PDGFRB

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
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L-tyrosyl-[protein]
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ADP
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H⁺
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O-phospho-L-tyrosyl-[protein]
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PROSITE-ProRule annotation
Manual assertion according to rulesⁱ
- PROSITE-ProRule:PRU10028
3 Publications
Manual assertion based on experiment inⁱ
- Ref.14
  "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.
- Ref.19
  "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.
- Ref.40
  "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.
EC:
2.7.10.1
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
PROSITE-ProRule annotation
Manual assertion according to rulesⁱ
- PROSITE-ProRule:PRU10028
3 Publications
Manual assertion based on experiment inⁱ
- Ref.14
  "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.
- Ref.19
  "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.
- Ref.40
  "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.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
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ATP
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L-tyrosyl-[protein]
L-tyrosine residue
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ADP
+
H⁺
+
O-phospho-L-tyrosyl-[protein]
L-tyrosine-phosphate residue
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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	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

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

View the complete GO annotation on QuickGO ...

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
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	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 5

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000113721.13
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:8804 PDGFRB
MIMⁱ	173410 gene
neXtProtⁱ	NX_P09619

Topology

Feature key	Position(s)	DescriptionActions	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, 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.

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.

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.

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.

Feature key	Position(s)	DescriptionActions	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.

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.

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.

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 Publication		1

Mutagenesis

Feature key	Position(s)	DescriptionActions	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-oncogene

Organism-specific databases

DisGeNET More...DisGeNETⁱ	5159
GeneReviewsⁱ	PDGFRB
MalaCards human disease database More...MalaCardsⁱ	PDGFRB
MIMⁱ	131440 phenotype 228550 phenotype 601626 phenotype 601812 phenotype 607785 phenotype 615007 phenotype 616592 phenotype
Open Targets More...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

Chemistry databases

ChEMBLⁱ	CHEMBL1913
Drug and drug target database More...DrugBankⁱ	DB00102 Becaplermin DB01254 Dasatinib DB00619 Imatinib DB06589 Pazopanib DB08896 Regorafenib DB00398 Sorafenib DB01268 Sunitinib DB05146 XL820 DB05014 XL999
IUPHAR/BPS Guide to PHARMACOLOGY More...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	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 conjugation

Proteomic databases

EPDⁱ	P09619
jPOSTⁱ	P09619
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P09619
PaxDbⁱ	P09619
PeptideAtlas More...PeptideAtlasⁱ	P09619
PRIDEⁱ	P09619
ProteomicsDBⁱ	52253

PTM databases

GlyConnectⁱ	1967
iPTMnetⁱ	P09619
PhosphoSitePlusⁱ	P09619

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000113721 Expressed in 215 organ(s), highest expression level in ectocervix
ExpressionAtlasⁱ	P09619 baseline and differential
Genevisibleⁱ	P09619 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB003842 CAB018144 HPA028499

HPAⁱ

CAB003842
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

With	Entry	#Exp.	IntAct	Notes
E5	P0CK45	2	EBI-641237,EBI-7015490	From Bovine papillomavirus type 1.
FYN	P06241	3	EBI-641237,EBI-515315
GRB7	Q14451	4	EBI-641237,EBI-970191
IL1R1	P14778	2	EBI-641237,EBI-525905
KDR	P35968	2	EBI-641237,EBI-1005487
Kdr	P35918	4	EBI-641237,EBI-1555005	From Mus musculus.
KLHL12	Q53G59	5	EBI-641237,EBI-740929
LRP6	O75581	3	EBI-641237,EBI-910915
PDGFB	P01127	16	EBI-641237,EBI-1554925
PIK3R1	P23727	6	EBI-641237,EBI-520244	From Bos taurus.
PIK3R1	P27986	19	EBI-641237,EBI-79464
PLCG1	P08487	3	EBI-641237,EBI-8013886	From Bos taurus.
PLCG1	P19174	6	EBI-641237,EBI-79387
PTEN	P60484	3	EBI-641237,EBI-696162
PTPN1	P18031	3	EBI-641237,EBI-968788
PTPN11	Q06124	8	EBI-641237,EBI-297779
PTPN12	Q05209	3	EBI-641237,EBI-2266035
PTPRJ	Q12913	4	EBI-641237,EBI-2264500
RAF1	P04049	2	EBI-641237,EBI-365996
RASA1	P20936	3	EBI-641237,EBI-1026476
SLA	Q13239	4	EBI-641237,EBI-726214
SLC9A3R1	O14745	5	EBI-641237,EBI-349787
TRIP6	Q15654	3	EBI-641237,EBI-742327
V-SRC	P25020	4	EBI-641237,EBI-8636140	From Rous sarcoma virus (strain H-19).

GO - Molecular functionⁱ

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	111185, 78 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
Database of interacting proteins More...DIPⁱ	DIP-558N
IntActⁱ	P09619, 86 interactors
Molecular INTeraction database More...MINTⁱ	P09619
STRINGⁱ	9606.ENSP00000261799

Chemistry databases

BindingDBⁱ

P09619

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	40 – 43	Combined sources	4
Beta strandⁱ	50 – 58	Combined sources	9
Beta strandⁱ	61 – 64	Combined sources	4
Beta strandⁱ	70 – 75	Combined sources	6
Beta strandⁱ	81 – 87	Combined sources	7
Helixⁱ	92 – 94	Combined sources	3
Beta strandⁱ	96 – 101	Combined sources	6
Beta strandⁱ	114 – 119	Combined sources	6
Helixⁱ	132 – 135	Combined sources	4
Beta strandⁱ	136 – 141	Combined sources	6
Beta strandⁱ	145 – 147	Combined sources	3
Beta strandⁱ	158 – 164	Combined sources	7
Turnⁱ	175 – 177	Combined sources	3
Beta strandⁱ	178 – 181	Combined sources	4
Beta strandⁱ	185 – 194	Combined sources	10
Beta strandⁱ	197 – 200	Combined sources	4
Beta strandⁱ	204 – 208	Combined sources	5
Beta strandⁱ	217 – 221	Combined sources	5
Beta strandⁱ	223 – 226	Combined sources	4
Beta strandⁱ	231 – 239	Combined sources	9
Beta strandⁱ	241 – 248	Combined sources	8
Beta strandⁱ	252 – 255	Combined sources	4
Beta strandⁱ	261 – 265	Combined sources	5
Turnⁱ	267 – 270	Combined sources	4
Beta strandⁱ	271 – 280	Combined sources	10
Beta strandⁱ	287 – 295	Combined sources	9
Turnⁱ	296 – 299	Combined sources	4
Beta strandⁱ	300 – 311	Combined sources	12
Helixⁱ	530 – 556	Combined sources	27

Show more details

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...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	[»]
ProteinModelPortalⁱ	P09619
SMRⁱ	P09619
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P09619

EvolutionaryTraceⁱ

P09619

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	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 helix

Phylogenomic databases

eggNOGⁱ	KOG0200 Eukaryota COG0515 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000157138
HOGENOMⁱ	HOG000112009
HOVERGENⁱ	HBG004335
InParanoidⁱ	P09619
KEGG Orthology (KO) More...KOⁱ	K05089
OMAⁱ	QPHLTWS
Database of Orthologous Groups More...OrthoDBⁱ	606683at2759
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
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF07679 I-set, 1 hit PF00047 ig, 1 hit PF07714 Pkinase_Tyr, 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. Align Add to basket

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show all Align All

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

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

« 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 
QDEKAINITV RAATCGSWER WAHYNLLSCI GAGHCR

Show »

Length:336

Mass (Da):37,412

Checksum:ⁱ5BEDAFC416865068

GO

Computationally mapped potential isoform sequencesⁱ

There are 3 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

E5RII0	E5RII0_HUMAN	Platelet-derived growth factor rece... Platelet-derived growth factor receptor beta	PDGFRB	174	Annotation score:
E5RJ14	E5RJ14_HUMAN	Platelet-derived growth factor rece... Platelet-derived growth factor receptor beta	PDGFRB	146	Annotation score:
E5RH16	E5RH16_HUMAN	Platelet-derived growth factor rece... Platelet-derived growth factor receptor beta	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	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 Publication	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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS4303.1 [P09619-1]
PIRⁱ	A28206 PFHUGB
NCBI Reference Sequences More...RefSeqⁱ	NP_002600.1, NM_002609.3 [P09619-1] XP_011535960.1, XM_011537658.1 XP_011535961.1, XM_011537659.1
UniGeneⁱ	Hs.509067

Genome annotation databases

Ensemblⁱ	ENST00000261799; ENSP00000261799; ENSG00000113721 [P09619-1]
GeneIDⁱ	5159
KEGGⁱ	hsa:5159
UCSC genome browser More...UCSCⁱ	uc003lro.4 human [P09619-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Chromosomal rearrangement, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P09619	Platelet-derived growth factor receptor beta (Fragment)		HUMAN		174	UniRef100_P09619

Protein	Similar proteins		Species	Score	Length	Source
P09619	Platelet-derived growth factor receptor beta (Fragment)		HUMAN		174	UniRef90_P09619
Platelet-derived growth factor receptor beta		AOTNA		1110
Platelet-derived growth factor receptor beta		CALJA		1108
Platelet-derived growth factor receptor beta		SAIBB		1108
Platelet-derived growth factor receptor beta		Cebus capucinus imitator		1108
+55
P09619-2	Uncharacterized protein		NOMLE		353	UniRef90_P09619-2
Uncharacterized protein		PANTR		351
Uncharacterized protein		PANPA		349
Uncharacterized protein		RHIRO		340
Uncharacterized protein		MANLE		340
+2

Protein	Similar proteins		Species	Score	Length	Source
P09619	Platelet-derived growth factor receptor beta (Fragment)		HUMAN		174	UniRef50_P09619
Platelet-derived growth factor receptor beta		AOTNA		1110
Platelet-derived growth factor receptor beta		CALJA		1108
Platelet-derived growth factor receptor beta		Cebus capucinus imitator		1108
Platelet-derived growth factor receptor beta		SAIBB		1108
+827
P09619-2	Uncharacterized protein		NOMLE		353	UniRef50_P09619-2
Uncharacterized protein		PANTR		351
Uncharacterized protein		PANPA		349
Uncharacterized protein		PAPAN		340
Uncharacterized protein		COLAP		340
+11

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
UniGeneⁱ	Hs.509067

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	[»]
ProteinModelPortalⁱ	P09619
SMRⁱ	P09619
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	111185, 78 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, 86 interactors
MINTⁱ	P09619
STRINGⁱ	9606.ENSP00000261799

Chemistry databases

BindingDBⁱ	P09619
ChEMBLⁱ	CHEMBL1913
DrugBankⁱ	DB00102 Becaplermin DB01254 Dasatinib DB00619 Imatinib DB06589 Pazopanib DB08896 Regorafenib DB00398 Sorafenib DB01268 Sunitinib DB05146 XL820 DB05014 XL999
GuidetoPHARMACOLOGYⁱ	1804

PTM databases

GlyConnectⁱ	1967
iPTMnetⁱ	P09619
PhosphoSitePlusⁱ	P09619

Polymorphism and mutation databases

BioMutaⁱ	PDGFRB
DMDMⁱ	129890

Proteomic databases

EPDⁱ	P09619
jPOSTⁱ	P09619
MaxQBⁱ	P09619
PaxDbⁱ	P09619
PeptideAtlasⁱ	P09619
PRIDEⁱ	P09619
ProteomicsDBⁱ	52253

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	5159
Structural Biology Knowledgebase	Search...

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	CAB003842 CAB018144 HPA028499
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
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0200 Eukaryota COG0515 LUCA
GeneTreeⁱ	ENSGT00940000157138
HOGENOMⁱ	HOG000112009
HOVERGENⁱ	HBG004335
InParanoidⁱ	P09619
KOⁱ	K05089
OMAⁱ	QPHLTWS
OrthoDBⁱ	606683at2759
PhylomeDBⁱ	P09619
TreeFamⁱ	TF325768

Enzyme and pathway databases

BRENDAⁱ	2.7.10.1 2681
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

ChiTaRSⁱ	PDGFRB human
EvolutionaryTraceⁱ	P09619
GeneWikiⁱ	PDGFRB
GenomeRNAiⁱ	5159
Protein Ontology More...PROⁱ	PR:P09619
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000113721 Expressed in 215 organ(s), highest expression level in ectocervix
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 Pkinase_Tyr, 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...

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:	February 13, 2019
	This is version 232 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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
SIMILARITY comments
Index of protein domains and families
Human chromosome 5
Human chromosome 5: entries, gene names and cross-references to MIM
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
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations

Annotation systems

Supporting data

UniProtKB - P09619 (PGFRB_HUMAN)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Platelet-derived growth factor receptor beta

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Lysosome

Plasma membrane

Other locations

Golgi apparatus

Lysosome

Nucleus

Plasma Membrane

Other locations

Topology

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Sites

Keywords - Diseasei

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ