PDGFRA
entrez
5156
canonical
uniprot
P16234
canonical
ensembl
ENSG00000134853
resolver
ensp
ENSP00000257290
resolver
ensp
ENSP00000540948
resolver
ensp
ENSP00000540949
resolver
ensp
ENSP00000628810
resolver
ensp
ENSP00000780289
resolver
genesymbol
PDGFRA
resolver
genesymbol_syn
PDGFR2
resolver
genesymbol_syn
RHEPDGFRA
resolver
hgnc
HGNC:8803
resolver
uniprot
B2RE69
resolver
uniprot
E9PBH0
resolver
uniprot
Q6P4H5
resolver
uniprot
Q96KZ7
resolver
uniprot
Q9UD28
resolver
uniprot_entry
PGFRA_HUMAN
resolver
uniprot_sec
B2RE69
resolver
uniprot_sec
E9PBH0
resolver
uniprot_sec
Q6P4H5
resolver
uniprot_sec
Q96KZ7
resolver
uniprot_sec
Q9UD28
resolver
activity_regulation
ACTIVITY REGULATION: Present in an inactive conformation in the absence of bound ligand. Binding of PDGFA and/or PDGFB leads to dimerization and activation by autophosphorylation on tyrosine residues. Inhibited by imatinib, nilotinib and sorafenib. {ECO:0000269|PubMed:15928335, ECO:0000269|PubMed:20972453, ECO:0000269|PubMed:21224473}.
uniprot
proteins
amino_acid_sequence
MGTSHPAFLVLGCLLTGLSLILCQLSLPSILPNENEKVVQLNSSFSLRCFGESEVSWQYPMSEEESSDVEIRNEENNSGLFVTVLEVSSASAAHTGLYTCYYNHTQTEENELEGRHIYIYVPDPDVAFVPLGMTDYLVIVEDDDSAIIPCRTTDPETPVTLHNSEGVVPASYDSRQGFNGTFTVGPYICEATVKGKKFQTIPFNVYALKATSELDLEMEALKTVYKSGETIVVTCAVFNNEVVDLQWTYPGEVKGKGITMLEEIKVPSIKLVYTLTVPEATVKDSGDYECAARQATREVKEMKKVTISVHEKGFIEIKPTFSQLEAVNLHEVKHFVVEVRAYPPPRISWLKNNLTLIENLTEITTDVEKIQEIRYRSKLKLIRAKEEDSGHYTIVAQNEDAVKSYTFELLTQVPSSILDLVDDHHGSTGGQTVRCTAEGTPLPDIEWMICKDIKKCNNETSWTILANNVSNIITEIHSRDRSTVEGRVTFAKVEETIAVRCLAKNLLGAENRELKLVAPTLRSELTVAAAVLVLLVIVIISLIVLVVIWKQKPRYEIRWRVIESISPDGHEYIYVDPMQLPYDSRWEFPRDGLVLGRVLGSGAFGKVVEGTAYGLSRSQPVMKVAVKMLKPTARSSEKQALMSELKIMTHLGPHLNIVNLLGACTKSGPIYIITEYCFYGDLVNYLHKNRDSFLSHHPEKPKKELDIFGLNPADESTRSYVILSFENNGDYMDMKQADTTQYVPMLERKEVSKYSDIQRSLYDRPASYKKKSMLDSEVKNLLSDDNSEGLTLLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDIMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGTPYPGMMVDSTFYNKIKSGYRMAKPDHATSEVYEIMVKCWNSEPEKRPSFYHLSEIVENLLPGQYKKSYEKIHLDFLKSDHPAVARMRVDSDNAYIGVTYKNEEDKLKDWEGGLDEQRLSADSGYIIPLPDIDPVPEEEDLGKRNRHSSQTSEESAIETGSSSSTFIKREDETIEDIDMMDDIGIDSSDLVEDSFL
uniprot
proteins
disease_involvement
DISEASE: Note=A chromosomal aberration involving PDGFRA is found in some cases of hypereosinophilic syndrome. Interstitial chromosomal deletion del(4)(q12q12) causes the fusion of FIP1L1 and PDGFRA (FIP1L1-PDGFRA). Mutations that cause overexpression and/or constitutive activation of PDGFRA may be a cause of hypereosinophilic syndrome. {ECO:0000269|PubMed:12808148}.; DISEASE: Gastrointestinal stromal tumor (GIST) [MIM:606764]: Common mesenchymal neoplasms arising in the gastrointestinal tract, most often in the stomach. They are histologically, immunohistochemically, and genetically different from typical leiomyomas, leiomyosarcomas, and schwannomas. Most GISTs are composed of a fairly uniform population of spindle-shaped cells. Some tumors are dominated by epithelioid cells or contain a mixture of spindle and epithelioid morphologies. Primary GISTs in the gastrointestinal tract commonly metastasize in the omentum and mesenteries, often as multiple nodules. However, primary tumors may also occur outside of the gastrointestinal tract, in other intra-abdominal locations, especially in the omentum and mesentery. {ECO:0000269|PubMed:12522257, ECO:0000269|PubMed:15928335}. Note=The gene represented in this entry may be involved in disease pathogenesis. Mutations causing PDGFRA constitutive activation have been found in gastrointestinal stromal tumors lacking KIT mutations (PubMed:12522257). {ECO:0000269|PubMed:12522257}.; DISEASE: GIST-plus syndrome (GISTPS) [MIM:175510]: A disorder characterized by multiple mesenchymal tumors of the gastrointestinal tract, including gastrointestinal stromal tumor, inflammatory fibroid polyps, and fibroid tumors. Additional features are coarse facies and skin, broad hands and feet, and premature tooth loss. GISTPS is an autosomal dominant disease with incomplete penetrance. Gastrointestinal stromal tumor and inflammatory fibroid polyps may also occur in isolation. {ECO:0000269|PubMed:14699510, ECO:0000269|PubMed:17087943, ECO:0000269|PubMed:25975287}. Note=The disease is 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 PDGFA, PDGFB and PDGFC and plays an essential role in the regulation of embryonic development, cell proliferation, survival and chemotaxis. Depending on the context, promotes or inhibits cell proliferation and cell migration. Plays an important role in the differentiation of bone marrow-derived mesenchymal stem cells. Required for normal skeleton development and cephalic closure during embryonic development. Required for normal development of the mucosa lining the gastrointestinal tract, and for recruitment of mesenchymal cells and normal development of intestinal villi. Plays a role in cell migration and chemotaxis in wound healing. Plays a role in platelet activation, secretion of agonists from platelet granules, and in thrombin-induced platelet aggregation. Binding of its cognate ligands - homodimeric PDGFA, homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFC -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 PIK3R1, PLCG1, and PTPN11. 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. Phosphorylates PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and thereby mediates activation of the AKT1 signaling pathway. Mediates activation of HRAS and of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3 and STAT5A and/or STAT5B. 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:10734113, ECO:0000269|PubMed:10947961, ECO:0000269|PubMed:11297552, ECO:0000269|PubMed:12522257, ECO:0000269|PubMed:1646396, ECO:0000269|PubMed:17087943, ECO:0000269|PubMed:1709159, ECO:0000269|PubMed:17141222, ECO:0000269|PubMed:20972453, ECO:0000269|PubMed:21224473, ECO:0000269|PubMed:21596750, ECO:0000269|PubMed:2554309, ECO:0000269|PubMed:8188664, ECO:0000269|PubMed:8760137, ECO:0000269|PubMed:8943348}.
uniprot
proteins
mass_dalton
122670
uniprot
proteins
mutagenesis
MUTAGEN 572; /note="Y->F: Abolishes interaction with SRC-family members and impairs internalization of the activated receptor; when associated with F-574."; /evidence="ECO:0000269|PubMed:10734113, ECO:0000269|PubMed:14644164"; MUTAGEN 574; /note="Y->F: Abolishes interaction with SRC-family members and impairs internalization of the activated receptor; when associated with F-572."; /evidence="ECO:0000269|PubMed:10734113, ECO:0000269|PubMed:14644164"; MUTAGEN 720; /note="Y->F: Strongly reduced interaction with PTPN11 and GRB2."; /evidence="ECO:0000269|PubMed:8943348"; MUTAGEN 731; /note="Y->F: No effect on autophosphorylation and phosphorylation of PLCG1. Abolishes activation of phosphatidylinositol 3-kinase."; /evidence="ECO:0000269|PubMed:1646396"; MUTAGEN 742; /note="Y->F: No effect on autophosphorylation and phosphorylation of PLCG1. Abolishes activation of phosphatidylinositol 3-kinase."; /evidence="ECO:0000269|PubMed:1646396"; MUTAGEN 762; /note="Y->F: Abolishes interaction with CRK."; /evidence="ECO:0000269|PubMed:10733900
uniprot
proteins
post_translational_modification
PTM: N-glycosylated.; PTM: Ubiquitinated, leading to its internalization and degradation. {ECO:0000305|PubMed:21596750}.; 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-731 and Tyr-742 is important for interaction with PIK3R1. Phosphorylation at Tyr-720 and Tyr-754 is important for interaction with PTPN11. Phosphorylation at Tyr-762 is important for interaction with CRK. Phosphorylation at Tyr-572 and Tyr-574 is important for interaction with SRC and SRC family members. Phosphorylation at Tyr-988 and Tyr-1018 is important for interaction with PLCG1. {ECO:0000269|PubMed:10733900, ECO:0000269|PubMed:10734113, ECO:0000269|PubMed:11095946, ECO:0000269|PubMed:1646396, ECO:0000269|PubMed:7535778, ECO:0000269|PubMed:8943348}.
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
10733900
uniprot
proteins
pubmed
10734113
uniprot
proteins
pubmed
10947961
uniprot
proteins
pubmed
11095946
uniprot
proteins
pubmed
11297552
uniprot
proteins
pubmed
11882663
uniprot
proteins
pubmed
12522257
uniprot
proteins
pubmed
12660384
uniprot
proteins
pubmed
12808148
uniprot
proteins
pubmed
14644164
uniprot
proteins
pubmed
14699510
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15207817
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
15928335
uniprot
proteins
pubmed
1646396
uniprot
proteins
pubmed
17087943
uniprot
proteins
pubmed
1709159
uniprot
proteins
pubmed
17141222
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17419949
uniprot
proteins
pubmed
17604334
uniprot
proteins
pubmed
18483217
uniprot
proteins
pubmed
20660204
uniprot
proteins
pubmed
20972453
uniprot
proteins
pubmed
21224473
uniprot
proteins
pubmed
21596750
uniprot
proteins
pubmed
2173144
uniprot
proteins
pubmed
2536956
uniprot
proteins
pubmed
2544881
uniprot
proteins
pubmed
2554309
uniprot
proteins
pubmed
25975287
uniprot
proteins
pubmed
28403202
uniprot
proteins
pubmed
33626330
uniprot
proteins
pubmed
7535778
uniprot
proteins
pubmed
7679113
uniprot
proteins
pubmed
7896447
uniprot
proteins
pubmed
8188664
uniprot
proteins
pubmed
8586421
uniprot
proteins
pubmed
8617789
uniprot
proteins
pubmed
8760137
uniprot
proteins
pubmed
8940081
uniprot
proteins
pubmed
8943348
uniprot
proteins
pubmed
9739761
uniprot
proteins
sequence_length
1089
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14644164, ECO:0000269|PubMed:2554309, ECO:0000269|PubMed:8188664}; Single-pass type I membrane protein {ECO:0000269|PubMed:14644164, ECO:0000269|PubMed:2554309, ECO:0000269|PubMed:8188664}. Cell projection, cilium {ECO:0000250|UniProtKB:P26618}. Golgi apparatus {ECO:0000250|UniProtKB:P26618}.
uniprot
proteins
transmembrane_region
TRANSMEM 529..549; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins