NMR | - | B | 1018-1029 | [»] | |
| 3MJG | X-ray | 2.30 | X/Y | 33-314 | [»] | |
| BMRBi | P09619 | |||||
| SMRi | P09619 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Protein-protein interaction databases
| BioGRIDi | 111185, 99 interactors |
| ComplexPortali | CPX-2882, PDGF receptor beta - PDGF-BB complex CPX-2883, PDGF receptor alpha-beta - PDGF-BB complex CPX-2886, PDGF receptor beta - PDGF-AB complex CPX-2888, PDGF receptor alpha-beta - PDGF-CC complex CPX-2889, PDGF receptor beta - PDGF-DD complex CPX-2890, PDGF receptor alpha-beta - PDGF-DD complex CPX-2891, PDGF receptor beta - PDGF-CC complex CPX-2892, PDGF receptor alpha-beta - PDGF-AB complex |
| CORUMi | P09619 |
| DIPi | DIP-558N |
| IntActi | P09619, 200 interactors |
| MINTi | P09619 |
| STRINGi | 9606.ENSP00000261799 |
Chemistry databases
| BindingDBi | P09619 |
| ChEMBLi | CHEMBL1913 |
| DrugBanki | DB00102, Becaplermin DB01254, Dasatinib DB12147, Erdafitinib DB10770, Foreskin fibroblast (neonatal) DB12010, Fostamatinib DB00619, Imatinib DB06595, Midostaurin DB09079, Nintedanib DB06589, Pazopanib DB12978, Pexidartinib DB09221, Polaprezinc DB08896, Regorafenib DB00398, Sorafenib DB01268, Sunitinib DB09283, Trapidil DB05146, XL820 DB05014, XL999 |
| DrugCentrali | P09619 |
| GuidetoPHARMACOLOGYi | 1804 |
PTM databases
| GlyConnecti | 1967, 4 N-Linked glycans (3 sites) |
| GlyGeni | P09619, 11 sites |
| iPTMneti | P09619 |
| PhosphoSitePlusi | P09619 |
Polymorphism and mutation databases
| BioMutai | PDGFRB |
| DMDMi | 129890 |
Proteomic databases
| CPTACi | CPTAC-1630 |
| EPDi | P09619 |
| jPOSTi | P09619 |
| MassIVEi | P09619 |
| MaxQBi | P09619 |
| PaxDbi | P09619 |
| PeptideAtlasi | P09619 |
| PRIDEi | P09619 |
| ProteomicsDBi | 52253 [P09619-1] |
Protocols and materials databases
| ABCDi | P09619, 1 sequenced antibody |
| Antibodypediai | 3424, 2051 antibodies |
| DNASUi | 5159 |
Genome annotation databases
| Ensembli | ENST00000261799; ENSP00000261799; ENSG00000113721 [P09619-1] |
| GeneIDi | 5159 |
| KEGGi | hsa:5159 |
| UCSCi | uc003lro.4, human [P09619-1] |
Organism-specific databases
| CTDi | 5159 |
| DisGeNETi | 5159 |
| EuPathDBi | HostDB:ENSG00000113721.13 |
| GeneCardsi | PDGFRB |
| GeneReviewsi | PDGFRB |
| HGNCi | HGNC:8804, PDGFRB |
| HPAi | ENSG00000113721, Low tissue specificity |
| MalaCardsi | PDGFRB |
| MIMi | 131440, phenotype 173410, gene 228550, phenotype 601626, phenotype 601812, phenotype 607785, phenotype 615007, phenotype 616592, phenotype |
| neXtProti | NX_P09619 |
| OpenTargetsi | ENSG00000113721 |
| Orphaneti | 363665, Acroosteolysis-keloid-like lesions-premature aging syndrome 1980, Bilateral striopallidodentate calcinosis 98823, Chronic myelomonocytic leukemia 86830, Chronic myeloproliferative disease, unclassifiable 2591, Infantile myofibromatosis 168950, Myeloid/lymphoid neoplasm associated with PDGFRB rearrangement 314950, Primary hypereosinophilic syndrome 477831, Skeletal overgrowth-craniofacial dysmorphism-hyperelastic skin-white matter lesions syndrome |
| PharmGKBi | PA33148 |
| GenAtlasi | Search... |
Phylogenomic databases
| eggNOGi | KOG0200, Eukaryota |
| GeneTreei | ENSGT00940000157138 |
| HOGENOMi | CLU_000288_49_0_1 |
| InParanoidi | P09619 |
| KOi | K05089 |
| OMAi | TYVCNVS |
| OrthoDBi | 269253at2759 |
| PhylomeDBi | P09619 |
| TreeFami | TF325768 |
Enzyme and pathway databases
| BRENDAi | 2.7.10.1, 2681 |
| PathwayCommonsi | P09619 |
| Reactomei | R-HSA-1257604, PIP3 activates AKT signaling R-HSA-186763, Downstream signal transduction R-HSA-186797, Signaling by PDGF R-HSA-2219530, Constitutive Signaling by Aberrant PI3K in Cancer R-HSA-5673001, RAF/MAP kinase cascade R-HSA-6811558, PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling |
| SignaLinki | P09619 |
| SIGNORi | P09619 |
Miscellaneous databases
| BioGRID-ORCSi | 5159, 11 hits in 904 CRISPR screens |
| ChiTaRSi | PDGFRB, human |
| EvolutionaryTracei | P09619 |
| GeneWikii | PDGFRB |
| GenomeRNAii | 5159 |
| Pharosi | P09619, Tclin |
| PROi | PR:P09619 |
| RNActi | P09619, protein |
| SOURCEi | Search... |
Gene expression databases
| Bgeei | ENSG00000113721, Expressed in stromal cell of endometrium and 224 other tissues |
| ExpressionAtlasi | P09619, baseline and differential |
| Genevisiblei | P09619, HS |
Family and domain databases
| Gene3Di | 2.60.40.10, 5 hits |
| InterProi | View protein in InterPro IPR007110, Ig-like_dom IPR036179, Ig-like_dom_sf IPR013783, Ig-like_fold IPR013098, Ig_I-set IPR003599, Ig_sub IPR003598, Ig_sub2 IPR013151, Immunoglobulin IPR011009, Kinase-like_dom_sf 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 IPR001824, Tyr_kinase_rcpt_3_CS |
| Pfami | View protein in Pfam PF07679, I-set, 1 hit PF00047, ig, 1 hit PF07714, PK_Tyr_Ser-Thr, 1 hit |
| PIRSFi | PIRSF500948, Beta-PDGF_receptor, 1 hit |
| SMARTi | View protein in SMART SM00409, IG, 3 hits SM00408, IGc2, 3 hits SM00219, TyrKc, 1 hit |
| SUPFAMi | SSF48726, SSF48726, 3 hits SSF56112, SSF56112, 1 hit |
| PROSITEi | View protein in PROSITE PS50835, 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 |
| ProtoNeti | Search... |
| MobiDBi | Search... |
Entry informationi
| Entry namei | PGFRB_HUMAN | |
| Accessioni | P09619Primary (citable) accession number: P09619 Secondary accession number(s): B5A957, Q8N5L4 | |
| Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1989 |
| Last sequence update: | July 1, 1989 | |
| Last modified: | October 7, 2020 | |
| This is version 244 of the entry and version 1 of the sequence. See complete history. | ||
| Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any 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. | |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Human and mouse protein kinases
Human and mouse protein kinases: classification and index - Human cell differentiation molecules
CD nomenclature of surface proteins of human leucocytes and list of entries - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Human chromosome 5
Human chromosome 5: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
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