PDGFRB
entrez
5159
canonical
uniprot
P09619
canonical
ensembl
ENSG00000113721
resolver
ensp
ENSP00000261799
resolver
genesymbol
PDGFRB
resolver
genesymbol_syn
PDGFR
resolver
genesymbol_syn
PDGFR1
resolver
hgnc
HGNC:8804
resolver
uniprot
B5A957
resolver
uniprot
Q59F04
resolver
uniprot
Q8N5L4
resolver
uniprot_entry
PGFRB_HUMAN
resolver
uniprot_entry
Q59F04_HUMAN
resolver
uniprot_sec
B5A957
resolver
uniprot_sec
Q8N5L4
resolver
activity_regulation
ACTIVITY REGULATION: Present in an inactive conformation in the absence of bound ligand. Binding of PDGFB and/or PDGFD leads to dimerization and activation by autophosphorylation on tyrosine residues. Inhibited by imatinib. {ECO:0000269|PubMed:15492236}.
uniprot
proteins
amino_acid_sequence
MRLPGAMPALALKGELLLLSLLLLLEPQISQGLVVTPPGPELVLNVSSTFVLTCSGSAPVVWERMSQEPPQEMAKAQDGTFSSVLTLTNLTGLDTGEYFCTHNDSRGLETDERKRLYIFVPDPTVGFLPNDAEELFIFLTEITEITIPCRVTDPQLVVTLHEKKGDVALPVPYDHQRGFSGIFEDRSYICKTTIGDREVDSDAYYVYRLQVSSINVSVNAVQTVVRQGENITLMCIVIGNEVVNFEWTYPRKESGRLVEPVTDFLLDMPYHIRSILHIPSAELEDSGTYTCNVTESVNDHQDEKAINITVVESGYVRLLGEVGTLQFAELHRSRTLQVVFEAYPPPTVLWFKDNRTLGDSSAGEIALSTRNVSETRYVSELTLVRVKVAEAGHYTMRAFHEDAEVQLSFQLQINVPVRVLELSESHPDSGEQTVRCRGRGMPQPNIIWSACRDLKRCPRELPPTLLGNSSEEESQLETNVTYWEEEQEFEVVSTLRLQHVDRPLSVRCTLRNAVGQDTQEVIVVPHSLPFKVVVISAILALVVLTIISLIILIMLWQKKPRYEIRWKVIESVSSDGHEYIYVDPMQLPYDSTWELPRDQLVLGRTLGSGAFGQVVEATAHGLSHSQATMKVAVKMLKSTARSSEKQALMSELKIMSHLGPHLNVVNLLGACTKGGPIYIITEYCRYGDLVDYLHRNKHTFLQHHSDKRRPPSAELYSNALPVGLPLPSHVSLTGESDGGYMDMSKDESVDYVPMLDMKGDVKYADIESSNYMAPYDNYVPSAPERTCRATLINESPVLSYMDLVGFSYQVANGMEFLASKNCVHRDLAARNVLICEGKLVKICDFGLARDIMRDSNYISKGSTFLPLKWMAPESIFNSLYTTLSDVWSFGILLWEIFTLGGTPYPELPMNEQFYNAIKRGYRMAQPAHASDEIYEIMQKCWEEKFEIRPPFSQLVLLLERLLGEGYKKKYQQVDEEFLRSDHPAILRSQARLPGFHGLRSPLDTSSVLYTAVQPNEGDNDYIIPLPDPKPEVADEGPLEGSPSLASSTLNEVNTSSTISCDSPLEPQDEPEPEPQLELQVEPEPELEQLPDSGCPAPRAEAEDSFL
uniprot
proteins
disease_involvement
DISEASE: Note=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).; DISEASE: Myeloproliferative disorder chronic with eosinophilia (MPE) [MIM:131440]: A hematologic disorder characterized by malignant eosinophils proliferation. Note=The gene represented in this entry may be involved in disease pathogenesis. Chromosomal aberrations involving PDGFRB have been found in many instances of chronic myeloproliferative disorder with eosinophilia. Translocation t(5;12) with ETV6 on chromosome 12 creating an PDGFRB-ETV6 fusion protein (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). {ECO:0000269|PubMed:12181402, ECO:0000269|PubMed:12907457, ECO:0000269|PubMed:15492236, ECO:0000269|PubMed:21938754}.; DISEASE: Leukemia, acute myelogenous (AML) [MIM:601626]: A subtype of acute leukemia, a cancer of the white blood cells. AML is a malignant disease of bone marrow characterized by maturational arrest of hematopoietic precursors at an early stage of development. Clonal expansion of myeloid blasts occurs in bone marrow, blood, and other tissue. Myelogenous leukemias develop from changes in cells that normally produce neutrophils, basophils, eosinophils and monocytes. Note=The gene represented in this entry may be involved in disease pathogenesis. A chromosomal aberration involving PDGFRB has been found in a patient with AML. Translocation t(5;14)(q33;q32) with TRIP11 (PubMed:9373237). {ECO:0000269|PubMed:9373237}.; DISEASE: Leukemia, juvenile myelomonocytic (JMML) [MIM:607785]: An aggressive pediatric myelodysplastic syndrome/myeloproliferative disorder characterized by malignant transformation in the hematopoietic stem cell compartment with proliferation of differentiated progeny. Patients have splenomegaly, enlarged lymph nodes, rashes, and hemorrhages. Note=The gene represented in this entry may be involved in disease pathogenesis. A chromosomal aberration involving PDGFRB has been found in a patient with JMML. Translocation t(5;17)(q33;p11.2) with SPECC1 (PubMed:15087372). {ECO:0000269|PubMed:15087372}.; DISEASE: Basal ganglia calcification, idiopathic, 4 (IBGC4) [MIM:615007]: A form of basal ganglia calcification, an autosomal dominant condition characterized by symmetric calcification in the basal ganglia and other brain regions. Affected individuals can either be asymptomatic or show a wide spectrum of neuropsychiatric symptoms, including parkinsonism, dystonia, tremor, ataxia, dementia, psychosis, seizures, and chronic headache. Serum levels of calcium, phosphate, alkaline phosphatase and parathyroid hormone are normal. The neuropathological hallmark of the disease is vascular and pericapillary calcification, mainly of calcium phosphate, in the affected brain areas. {ECO:0000269|PubMed:23255827, ECO:0000269|PubMed:24065723, ECO:0000269|PubMed:26599395}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Myofibromatosis, infantile 1 (IMF1) [MIM:228550]: A rare mesenchymal disorder characterized by the development of benign tumors in the skin, striated muscles, bones, and, more rarely, visceral organs. Subcutaneous or soft tissue nodules commonly involve the skin of the head, neck, and trunk. Skeletal and muscular lesions occur in about half of the patients. Lesions may be solitary or multicentric, and they may be present at birth or become apparent in early infancy or occasionally in adult life. Visceral lesions are associated with high morbidity and mortality. {ECO:0000269|PubMed:23731537, ECO:0000269|PubMed:23731542}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Kosaki overgrowth syndrome (KOGS) [MIM:616592]: A syndrome characterized by somatic overgrowth, distinctive facial features, hyperelastic and fragile skin, and progressive neurologic deterioration with white matter lesions on brain imaging. {ECO:0000269|PubMed:25454926}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Premature aging syndrome, Penttinen type (PENTT) [MIM:601812]: An autosomal dominant 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. {ECO:0000269|PubMed:26279204, ECO:0000269|PubMed:30573803}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Ocular pterygium-digital keloid dysplasia syndrome (OPDKD) [MIM:621091]: An autosomal dominant disorder that presents in childhood with aggressive ingrowth of vascularized connective tissue on the cornea, ultimately leading to loss of vision. Later, affected individuals develop keloids on digits after minor trauma, but are otherwise healthy. {ECO:0000269|PubMed:33450762}. Note=The disease may be caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.10.1
uniprot
proteins
function
FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA and PDGFB, and plays an essential role in the regulation of embryonic development, cell proliferation, survival, differentiation, chemotaxis and migration. Plays an essential role in blood vessel development by promoting proliferation, migration and recruitment of pericytes and smooth muscle cells to endothelial cells. Plays a role in the migration of vascular smooth muscle cells and the formation of neointima at vascular injury sites. Required for normal development of the cardiovascular system. Required for normal recruitment of pericytes (mesangial cells) in the kidney glomerulus, and for normal formation of a branched network of capillaries in kidney glomeruli. Promotes rearrangement of the actin cytoskeleton and the formation of membrane ruffles. Binding of its cognate ligands - homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFD -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PLCG1, PIK3R1, PTPN11, RASA1/GAP, CBL, SHC1 and NCK1. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca(2+) and the activation of protein kinase C. Phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leads to the activation of the AKT1 signaling pathway. Phosphorylation of SHC1, or of the C-terminus of PTPN11, creates a binding site for GRB2, resulting in the activation of HRAS, RAF1 and down-stream MAP kinases, including MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation and activation of SRC family kinases. Promotes phosphorylation of PDCD6IP/ALIX and STAM. Receptor signaling is down-regulated by protein phosphatases that dephosphorylate the receptor and its down-stream effectors, and by rapid internalization of the activated receptor. {ECO:0000269|PubMed:11297552, ECO:0000269|PubMed:11331881, ECO:0000269|PubMed:1314164, ECO:0000269|PubMed:1396585, ECO:0000269|PubMed:1653029, ECO:0000269|PubMed:1709159, ECO:0000269|PubMed:1846866, ECO:0000269|PubMed:20494825, ECO:0000269|PubMed:20529858, ECO:0000269|PubMed:21098708, ECO:0000269|PubMed:21679854, ECO:0000269|PubMed:21733313, ECO:0000269|PubMed:2554309, ECO:0000269|PubMed:26599395, ECO:0000269|PubMed:2835772, ECO:0000269|PubMed:2850496, ECO:0000269|PubMed:7685273, ECO:0000269|PubMed:7691811, ECO:0000269|PubMed:7692233, ECO:0000269|PubMed:8195171}.
uniprot
proteins
mass_dalton
123968
uniprot
proteins
mutagenesis
MUTAGEN 579; /note="Y->F: Loss of kinase activity; when associated with F-581. Strongly reduces interaction with SRC family kinases. No effect on interaction with GRB10."; /evidence="ECO:0000269|PubMed:10454568, ECO:0000269|PubMed:7685273"; MUTAGEN 581; /note="Y->F: Loss of kinase activity; when associated with F-579. No effect on interaction with GRB10."; /evidence="ECO:0000269|PubMed:10454568, ECO:0000269|PubMed:7685273"; MUTAGEN 634; /note="K->A,R: Loss of kinase activity. Abolishes interaction with RASA1. No effect on phosphatidylinositol 3-kinase activity."; /evidence="ECO:0000269|PubMed:1314164, ECO:0000269|PubMed:1846866, ECO:0000269|PubMed:20494825"; MUTAGEN 716; /note="Y->F: No effect neither on interaction with GRB10 and RASA1 nor on phosphatidylinositol 3-kinase activity."; /evidence="ECO:0000269|PubMed:10454568, ECO:0000269|PubMed:1314164"; MUTAGEN 740; /note="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."; /evidence="ECO:0000269|PubMed:10454568, ECO:0000269|PubMed:1314164, ECO:0000269|PubMed:1375321, ECO:0000269|PubMed:21679854"; MUTAGEN 751; /note="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."; /evidence="ECO:0000269|PubMed:10454568, ECO:0000269|PubMed:1314164, ECO:0000269|PubMed:1375321, ECO:0000269|PubMed:1653029, ECO:0000269|PubMed:21679854, ECO:0000269|PubMed:7692233"; MUTAGEN 763; /note="Y->F: No effect on interaction with RASA1 and on phosphatidylinositol 3-kinase activity."; /evidence="ECO:0000269|PubMed:1314164"; MUTAGEN 771; /note="Y->F: Loss of interaction with GRB10. Abolishes interaction with RASA1. No effect on phosphatidylinositol 3-kinase activity."; /evidence="ECO:0000269|PubMed:10454568, ECO:0000269|PubMed:1314164, ECO:0000269|PubMed:1375321"; MUTAGEN 775; /note="Y->F: No effect on interaction with RASA1 and on phosphatidylinositol 3-kinase activity."; /evidence="ECO:0000269|PubMed:1314164"; MUTAGEN 778; /note="Y->F: Strongly reduces expression levels."; /evidence="ECO:0000269|PubMed:1314164"; MUTAGEN 857; /note="Y->F: Reduces kinase activity. No effect on interaction with GRB10. Abolishes interaction with RASA1. No effect on phosphatidylinositol 3-kinase activity."; /evidence="ECO:0000269|PubMed:10454568, ECO:0000269|PubMed:1314164, ECO:0000269|PubMed:1653029, ECO:0000269|PubMed:20494825"; MUTAGEN 1009; /note="Y->F: No effect on interaction with GRB10. Abolishes interaction with PLCG1; when associated with F-1021."; /evidence="ECO:0000269|PubMed:10454568, ECO:0000269|PubMed:1396585, ECO:0000269|PubMed:7691811"; MUTAGEN 1021; /note="Y->F: Strongly reduces up-regulation of cell proliferation. Abolishes interaction with PLCG1; when associated with F-1009. No effect on interaction with GRB10."; /evidence="ECO:0000269|PubMed:10454568, ECO:0000269|PubMed:1396585, ECO:0000269|PubMed:17620338, ECO:0000269|PubMed:21679854
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000269|PubMed:10821867, ECO:0000269|PubMed:1314164, ECO:0000269|PubMed:1396585, ECO:0000269|PubMed:14966296, ECO:0000269|PubMed:15902258, ECO:0000269|PubMed:1709159, ECO:0000269|PubMed:2550144, ECO:0000269|PubMed:7685273}.; PTM: N-glycosylated. {ECO:0000269|PubMed:20534510, ECO:0000269|PubMed:2850496}.; PTM: Ubiquitinated. After autophosphorylation, the receptor is polyubiquitinated, leading to its degradation. {ECO:0000269|PubMed:1313434, ECO:0000269|PubMed:17620338}.
uniprot
proteins
protein_family
CSF-1/PDGF receptor subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
10454568
uniprot
proteins
pubmed
10805725
uniprot
proteins
pubmed
10821867
uniprot
proteins
pubmed
11297552
uniprot
proteins
pubmed
11331881
uniprot
proteins
pubmed
11567151
uniprot
proteins
pubmed
11882663
uniprot
proteins
pubmed
12181402
uniprot
proteins
pubmed
12907457
uniprot
proteins
pubmed
1313434
uniprot
proteins
pubmed
1314164
uniprot
proteins
pubmed
1375321
uniprot
proteins
pubmed
1396585
uniprot
proteins
pubmed
14966296
uniprot
proteins
pubmed
15087372
uniprot
proteins
pubmed
15207817
uniprot
proteins
pubmed
15340161
uniprot
proteins
pubmed
15372022
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15492236
uniprot
proteins
pubmed
15902258
uniprot
proteins
pubmed
1653029
uniprot
proteins
pubmed
1709159
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17419949
uniprot
proteins
pubmed
17620338
uniprot
proteins
pubmed
1846866
uniprot
proteins
pubmed
18483217
uniprot
proteins
pubmed
18593464
uniprot
proteins
pubmed
20494825
uniprot
proteins
pubmed
20529858
uniprot
proteins
pubmed
20534510
uniprot
proteins
pubmed
21098708
uniprot
proteins
pubmed
21679854
uniprot
proteins
pubmed
21733313
uniprot
proteins
pubmed
21938754
uniprot
proteins
pubmed
23255827
uniprot
proteins
pubmed
23731537
uniprot
proteins
pubmed
23731542
uniprot
proteins
pubmed
24065723
uniprot
proteins
pubmed
25454926
uniprot
proteins
pubmed
2550144
uniprot
proteins
pubmed
2554309
uniprot
proteins
pubmed
26279204
uniprot
proteins
pubmed
26599395
uniprot
proteins
pubmed
2835772
uniprot
proteins
pubmed
2846185
uniprot
proteins
pubmed
2850496
uniprot
proteins
pubmed
30573803
uniprot
proteins
pubmed
33450762
uniprot
proteins
pubmed
7679113
uniprot
proteins
pubmed
7685273
uniprot
proteins
pubmed
7691811
uniprot
proteins
pubmed
7692233
uniprot
proteins
pubmed
8195171
uniprot
proteins
pubmed
8302579
uniprot
proteins
pubmed
8940081
uniprot
proteins
pubmed
9285559
uniprot
proteins
pubmed
9373237
uniprot
proteins
pubmed
9739761
uniprot
proteins
pubmed
9989826
uniprot
proteins
sequence_length
1106
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cytoplasmic vesicle. Lysosome lumen. Note=After ligand binding, the autophosphorylated receptor is ubiquitinated and internalized, leading to its degradation.
uniprot
proteins
transmembrane_region
TRANSMEM 533..553; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins