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P16234 (PGFRA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 167. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Platelet-derived growth factor receptor alpha

Short name=PDGF-R-alpha
Short name=PDGFR-alpha
EC=2.7.10.1
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
Gene names
Name:PDGFRA
Synonyms:PDGFR2, RHEPDGFRA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1089 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 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. Ref.9 Ref.11 Ref.12 Ref.14 Ref.16 Ref.18 Ref.21 Ref.22 Ref.23 Ref.26 Ref.28 Ref.30 Ref.31 Ref.32

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Enzyme 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. Ref.27 Ref.30 Ref.32

Subunit structure

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 human cytomegalovirus/HHV-5 envelop glycoprotein B/gB. Ref.1 Ref.2 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20 Ref.23 Ref.24 Ref.29

Subcellular location

Cell membrane; Single-pass type I membrane protein. Note: The activated receptor is rapidly internalized and degraded. Ref.9 Ref.14 Ref.24

Tissue specificity

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. Ref.2 Ref.8 Ref.14

Post-translational modification

N-glycosylated.

Ubiquitinated, leading to its degradation Probable. Ref.22 Ref.31

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. Ref.2 Ref.11 Ref.12 Ref.14 Ref.15 Ref.18 Ref.19 Ref.20 Ref.22

Involvement in disease

A chromosomal aberration involving PDGFRA is found in some cases of hypereosinophilic syndrome. Interstitial chromosomal deletion del4(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. Ref.7 Ref.32

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.
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 (Ref.26). Ref.7 Ref.26 Ref.27 Ref.32

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily.

Contains 5 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 protein kinase domain.

Sequence caution

The sequence AAP69563.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processChemotaxis
Host-virus interaction
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseProto-oncogene
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

Leydig cell differentiation

Inferred from electronic annotation. Source: Ensembl

adrenal gland development

Inferred from electronic annotation. Source: Ensembl

cardiac myofibril assembly

Inferred from sequence or structural similarity. Source: UniProtKB

cell activation

Traceable author statement PubMed 10508235. Source: BHF-UCL

cell chemotaxis

Inferred from mutant phenotype Ref.12. Source: UniProtKB

cellular response to amino acid stimulus

Inferred from electronic annotation. Source: Ensembl

embryonic cranial skeleton morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

embryonic digestive tract morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

embryonic skeletal system morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

estrogen metabolic process

Inferred from electronic annotation. Source: Ensembl

extracellular matrix organization

Inferred from electronic annotation. Source: Ensembl

face morphogenesis

Inferred from electronic annotation. Source: Ensembl

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

lung development

Inferred from electronic annotation. Source: Ensembl

luteinization

Inferred from sequence or structural similarity. Source: UniProtKB

male genitalia development

Inferred from electronic annotation. Source: Ensembl

metanephric glomerular capillary formation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of platelet activation

Inferred from direct assay Ref.14. Source: UniProtKB

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

odontogenesis of dentin-containing tooth

Inferred from electronic annotation. Source: Ensembl

palate development

Inferred from electronic annotation. Source: Ensembl

peptidyl-tyrosine phosphorylation

Inferred from direct assay Ref.12Ref.14. Source: UniProtKB

phosphatidylinositol-mediated signaling

Inferred from mutant phenotype Ref.9. Source: UniProtKB

platelet aggregation

Inferred from mutant phenotype Ref.14. Source: UniProtKB

platelet-derived growth factor receptor signaling pathway

Inferred from direct assay PubMed 10806482Ref.2. Source: BHF-UCL

platelet-derived growth factor receptor-alpha signaling pathway

Inferred from mutant phenotype Ref.9. Source: UniProtKB

positive regulation of DNA replication

Inferred from direct assay PubMed 10806482. Source: BHF-UCL

positive regulation of ERK1 and ERK2 cascade

Inferred from mutant phenotype Ref.22. Source: UniProtKB

positive regulation of cell migration

Inferred from mutant phenotype Ref.12. Source: UniProtKB

positive regulation of cell proliferation

Inferred from mutant phenotype Ref.9. Source: UniProtKB

positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway

Inferred from direct assay PubMed 17470632. Source: BHF-UCL

positive regulation of cytosolic calcium ion concentration

Inferred from mutant phenotype Ref.9. Source: UniProtKB

positive regulation of fibroblast proliferation

Inferred from direct assay PubMed 10806482. Source: BHF-UCL

positive regulation of phosphatidylinositol 3-kinase activity

Inferred from mutant phenotype Ref.12. Source: UniProtKB

positive regulation of phosphatidylinositol 3-kinase signaling

Traceable author statement Ref.22. Source: UniProtKB

positive regulation of phospholipase C activity

Inferred from mutant phenotype Ref.12. Source: UniProtKB

protein autophosphorylation

Inferred from direct assay Ref.12Ref.14. Source: UniProtKB

regulation of actin cytoskeleton reorganization

Traceable author statement Ref.22. Source: UniProtKB

regulation of chemotaxis

Inferred from mutant phenotype Ref.9. Source: UniProtKB

regulation of mesenchymal stem cell differentiation

Inferred from mutant phenotype Ref.31. Source: UniProtKB

retina vasculature development in camera-type eye

Inferred from sequence or structural similarity. Source: UniProtKB

signal transduction involved in regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

wound healing

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Inferred from direct assay Ref.2. Source: BHF-UCL

intrinsic component of plasma membrane

Inferred from direct assay Ref.9. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

platelet-derived growth factor alpha-receptor activity

Inferred from direct assay Ref.14. Source: UniProtKB

platelet-derived growth factor binding

Inferred from direct assay Ref.9Ref.14. Source: UniProtKB

platelet-derived growth factor receptor binding

Inferred from physical interaction PubMed 2542288. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 17470632. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay PubMed 2542288. Source: BHF-UCL

transmembrane receptor protein tyrosine kinase activity

Inferred from direct assay Ref.12. Source: UniProtKB

vascular endothelial growth factor binding

Inferred from physical interaction PubMed 17470632. Source: BHF-UCL

vascular endothelial growth factor-activated receptor activity

Inferred from direct assay PubMed 17470632. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P16234-1)

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.
Isoform 2 (identifier: P16234-2)

The sequence of this isoform differs from the canonical sequence as follows:
     210-218: ATSELDLEM → GTCIISFLL
     219-1089: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P16234-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323
Chain24 – 10891066Platelet-derived growth factor receptor alpha
PRO_0000016760

Regions

Topological domain24 – 528505Extracellular Potential
Transmembrane529 – 54921Helical; Potential
Topological domain550 – 1089540Cytoplasmic Potential
Domain24 – 11390Ig-like C2-type 1
Domain117 – 20185Ig-like C2-type 2
Domain202 – 306105Ig-like C2-type 3
Domain319 – 41092Ig-like C2-type 4
Domain414 – 517104Ig-like C2-type 5
Domain593 – 954362Protein kinase
Nucleotide binding599 – 6079ATP By similarity
Compositional bias1041 – 108747Ser-rich

Sites

Active site8181Proton acceptor By similarity
Binding site6271ATP By similarity
Site578 – 5792Breakpoint for interstitial deletion to form the FIP1L1-PDGFRA fusion protein

Amino acid modifications

Modified residue5551Phosphotyrosine
Modified residue5721Phosphotyrosine; by autocatalysis Ref.22
Modified residue5741Phosphotyrosine; by autocatalysis Ref.22
Modified residue5821Phosphotyrosine
Modified residue7201Phosphotyrosine; by autocatalysis Ref.18 Ref.20
Modified residue7311Phosphotyrosine; by autocatalysis Ref.12
Modified residue7421Phosphotyrosine; by autocatalysis Ref.12
Modified residue7541Phosphotyrosine; by autocatalysis
Modified residue7621Phosphotyrosine; by autocatalysis Ref.19
Modified residue7681Phosphotyrosine; by autocatalysis
Modified residue8491Phosphotyrosine; by autocatalysis By similarity
Modified residue9441Phosphotyrosine
Modified residue9581Phosphotyrosine
Modified residue9621Phosphotyrosine
Modified residue9881Phosphotyrosine; by autocatalysis Ref.15
Modified residue9931Phosphotyrosine
Modified residue10181Phosphotyrosine; by autocatalysis Ref.15
Glycosylation421N-linked (GlcNAc...) Potential
Glycosylation761N-linked (GlcNAc...) Potential
Glycosylation1031N-linked (GlcNAc...) Potential
Glycosylation1791N-linked (GlcNAc...) Potential
Glycosylation3531N-linked (GlcNAc...) Potential
Glycosylation3591N-linked (GlcNAc...) Potential
Glycosylation4581N-linked (GlcNAc...) Potential
Glycosylation4681N-linked (GlcNAc...) Potential
Disulfide bond49 ↔ 100 By similarity
Disulfide bond150 ↔ 189 By similarity
Disulfide bond235 ↔ 290 By similarity
Disulfide bond435 ↔ 501 By similarity

Natural variations

Alternative sequence210 – 2189ATSELDLEM → GTCIISFLL in isoform 2.
VSP_007833
Alternative sequence219 – 1089871Missing in isoform 2.
VSP_007834
Alternative sequence720 – 74324YVILS…TTQYV → SGQGCLSSGTLQELSVDLQA RGPC in isoform 3.
VSP_042015
Alternative sequence744 – 1089346Missing in isoform 3.
VSP_042016
Natural variant791G → D. Ref.38
Corresponds to variant rs36035373 [ dbSNP | Ensembl ].
VAR_042032
Natural variant4261G → D. Ref.38
Corresponds to variant rs55865821 [ dbSNP | Ensembl ].
VAR_042033
Natural variant4781S → P. Ref.4 Ref.6 Ref.38
Corresponds to variant rs35597368 [ dbSNP | Ensembl ].
VAR_034378
Natural variant4811R → G in a hypereosinophilic syndrome sample; does not lead to constitutive kinase activation. Ref.30
VAR_066460
Natural variant5071L → P in a hypereosinophilic syndrome sample; does not lead to constitutive kinase activation. Ref.30
VAR_066461
Natural variant5611V → D in a GIST sample; constitutively activated kinase. Ref.26 Ref.27
VAR_066462
Natural variant5621I → M in a hypereosinophilic syndrome sample; does not lead to constitutive kinase activation. Ref.30
VAR_066463
Natural variant5701H → R in a hypereosinophilic syndrome sample; does not lead to constitutive kinase activation. Ref.30
VAR_066464
Natural variant6501H → Q in a hypereosinophilic syndrome sample; constitutively activated kinase. Ref.30
VAR_066465
Natural variant6591N → K in GIST sample; constitutively activated kinase. Ref.27
VAR_066466
Natural variant6591N → S in a hypereosinophilic syndrome sample; constitutively activated kinase. Ref.30
VAR_066467
Natural variant7051L → P in a hypereosinophilic syndrome sample; does not lead to constitutive kinase activation. Ref.30
VAR_066468
Natural variant7481R → G in a hypereosinophilic syndrome sample; constitutively activated kinase. Ref.30
VAR_066469
Natural variant7641R → C. Ref.38
Corresponds to variant rs34392012 [ dbSNP | Ensembl ].
VAR_042034
Natural variant8291G → R in a glioblastoma multiforme sample; somatic mutation. Ref.38
VAR_042035
Natural variant842 – 8454Missing in a GIST sample; constitutively activated kinase.
VAR_066470
Natural variant8421D → V in a GIST sample; imatinib resistant, constitutively activated kinase. Ref.26 Ref.27 Ref.32
VAR_066471
Natural variant8421D → Y in a GIST sample; imatinib sensitive, constitutively activated kinase. Ref.27
VAR_066472
Natural variant845 – 8484Missing in a GIST sample; constitutively activated kinase.
VAR_066473
Natural variant8491Y → C in GIST. Ref.27
VAR_066474
Natural variant8491Y → S in a hypereosinophilic syndrome sample; constitutively activated kinase. Ref.30
VAR_066475
Natural variant9961E → K in a metastatic melanoma sample; somatic mutation. Ref.38
VAR_042036
Natural variant10711D → N in a lung neuroendocrine carcinoma sample; somatic mutation. Ref.38
VAR_042037

Experimental info

Mutagenesis5721Y → F: Abolishes interaction with SRC-family members and impairs internalization of the activated receptor; when associated with F-574. Ref.22 Ref.24
Mutagenesis5741Y → F: Abolishes interaction with SRC-family members and impairs internalization of the activated receptor; when associated with F-572. Ref.22 Ref.24
Mutagenesis7201Y → F: Strongly reduced interaction with PTPN11 and GRB2. Ref.18
Mutagenesis7311Y → F: No effect on autophosphorylation and phosphorylation of PLCG1. Abolishes activation of phosphatidylinositol 3-kinase. Ref.12
Mutagenesis7421Y → F: No effect on autophosphorylation and phosphorylation of PLCG1. Abolishes activation of phosphatidylinositol 3-kinase. Ref.12
Mutagenesis7621Y → F: Abolishes interaction with CRK. Ref.19

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 5E3FB9940ACD1BE8

FASTA1,089122,670
        10         20         30         40         50         60 
MGTSHPAFLV LGCLLTGLSL ILCQLSLPSI LPNENEKVVQ LNSSFSLRCF GESEVSWQYP 

        70         80         90        100        110        120 
MSEEESSDVE IRNEENNSGL FVTVLEVSSA SAAHTGLYTC YYNHTQTEEN ELEGRHIYIY 

       130        140        150        160        170        180 
VPDPDVAFVP LGMTDYLVIV EDDDSAIIPC RTTDPETPVT LHNSEGVVPA SYDSRQGFNG 

       190        200        210        220        230        240 
TFTVGPYICE ATVKGKKFQT IPFNVYALKA TSELDLEMEA LKTVYKSGET IVVTCAVFNN 

       250        260        270        280        290        300 
EVVDLQWTYP GEVKGKGITM LEEIKVPSIK LVYTLTVPEA TVKDSGDYEC AARQATREVK 

       310        320        330        340        350        360 
EMKKVTISVH EKGFIEIKPT FSQLEAVNLH EVKHFVVEVR AYPPPRISWL KNNLTLIENL 

       370        380        390        400        410        420 
TEITTDVEKI QEIRYRSKLK LIRAKEEDSG HYTIVAQNED AVKSYTFELL TQVPSSILDL 

       430        440        450        460        470        480 
VDDHHGSTGG QTVRCTAEGT PLPDIEWMIC KDIKKCNNET SWTILANNVS NIITEIHSRD 

       490        500        510        520        530        540 
RSTVEGRVTF AKVEETIAVR CLAKNLLGAE NRELKLVAPT LRSELTVAAA VLVLLVIVII 

       550        560        570        580        590        600 
SLIVLVVIWK QKPRYEIRWR VIESISPDGH EYIYVDPMQL PYDSRWEFPR DGLVLGRVLG 

       610        620        630        640        650        660 
SGAFGKVVEG TAYGLSRSQP VMKVAVKMLK PTARSSEKQA LMSELKIMTH LGPHLNIVNL 

       670        680        690        700        710        720 
LGACTKSGPI YIITEYCFYG DLVNYLHKNR DSFLSHHPEK PKKELDIFGL NPADESTRSY 

       730        740        750        760        770        780 
VILSFENNGD YMDMKQADTT QYVPMLERKE VSKYSDIQRS LYDRPASYKK KSMLDSEVKN 

       790        800        810        820        830        840 
LLSDDNSEGL TLLDLLSFTY QVARGMEFLA SKNCVHRDLA ARNVLLAQGK IVKICDFGLA 

       850        860        870        880        890        900 
RDIMHDSNYV SKGSTFLPVK WMAPESIFDN LYTTLSDVWS YGILLWEIFS LGGTPYPGMM 

       910        920        930        940        950        960 
VDSTFYNKIK SGYRMAKPDH ATSEVYEIMV KCWNSEPEKR PSFYHLSEIV ENLLPGQYKK 

       970        980        990       1000       1010       1020 
SYEKIHLDFL KSDHPAVARM RVDSDNAYIG VTYKNEEDKL KDWEGGLDEQ RLSADSGYII 

      1030       1040       1050       1060       1070       1080 
PLPDIDPVPE EEDLGKRNRH SSQTSEESAI ETGSSSSTFI KREDETIEDI DMMDDIGIDS 


SDLVEDSFL 

« Hide

Isoform 2 [UniParc].

Checksum: E8144A73DFD069BF
Show »

FASTA21824,023
Isoform 3 [UniParc].

Checksum: 2456B1766606C60F
Show »

FASTA74382,809

References

« Hide 'large scale' references
[1]"cDNA cloning and expression of the human A-type platelet-derived growth factor (PDGF) receptor establishes structural similarity to the B-type PDGF receptor."
Claesson-Welsh L., Eriksson A., Westermark B., Heldin C.H.
Proc. Natl. Acad. Sci. U.S.A. 86:4917-4921(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH PDGFA AND PDGFB.
Tissue: Foreskin.
[2]"Isolation of a novel receptor cDNA establishes the existence of two PDGF receptor genes."
Matsui T., Heidaran M., Miki T., Popescu N., la Rochelle W., Kraus M., Pierce J., Aaronson S.
Science 243:800-804(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AUTOPHOSPHORYLATION, TISSUE SPECIFICITY, INTERACTION WITH PDGFA AND PDGFB.
Tissue: Brain.
[3]"Structure, organization, and transcription units of the human alpha-platelet-derived growth factor receptor gene, PDGFRA."
Kawagishi J., Ku T.
Genomics 30:224-232(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Blood.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT PRO-478.
Tissue: Lung and Trachea.
[5]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), VARIANT PRO-478.
Tissue: Placenta.
[7]"Discovery of a fusion kinase in EOL-1 cells and idiopathic hypereosinophilic syndrome."
Griffin J.H., Leung J., Bruner R.J., Caligiuri M.A., Briesewitz R.
Proc. Natl. Acad. Sci. U.S.A. 100:7830-7835(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 579-1089, DISEASE, IDENTIFICATION BY MASS SPECTROMETRY OF FIP1L1-PDGFRA FUSION PROTEIN.
Tissue: Eosinophil.
[8]"Receptor tyrosine kinases expressed in metastatic colon cancer."
Craven R.J., Xu L.H., Weiner T.M., Fridell Y.-W., Dent G.A., Srivastava S., Varnum B., Liu E.T., Cance W.G.
Int. J. Cancer 60:791-797(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 823-876, TISSUE SPECIFICITY.
Tissue: Colon tumor.
[9]"Independent expression of human alpha or beta platelet-derived growth factor receptor cDNAs in a naive hematopoietic cell leads to functional coupling with mitogenic and chemotactic signaling pathways."
Matsui T., Pierce J.H., Fleming T.P., Greenberger J.S., LaRochelle W.J., Ruggiero M., Aaronson S.A.
Proc. Natl. Acad. Sci. U.S.A. 86:8314-8318(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS PDGFA AND PDGFB RECEPTOR IN CELL PROLIFERATION AND CHEMOTAXIS, SUBCELLULAR LOCATION.
[10]"Binding of SH2 domains of phospholipase C gamma 1, GAP, and Src to activated growth factor receptors."
Anderson D., Koch C.A., Grey L., Ellis C., Moran M.F., Pawson T.
Science 250:979-982(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PLCG1 AND SRC.
[11]"Platelet-derived growth factor (PDGF) stimulates PDGF receptor subunit dimerization and intersubunit trans-phosphorylation."
Kelly J.D., Haldeman B.A., Grant F.J., Murray M.J., Seifert R.A., Bowen-Pope D.F., Cooper J.A., Kazlauskas A.
J. Biol. Chem. 266:8987-8992(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDGFRA; PDGFA AND PDGFB, FUNCTION AS RECEPTOR FOR PDGFA AND PDGFB, AUTOPHOSPHORYLATION.
[12]"Tyrosine mutations within the alpha platelet-derived growth factor receptor kinase insert domain abrogate receptor-associated phosphatidylinositol-3 kinase activity without affecting mitogenic or chemotactic signal transduction."
Yu J.C., Heidaran M.A., Pierce J.H., Gutkind J.S., Lombardi D., Ruggiero M., Aaronson S.A.
Mol. Cell. Biol. 11:3780-3785(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS PDGFB RECEPTOR IN CHEMOTAXIS; CELL PROLIFERATION; PHOSPHORYLATION OF PLCG1; ACTIVATION OF PHOSPHATIDYLINOSITOL 3-KINASE AND REGULATION OF PHOSPHATIDYLINOSITOL METABOLISM, INTERACTION WITH PIK3R, PHOSPHORYLATION AT TYR-731 AND TYR-742, MUTAGENESIS OF TYR-731 AND TYR-742.
[13]"Mechanism of platelet-derived growth factor (PDGF) AA, AB, and BB binding to alpha and beta PDGF receptor."
Fretto L.J., Snape A.J., Tomlinson J.E., Seroogy J.J., Wolf D.L., LaRochelle W.J., Giese N.A.
J. Biol. Chem. 268:3625-3631(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDGFA AND PDGFB.
[14]"Negative feedback regulation of human platelets via autocrine activation of the platelet-derived growth factor alpha-receptor."
Vassbotn F.S., Havnen O.K., Heldin C.H., Holmsen H.
J. Biol. Chem. 269:13874-13879(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS PDGFA RECEPTOR IN REGULATION OF PLATELET ACTIVATION, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, TISSUE SPECIFICITY.
[15]"Demonstration of functionally different interactions between phospholipase C-gamma and the two types of platelet-derived growth factor receptors."
Eriksson A., Naanberg E., Roennstrand L., Engstroem U., Hellman U., Rupp E., Carpenter G., Heldin C.H., Claesson-Welsh L.
J. Biol. Chem. 270:7773-7781(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-988 AND TYR-1018, INTERACTION WITH PLCG1.
[16]"Maximal PDGF-induced lung fibroblast chemotaxis requires PDGF receptor-alpha."
Osornio-Vargas A.R., Lindroos P.M., Coin P.G., Badgett A., Hernandez-Rodriguez N.A., Bonner J.C.
Am. J. Physiol. 271:L93-L99(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PROMOTING CHEMOTAXIS.
[17]"Grb7 is a downstream signaling component of platelet-derived growth factor alpha- and beta-receptors."
Yokote K., Margolis B., Heldin C.H., Claesson-Welsh L.
J. Biol. Chem. 271:30942-30949(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GRB7 AND PIK3R1.
[18]"Phosphorylation of tyrosine 720 in the platelet-derived growth factor alpha receptor is required for binding of Grb2 and SHP-2 but not for activation of Ras or cell proliferation."
Bazenet C.E., Gelderloos J.A., Kazlauskas A.
Mol. Cell. Biol. 16:6926-6936(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF PTPN11; ACTIVATION OF HRAS AND REGULATION OF CELL PROLIFERATION, PHOSPHORYLATION AT TYR-720, INTERACTION WITH GRB2; PTPN11; PLCG1 AND PIK3R1, AUTOPHOSPHORYLATION, MUTAGENESIS OF TYR-720.
[19]"Differential interaction of CrkII adaptor protein with platelet-derived growth factor alpha- and beta-receptors is determined by its internal tyrosine phosphorylation."
Matsumoto T., Yokote K., Take A., Takemoto M., Asaumi S., Hashimoto Y., Matsuda M., Saito Y., Mori S.
Biochem. Biophys. Res. Commun. 270:28-33(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CRK, PHOSPHORYLATION AT TYR-762, MUTAGENESIS OF TYR-762.
[20]"Shf, a Shb-like adapter protein, is involved in PDGF-alpha-receptor regulation of apoptosis."
Lindholm C.K., Frantz J.D., Shoelson S.E., Welsh M.
Biochem. Biophys. Res. Commun. 278:537-543(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SHF, PHOSPHORYLATION AT TYR-720.
[21]"Platelet-derived-growth-factor-induced signalling in human platelets: phosphoinositide-3-kinase-dependent inhibition of platelet activation."
Selheim F., Fukami M.H., Holmsen H., Vassbotn F.S.
Biochem. J. 350:469-475(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PLATELET ACTIVATION.
[22]"Src family kinases negatively regulate platelet-derived growth factor alpha receptor-dependent signaling and disease progression."
Rosenkranz S., Ikuno Y., Leong F.L., Klinghoffer R.A., Miyake S., Band H., Kazlauskas A.
J. Biol. Chem. 275:9620-9627(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ACTIVATION OF MAPK1/ERK2 AND/OR MAPK3/ERK1, DEGRADATION, PHOSPHORYLATION AT TYR-572 AND TYR-574, MUTAGENESIS OF TYR-572 AND TYR-574.
[23]"Platelet-derived growth factor C (PDGF-C), a novel growth factor that binds to PDGF alpha and beta receptor."
Gilbertson D.G., Duff M.E., West J.W., Kelly J.D., Sheppard P.O., Hofstrand P.D., Gao Z., Shoemaker K., Bukowski T.R., Moore M., Feldhaus A.L., Humes J.M., Palmer T.E., Hart C.E.
J. Biol. Chem. 276:27406-27414(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A RECEPTOR FOR PDGFC, INTERACTION WITH PDGFC.
[24]"The role of c-Src in platelet-derived growth factor alpha receptor internalization."
Avrov K., Kazlauskas A.
Exp. Cell Res. 291:426-434(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SRC, MUTAGENESIS OF TYR-572 AND TYR-574.
[25]"A tyrosine kinase created by fusion of the PDGFRA and FIP1L1 genes as a therapeutic target of imatinib in idiopathic hypereosinophilic syndrome."
Cools J., DeAngelo D.J., Gotlib J., Stover E.H., Legare R.D., Cortes J., Kutok J., Clark J., Galinsky I., Griffin J.D., Cross N.C., Tefferi A., Malone J., Alam R., Schrier S.L., Schmid J., Rose M., Vandenberghe P. expand/collapse author list , Verhoef G., Boogaerts M., Wlodarska I., Kantarjian H., Marynen P., Coutre S.E., Stone R., Gilliland D.G.
N. Engl. J. Med. 348:1201-1214(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN HES.
[26]"PDGFRA activating mutations in gastrointestinal stromal tumors."
Heinrich M.C., Corless C.L., Duensing A., McGreevey L., Chen C.J., Joseph N., Singer S., Griffith D.J., Haley A., Town A., Demetri G.D., Fletcher C.D., Fletcher J.A.
Science 299:708-710(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF AKT1; MAP KINASES; STAT1 AND STAT3, INVOLVEMENT IN GIST, VARIANTS ASP-561; VAL-842; 842-ASP--HIS-845 DEL AND 845-HIS--PRO-448 DEL, CHARACTERIZATION OF VARIANTS ASP-561; VAL-842; 842-ASP--HIS-845 DEL AND 845-HIS--PRO-448 DEL.
[27]"PDGFRA mutations in gastrointestinal stromal tumors: frequency, spectrum and in vitro sensitivity to imatinib."
Corless C.L., Schroeder A., Griffith D., Town A., McGreevey L., Harrell P., Shiraga S., Bainbridge T., Morich J., Heinrich M.C.
J. Clin. Oncol. 23:5357-5364(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN GIST, VARIANTS ASP-561; LYS-659; TYR-842; VAL-842; 842-ASP--HIS-845 DEL 845-HIS--PRO-448 DEL AND CYS-849, CHARACTERIZATION OF VARIANTS ASP-561; LYS-659; TYR-842; VAL-842; 842-ASP--HIS-845 DEL 845-HIS--PRO-448 DEL AND CYS-849, ENZYME REGULATION.
[28]"PI3-kinase/Akt-dependent antiapoptotic signaling by the PDGF alpha receptor is negatively regulated by Src family kinases."
Vantler M., Huntgeburth M., Caglayan E., Ten Freyhaus H., Schnabel P., Rosenkranz S.
FEBS Lett. 580:6769-6776(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL SURVIVAL.
[29]"The glycoprotein B disintegrin-like domain binds beta 1 integrin to mediate cytomegalovirus entry."
Feire A.L., Roy R.M., Manley K., Compton T.
J. Virol. 84:10026-10037(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HHV-5 GB.
[30]"Novel imatinib-sensitive PDGFRA-activating point mutations in hypereosinophilic syndrome induce growth factor independence and leukemia-like disease."
Elling C., Erben P., Walz C., Frickenhaus M., Schemionek M., Stehling M., Serve H., Cross N.C., Hochhaus A., Hofmann W.K., Berdel W.E., Muller-Tidow C., Reiter A., Koschmieder S.
Blood 117:2935-2943(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF STAT 5A AND/OR STAT5B, ROLE IN HYPEREOSINOPHILIC SYNDROME, VARIANTS GLY-481; PRO-507; MET-562; ARG-570; GLN-650; SER-659; PRO-705; GLY-748 AND SER-849, CHARACTERIZATION OF VARIANTS GLY-481; PRO-507; MET-562; ARG-570; GLN-650; SER-659; PRO-705; GLY-748 AND SER-849, ENZYME REGULATION.
[31]"The Casitas B lineage lymphoma (Cbl) mutant G306E enhances osteogenic differentiation in human mesenchymal stromal cells in part by decreased Cbl-mediated platelet-derived growth factor receptor alpha and fibroblast growth factor receptor 2 ubiquitination."
Severe N., Miraoui H., Marie P.J.
J. Biol. Chem. 286:24443-24450(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL DIFFERENTIATION, UBIQUITINATION.
[32]"The low frequency of clinical resistance to PDGFR inhibitors in myeloid neoplasms with abnormalities of PDGFRA might be related to the limited repertoire of possible PDGFRA kinase domain mutations in vitro."
von Bubnoff N., Gorantla S.P., Engh R.A., Oliveira T.M., Thone S., Aberg E., Peschel C., Duyster J.
Oncogene 30:933-943(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE IN DISEASE, CHARACTERIZATION OF VARIANT VAL-842, ENZYME REGULATION.
[33]"Signal transduction via platelet-derived growth factor receptors."
Heldin C.H., Ostman A., Ronnstrand L.
Biochim. Biophys. Acta 1378:F79-113(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON SIGNALING AND AUTOPHOSPHORYLATION.
[34]"PDGF receptors-mediators of autocrine tumor growth and regulators of tumor vasculature and stroma."
Ostman A.
Cytokine Growth Factor Rev. 15:275-286(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON ROLE IN DISEASE AND ENZYME REGULATION.
[35]"PDGF receptors as targets in tumor treatment."
Ostman A., Heldin C.H.
Adv. Cancer Res. 97:247-274(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON ROLE IN DISEASE AND ENZYME REGULATION.
[36]"Role of platelet-derived growth factors in physiology and medicine."
Andrae J., Gallini R., Betsholtz C.
Genes Dev. 22:1276-1312(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION IN DEVELOPMENT AND DISEASE; LIGANDS AND SIGNALING PATHWAYS.
[37]"Structural determinants of the Na+/H+ exchanger regulatory factor interaction with the beta 2 adrenergic and platelet-derived growth factor receptors."
Karthikeyan S., Leung T., Ladias J.A.A.
J. Biol. Chem. 277:18973-18978(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1185-1189 IN COMPLEX WITH SLC9A3R1 AND PDGFRB.
[38]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASP-79; ASP-426; PRO-478; CYS-764; ARG-829; LYS-996 AND ASN-1071.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS3495.1. [P16234-1]
PIRPFHUGA. A40162.
RefSeqNP_006197.1. NM_006206.4. [P16234-1]
XP_005265800.1. XM_005265743.1. [P16234-1]
UniGeneHs.74615.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GQ5X-ray2.20
ProteinModelPortalP16234.
SMRP16234. Positions 26-516, 553-997.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111182. 26 interactions.
DIPDIP-5736N.
IntActP16234. 12 interactions.
MINTMINT-4529366.
STRING9606.ENSP00000257290.

Chemistry

BindingDBP16234.
ChEMBLCHEMBL2007.
DrugBankDB00102. Becaplermin.
DB00619. Imatinib.
DB01268. Sunitinib.
GuidetoPHARMACOLOGY1803.

PTM databases

PhosphoSiteP16234.

Polymorphism databases

DMDM129892.

Proteomic databases

MaxQBP16234.
PaxDbP16234.
PRIDEP16234.

Protocols and materials databases

DNASU5156.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000257290; ENSP00000257290; ENSG00000134853. [P16234-1]
ENST00000508170; ENSP00000425648; ENSG00000134853. [P16234-2]
ENST00000509490; ENSP00000424218; ENSG00000134853. [P16234-3]
GeneID5156.
KEGGhsa:5156.
UCSCuc003hal.3. human. [P16234-2]
uc003han.4. human. [P16234-1]

Organism-specific databases

CTD5156.
GeneCardsGC04P055095.
HGNCHGNC:8803. PDGFRA.
HPACAB018143.
MIM173490. gene.
606764. phenotype.
607685. phenotype.
neXtProtNX_P16234.
Orphanet44890. Gastrointestinal stromal tumor.
3260. Idiopathic hypereosinophilic syndrome.
168947. Myeloid neoplasm associated with PDGFRA rearrangement.
99860. Precursor B-cell acute lymphoblastic leukemia.
PharmGKBPA33147.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000112009.
HOVERGENHBG004335.
InParanoidP16234.
KOK04363.
OMADYECAAR.
OrthoDBEOG71G9T1.
PhylomeDBP16234.
TreeFamTF325768.

Enzyme and pathway databases

BRENDA2.7.10.1. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.
SignaLinkP16234.

Gene expression databases

ArrayExpressP16234.
BgeeP16234.
CleanExHS_PDGFRA.
GenevestigatorP16234.

Family and domain databases

Gene3D2.60.40.10. 4 hits.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
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.
IPR016243. Tyr_kinase_CSF1/PDGF_rcpt.
IPR001824. Tyr_kinase_rcpt_3_CS.
[Graphical view]
PANTHERPTHR24416:SF52. PTHR24416:SF52. 1 hit.
PfamPF07679. I-set. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFPIRSF500950. Alpha-PDGF_receptor. 1 hit.
PIRSF000615. TyrPK_CSF1-R. 1 hit.
SMARTSM00409. IG. 2 hits.
SM00408. IGc2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 2 hits.
PROSITEPS50835. 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.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPDGFRA. human.
EvolutionaryTraceP16234.
GeneWikiPDGFRA.
GenomeRNAi5156.
NextBio19946.
PROP16234.
SOURCESearch...

Entry information

Entry namePGFRA_HUMAN
AccessionPrimary (citable) accession number: P16234
Secondary accession number(s): B2RE69 expand/collapse secondary AC list , E9PBH0, Q6P4H5, Q96KZ7, Q9UD28
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: July 9, 2014
This is version 167 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries