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P16234

- PGFRA_HUMAN

UniProt

P16234 - PGFRA_HUMAN

Protein

Platelet-derived growth factor receptor alpha

Gene

PDGFRA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    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

    Catalytic activityi

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

    Enzyme 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)LengthDescriptionGraphical viewFeature identifierActions
    Sitei578 – 5792Breakpoint for interstitial deletion to form the FIP1L1-PDGFRA fusion protein
    Binding sitei627 – 6271ATPPROSITE-ProRule annotation
    Active sitei818 – 8181Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi599 – 6079ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. platelet-derived growth factor alpha-receptor activity Source: UniProtKB
    3. platelet-derived growth factor binding Source: UniProtKB
    4. platelet-derived growth factor receptor binding Source: BHF-UCL
    5. protein binding Source: UniProtKB
    6. protein homodimerization activity Source: BHF-UCL
    7. transmembrane receptor protein tyrosine kinase activity Source: UniProtKB
    8. vascular endothelial growth factor-activated receptor activity Source: BHF-UCL
    9. vascular endothelial growth factor binding Source: BHF-UCL

    GO - Biological processi

    1. adrenal gland development Source: Ensembl
    2. cardiac myofibril assembly Source: UniProtKB
    3. cell activation Source: BHF-UCL
    4. cell chemotaxis Source: UniProtKB
    5. cellular response to amino acid stimulus Source: Ensembl
    6. embryonic cranial skeleton morphogenesis Source: UniProtKB
    7. embryonic digestive tract morphogenesis Source: UniProtKB
    8. embryonic skeletal system morphogenesis Source: UniProtKB
    9. epidermal growth factor receptor signaling pathway Source: Reactome
    10. estrogen metabolic process Source: Ensembl
    11. extracellular matrix organization Source: Ensembl
    12. face morphogenesis Source: Ensembl
    13. Fc-epsilon receptor signaling pathway Source: Reactome
    14. fibroblast growth factor receptor signaling pathway Source: Reactome
    15. innate immune response Source: Reactome
    16. in utero embryonic development Source: Ensembl
    17. Leydig cell differentiation Source: Ensembl
    18. lung development Source: Ensembl
    19. luteinization Source: UniProtKB
    20. male genitalia development Source: Ensembl
    21. metanephric glomerular capillary formation Source: UniProtKB
    22. negative regulation of platelet activation Source: UniProtKB
    23. neurotrophin TRK receptor signaling pathway Source: Reactome
    24. odontogenesis of dentin-containing tooth Source: Ensembl
    25. palate development Source: Ensembl
    26. peptidyl-tyrosine phosphorylation Source: UniProtKB
    27. phosphatidylinositol-mediated signaling Source: UniProtKB
    28. platelet aggregation Source: UniProtKB
    29. platelet-derived growth factor receptor-alpha signaling pathway Source: UniProtKB
    30. platelet-derived growth factor receptor signaling pathway Source: BHF-UCL
    31. positive regulation of cell migration Source: UniProtKB
    32. positive regulation of cell proliferation Source: UniProtKB
    33. positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway Source: BHF-UCL
    34. positive regulation of cytosolic calcium ion concentration Source: UniProtKB
    35. positive regulation of DNA replication Source: BHF-UCL
    36. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
    37. positive regulation of fibroblast proliferation Source: BHF-UCL
    38. positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
    39. positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
    40. positive regulation of phospholipase C activity Source: UniProtKB
    41. protein autophosphorylation Source: UniProtKB
    42. regulation of actin cytoskeleton reorganization Source: UniProtKB
    43. regulation of chemotaxis Source: UniProtKB
    44. regulation of mesenchymal stem cell differentiation Source: UniProtKB
    45. retina vasculature development in camera-type eye Source: UniProtKB
    46. signal transduction involved in regulation of gene expression Source: Ensembl
    47. viral process Source: UniProtKB-KW
    48. wound healing Source: UniProtKB

    Keywords - Molecular functioni

    Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Chemotaxis, Host-virus interaction

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 2681.
    ReactomeiREACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_16888. Signaling by PDGF.
    REACT_17025. Downstream signal transduction.
    REACT_75829. PIP3 activates AKT signaling.
    SignaLinkiP16234.

    Names & Taxonomyi

    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
    Gene namesi
    Name:PDGFRA
    Synonyms:PDGFR2, RHEPDGFRA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:8803. PDGFRA.

    Subcellular locationi

    Cell membrane 3 Publications; Single-pass type I membrane protein 3 Publications
    Note: The activated receptor is rapidly internalized and degraded.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. external side of plasma membrane Source: Ensembl
    3. integral component of plasma membrane Source: BHF-UCL
    4. intrinsic component of plasma membrane Source: UniProtKB
    5. membrane Source: UniProtKB
    6. nucleus Source: UniProtKB
    7. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    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.2 Publications
    Note: The gene represented in this entry may be involved in disease pathogenesis. Mutations causing PDGFRA constitutive activation have been found in gastrointestinal stromal tumors lacking KIT mutations (PubMed:12522257).1 Publication
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti561 – 5611V → D in a GIST sample; constitutively activated kinase. 2 Publications
    VAR_066462
    Natural varianti659 – 6591N → K in GIST sample; constitutively activated kinase. 1 Publication
    VAR_066466
    Natural varianti842 – 8454Missing in a GIST sample; constitutively activated kinase. 1 Publication
    VAR_066470
    Natural varianti842 – 8421D → V in a GIST sample; imatinib resistant, constitutively activated kinase. 2 Publications
    VAR_066471
    Natural varianti842 – 8421D → Y in a GIST sample; imatinib sensitive, constitutively activated kinase. 1 Publication
    VAR_066472
    Natural varianti845 – 8484Missing in a GIST sample; constitutively activated kinase.
    VAR_066473
    Natural varianti849 – 8491Y → C in GIST. 1 Publication
    VAR_066474

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi572 – 5721Y → F: Abolishes interaction with SRC-family members and impairs internalization of the activated receptor; when associated with F-574. 2 Publications
    Mutagenesisi574 – 5741Y → F: Abolishes interaction with SRC-family members and impairs internalization of the activated receptor; when associated with F-572. 2 Publications
    Mutagenesisi720 – 7201Y → F: Strongly reduced interaction with PTPN11 and GRB2. 1 Publication
    Mutagenesisi731 – 7311Y → F: No effect on autophosphorylation and phosphorylation of PLCG1. Abolishes activation of phosphatidylinositol 3-kinase. 1 Publication
    Mutagenesisi742 – 7421Y → F: No effect on autophosphorylation and phosphorylation of PLCG1. Abolishes activation of phosphatidylinositol 3-kinase. 1 Publication
    Mutagenesisi762 – 7621Y → F: Abolishes interaction with CRK. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    MIMi606764. phenotype.
    607685. phenotype.
    Orphaneti44890. Gastrointestinal stromal tumor.
    3260. Idiopathic hypereosinophilic syndrome.
    168947. Myeloid neoplasm associated with PDGFRA rearrangement.
    99860. Precursor B-cell acute lymphoblastic leukemia.
    PharmGKBiPA33147.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Add
    BLAST
    Chaini24 – 10891066Platelet-derived growth factor receptor alphaPRO_0000016760Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi42 – 421N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi49 ↔ 100PROSITE-ProRule annotation
    Glycosylationi76 – 761N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi103 – 1031N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi150 ↔ 189PROSITE-ProRule annotation
    Glycosylationi179 – 1791N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi235 ↔ 290PROSITE-ProRule annotation
    Glycosylationi353 – 3531N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi359 – 3591N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi435 ↔ 501PROSITE-ProRule annotation
    Glycosylationi458 – 4581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi468 – 4681N-linked (GlcNAc...)Sequence Analysis
    Modified residuei555 – 5551Phosphotyrosine
    Modified residuei572 – 5721Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei574 – 5741Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei582 – 5821Phosphotyrosine
    Modified residuei720 – 7201Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei731 – 7311Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei742 – 7421Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei754 – 7541Phosphotyrosine; by autocatalysis
    Modified residuei762 – 7621Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei768 – 7681Phosphotyrosine; by autocatalysis
    Modified residuei849 – 8491Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei944 – 9441Phosphotyrosine
    Modified residuei958 – 9581Phosphotyrosine
    Modified residuei962 – 9621Phosphotyrosine
    Modified residuei988 – 9881Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei993 – 9931Phosphotyrosine
    Modified residuei1018 – 10181Phosphotyrosine; by autocatalysis1 Publication

    Post-translational modificationi

    N-glycosylated.
    Ubiquitinated, leading to its 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

    MaxQBiP16234.
    PaxDbiP16234.
    PRIDEiP16234.

    PTM databases

    PhosphoSiteiP16234.

    Expressioni

    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

    ArrayExpressiP16234.
    BgeeiP16234.
    CleanExiHS_PDGFRA.
    GenevestigatoriP16234.

    Organism-specific databases

    HPAiCAB018143.

    Interactioni

    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. Interacts with human cytomegalovirus/HHV-5 envelop glycoprotein B/gB.By similarity15 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CRKP461084EBI-2861522,EBI-886
    CRKLP461093EBI-2861522,EBI-910
    PDGFAP040856EBI-2861522,EBI-2881386
    PDGFBP0112711EBI-2861522,EBI-1554925
    PDGFCQ9NRA12EBI-2861522,EBI-8833587

    Protein-protein interaction databases

    BioGridi111182. 26 interactions.
    DIPiDIP-5736N.
    IntActiP16234. 16 interactions.
    MINTiMINT-4529366.
    STRINGi9606.ENSP00000257290.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GQ5X-ray2.20
    ProteinModelPortaliP16234.
    SMRiP16234. Positions 26-516, 553-997.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP16234.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini24 – 528505ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini550 – 1089540CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei529 – 54921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini24 – 11390Ig-like C2-type 1Add
    BLAST
    Domaini117 – 20185Ig-like C2-type 2Add
    BLAST
    Domaini202 – 306105Ig-like C2-type 3Add
    BLAST
    Domaini319 – 41092Ig-like C2-type 4Add
    BLAST
    Domaini414 – 517104Ig-like C2-type 5Add
    BLAST
    Domaini593 – 954362Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1041 – 108747Ser-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000112009.
    HOVERGENiHBG004335.
    InParanoidiP16234.
    KOiK04363.
    OMAiDYECAAR.
    OrthoDBiEOG71G9T1.
    PhylomeDBiP16234.
    TreeFamiTF325768.

    Family and domain databases

    Gene3Di2.60.40.10. 4 hits.
    InterProiIPR007110. 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]
    PANTHERiPTHR24416:SF52. PTHR24416:SF52. 1 hit.
    PfamiPF07679. I-set. 2 hits.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view]
    PIRSFiPIRSF500950. Alpha-PDGF_receptor. 1 hit.
    PIRSF000615. TyrPK_CSF1-R. 1 hit.
    SMARTiSM00409. IG. 2 hits.
    SM00408. IGc2. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 2 hits.
    PROSITEiPS50835. 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]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    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

    MGTSHPAFLV LGCLLTGLSL ILCQLSLPSI LPNENEKVVQ LNSSFSLRCF     50
    GESEVSWQYP MSEEESSDVE IRNEENNSGL FVTVLEVSSA SAAHTGLYTC 100
    YYNHTQTEEN ELEGRHIYIY VPDPDVAFVP LGMTDYLVIV EDDDSAIIPC 150
    RTTDPETPVT LHNSEGVVPA SYDSRQGFNG TFTVGPYICE ATVKGKKFQT 200
    IPFNVYALKA TSELDLEMEA LKTVYKSGET IVVTCAVFNN EVVDLQWTYP 250
    GEVKGKGITM LEEIKVPSIK LVYTLTVPEA TVKDSGDYEC AARQATREVK 300
    EMKKVTISVH EKGFIEIKPT FSQLEAVNLH EVKHFVVEVR AYPPPRISWL 350
    KNNLTLIENL TEITTDVEKI QEIRYRSKLK LIRAKEEDSG HYTIVAQNED 400
    AVKSYTFELL TQVPSSILDL VDDHHGSTGG QTVRCTAEGT PLPDIEWMIC 450
    KDIKKCNNET SWTILANNVS NIITEIHSRD RSTVEGRVTF AKVEETIAVR 500
    CLAKNLLGAE NRELKLVAPT LRSELTVAAA VLVLLVIVII SLIVLVVIWK 550
    QKPRYEIRWR VIESISPDGH EYIYVDPMQL PYDSRWEFPR DGLVLGRVLG 600
    SGAFGKVVEG TAYGLSRSQP VMKVAVKMLK PTARSSEKQA LMSELKIMTH 650
    LGPHLNIVNL LGACTKSGPI YIITEYCFYG DLVNYLHKNR DSFLSHHPEK 700
    PKKELDIFGL NPADESTRSY VILSFENNGD YMDMKQADTT QYVPMLERKE 750
    VSKYSDIQRS LYDRPASYKK KSMLDSEVKN LLSDDNSEGL TLLDLLSFTY 800
    QVARGMEFLA SKNCVHRDLA ARNVLLAQGK IVKICDFGLA RDIMHDSNYV 850
    SKGSTFLPVK WMAPESIFDN LYTTLSDVWS YGILLWEIFS LGGTPYPGMM 900
    VDSTFYNKIK SGYRMAKPDH ATSEVYEIMV KCWNSEPEKR PSFYHLSEIV 950
    ENLLPGQYKK SYEKIHLDFL KSDHPAVARM RVDSDNAYIG VTYKNEEDKL 1000
    KDWEGGLDEQ RLSADSGYII PLPDIDPVPE EEDLGKRNRH SSQTSEESAI 1050
    ETGSSSSTFI KREDETIEDI DMMDDIGIDS SDLVEDSFL 1089
    Length:1,089
    Mass (Da):122,670
    Last modified:April 1, 1990 - v1
    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

    Sequence cautioni

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

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti79 – 791G → D.1 Publication
    Corresponds to variant rs36035373 [ dbSNP | Ensembl ].
    VAR_042032
    Natural varianti426 – 4261G → D.1 Publication
    Corresponds to variant rs55865821 [ dbSNP | Ensembl ].
    VAR_042033
    Natural varianti478 – 4781S → P.3 Publications
    Corresponds to variant rs35597368 [ dbSNP | Ensembl ].
    VAR_034378
    Natural varianti481 – 4811R → G in a hypereosinophilic syndrome sample; does not lead to constitutive kinase activation. 1 Publication
    VAR_066460
    Natural varianti507 – 5071L → P in a hypereosinophilic syndrome sample; does not lead to constitutive kinase activation. 1 Publication
    VAR_066461
    Natural varianti561 – 5611V → D in a GIST sample; constitutively activated kinase. 2 Publications
    VAR_066462
    Natural varianti562 – 5621I → M in a hypereosinophilic syndrome sample; does not lead to constitutive kinase activation. 1 Publication
    VAR_066463
    Natural varianti570 – 5701H → R in a hypereosinophilic syndrome sample; does not lead to constitutive kinase activation. 1 Publication
    VAR_066464
    Natural varianti650 – 6501H → Q in a hypereosinophilic syndrome sample; constitutively activated kinase. 1 Publication
    VAR_066465
    Natural varianti659 – 6591N → K in GIST sample; constitutively activated kinase. 1 Publication
    VAR_066466
    Natural varianti659 – 6591N → S in a hypereosinophilic syndrome sample; constitutively activated kinase. 1 Publication
    VAR_066467
    Natural varianti705 – 7051L → P in a hypereosinophilic syndrome sample; does not lead to constitutive kinase activation. 1 Publication
    VAR_066468
    Natural varianti748 – 7481R → G in a hypereosinophilic syndrome sample; constitutively activated kinase. 1 Publication
    VAR_066469
    Natural varianti764 – 7641R → C.1 Publication
    Corresponds to variant rs34392012 [ dbSNP | Ensembl ].
    VAR_042034
    Natural varianti829 – 8291G → R in a glioblastoma multiforme sample; somatic mutation. 1 Publication
    VAR_042035
    Natural varianti842 – 8454Missing in a GIST sample; constitutively activated kinase. 1 Publication
    VAR_066470
    Natural varianti842 – 8421D → V in a GIST sample; imatinib resistant, constitutively activated kinase. 2 Publications
    VAR_066471
    Natural varianti842 – 8421D → Y in a GIST sample; imatinib sensitive, constitutively activated kinase. 1 Publication
    VAR_066472
    Natural varianti845 – 8484Missing in a GIST sample; constitutively activated kinase.
    VAR_066473
    Natural varianti849 – 8491Y → C in GIST. 1 Publication
    VAR_066474
    Natural varianti849 – 8491Y → S in a hypereosinophilic syndrome sample; constitutively activated kinase. 1 Publication
    VAR_066475
    Natural varianti996 – 9961E → K in a metastatic melanoma sample; somatic mutation. 1 Publication
    VAR_042036
    Natural varianti1071 – 10711D → N in a lung neuroendocrine carcinoma sample; somatic mutation. 1 Publication
    VAR_042037

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei210 – 2189ATSELDLEM → GTCIISFLL in isoform 2. 1 PublicationVSP_007833
    Alternative sequencei219 – 1089871Missing in isoform 2. 1 PublicationVSP_007834Add
    BLAST
    Alternative sequencei720 – 74324YVILS…TTQYV → SGQGCLSSGTLQELSVDLQA RGPC in isoform 3. 1 PublicationVSP_042015Add
    BLAST
    Alternative sequencei744 – 1089346Missing in isoform 3. 1 PublicationVSP_042016Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_006197.1. NM_006206.4. [P16234-1]
    XP_005265800.1. XM_005265743.1. [P16234-1]
    UniGeneiHs.74615.

    Genome annotation databases

    EnsembliENST00000257290; ENSP00000257290; ENSG00000134853. [P16234-1]
    ENST00000508170; ENSP00000425648; ENSG00000134853. [P16234-2]
    ENST00000509490; ENSP00000424218; ENSG00000134853. [P16234-3]
    GeneIDi5156.
    KEGGihsa:5156.
    UCSCiuc003hal.3. human. [P16234-2]
    uc003han.4. human. [P16234-1]

    Polymorphism databases

    DMDMi129892.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSi CCDS3495.1. [P16234-1 ]
    PIRi A40162. PFHUGA.
    RefSeqi NP_006197.1. NM_006206.4. [P16234-1 ]
    XP_005265800.1. XM_005265743.1. [P16234-1 ]
    UniGenei Hs.74615.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GQ5 X-ray 2.20
    ProteinModelPortali P16234.
    SMRi P16234. Positions 26-516, 553-997.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111182. 26 interactions.
    DIPi DIP-5736N.
    IntActi P16234. 16 interactions.
    MINTi MINT-4529366.
    STRINGi 9606.ENSP00000257290.

    Chemistry

    BindingDBi P16234.
    ChEMBLi CHEMBL2007.
    DrugBanki DB00102. Becaplermin.
    DB00619. Imatinib.
    DB01268. Sunitinib.
    GuidetoPHARMACOLOGYi 1803.

    PTM databases

    PhosphoSitei P16234.

    Polymorphism databases

    DMDMi 129892.

    Proteomic databases

    MaxQBi P16234.
    PaxDbi P16234.
    PRIDEi P16234.

    Protocols and materials databases

    DNASUi 5156.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000257290 ; ENSP00000257290 ; ENSG00000134853 . [P16234-1 ]
    ENST00000508170 ; ENSP00000425648 ; ENSG00000134853 . [P16234-2 ]
    ENST00000509490 ; ENSP00000424218 ; ENSG00000134853 . [P16234-3 ]
    GeneIDi 5156.
    KEGGi hsa:5156.
    UCSCi uc003hal.3. human. [P16234-2 ]
    uc003han.4. human. [P16234-1 ]

    Organism-specific databases

    CTDi 5156.
    GeneCardsi GC04P055095.
    HGNCi HGNC:8803. PDGFRA.
    HPAi CAB018143.
    MIMi 173490. gene.
    606764. phenotype.
    607685. phenotype.
    neXtProti NX_P16234.
    Orphaneti 44890. Gastrointestinal stromal tumor.
    3260. Idiopathic hypereosinophilic syndrome.
    168947. Myeloid neoplasm associated with PDGFRA rearrangement.
    99860. Precursor B-cell acute lymphoblastic leukemia.
    PharmGKBi PA33147.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000112009.
    HOVERGENi HBG004335.
    InParanoidi P16234.
    KOi K04363.
    OMAi DYECAAR.
    OrthoDBi EOG71G9T1.
    PhylomeDBi P16234.
    TreeFami TF325768.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 2681.
    Reactomei REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_16888. Signaling by PDGF.
    REACT_17025. Downstream signal transduction.
    REACT_75829. PIP3 activates AKT signaling.
    SignaLinki P16234.

    Miscellaneous databases

    ChiTaRSi PDGFRA. human.
    EvolutionaryTracei P16234.
    GeneWikii PDGFRA.
    GenomeRNAii 5156.
    NextBioi 19946.
    PROi P16234.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P16234.
    Bgeei P16234.
    CleanExi HS_PDGFRA.
    Genevestigatori P16234.

    Family and domain databases

    Gene3Di 2.60.40.10. 4 hits.
    InterProi IPR007110. 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 ]
    PANTHERi PTHR24416:SF52. PTHR24416:SF52. 1 hit.
    Pfami PF07679. I-set. 2 hits.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF500950. Alpha-PDGF_receptor. 1 hit.
    PIRSF000615. TyrPK_CSF1-R. 1 hit.
    SMARTi SM00409. IG. 2 hits.
    SM00408. IGc2. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 2 hits.
    PROSITEi 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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. Cited for: INVOLVEMENT IN HES.
    26. 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.
      , 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.

    Entry informationi

    Entry nameiPGFRA_HUMAN
    AccessioniPrimary (citable) accession number: P16234
    Secondary accession number(s): B2RE69
    , E9PBH0, Q6P4H5, Q96KZ7, Q9UD28
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 169 of the entry and version 1 of the sequence. [Complete history]
    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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3