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UniProtKB - P09619 (PGFRB_HUMAN)

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Protein

Platelet-derived growth factor receptor beta

Gene

PDGFRB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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 + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation3 Publications

Enzyme 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 keyPosition(s)DescriptionActionsGraphical viewLength
Sitei527 – 528Breakpoint for insertion to form PDE4DIP-PDGFRB fusion protein2
Binding sitei634ATPCurated1
Active sitei826Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi606 – 614ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • enzyme binding Source: BHF-UCL
  • phosphatidylinositol 3-kinase binding Source: Ensembl
  • phosphatidylinositol-4,5-bisphosphate 3-kinase activity Source: Reactome
  • platelet activating factor receptor activity Source: ProtInc
  • platelet-derived growth factor-activated receptor activity Source: ProtInc
  • 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
  • Ras guanyl-nucleotide exchange factor activity Source: Reactome
  • signaling receptor binding Source: UniProtKB
  • vascular endothelial growth factor binding Source: BHF-UCL
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionDevelopmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase
Biological processChemotaxis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1 2681
ReactomeiR-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
SignaLinkiP09619
SIGNORiP09619

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

EuPathDBiHostDB:ENSG00000113721.13
HGNCiHGNC:8804 PDGFRB
MIMi173410 gene
neXtProtiNX_P09619

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini33 – 532ExtracellularSequence analysisAdd BLAST500
Transmembranei533 – 553HelicalSequence analysisAdd BLAST21
Topological domaini554 – 1106CytoplasmicSequence analysisAdd BLAST553

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Lysosome, Membrane

Pathology & 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.
See also OMIM:131440
Leukemia, 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.
See also OMIM:601626
Leukemia, 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.
See also OMIM:607785
Basal 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.
See also OMIM:615007
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_069320658L → P in IBGC4; no effect on protein abundance; loss of PDGF beta receptor activity. 3 PublicationsCorresponds to variant dbSNP:rs397509381EnsemblClinVar.1
Natural variantiVAR_069321987R → W in IBGC4; decreased protein abundance; no effect on receptor activity; decreased PDGF signaling pathway. 3 PublicationsCorresponds to variant dbSNP:rs397509382EnsemblClinVar.1
Natural variantiVAR_0753951071E → V in IBGC4; no effect on protein abundance; no effect on receptor activity; decreased PDGF signaling pathway. 2 Publications1
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.
See also OMIM:228550
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_069925561R → C in IMF1. 1 PublicationCorresponds to variant dbSNP:rs367543286EnsemblClinVar.1
Natural variantiVAR_069926660P → 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.
See also OMIM:616592
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_075865584P → 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.
See also OMIM:601812
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_075866665V → A in PENTT; gain of function in protein tyrosine kinase activity; shows ligand-independent constitutive signaling. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi579Y → F: Loss of kinase activity; when associated with F-581. Strongly reduces interaction with SRC family kinases. No effect on interaction with GRB10. 2 Publications1
Mutagenesisi581Y → F: Loss of kinase activity; when associated with F-579. No effect on interaction with GRB10. 2 Publications1
Mutagenesisi634K → A or R: Loss of kinase activity. Abolishes interaction with RASA1. No effect on phosphatidylinositol 3-kinase activity. 3 Publications1
Mutagenesisi716Y → F: No effect neither on interaction with GRB10 and RASA1 nor on phosphatidylinositol 3-kinase activity. 2 Publications1
Mutagenesisi740Y → 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 Publications1
Mutagenesisi751Y → 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 Publications1
Mutagenesisi763Y → F: No effect on interaction with RASA1 and on phosphatidylinositol 3-kinase activity. 1 Publication1
Mutagenesisi771Y → F: Loss of interaction with GRB10. Abolishes interaction with RASA1. No effect on phosphatidylinositol 3-kinase activity. 3 Publications1
Mutagenesisi775Y → F: No effect on interaction with RASA1 and on phosphatidylinositol 3-kinase activity. 1 Publication1
Mutagenesisi778Y → F: Strongly reduces expression levels. 1 Publication1
Mutagenesisi857Y → F: Reduces kinase activity. No effect on interaction with GRB10. Abolishes interaction with RASA1. No effect on phosphatidylinositol 3-kinase activity. 4 Publications1
Mutagenesisi1009Y → F: No effect on interaction with GRB10. Abolishes interaction with PLCG1; when associated with F-1021. 3 Publications1
Mutagenesisi1021Y → F: Strongly reduces up-regulation of cell proliferation. Abolishes interaction with PLCG1; when associated with F-1009. No effect on interaction with GRB10. 4 Publications1

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei527 – 528Breakpoint for translocation to form TRIP11-PDGFRB2
Sitei558 – 559Breakpoint for translocation to form the CEP85L-PDGFRB fusion protein2

Keywords - Diseasei

Disease mutation, Proto-oncogene

Organism-specific databases

DisGeNETi5159
GeneReviewsiPDGFRB
MalaCardsiPDGFRB
MIMi131440 phenotype
228550 phenotype
601626 phenotype
601812 phenotype
607785 phenotype
615007 phenotype
616592 phenotype
OpenTargetsiENSG00000113721
Orphaneti1980 Bilateral striopallidodentate calcinosis
98823 Chronic myelomonocytic leukemia
2591 Infantile myofibromatosis
168950 Myeloid neoplasm associated with PDGFRB rearrangement
314950 Primary hypereosinophilic syndrome
86830 Unclassified chronic myeloproliferative disease
PharmGKBiPA33148

Chemistry databases

ChEMBLiCHEMBL1913
DrugBankiDB00102 Becaplermin
DB01254 Dasatinib
DB00619 Imatinib
DB06589 Pazopanib
DB08896 Regorafenib
DB00398 Sorafenib
DB01268 Sunitinib
DB05146 XL820
DB05014 XL999
GuidetoPHARMACOLOGYi1804

Polymorphism and mutation databases

BioMutaiPDGFRB
DMDMi129890

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 321 PublicationAdd BLAST32
ChainiPRO_000001675733 – 1106Platelet-derived growth factor receptor betaAdd BLAST1074

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi45N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi54 ↔ 100PROSITE-ProRule annotation1 Publication
Glycosylationi89N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi103N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi149 ↔ 190PROSITE-ProRule annotation1 Publication
Glycosylationi215N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi230N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi235 ↔ 291PROSITE-ProRule annotation1 Publication
Glycosylationi292N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi307N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi354N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi371N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi436 ↔ 508PROSITE-ProRule annotation
Glycosylationi468N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi479N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei562Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei579Phosphotyrosine; by autocatalysis3 Publications1
Modified residuei581Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei686Phosphotyrosine; by ABL1 and ABL2By similarity1
Modified residuei716Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei740Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei751Phosphotyrosine; by autocatalysis5 Publications1
Modified residuei763Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei771Phosphotyrosine; by autocatalysis4 Publications1
Modified residuei775Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei778Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei857Phosphotyrosine; by autocatalysis5 Publications1
Modified residuei934Phosphotyrosine; by ABL1 and ABL2By similarity1
Modified residuei970Phosphotyrosine; by ABL1 and ABL2By similarity1
Modified residuei1009Phosphotyrosine; by autocatalysis3 Publications1
Modified residuei1021Phosphotyrosine; by autocatalysis4 Publications1

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 conjugation

Proteomic databases

EPDiP09619
MaxQBiP09619
PaxDbiP09619
PeptideAtlasiP09619
PRIDEiP09619
ProteomicsDBi52253

PTM databases

iPTMnetiP09619
PhosphoSitePlusiP09619

Expressioni

Gene expression databases

BgeeiENSG00000113721
CleanExiHS_PDGFRB
ExpressionAtlasiP09619 baseline and differential
GenevisibleiP09619 HS

Organism-specific databases

HPAiCAB003842
CAB018144
HPA028499

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 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • enzyme binding Source: BHF-UCL
  • 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
  • Ras guanyl-nucleotide exchange factor activity Source: Reactome
  • signaling receptor binding Source: UniProtKB
  • vascular endothelial growth factor binding Source: BHF-UCL
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi111185, 75 interactors
ComplexPortaliCPX-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
CORUMiP09619
DIPiDIP-558N
IntActiP09619, 87 interactors
MINTiP09619
STRINGi9606.ENSP00000261799

Chemistry databases

BindingDBiP09619

Structurei

Secondary structure

11106
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi40 – 43Combined sources4
Beta strandi50 – 58Combined sources9
Beta strandi61 – 64Combined sources4
Beta strandi70 – 75Combined sources6
Beta strandi81 – 87Combined sources7
Helixi92 – 94Combined sources3
Beta strandi96 – 101Combined sources6
Beta strandi114 – 119Combined sources6
Helixi132 – 135Combined sources4
Beta strandi136 – 141Combined sources6
Beta strandi145 – 147Combined sources3
Beta strandi158 – 164Combined sources7
Turni175 – 177Combined sources3
Beta strandi178 – 181Combined sources4
Beta strandi185 – 194Combined sources10
Beta strandi197 – 200Combined sources4
Beta strandi204 – 208Combined sources5
Beta strandi217 – 221Combined sources5
Beta strandi223 – 226Combined sources4
Beta strandi231 – 239Combined sources9
Beta strandi241 – 248Combined sources8
Beta strandi252 – 255Combined sources4
Beta strandi261 – 265Combined sources5
Turni267 – 270Combined sources4
Beta strandi271 – 280Combined sources10
Beta strandi287 – 295Combined sources9
Turni296 – 299Combined sources4
Beta strandi300 – 311Combined sources12
Helixi530 – 556Combined sources27

3D structure databases

ProteinModelPortaliP09619
SMRiP09619
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09619

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini33 – 120Ig-like C2-type 1Add BLAST88
Domaini129 – 210Ig-like C2-type 2Add BLAST82
Domaini214 – 309Ig-like C2-type 3Add BLAST96
Domaini331 – 403Ig-like C2-type 4Add BLAST73
Domaini416 – 524Ig-like C2-type 5Add BLAST109
Domaini600 – 962Protein kinasePROSITE-ProRule annotationAdd BLAST363

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 helix

Phylogenomic databases

eggNOGiKOG0200 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00760000118923
HOGENOMiHOG000112009
HOVERGENiHBG004335
InParanoidiP09619
KOiK05089
OMAiAPYDNYV
OrthoDBiEOG091G01TL
PhylomeDBiP09619
TreeFamiTF325768

Family and domain databases

Gene3Di2.60.40.10, 5 hits
InterProiView 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
PfamiView protein in Pfam
PF07679 I-set, 1 hit
PF00047 ig, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PIRSFiPIRSF500948 Beta-PDGF_receptor, 1 hit
SMARTiView protein in SMART
SM00409 IG, 3 hits
SM00408 IGc2, 3 hits
SM00219 TyrKc, 1 hit
SUPFAMiSSF48726 SSF48726, 3 hits
SSF56112 SSF56112, 2 hits
PROSITEiView 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 basket

Isoform 1 (identifier: P09619-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        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
Length:1,106
Mass (Da):123,968
Last modified:July 1, 1989 - v1
Checksum:i038C15E531D6E89D
GO
Isoform 2 (identifier: P09619-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     311-336: VESGYVRLLGEVGTLQFAELHRSRTL → RAATCGSWERWAHYNLLSCIGAGHCR
     337-1106: Missing.

Show »
Length:336
Mass (Da):37,412
Checksum:i5BEDAFC416865068
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti241E → D in AAA36427 (PubMed:2850496).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03437729I → F1 PublicationCorresponds to variant dbSNP:rs17110944EnsemblClinVar.1
Natural variantiVAR_035125180S → F1 PublicationCorresponds to variant dbSNP:rs17853027Ensembl.1
Natural variantiVAR_042027282E → K1 PublicationCorresponds to variant dbSNP:rs34586048Ensembl.1
Natural variantiVAR_049717345P → S. Corresponds to variant dbSNP:rs2229558EnsemblClinVar.1
Natural variantiVAR_042028485E → K1 PublicationCorresponds to variant dbSNP:rs41287110EnsemblClinVar.1
Natural variantiVAR_069925561R → C in IMF1. 1 PublicationCorresponds to variant dbSNP:rs367543286EnsemblClinVar.1
Natural variantiVAR_075865584P → R in KOGS. 1 PublicationCorresponds to variant dbSNP:rs863224946EnsemblClinVar.1
Natural variantiVAR_042029589Y → H in a gastric adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_069320658L → P in IBGC4; no effect on protein abundance; loss of PDGF beta receptor activity. 3 PublicationsCorresponds to variant dbSNP:rs397509381EnsemblClinVar.1
Natural variantiVAR_069926660P → T in IMF1. 1 PublicationCorresponds to variant dbSNP:rs144050370EnsemblClinVar.1
Natural variantiVAR_075866665V → A in PENTT; gain of function in protein tyrosine kinase activity; shows ligand-independent constitutive signaling. 1 Publication1
Natural variantiVAR_042030718N → Y1 PublicationCorresponds to variant dbSNP:rs35322465Ensembl.1
Natural variantiVAR_042031882T → I in a breast infiltrating ductal carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_069321987R → W in IBGC4; decreased protein abundance; no effect on receptor activity; decreased PDGF signaling pathway. 3 PublicationsCorresponds to variant dbSNP:rs397509382EnsemblClinVar.1
Natural variantiVAR_0753951071E → V in IBGC4; no effect on protein abundance; no effect on receptor activity; decreased PDGF signaling pathway. 2 Publications1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_056008311 – 336VESGY…RSRTL → RAATCGSWERWAHYNLLSCI GAGHCR in isoform 2. 1 PublicationAdd BLAST26
Alternative sequenceiVSP_056009337 – 1106Missing in isoform 2. 1 PublicationAdd BLAST770

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
CCDSiCCDS4303.1 [P09619-1]
PIRiA28206 PFHUGB
RefSeqiNP_002600.1, NM_002609.3 [P09619-1]
XP_011535960.1, XM_011537658.1 [P09619-1]
XP_011535961.1, XM_011537659.1 [P09619-1]
UniGeneiHs.509067

Genome annotation databases

EnsembliENST00000261799; ENSP00000261799; ENSG00000113721 [P09619-1]
GeneIDi5159
KEGGihsa:5159
UCSCiuc003lro.4 human [P09619-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiPGFRB_HUMAN
AccessioniPrimary (citable) accession number: P09619
Secondary accession number(s): B5A957, Q8N5L4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: July 18, 2018
This is version 226 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  8. SIMILARITY comments
    Index of protein domains and families

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