{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P16234","secondaryAccessions":["B2RE69","E9PBH0","Q6P4H5","Q96KZ7","Q9UD28"],"uniProtkbId":"PGFRA_HUMAN","entryAudit":{"firstPublicDate":"1990-04-01","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"1990-04-01","entryVersion":254,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Platelet-derived growth factor receptor alpha"},"shortNames":[{"value":"PDGF-R-alpha"},{"value":"PDGFR-alpha"}],"ecNumbers":[{"value":"2.7.10.1"}]},"alternativeNames":[{"fullName":{"value":"Alpha platelet-derived growth factor receptor"}},{"fullName":{"value":"Alpha-type platelet-derived growth factor receptor"}},{"fullName":{"value":"CD140 antigen-like family member A"}},{"fullName":{"value":"CD140a antigen"}},{"fullName":{"value":"Platelet-derived growth factor alpha receptor"}},{"fullName":{"value":"Platelet-derived growth factor receptor 2"},"shortNames":[{"value":"PDGFR-2"}]}],"cdAntigenNames":[{"value":"CD140a"}],"flag":"Precursor"},"genes":[{"geneName":{"value":"PDGFRA"},"synonyms":[{"value":"PDGFR2"},{"value":"RHEPDGFRA"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10734113"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10947961"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11297552"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12522257"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1646396"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17087943"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1709159"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17141222"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20972453"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21224473"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21596750"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2554309"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8188664"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8760137"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8943348"}],"value":"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"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10596"},{"database":"Rhea","id":"RHEA-COMP:10136"},{"database":"Rhea","id":"RHEA-COMP:20101"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:46858"},{"database":"ChEBI","id":"CHEBI:61978"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.10.1","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU10028"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15928335"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20972453"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21224473"}],"value":"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"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P26618"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10733900"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11095946"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11297552"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11882663"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14644164"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1646396"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1709159"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2173144"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2536956"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2544881"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7535778"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7679113"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8940081"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8943348"}],"value":"Interacts with homodimeric PDGFA, PDGFB and PDGFC, and with heterodimers formed by PDGFA and PDGFB. Monomer in the absence of bound ligand. Interaction with dimeric PDGFA, PDGFB and/or PDGFC leads to receptor dimerization, where both PDGFRA homodimers and heterodimers with PDGFRB are observed. Interacts (tyrosine phosphorylated) with SHB (via SH2 domain) (By similarity). Interacts (tyrosine phosphorylated) with SHF (via SH2 domain). Interacts (tyrosine phosphorylated) with SRC (via SH2 domain). Interacts (tyrosine phosphorylated) with PIK3R1. Interacts (tyrosine phosphorylated) with PLCG1 (via SH2 domain). Interacts (tyrosine phosphorylated) with CRK, GRB2 and GRB7. Interacts with CD248; this interaction promotes PDGF receptor signaling pathway (By similarity)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20660204"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28403202"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33626330"}],"value":"(Microbial infection) Interacts with human cytomegalovirus/HHV-5 envelope glycoprotein B/gB. Also interacts with the trimeric complex gH-gL-gO. Trimer-PDGFRA interaction has an inhibitory effect on PDGFRA signaling (PubMed:33626330)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P16234","intActId":"EBI-2861522"},"interactantTwo":{"uniProtKBAccession":"P46108","geneName":"CRK","intActId":"EBI-886"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P16234","intActId":"EBI-2861522"},"interactantTwo":{"uniProtKBAccession":"P46109","geneName":"CRKL","intActId":"EBI-910"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P16234","intActId":"EBI-2861522"},"interactantTwo":{"uniProtKBAccession":"P00533","geneName":"EGFR","intActId":"EBI-297353"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P16234","intActId":"EBI-2861522"},"interactantTwo":{"uniProtKBAccession":"Q8N6L0","geneName":"KASH5","intActId":"EBI-749265"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P16234","intActId":"EBI-2861522"},"interactantTwo":{"uniProtKBAccession":"P04085","geneName":"PDGFA","intActId":"EBI-2881386"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P16234","intActId":"EBI-2861522"},"interactantTwo":{"uniProtKBAccession":"P01127","geneName":"PDGFB","intActId":"EBI-1554925"},"numberOfExperiments":11,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P16234","intActId":"EBI-2861522"},"interactantTwo":{"uniProtKBAccession":"Q9NRA1","geneName":"PDGFC","intActId":"EBI-8833587"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P16234","intActId":"EBI-2861522"},"interactantTwo":{"uniProtKBAccession":"Q15238","geneName":"PSG5","intActId":"EBI-4314891"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P16234","intActId":"EBI-2861522"},"interactantTwo":{"uniProtKBAccession":"P31947","geneName":"SFN","intActId":"EBI-476295"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P16234","intActId":"EBI-2861522"},"interactantTwo":{"uniProtKBAccession":"P62258","geneName":"YWHAE","intActId":"EBI-356498"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P16234-1","intActId":"EBI-15499330"},"interactantTwo":{"uniProtKBAccession":"Q9NRA1-1","geneName":"PDGFC","intActId":"EBI-15499301"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P16234-1","intActId":"EBI-15499330"},"interactantTwo":{"uniProtKBAccession":"A8T7D5","geneName":"UL55","intActId":"EBI-15722055"},"numberOfExperiments":2,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P16234-2","intActId":"EBI-13380852"},"interactantTwo":{"uniProtKBAccession":"P05067","geneName":"APP","intActId":"EBI-77613"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P16234-2","intActId":"EBI-13380852"},"interactantTwo":{"uniProtKBAccession":"Q8IY26","geneName":"PLPP6","intActId":"EBI-11721828"},"numberOfExperiments":3,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14644164"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2554309"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8188664"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14644164"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2554309"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8188664"}],"value":"Single-pass type I membrane protein","id":"SL-9905"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P26618"}],"value":"Cell projection, cilium","id":"SL-0066"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P26618"}],"value":"Golgi apparatus","id":"SL-0132"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["P16234-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["P16234-2"],"sequenceIds":["VSP_007833","VSP_007834"],"isoformSequenceStatus":"Described"},{"name":{"value":"3"},"isoformIds":["P16234-3"],"sequenceIds":["VSP_042015","VSP_042016"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2536956"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7896447"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8188664"}],"value":"Detected in platelets (at protein level). Widely expressed. Detected in brain, fibroblasts, smooth muscle, heart, and embryo. Expressed in primary and metastatic colon tumors and in normal colon tissue"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"value":"N-glycosylated"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21596750"}],"value":"Ubiquitinated, leading to its internalization and degradation"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10733900"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10734113"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11095946"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1646396"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7535778"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8943348"}],"value":"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"}],"commentType":"PTM"},{"commentType":"DISEASE","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12808148"}],"value":"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"}]}},{"commentType":"DISEASE","disease":{"diseaseId":"Gastrointestinal stromal tumor","diseaseAccession":"DI-01646","acronym":"GIST","description":"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.","diseaseCrossReference":{"database":"MIM","id":"606764"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12522257"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15928335"}]},"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12522257"}],"value":"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)"}]}},{"commentType":"DISEASE","disease":{"diseaseId":"GIST-plus syndrome","diseaseAccession":"DI-05623","acronym":"GISTPS","description":"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.","diseaseCrossReference":{"database":"MIM","id":"175510"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14699510"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17087943"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25975287"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00159"}],"value":"Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily"}],"commentType":"SIMILARITY"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"AAP69563.1","note":"Extended N-terminus.","evidences":[{"evidenceCode":"ECO:0000305"}]}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":""},{"type":"Chain","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":1089,"modifier":"EXACT"}},"description":"Platelet-derived growth factor receptor alpha","featureId":"PRO_0000016760"},{"type":"Topological domain","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":528,"modifier":"EXACT"}},"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":529,"modifier":"EXACT"},"end":{"value":549,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Topological 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