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P16234

- PGFRA_HUMAN

UniProt

P16234 - PGFRA_HUMAN

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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

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 homodimerization activity Source: BHF-UCL
  6. transmembrane receptor protein tyrosine kinase activity Source: UniProtKB
  7. vascular endothelial growth factor-activated receptor activity Source: BHF-UCL
  8. 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. hematopoietic progenitor cell differentiation Source: Ensembl
  16. innate immune response Source: Reactome
  17. in utero embryonic development Source: Ensembl
  18. Leydig cell differentiation Source: Ensembl
  19. lung development Source: Ensembl
  20. luteinization Source: UniProtKB
  21. male genitalia development Source: Ensembl
  22. metanephric glomerular capillary formation Source: UniProtKB
  23. negative regulation of platelet activation Source: UniProtKB
  24. neurotrophin TRK receptor signaling pathway Source: Reactome
  25. odontogenesis of dentin-containing tooth Source: Ensembl
  26. palate development Source: Ensembl
  27. peptidyl-tyrosine phosphorylation Source: UniProtKB
  28. phosphatidylinositol-mediated signaling Source: UniProtKB
  29. platelet aggregation Source: UniProtKB
  30. platelet-derived growth factor receptor-alpha signaling pathway Source: UniProtKB
  31. platelet-derived growth factor receptor signaling pathway Source: BHF-UCL
  32. positive regulation of cell migration Source: UniProtKB
  33. positive regulation of cell proliferation Source: UniProtKB
  34. positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway Source: BHF-UCL
  35. positive regulation of cytosolic calcium ion concentration Source: UniProtKB
  36. positive regulation of DNA replication Source: BHF-UCL
  37. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  38. positive regulation of fibroblast proliferation Source: BHF-UCL
  39. positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
  40. positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
  41. positive regulation of phospholipase C activity Source: UniProtKB
  42. protein autophosphorylation Source: UniProtKB
  43. regulation of actin cytoskeleton reorganization Source: UniProtKB
  44. regulation of chemotaxis Source: UniProtKB
  45. regulation of mesenchymal stem cell differentiation Source: UniProtKB
  46. retina vasculature development in camera-type eye Source: UniProtKB
  47. signal transduction involved in regulation of gene expression Source: Ensembl
  48. viral process Source: UniProtKB-KW
  49. wound healing Source: UniProtKB
Complete GO annotation...

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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 528505ExtracellularSequence AnalysisAdd
BLAST
Transmembranei529 – 54921HelicalSequence AnalysisAdd
BLAST
Topological domaini550 – 1089540CytoplasmicSequence AnalysisAdd
BLAST

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. microvillus Source: Ensembl
  7. nucleus Source: UniProtKB
  8. plasma membrane Source: Reactome
Complete GO annotation...

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

BgeeiP16234.
CleanExiHS_PDGFRA.
ExpressionAtlasiP16234. baseline and differential.
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
EGFRP005333EBI-2861522,EBI-297353
PDGFAP040856EBI-2861522,EBI-2881386
PDGFBP0112711EBI-2861522,EBI-1554925
PDGFCQ9NRA12EBI-2861522,EBI-8833587

Protein-protein interaction databases

BioGridi111182. 26 interactions.
DIPiDIP-5736N.
IntActiP16234. 17 interactions.
MINTiMINT-4529366.
STRINGi9606.ENSP00000257290.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GQ5X-ray2.20
ProteinModelPortaliP16234.
SMRiP16234. Positions 26-509, 553-997.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16234.

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.
GeneTreeiENSGT00760000118923.
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

        10         20         30         40         50
MGTSHPAFLV LGCLLTGLSL ILCQLSLPSI LPNENEKVVQ LNSSFSLRCF
60 70 80 90 100
GESEVSWQYP MSEEESSDVE IRNEENNSGL FVTVLEVSSA SAAHTGLYTC
110 120 130 140 150
YYNHTQTEEN ELEGRHIYIY VPDPDVAFVP LGMTDYLVIV EDDDSAIIPC
160 170 180 190 200
RTTDPETPVT LHNSEGVVPA SYDSRQGFNG TFTVGPYICE ATVKGKKFQT
210 220 230 240 250
IPFNVYALKA TSELDLEMEA LKTVYKSGET IVVTCAVFNN EVVDLQWTYP
260 270 280 290 300
GEVKGKGITM LEEIKVPSIK LVYTLTVPEA TVKDSGDYEC AARQATREVK
310 320 330 340 350
EMKKVTISVH EKGFIEIKPT FSQLEAVNLH EVKHFVVEVR AYPPPRISWL
360 370 380 390 400
KNNLTLIENL TEITTDVEKI QEIRYRSKLK LIRAKEEDSG HYTIVAQNED
410 420 430 440 450
AVKSYTFELL TQVPSSILDL VDDHHGSTGG QTVRCTAEGT PLPDIEWMIC
460 470 480 490 500
KDIKKCNNET SWTILANNVS NIITEIHSRD RSTVEGRVTF AKVEETIAVR
510 520 530 540 550
CLAKNLLGAE NRELKLVAPT LRSELTVAAA VLVLLVIVII SLIVLVVIWK
560 570 580 590 600
QKPRYEIRWR VIESISPDGH EYIYVDPMQL PYDSRWEFPR DGLVLGRVLG
610 620 630 640 650
SGAFGKVVEG TAYGLSRSQP VMKVAVKMLK PTARSSEKQA LMSELKIMTH
660 670 680 690 700
LGPHLNIVNL LGACTKSGPI YIITEYCFYG DLVNYLHKNR DSFLSHHPEK
710 720 730 740 750
PKKELDIFGL NPADESTRSY VILSFENNGD YMDMKQADTT QYVPMLERKE
760 770 780 790 800
VSKYSDIQRS LYDRPASYKK KSMLDSEVKN LLSDDNSEGL TLLDLLSFTY
810 820 830 840 850
QVARGMEFLA SKNCVHRDLA ARNVLLAQGK IVKICDFGLA RDIMHDSNYV
860 870 880 890 900
SKGSTFLPVK WMAPESIFDN LYTTLSDVWS YGILLWEIFS LGGTPYPGMM
910 920 930 940 950
VDSTFYNKIK SGYRMAKPDH ATSEVYEIMV KCWNSEPEKR PSFYHLSEIV
960 970 980 990 1000
ENLLPGQYKK SYEKIHLDFL KSDHPAVARM RVDSDNAYIG VTYKNEEDKL
1010 1020 1030 1040 1050
KDWEGGLDEQ RLSADSGYII PLPDIDPVPE EEDLGKRNRH SSQTSEESAI
1060 1070 1080
ETGSSSSTFI KREDETIEDI DMMDDIGIDS SDLVEDSFL
Length:1,089
Mass (Da):122,670
Last modified:April 1, 1990 - v1
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.Curated

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:
EMBLi
GenBanki
DDBJi
Links Updated
M22734 mRNA. Translation: AAA60048.1.
M21574 mRNA. Translation: AAA96715.1.
D50017 Genomic DNA. Translation: BAA08742.1.
AK316578 mRNA. Translation: BAG38166.1.
AC098587 Genomic DNA. No translation available.
AC138779 Genomic DNA. No translation available.
BC015186 mRNA. Translation: AAH15186.1.
BC063414 mRNA. Translation: AAH63414.1.
AY229892 mRNA. Translation: AAP69563.1. Different initiation.
CCDSiCCDS3495.1. [P16234-1]
PIRiA40162. PFHUGA.
RefSeqiNP_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:
EMBLi
GenBanki
DDBJi
Links Updated
M22734 mRNA. Translation: AAA60048.1 .
M21574 mRNA. Translation: AAA96715.1 .
D50017 Genomic DNA. Translation: BAA08742.1 .
AK316578 mRNA. Translation: BAG38166.1 .
AC098587 Genomic DNA. No translation available.
AC138779 Genomic DNA. No translation available.
BC015186 mRNA. Translation: AAH15186.1 .
BC063414 mRNA. Translation: AAH63414.1 .
AY229892 mRNA. Translation: AAP69563.1 . Different initiation.
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:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GQ5 X-ray 2.20
ProteinModelPortali P16234.
SMRi P16234. Positions 26-509, 553-997.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111182. 26 interactions.
DIPi DIP-5736N.
IntActi P16234. 17 interactions.
MINTi MINT-4529366.
STRINGi 9606.ENSP00000257290.

Chemistry

BindingDBi P16234.
ChEMBLi CHEMBL2095189.
DrugBanki DB00102. Becaplermin.
DB00619. Imatinib.
DB06589. Pazopanib.
DB08901. Ponatinib.
DB08896. Regorafenib.
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.
GeneTreei ENSGT00760000118923.
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

Bgeei P16234.
CleanExi HS_PDGFRA.
ExpressionAtlasi P16234. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 170 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