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Protein

Platelet-derived growth factor receptor alpha

Gene

PDGFRA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

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 Ca2+ 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.14 Publications

<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

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei578 – 579Breakpoint for interstitial deletion to form the FIP1L1-PDGFRA fusion protein2
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei627ATPPROSITE-ProRule annotation1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei818Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi599 – 607ATPPROSITE-ProRule annotation9

<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

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
2.7.10.1 2681

Reactome - a knowledgebase of biological pathways and processes

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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

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P16234

SIGNOR Signaling Network Open Resource

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SIGNORi
P16234

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Platelet-derived growth factor receptor alpha (EC:2.7.10.1)
Short name:
PDGF-R-alpha
Short name:
PDGFR-alpha
Alternative name(s):
Alpha platelet-derived growth factor receptor
Alpha-type platelet-derived growth factor receptor
CD140 antigen-like family member A
CD140a antigen
Platelet-derived growth factor alpha receptor
Platelet-derived growth factor receptor 2
Short name:
PDGFR-2
CD_antigen: CD140a
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PDGFRA
Synonyms:PDGFR2, RHEPDGFRA
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 4

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000134853.11

Human Gene Nomenclature Database

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HGNCi
HGNC:8803 PDGFRA

Online Mendelian Inheritance in Man (OMIM)

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MIMi
173490 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P16234

<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

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini24 – 528ExtracellularSequence analysisAdd BLAST505
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei529 – 549HelicalSequence analysisAdd BLAST21
Topological domaini550 – 1089CytoplasmicSequence analysisAdd BLAST540

Keywords - Cellular componenti

Cell membrane, Cell projection, Golgi apparatus, Membrane

<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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

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.1 Publication
Gastrointestinal stromal tumor (GIST)2 Publications
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).1 Publication
Disease descriptionCommon 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.
See also OMIM:606764
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_066474849Y → C in GIST. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi572Y → F: Abolishes interaction with SRC-family members and impairs internalization of the activated receptor; when associated with F-574. 2 Publications1
Mutagenesisi574Y → F: Abolishes interaction with SRC-family members and impairs internalization of the activated receptor; when associated with F-572. 2 Publications1
Mutagenesisi720Y → F: Strongly reduced interaction with PTPN11 and GRB2. 1 Publication1
Mutagenesisi731Y → F: No effect on autophosphorylation and phosphorylation of PLCG1. Abolishes activation of phosphatidylinositol 3-kinase. 1 Publication1
Mutagenesisi742Y → F: No effect on autophosphorylation and phosphorylation of PLCG1. Abolishes activation of phosphatidylinositol 3-kinase. 1 Publication1
Mutagenesisi762Y → F: Abolishes interaction with CRK. 1 Publication1

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNET

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DisGeNETi
5156

MalaCards human disease database

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MalaCardsi
PDGFRA
MIMi606764 phenotype
607685 phenotype

Open Targets

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OpenTargetsi
ENSG00000134853

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
168940 Chronic eosinophilic leukemia
44890 Gastrointestinal stromal tumor
168947 Myeloid/lymphoid neoplasm associated with PDGFRA rearrangement
99860 Precursor B-cell acute lymphoblastic leukemia
314950 Primary hypereosinophilic syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA33147

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2007

Drug and drug target database

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DrugBanki
DB00102 Becaplermin
DB00619 Imatinib
DB05216 MP470
DB06043 Olaratumab
DB06589 Pazopanib
DB08901 Ponatinib
DB08896 Regorafenib
DB01268 Sunitinib
DB05146 XL820

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1803

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
PDGFRA

Domain mapping of disease mutations (DMDM)

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DMDMi
129892

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 23Add BLAST23
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001676024 – 1089Platelet-derived growth factor receptor alphaAdd BLAST1066

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi42N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi49 ↔ 100PROSITE-ProRule annotation
Glycosylationi76N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi103N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi150 ↔ 189PROSITE-ProRule annotation
Glycosylationi179N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi235 ↔ 290PROSITE-ProRule annotation
Glycosylationi353N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi359N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi435 ↔ 501PROSITE-ProRule annotation
Glycosylationi458N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi468N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei572Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei574Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei720Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei731Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei742Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei754Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei762Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei768Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei849Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei988Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei1018Phosphotyrosine; by autocatalysis1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

N-glycosylated.
Ubiquitinated, leading to its internalization and degradation.1 Publication
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 PLCG1.6 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P16234

MaxQB - The MaxQuant DataBase

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MaxQBi
P16234

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P16234

PeptideAtlas

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PeptideAtlasi
P16234

PRoteomics IDEntifications database

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PRIDEi
P16234

ProteomicsDB human proteome resource

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ProteomicsDBi
53328
53329 [P16234-2]
53330 [P16234-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P16234

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P16234

<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

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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.3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000134853 Expressed in 236 organ(s), highest expression level in endometrium

CleanEx database of gene expression profiles

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CleanExi
HS_PDGFRA

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P16234 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P16234 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB018143
HPA004947

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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.By similarity14 Publications
(Microbial infection) Interacts with human cytomegalovirus/HHV-5 envelope glycoprotein B/gB. Interacts also with the trimeric complex gH-gL-gO.2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
111182, 90 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-2881 PDGF receptor alpha - PDGF-AA complex
CPX-2883 PDGF receptor alpha-beta - PDGF-BB complex
CPX-2884 PDGF receptor alpha - PDGF-BB complex
CPX-2885 PDGF receptor alpha - PDGF-AB complex
CPX-2887 PDGF receptor alpha - PDGF-CC complex
CPX-2888 PDGF receptor alpha-beta - PDGF-CC complex
CPX-2890 PDGF receptor alpha-beta - PDGF-DD complex
CPX-2892 PDGF receptor alpha-beta - PDGF-AB complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P16234

Database of interacting proteins

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DIPi
DIP-5736N

Protein interaction database and analysis system

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IntActi
P16234, 39 interactors

Molecular INTeraction database

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MINTi
P16234

STRING: functional protein association networks

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STRINGi
9606.ENSP00000257290

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P16234

<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

11089
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GQ5X-ray2.20
5GRNX-ray1.77A550-973[»]
5K5XX-ray2.17A550-973[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P16234

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P16234

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P16234

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini24 – 113Ig-like C2-type 1Add BLAST90
Domaini117 – 201Ig-like C2-type 2Add BLAST85
Domaini202 – 306Ig-like C2-type 3Add BLAST105
Domaini319 – 410Ig-like C2-type 4Add BLAST92
Domaini414 – 517Ig-like C2-type 5Add BLAST104
Domaini593 – 954Protein kinasePROSITE-ProRule annotationAdd BLAST362

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1041 – 1087Ser-richAdd BLAST47

<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

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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0200 Eukaryota
COG0515 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000156021

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000112009

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG004335

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P16234

KEGG Orthology (KO)

More...
KOi
K04363

Identification of Orthologs from Complete Genome Data

More...
OMAi
CKDIKKC

Database of Orthologous Groups

More...
OrthoDBi
236292at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P16234

TreeFam database of animal gene trees

More...
TreeFami
TF325768

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.10, 5 hits

Integrated resource of protein families, domains and functional sites

More...
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
IPR011009 Kinase-like_dom_sf
IPR027290 PDGFRA
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, 2 hits
PF07714 Pkinase_Tyr, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF500950 Alpha-PDGF_receptor, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00409 IG, 4 hits
SM00408 IGc2, 3 hits
SM00220 S_TKc, 1 hit
SM00219 TyrKc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48726 SSF48726, 4 hits
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P16234-1) [UniParc]FASTAAdd to basket

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

« Hide
        10         20         30         40         50
MGTSHPAFLV LGCLLTGLSL ILCQLSLPSI LPNENEKVVQ LNSSFSLRCF
60 70 80 90 100
GESEVSWQYP MSEEESSDVE IRNEENNSGL FVTVLEVSSA SAAHTGLYTC
110 120 130 140 150
YYNHTQTEEN ELEGRHIYIY VPDPDVAFVP LGMTDYLVIV EDDDSAIIPC
160 170 180 190 200
RTTDPETPVT LHNSEGVVPA SYDSRQGFNG TFTVGPYICE ATVKGKKFQT
210 220 230 240 250
IPFNVYALKA TSELDLEMEA LKTVYKSGET IVVTCAVFNN EVVDLQWTYP
260 270 280 290 300
GEVKGKGITM LEEIKVPSIK LVYTLTVPEA TVKDSGDYEC AARQATREVK
310 320 330 340 350
EMKKVTISVH EKGFIEIKPT FSQLEAVNLH EVKHFVVEVR AYPPPRISWL
360 370 380 390 400
KNNLTLIENL TEITTDVEKI QEIRYRSKLK LIRAKEEDSG HYTIVAQNED
410 420 430 440 450
AVKSYTFELL TQVPSSILDL VDDHHGSTGG QTVRCTAEGT PLPDIEWMIC
460 470 480 490 500
KDIKKCNNET SWTILANNVS NIITEIHSRD RSTVEGRVTF AKVEETIAVR
510 520 530 540 550
CLAKNLLGAE NRELKLVAPT LRSELTVAAA VLVLLVIVII SLIVLVVIWK
560 570 580 590 600
QKPRYEIRWR VIESISPDGH EYIYVDPMQL PYDSRWEFPR DGLVLGRVLG
610 620 630 640 650
SGAFGKVVEG TAYGLSRSQP VMKVAVKMLK PTARSSEKQA LMSELKIMTH
660 670 680 690 700
LGPHLNIVNL LGACTKSGPI YIITEYCFYG DLVNYLHKNR DSFLSHHPEK
710 720 730 740 750
PKKELDIFGL NPADESTRSY VILSFENNGD YMDMKQADTT QYVPMLERKE
760 770 780 790 800
VSKYSDIQRS LYDRPASYKK KSMLDSEVKN LLSDDNSEGL TLLDLLSFTY
810 820 830 840 850
QVARGMEFLA SKNCVHRDLA ARNVLLAQGK IVKICDFGLA RDIMHDSNYV
860 870 880 890 900
SKGSTFLPVK WMAPESIFDN LYTTLSDVWS YGILLWEIFS LGGTPYPGMM
910 920 930 940 950
VDSTFYNKIK SGYRMAKPDH ATSEVYEIMV KCWNSEPEKR PSFYHLSEIV
960 970 980 990 1000
ENLLPGQYKK SYEKIHLDFL KSDHPAVARM RVDSDNAYIG VTYKNEEDKL
1010 1020 1030 1040 1050
KDWEGGLDEQ RLSADSGYII PLPDIDPVPE EEDLGKRNRH SSQTSEESAI
1060 1070 1080
ETGSSSSTFI KREDETIEDI DMMDDIGIDS SDLVEDSFL
Length:1,089
Mass (Da):122,670
Last modified:April 1, 1990 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i5E3FB9940ACD1BE8
GO
Isoform 2 (identifier: P16234-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     210-218: ATSELDLEM → GTCIISFLL
     219-1089: Missing.

Note: No experimental confirmation available.
Show »
Length:218
Mass (Da):24,023
Checksum:iE8144A73DFD069BF
GO
Isoform 3 (identifier: P16234-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     720-743: YVILSFENNGDYMDMKQADTTQYV → SGQGCLSSGTLQELSVDLQARGPC
     744-1089: Missing.

Show »
Length:743
Mass (Da):82,809
Checksum:i2456B1766606C60F
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D6RIG5D6RIG5_HUMAN
Platelet-derived growth factor rece...
PDGFRA
159Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
D6RG11D6RG11_HUMAN
Platelet-derived growth factor rece...
PDGFRA
158Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
D6RDX0D6RDX0_HUMAN
Platelet-derived growth factor rece...
PDGFRA
154Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
D6RJH0D6RJH0_HUMAN
Platelet-derived growth factor rece...
PDGFRA
147Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAP69563 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04203279G → D1 PublicationCorresponds to variant dbSNP:rs36035373EnsemblClinVar.1
Natural variantiVAR_042033426G → D1 PublicationCorresponds to variant dbSNP:rs55865821Ensembl.1
Natural variantiVAR_034378478S → P3 PublicationsCorresponds to variant dbSNP:rs35597368EnsemblClinVar.1
Natural variantiVAR_066460481R → G in a hypereosinophilic syndrome sample; does not lead to constitutive kinase activation. 1 Publication1
Natural variantiVAR_066461507L → P in a hypereosinophilic syndrome sample; does not lead to constitutive kinase activation. 1 Publication1
Natural variantiVAR_066462561V → D in a GIST sample; constitutively activated kinase. 2 PublicationsCorresponds to variant dbSNP:rs121908586EnsemblClinVar.1
Natural variantiVAR_066463562I → M in a hypereosinophilic syndrome sample; does not lead to constitutive kinase activation. 1 Publication1
Natural variantiVAR_066464570H → R in a hypereosinophilic syndrome sample; does not lead to constitutive kinase activation. 1 Publication1
Natural variantiVAR_066465650H → Q in a hypereosinophilic syndrome sample; constitutively activated kinase. 1 Publication1
Natural variantiVAR_066466659N → K in GIST sample; constitutively activated kinase. 1 PublicationCorresponds to variant dbSNP:rs1057519700Ensembl.1
Natural variantiVAR_066467659N → S in a hypereosinophilic syndrome sample; constitutively activated kinase. 1 Publication1
Natural variantiVAR_066468705L → P in a hypereosinophilic syndrome sample; does not lead to constitutive kinase activation. 1 Publication1
Natural variantiVAR_066469748R → G in a hypereosinophilic syndrome sample; constitutively activated kinase. 1 Publication1
Natural variantiVAR_042034764R → C1 PublicationCorresponds to variant dbSNP:rs34392012EnsemblClinVar.1
Natural variantiVAR_042035829G → R in a glioblastoma multiforme sample; somatic mutation. 1 Publication1
Natural variantiVAR_066470842 – 845Missing in a GIST sample; constitutively activated kinase. 2 Publications4
Natural variantiVAR_066471842D → V in a GIST sample; imatinib resistant, constitutively activated kinase. 3 PublicationsCorresponds to variant dbSNP:rs121908585EnsemblClinVar.1
Natural variantiVAR_066472842D → Y in a GIST sample; imatinib sensitive, constitutively activated kinase. 1 PublicationCorresponds to variant dbSNP:rs121913265EnsemblClinVar.1
Natural variantiVAR_066473845 – 848Missing in a GIST sample; constitutively activated kinase. 2 Publications4
Natural variantiVAR_066474849Y → C in GIST. 1 Publication1
Natural variantiVAR_066475849Y → S in a hypereosinophilic syndrome sample; constitutively activated kinase. 1 Publication1
Natural variantiVAR_042036996E → K in a metastatic melanoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs779173667Ensembl.1
Natural variantiVAR_0420371071D → N in a lung neuroendocrine carcinoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs376544204EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_007833210 – 218ATSELDLEM → GTCIISFLL in isoform 2. 1 Publication9
Alternative sequenceiVSP_007834219 – 1089Missing in isoform 2. 1 PublicationAdd BLAST871
Alternative sequenceiVSP_042015720 – 743YVILS…TTQYV → SGQGCLSSGTLQELSVDLQA RGPC in isoform 3. 1 PublicationAdd BLAST24
Alternative sequenceiVSP_042016744 – 1089Missing in isoform 3. 1 PublicationAdd BLAST346

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M22734 mRNA Translation: AAA60048.1
M21574 mRNA Translation: AAA96715.1
D50017 Genomic DNA Translation: BAA08742.1
AK316578 mRNA Translation: BAG38166.1
AC098587 Genomic DNA No translation available.
AC138779 Genomic DNA No translation available.
BC015186 mRNA Translation: AAH15186.1
BC063414 mRNA Translation: AAH63414.1
AY229892 mRNA Translation: AAP69563.1 Different initiation.

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS3495.1 [P16234-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
A40162 PFHUGA

NCBI Reference Sequences

More...
RefSeqi
NP_001334758.1, NM_001347829.1 [P16234-1]
NP_006197.1, NM_006206.5 [P16234-1]
XP_005265800.1, XM_005265743.1 [P16234-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.74615

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000257290; ENSP00000257290; ENSG00000134853 [P16234-1]
ENST00000508170; ENSP00000425648; ENSG00000134853 [P16234-2]
ENST00000509490; ENSP00000424218; ENSG00000134853 [P16234-3]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5156

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:5156

UCSC genome browser

More...
UCSCi
uc003hal.4 human [P16234-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22734 mRNA Translation: AAA60048.1
M21574 mRNA Translation: AAA96715.1
D50017 Genomic DNA Translation: BAA08742.1
AK316578 mRNA Translation: BAG38166.1
AC098587 Genomic DNA No translation available.
AC138779 Genomic DNA No translation available.
BC015186 mRNA Translation: AAH15186.1
BC063414 mRNA Translation: AAH63414.1
AY229892 mRNA Translation: AAP69563.1 Different initiation.
CCDSiCCDS3495.1 [P16234-1]
PIRiA40162 PFHUGA
RefSeqiNP_001334758.1, NM_001347829.1 [P16234-1]
NP_006197.1, NM_006206.5 [P16234-1]
XP_005265800.1, XM_005265743.1 [P16234-1]
UniGeneiHs.74615

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GQ5X-ray2.20
5GRNX-ray1.77A550-973[»]
5K5XX-ray2.17A550-973[»]
ProteinModelPortaliP16234
SMRiP16234
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111182, 90 interactors
ComplexPortaliCPX-2881 PDGF receptor alpha - PDGF-AA complex
CPX-2883 PDGF receptor alpha-beta - PDGF-BB complex
CPX-2884 PDGF receptor alpha - PDGF-BB complex
CPX-2885 PDGF receptor alpha - PDGF-AB complex
CPX-2887 PDGF receptor alpha - PDGF-CC complex
CPX-2888 PDGF receptor alpha-beta - PDGF-CC complex
CPX-2890 PDGF receptor alpha-beta - PDGF-DD complex
CPX-2892 PDGF receptor alpha-beta - PDGF-AB complex
CORUMiP16234
DIPiDIP-5736N
IntActiP16234, 39 interactors
MINTiP16234
STRINGi9606.ENSP00000257290

Chemistry databases

BindingDBiP16234
ChEMBLiCHEMBL2007
DrugBankiDB00102 Becaplermin
DB00619 Imatinib
DB05216 MP470
DB06043 Olaratumab
DB06589 Pazopanib
DB08901 Ponatinib
DB08896 Regorafenib
DB01268 Sunitinib
DB05146 XL820
GuidetoPHARMACOLOGYi1803

PTM databases

iPTMnetiP16234
PhosphoSitePlusiP16234

Polymorphism and mutation databases

BioMutaiPDGFRA
DMDMi129892

Proteomic databases

jPOSTiP16234
MaxQBiP16234
PaxDbiP16234
PeptideAtlasiP16234
PRIDEiP16234
ProteomicsDBi53328
53329 [P16234-2]
53330 [P16234-3]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
5156
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000257290; ENSP00000257290; ENSG00000134853 [P16234-1]
ENST00000508170; ENSP00000425648; ENSG00000134853 [P16234-2]
ENST00000509490; ENSP00000424218; ENSG00000134853 [P16234-3]
GeneIDi5156
KEGGihsa:5156
UCSCiuc003hal.4 human [P16234-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5156
DisGeNETi5156
EuPathDBiHostDB:ENSG00000134853.11

GeneCards: human genes, protein and diseases

More...
GeneCardsi
PDGFRA
HGNCiHGNC:8803 PDGFRA
HPAiCAB018143
HPA004947
MalaCardsiPDGFRA
MIMi173490 gene
606764 phenotype
607685 phenotype
neXtProtiNX_P16234
OpenTargetsiENSG00000134853
Orphaneti168940 Chronic eosinophilic leukemia
44890 Gastrointestinal stromal tumor
168947 Myeloid/lymphoid neoplasm associated with PDGFRA rearrangement
99860 Precursor B-cell acute lymphoblastic leukemia
314950 Primary hypereosinophilic syndrome
PharmGKBiPA33147

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0200 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00940000156021
HOGENOMiHOG000112009
HOVERGENiHBG004335
InParanoidiP16234
KOiK04363
OMAiCKDIKKC
OrthoDBi236292at2759
PhylomeDBiP16234
TreeFamiTF325768

Enzyme and pathway databases

BRENDAi2.7.10.1 2681
ReactomeiR-HSA-1257604 PIP3 activates AKT signaling
R-HSA-186763 Downstream signal transduction
R-HSA-186797 Signaling by PDGF
R-HSA-2219530 Constitutive Signaling by Aberrant PI3K in Cancer
R-HSA-5673001 RAF/MAP kinase cascade
R-HSA-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
SignaLinkiP16234
SIGNORiP16234

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
PDGFRA human
EvolutionaryTraceiP16234

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
PDGFRA

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
5156

Protein Ontology

More...
PROi
PR:P16234

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000134853 Expressed in 236 organ(s), highest expression level in endometrium
CleanExiHS_PDGFRA
ExpressionAtlasiP16234 baseline and differential
GenevisibleiP16234 HS

Family and domain databases

Gene3Di2.60.40.10, 5 hits
InterProiView protein in InterPro
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR013098 Ig_I-set
IPR003599 Ig_sub
IPR003598 Ig_sub2
IPR011009 Kinase-like_dom_sf
IPR027290 PDGFRA
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
IPR001824 Tyr_kinase_rcpt_3_CS
PfamiView protein in Pfam
PF07679 I-set, 2 hits
PF07714 Pkinase_Tyr, 1 hit
PIRSFiPIRSF500950 Alpha-PDGF_receptor, 1 hit
SMARTiView protein in SMART
SM00409 IG, 4 hits
SM00408 IGc2, 3 hits
SM00220 S_TKc, 1 hit
SM00219 TyrKc, 1 hit
SUPFAMiSSF48726 SSF48726, 4 hits
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50835 IG_LIKE, 2 hits
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit
PS00240 RECEPTOR_TYR_KIN_III, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPGFRA_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P16234
Secondary accession number(s): B2RE69
, E9PBH0, Q6P4H5, Q96KZ7, Q9UD28
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: January 16, 2019
This is version 214 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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