P16234 (PGFRA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Platelet-derived growth factor receptor alpha
Short name=PDGF-R-alpha
Short name=PDGFR-alpha
EC=2.7.10.1

Alternative name(s):
Alpha platelet-derived growth factor receptor
Alpha-type platelet-derived growth factor receptor
CD140 antigen-like family member A
CD140a antigen
Platelet-derived growth factor alpha receptor
Platelet-derived growth factor receptor 2
Short name=PDGFR-2
CD_antigen=CD140a

Gene names

Name:	PDGFRA
Synonyms:	PDGFR2, RHEPDGFRA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1089 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Tyrosine-protein kinase that acts as a cell-surface receptor for PDGFA, PDGFB and PDGFC and plays an essential role in the regulation of embryonic development, cell proliferation, survival and chemotaxis. Depending on the context, promotes or inhibits cell proliferation and cell migration. Plays an important role in the differentiation of bone marrow-derived mesenchymal stem cells. Required for normal skeleton development and cephalic closure during embryonic development. Required for normal development of the mucosa lining the gastrointestinal tract, and for recruitment of mesenchymal cells and normal development of intestinal villi. Plays a role in cell migration and chemotaxis in wound healing. Plays a role in platelet activation, secretion of agonists from platelet granules, and in thrombin-induced platelet aggregation. Binding of its cognate ligands - homodimeric PDGFA, homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFC -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PIK3R1, PLCG1, and PTPN11. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca2+ and the activation of protein kinase C. Phosphorylates PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and thereby mediates activation of the AKT1 signaling pathway. Mediates activation of HRAS and of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3 and STAT5A and/or STAT5B. Receptor signaling is down-regulated by protein phosphatases that dephosphorylate the receptor and its down-stream effectors, and by rapid internalization of the activated receptor. Ref.9 Ref.11 Ref.12 Ref.14 Ref.15 Ref.17 Ref.20 Ref.21 Ref.22 Ref.25 Ref.27 Ref.29 Ref.30 Ref.31
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Enzyme regulation	Present in an inactive conformation in the absence of bound ligand. Binding of PDGFA and/or PDGFB leads to dimerization and activation by autophosphorylation on tyrosine residues. Inhibited by imatinib, nilotinib and sorafenib. Ref.26 Ref.29 Ref.31
Subunit structure	Interacts with homodimeric PDGFA, PDGFB and PDGFC, and with heterodimers formed by PDGFA and PDGFB. Monomer in the absence of bound ligand. Interaction with dimeric PDGFA, PDGFB and/or PDGFC leads to receptor dimerization, where both PDGFRA homodimers and heterodimers with PDGFRB are observed. Interacts (tyrosine phosphorylated) with SHB (via SH2 domain) By similarity. Interacts (tyrosine phosphorylated) with SHF (via SH2 domain). Interacts (tyrosine phosphorylated) with SRC (via SH2 domain). Interacts (tyrosine phosphorylated) with PIK3R1. Interacts (tyrosine phosphorylated) with PLCG1 (via SH2 domain). Interacts (tyrosine phosphorylated) with CRK, GRB2 and GRB7. Interacts with human cytomegalovirus/HHV-5 envelop glycoprotein B/gB. Ref.1 Ref.2 Ref.10 Ref.11 Ref.12 Ref.13 Ref.16 Ref.17 Ref.18 Ref.19 Ref.22 Ref.23 Ref.28
Subcellular location	Cell membrane; Single-pass type I membrane protein. Note: The activated receptor is rapidly internalized and degraded. Ref.9 Ref.14 Ref.23
Tissue specificity	Detected in platelets (at protein level). Widely expressed. Detected in brain, fibroblasts, smooth muscle, heart, and embryo. Expressed in primary and metastatic colon tumors and in normal colon tissue. Ref.2 Ref.8 Ref.14
Post-translational modification	N-glycosylated. Ubiquitinated, leading to its degradation Probable. Ref.21 Ref.30 Autophosphorylated on tyrosine residues upon ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation at Tyr-731 and Tyr-742 is important for interaction with PIK3R1. Phosphorylation at Tyr-720 and Tyr-754 is important for interaction with PTPN11. Phosphorylation at Tyr-762 is important for interaction with CRK. Phosphorylation at Tyr-572 and Tyr-574 is important for interaction with SRC and SRC family members. Phosphorylation at Tyr-988 and Tyr-1018 is important for interaction with PLCG1. Ref.2 Ref.11 Ref.12 Ref.14 Ref.17 Ref.19
Involvement in disease	A chromosomal aberration involving PDGFRA is found in some cases of hypereosinophilic syndrome. Interstitial chromosomal deletion del4(q12q12) causes the fusion of FIP1L1 and PDGFRA (FIP1L1-PDGFRA). Mutations that cause overexpression and/or constitutive activation of PDGFRA may be a cause of hypereosinophilic syndrome. Ref.7 Ref.31 Gastrointestinal stromal tumor (GIST) [MIM:606764]: Common mesenchymal neoplasms arising in the gastrointestinal tract, most often in the stomach. They are histologically, immunohistochemically, and genetically different from typical leiomyomas, leiomyosarcomas, and schwannomas. Most GISTs are composed of a fairly uniform population of spindle-shaped cells. Some tumors are dominated by epithelioid cells or contain a mixture of spindle and epithelioid morphologies. Primary GISTs in the gastrointestinal tract commonly metastasize in the omentum and mesenteries, often as multiple nodules. However, primary tumors may also occur outside of the gastrointestinal tract, in other intra-abdominal locations, especially in the omentum and mesentery. Note: The gene represented in this entry may be involved in disease pathogenesis. Mutations causing PDGFRA constitutive activation have been found in gastrointestinal stromal tumors lacking KIT mutations (Ref.25). Ref.7 Ref.25 Ref.26 Ref.31
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily. Contains 5 Ig-like C2-type (immunoglobulin-like) domains. Contains 1 protein kinase domain.
Sequence caution	The sequence AAP69563.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Chemotaxis Host-virus interaction
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Proto-oncogene
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Disulfide bond Glycoprotein Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Leydig cell differentiation Inferred from electronic annotation. Source: Compara adrenal gland development Inferred from electronic annotation. Source: Compara cardiac myofibril assembly Inferred from sequence or structural similarity. Source: UniProtKB cell chemotaxis Inferred from mutant phenotype Ref.12. Source: UniProtKB cellular response to amino acid stimulus Inferred from electronic annotation. Source: Compara elevation of cytosolic calcium ion concentration Inferred from mutant phenotype Ref.9. Source: UniProtKB embryonic cranial skeleton morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB embryonic digestive tract morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB estrogen metabolic process Inferred from electronic annotation. Source: Compara extracellular matrix organization Inferred from electronic annotation. Source: Compara face morphogenesis Inferred from electronic annotation. Source: Compara in utero embryonic development Inferred from electronic annotation. Source: Compara lung development Inferred from electronic annotation. Source: Compara luteinization Inferred from sequence or structural similarity. Source: UniProtKB male genitalia development Inferred from electronic annotation. Source: Compara metanephric glomerular capillary formation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of platelet activation Inferred from direct assay Ref.14. Source: UniProtKB odontogenesis of dentin-containing tooth Inferred from electronic annotation. Source: Compara palate development Inferred from electronic annotation. Source: Compara peptidyl-tyrosine phosphorylation Inferred from direct assay Ref.12Ref.14. Source: UniProtKB phosphatidylinositol-mediated signaling Inferred from mutant phenotype Ref.9. Source: UniProtKB platelet aggregation Inferred from mutant phenotype Ref.14. Source: UniProtKB positive regulation of DNA replication Inferred from direct assay PubMed 10806482. Source: BHF-UCL positive regulation of ERK1 and ERK2 cascade Inferred from mutant phenotype Ref.21. Source: UniProtKB positive regulation of cell migration Inferred from mutant phenotype Ref.12. Source: UniProtKB positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway Inferred from direct assay PubMed 17470632. Source: BHF-UCL positive regulation of fibroblast proliferation Inferred from direct assay PubMed 10806482. Source: BHF-UCL positive regulation of phosphatidylinositol 3-kinase activity Inferred from mutant phenotype Ref.12. Source: UniProtKB positive regulation of phosphatidylinositol 3-kinase cascade Traceable author statement Ref.21. Source: UniProtKB positive regulation of phospholipase C activity Inferred from mutant phenotype Ref.12. Source: UniProtKB protein autophosphorylation Inferred from direct assay Ref.12Ref.14. Source: UniProtKB regulation of actin cytoskeleton reorganization Traceable author statement Ref.21. Source: UniProtKB regulation of chemotaxis Inferred from mutant phenotype Ref.9. Source: UniProtKB regulation of mesenchymal stem cell differentiation Inferred from mutant phenotype Ref.30. Source: UniProtKB retina vasculature development in camera-type eye Inferred from sequence or structural similarity. Source: UniProtKB signal transduction involved in regulation of gene expression Inferred from electronic annotation. Source: Compara vascular endothelial growth factor receptor signaling pathway Inferred from electronic annotation. Source: InterPro virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB external side of plasma membrane Inferred from electronic annotation. Source: Compara integral to plasma membrane Inferred from direct assay Ref.2. Source: BHF-UCL nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW platelet-derived growth factor alpha-receptor activity Inferred from direct assay Ref.14. Source: UniProtKB platelet-derived growth factor binding Inferred from direct assay Ref.9Ref.14. Source: UniProtKB protein homodimerization activity Inferred from direct assay PubMed 2542288. Source: BHF-UCL vascular endothelial growth factor-activated receptor activity Inferred from direct assay PubMed 17470632. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P16234-1)

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

Isoform 2 (identifier: P16234-2)

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

Note: No experimental confirmation available.

Isoform 3 (identifier: P16234-3)

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23
	Chain	24 – 1089	1066	Platelet-derived growth factor receptor alpha		PRO_0000016760
Regions
	Topological domain	24 – 528	505	Extracellular Potential
	Transmembrane	529 – 549	21	Helical; Potential
	Topological domain	550 – 1089	540	Cytoplasmic Potential
	Domain	24 – 113	90	Ig-like C2-type 1
	Domain	117 – 201	85	Ig-like C2-type 2
	Domain	202 – 306	105	Ig-like C2-type 3
	Domain	319 – 410	92	Ig-like C2-type 4
	Domain	414 – 517	104	Ig-like C2-type 5
	Domain	593 – 954	362	Protein kinase
	Nucleotide binding	599 – 607	9	ATP By similarity
	Compositional bias	1041 – 1087	47	Ser-rich
Sites
	Active site	818	1	Proton acceptor By similarity
	Binding site	627	1	ATP By similarity
	Site	578 – 579	2	Breakpoint for interstitial deletion to form the FIP1L1-PDGFRA fusion protein
Amino acid modifications
	Modified residue	555	1	Phosphotyrosine
	Modified residue	572	1	Phosphotyrosine; by autocatalysis
	Modified residue	574	1	Phosphotyrosine; by autocatalysis
	Modified residue	582	1	Phosphotyrosine
	Modified residue	720	1	Phosphotyrosine; by autocatalysis Ref.17 Ref.19
	Modified residue	731	1	Phosphotyrosine; by autocatalysis
	Modified residue	742	1	Phosphotyrosine; by autocatalysis
	Modified residue	754	1	Phosphotyrosine; by autocatalysis
	Modified residue	762	1	Phosphotyrosine; by autocatalysis
	Modified residue	768	1	Phosphotyrosine; by autocatalysis
	Modified residue	849	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	944	1	Phosphotyrosine
	Modified residue	958	1	Phosphotyrosine
	Modified residue	962	1	Phosphotyrosine
	Modified residue	988	1	Phosphotyrosine; by autocatalysis
	Modified residue	993	1	Phosphotyrosine
	Modified residue	1018	1	Phosphotyrosine; by autocatalysis
	Glycosylation	42	1	N-linked (GlcNAc...) Potential
	Glycosylation	76	1	N-linked (GlcNAc...) Potential
	Glycosylation	103	1	N-linked (GlcNAc...) Potential
	Glycosylation	179	1	N-linked (GlcNAc...) Potential
	Glycosylation	353	1	N-linked (GlcNAc...) Potential
	Glycosylation	359	1	N-linked (GlcNAc...) Potential
	Glycosylation	458	1	N-linked (GlcNAc...) Potential
	Glycosylation	468	1	N-linked (GlcNAc...) Potential
	Disulfide bond	49 ↔ 100		By similarity
	Disulfide bond	150 ↔ 189		By similarity
	Disulfide bond	235 ↔ 290		By similarity
	Disulfide bond	435 ↔ 501		By similarity
Natural variations
	Alternative sequence	210 – 218	9	ATSELDLEM → GTCIISFLL in isoform 2.		VSP_007833
	Alternative sequence	219 – 1089	871	Missing in isoform 2.		VSP_007834
	Alternative sequence	720 – 743	24	YVILS…TTQYV → SGQGCLSSGTLQELSVDLQA RGPC in isoform 3.		VSP_042015
	Alternative sequence	744 – 1089	346	Missing in isoform 3.		VSP_042016
	Natural variant	79	1	G → D. Ref.37 Corresponds to variant rs36035373 [ dbSNP | Ensembl ].		VAR_042032
	Natural variant	426	1	G → D. Ref.37 Corresponds to variant rs55865821 [ dbSNP | Ensembl ].		VAR_042033
	Natural variant	478	1	S → P. Ref.4 Ref.6 Ref.37 Corresponds to variant rs35597368 [ dbSNP | Ensembl ].		VAR_034378
	Natural variant	481	1	R → G in a hypereosinophilic syndrome sample; does not lead to constitutive kinase activation. Ref.29		VAR_066460
	Natural variant	507	1	L → P in a hypereosinophilic syndrome sample; does not lead to constitutive kinase activation. Ref.29		VAR_066461
	Natural variant	561	1	V → D in a GIST sample; constitutively activated kinase. Ref.25 Ref.26		VAR_066462
	Natural variant	562	1	I → M in a hypereosinophilic syndrome sample; does not lead to constitutive kinase activation. Ref.29		VAR_066463
	Natural variant	570	1	H → R in a hypereosinophilic syndrome sample; does not lead to constitutive kinase activation. Ref.29		VAR_066464
	Natural variant	650	1	H → Q in a hypereosinophilic syndrome sample; constitutively activated kinase. Ref.29		VAR_066465
	Natural variant	659	1	N → K in GIST sample; constitutively activated kinase. Ref.26		VAR_066466
	Natural variant	659	1	N → S in a hypereosinophilic syndrome sample; constitutively activated kinase. Ref.29		VAR_066467
	Natural variant	705	1	L → P in a hypereosinophilic syndrome sample; does not lead to constitutive kinase activation. Ref.29		VAR_066468
	Natural variant	748	1	R → G in a hypereosinophilic syndrome sample; constitutively activated kinase. Ref.29		VAR_066469
	Natural variant	764	1	R → C. Ref.37 Corresponds to variant rs34392012 [ dbSNP | Ensembl ].		VAR_042034
	Natural variant	829	1	G → R in a glioblastoma multiforme sample; somatic mutation. Ref.37		VAR_042035
	Natural variant	842 – 845	4	Missing in a GIST sample; constitutively activated kinase.		VAR_066470
	Natural variant	842	1	D → V in a GIST sample; imatinib resistant, constitutively activated kinase. Ref.25 Ref.26 Ref.31		VAR_066471
	Natural variant	842	1	D → Y in a GIST sample; imatinib sensitive, constitutively activated kinase. Ref.26		VAR_066472
	Natural variant	845 – 848	4	Missing in a GIST sample; constitutively activated kinase.		VAR_066473
	Natural variant	849	1	Y → C in GIST. Ref.26		VAR_066474
	Natural variant	849	1	Y → S in a hypereosinophilic syndrome sample; constitutively activated kinase. Ref.29		VAR_066475
	Natural variant	996	1	E → K in a metastatic melanoma sample; somatic mutation. Ref.37		VAR_042036
	Natural variant	1071	1	D → N in a lung neuroendocrine carcinoma sample; somatic mutation. Ref.37		VAR_042037
Experimental info
	Mutagenesis	572	1	Y → F: Abolishes interaction with SRC-family members and impairs internalization of the activated receptor; when associated with F-574. Ref.21 Ref.23
	Mutagenesis	574	1	Y → F: Abolishes interaction with SRC-family members and impairs internalization of the activated receptor; when associated with F-572. Ref.21 Ref.23
	Mutagenesis	720	1	Y → F: Strongly reduced interaction with PTPN11 and GRB2. Ref.17
	Mutagenesis	731	1	Y → F: No effect on autophosphorylation and phosphorylation of PLCG1. Abolishes activation of phosphatidylinositol 3-kinase. Ref.12
	Mutagenesis	742	1	Y → F: No effect on autophosphorylation and phosphorylation of PLCG1. Abolishes activation of phosphatidylinositol 3-kinase. Ref.12
	Mutagenesis	762	1	Y → F: Abolishes interaction with CRK. Ref.18

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 5E3FB9940ACD1BE8	FASTA	1,089	122,670
	10 20 30 40 50 60 MGTSHPAFLV LGCLLTGLSL ILCQLSLPSI LPNENEKVVQ LNSSFSLRCF GESEVSWQYP 70 80 90 100 110 120 MSEEESSDVE IRNEENNSGL FVTVLEVSSA SAAHTGLYTC YYNHTQTEEN ELEGRHIYIY 130 140 150 160 170 180 VPDPDVAFVP LGMTDYLVIV EDDDSAIIPC RTTDPETPVT LHNSEGVVPA SYDSRQGFNG 190 200 210 220 230 240 TFTVGPYICE ATVKGKKFQT IPFNVYALKA TSELDLEMEA LKTVYKSGET IVVTCAVFNN 250 260 270 280 290 300 EVVDLQWTYP GEVKGKGITM LEEIKVPSIK LVYTLTVPEA TVKDSGDYEC AARQATREVK 310 320 330 340 350 360 EMKKVTISVH EKGFIEIKPT FSQLEAVNLH EVKHFVVEVR AYPPPRISWL KNNLTLIENL 370 380 390 400 410 420 TEITTDVEKI QEIRYRSKLK LIRAKEEDSG HYTIVAQNED AVKSYTFELL TQVPSSILDL 430 440 450 460 470 480 VDDHHGSTGG QTVRCTAEGT PLPDIEWMIC KDIKKCNNET SWTILANNVS NIITEIHSRD 490 500 510 520 530 540 RSTVEGRVTF AKVEETIAVR CLAKNLLGAE NRELKLVAPT LRSELTVAAA VLVLLVIVII 550 560 570 580 590 600 SLIVLVVIWK QKPRYEIRWR VIESISPDGH EYIYVDPMQL PYDSRWEFPR DGLVLGRVLG 610 620 630 640 650 660 SGAFGKVVEG TAYGLSRSQP VMKVAVKMLK PTARSSEKQA LMSELKIMTH LGPHLNIVNL 670 680 690 700 710 720 LGACTKSGPI YIITEYCFYG DLVNYLHKNR DSFLSHHPEK PKKELDIFGL NPADESTRSY 730 740 750 760 770 780 VILSFENNGD YMDMKQADTT QYVPMLERKE VSKYSDIQRS LYDRPASYKK KSMLDSEVKN 790 800 810 820 830 840 LLSDDNSEGL TLLDLLSFTY QVARGMEFLA SKNCVHRDLA ARNVLLAQGK IVKICDFGLA 850 860 870 880 890 900 RDIMHDSNYV SKGSTFLPVK WMAPESIFDN LYTTLSDVWS YGILLWEIFS LGGTPYPGMM 910 920 930 940 950 960 VDSTFYNKIK SGYRMAKPDH ATSEVYEIMV KCWNSEPEKR PSFYHLSEIV ENLLPGQYKK 970 980 990 1000 1010 1020 SYEKIHLDFL KSDHPAVARM RVDSDNAYIG VTYKNEEDKL KDWEGGLDEQ RLSADSGYII 1030 1040 1050 1060 1070 1080 PLPDIDPVPE EEDLGKRNRH SSQTSEESAI ETGSSSSTFI KREDETIEDI DMMDDIGIDS SDLVEDSFL
	Isoform 2 [UniParc]. Checksum: E8144A73DFD069BF	FASTA	218	24,023
	10 20 30 40 50 60 MGTSHPAFLV LGCLLTGLSL ILCQLSLPSI LPNENEKVVQ LNSSFSLRCF GESEVSWQYP 70 80 90 100 110 120 MSEEESSDVE IRNEENNSGL FVTVLEVSSA SAAHTGLYTC YYNHTQTEEN ELEGRHIYIY 130 140 150 160 170 180 VPDPDVAFVP LGMTDYLVIV EDDDSAIIPC RTTDPETPVT LHNSEGVVPA SYDSRQGFNG 190 200 210 TFTVGPYICE ATVKGKKFQT IPFNVYALKG TCIISFLL
	Isoform 3 [UniParc]. Checksum: 2456B1766606C60F	FASTA	743	82,809
	10 20 30 40 50 60 MGTSHPAFLV LGCLLTGLSL ILCQLSLPSI LPNENEKVVQ LNSSFSLRCF GESEVSWQYP 70 80 90 100 110 120 MSEEESSDVE IRNEENNSGL FVTVLEVSSA SAAHTGLYTC YYNHTQTEEN ELEGRHIYIY 130 140 150 160 170 180 VPDPDVAFVP LGMTDYLVIV EDDDSAIIPC RTTDPETPVT LHNSEGVVPA SYDSRQGFNG 190 200 210 220 230 240 TFTVGPYICE ATVKGKKFQT IPFNVYALKA TSELDLEMEA LKTVYKSGET IVVTCAVFNN 250 260 270 280 290 300 EVVDLQWTYP GEVKGKGITM LEEIKVPSIK LVYTLTVPEA TVKDSGDYEC AARQATREVK 310 320 330 340 350 360 EMKKVTISVH EKGFIEIKPT FSQLEAVNLH EVKHFVVEVR AYPPPRISWL KNNLTLIENL 370 380 390 400 410 420 TEITTDVEKI QEIRYRSKLK LIRAKEEDSG HYTIVAQNED AVKSYTFELL TQVPSSILDL 430 440 450 460 470 480 VDDHHGSTGG QTVRCTAEGT PLPDIEWMIC KDIKKCNNET SWTILANNVS NIITEIHSRD 490 500 510 520 530 540 RSTVEGRVTF AKVEETIAVR CLAKNLLGAE NRELKLVAPT LRSELTVAAA VLVLLVIVII 550 560 570 580 590 600 SLIVLVVIWK QKPRYEIRWR VIESISPDGH EYIYVDPMQL PYDSRWEFPR DGLVLGRVLG 610 620 630 640 650 660 SGAFGKVVEG TAYGLSRSQP VMKVAVKMLK PTARSSEKQA LMSELKIMTH LGPHLNIVNL 670 680 690 700 710 720 LGACTKSGPI YIITEYCFYG DLVNYLHKNR DSFLSHHPEK PKKELDIFGL NPADESTRSS 730 740 GQGCLSSGTL QELSVDLQAR GPC

References

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[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]	"Receptor tyrosine kinases expressed in metastatic colon cancer." Craven R.J., Xu L.H., Weiner T.M., Fridell Y.-W., Dent G.A., Srivastava S., Varnum B., Liu E.T., Cance W.G. Int. J. Cancer 60:791-797(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 823-876, TISSUE SPECIFICITY. Tissue: Colon tumor.
[9]	"Independent expression of human alpha or beta platelet-derived growth factor receptor cDNAs in a naive hematopoietic cell leads to functional coupling with mitogenic and chemotactic signaling pathways." Matsui T., Pierce J.H., Fleming T.P., Greenberger J.S., LaRochelle W.J., Ruggiero M., Aaronson S.A. Proc. Natl. Acad. Sci. U.S.A. 86:8314-8318(1989) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS PDGFA AND PDGFB RECEPTOR IN CELL PROLIFERATION AND CHEMOTAXIS, SUBCELLULAR LOCATION.
[10]	"Binding of SH2 domains of phospholipase C gamma 1, GAP, and Src to activated growth factor receptors." Anderson D., Koch C.A., Grey L., Ellis C., Moran M.F., Pawson T. Science 250:979-982(1990) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PLCG1 AND SRC.
[11]	"Platelet-derived growth factor (PDGF) stimulates PDGF receptor subunit dimerization and intersubunit trans-phosphorylation." Kelly J.D., Haldeman B.A., Grant F.J., Murray M.J., Seifert R.A., Bowen-Pope D.F., Cooper J.A., Kazlauskas A. J. Biol. Chem. 266:8987-8992(1991) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PDGFRA; PDGFA AND PDGFB, FUNCTION AS RECEPTOR FOR PDGFA AND PDGFB, AUTOPHOSPHORYLATION.
[12]	"Tyrosine mutations within the alpha platelet-derived growth factor receptor kinase insert domain abrogate receptor-associated phosphatidylinositol-3 kinase activity without affecting mitogenic or chemotactic signal transduction." Yu J.C., Heidaran M.A., Pierce J.H., Gutkind J.S., Lombardi D., Ruggiero M., Aaronson S.A. Mol. Cell. Biol. 11:3780-3785(1991) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS PDGFB RECEPTOR IN CHEMOTAXIS; CELL PROLIFERATION; PHOSPHORYLATION OF PLCG1; ACTIVATION OF PHOSPHATIDYLINOSITOL 3-KINASE AND REGULATION OF PHOSPHATIDYLINOSITOL METABOLISM, INTERACTION WITH PIK3R, 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]	"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.
[16]	"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.
[17]	"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.
[18]	"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, MUTAGENESIS OF TYR-762.
[19]	"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, PROBABLE PHOSPHORYLATION AT TYR-720.
[20]	"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.
[21]	"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, MUTAGENESIS OF TYR-572 AND TYR-574.
[22]	"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.
[23]	"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.
[24]	"A tyrosine kinase created by fusion of the PDGFRA and FIP1L1 genes as a therapeutic target of imatinib in idiopathic hypereosinophilic syndrome." Cools J., DeAngelo D.J., Gotlib J., Stover E.H., Legare R.D., Cortes J., Kutok J., Clark J., Galinsky I., Griffin J.D., Cross N.C., Tefferi A., Malone J., Alam R., Schrier S.L., Schmid J., Rose M., Vandenberghe P. , Verhoef G., Boogaerts M., Wlodarska I., Kantarjian H., Marynen P., Coutre S.E., Stone R., Gilliland D.G. N. Engl. J. Med. 348:1201-1214(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN HES.
[25]	"PDGFRA activating mutations in gastrointestinal stromal tumors." Heinrich M.C., Corless C.L., Duensing A., McGreevey L., Chen C.J., Joseph N., Singer S., Griffith D.J., Haley A., Town A., Demetri G.D., Fletcher C.D., Fletcher J.A. Science 299:708-710(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF AKT1; MAP KINASES; STAT1 AND STAT3, INVOLVEMENT IN GIST, VARIANTS ASP-561; VAL-842; 842-ASP--HIS-845 DEL AND 845-HIS--PRO-448 DEL, CHARACTERIZATION OF VARIANTS ASP-561; VAL-842; 842-ASP--HIS-845 DEL AND 845-HIS--PRO-448 DEL.
[26]	"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.
[27]	"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.
[28]	"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.
[29]	"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.
[30]	"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.
[31]	"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.
[32]	"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.
[33]	"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.
[34]	"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.
[35]	"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.
[36]	"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.
[37]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

IPI

IPI00027721.
IPI00336178.

PIR

PFHUGA. A40162.

RefSeq

NP_006197.1. NM_006206.4.

UniGene

Hs.74615.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GQ5	X-ray	2.20

ProteinModelPortal

P16234.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5736N.

IntAct

P16234. 3 interactions.

STRING

9606.ENSP00000257290.

PTM databases

PhosphoSite

P16234.

Polymorphism databases

DMDM

129892.

Proteomic databases

PaxDb

P16234.

PRIDE

P16234.

Protocols and materials databases

DNASU

5156.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000257290; ENSP00000257290; ENSG00000134853.
ENST00000508170; ENSP00000425648; ENSG00000134853.
ENST00000509490; ENSP00000424218; ENSG00000134853.

GeneID

5156.

KEGG

hsa:5156.

UCSC

uc003hal.3. human.
uc003han.4. human.

Organism-specific databases

CTD

5156.

GeneCards

GC04P055095.

HGNC

HGNC:8803. PDGFRA.

HPA

CAB018143.

MIM

173490. gene.
606764. phenotype.
607685. phenotype.

neXtProt

NX_P16234.

Orphanet

44890. Gastrointestinal stromal tumor.
3260. Idiopathic hypereosinophilic syndrome.
168947. Myeloid neoplasm associated with PDGFRA rearrangement.
99860. Precursor B-cell acute lymphoblastic leukemia.

PharmGKB

PA33147.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000112009.

HOVERGEN

HBG004335.

InParanoid

P16234.

KO

K04363.

OMA

DLQWTYP.

OrthoDB

EOG4XWFX0.

PhylomeDB

P16234.

Enzyme and pathway databases

BRENDA

2.7.10.1. 2681.

Pathway_Interaction_DB

pdgfrapathway. PDGFR-alpha signaling pathway.

Reactome

REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P16234.

Bgee

P16234.

CleanEx

HS_PDGFRA.

Genevestigator

P16234.

GermOnline

ENSG00000134853. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 4 hits.

InterPro

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_cat_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.
IPR009134. Tyr_kinase_VEGFR_rcpt_N.
[Graphical view]

Pfam

PF07679. I-set. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]

PIRSF

PIRSF500950. Alpha-PDGF_receptor. 1 hit.
PIRSF000615. TyrPK_CSF1-R. 1 hit.

PRINTS

PR01832. VEGFRECEPTOR.

SMART

SM00409. IG. 2 hits.
SM00408. IGc2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS50835. IG_LIKE. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P16234.

ChEMBL

CHEMBL2007.

ChiTaRS

PDGFRA. human.

DrugBank

DB00102. Becaplermin.
DB00619. Imatinib.
DB01268. Sunitinib.

EvolutionaryTrace

P16234.

GenomeRNAi

5156.

NextBio

19946.

SOURCE

Search...

Entry information

Entry name

PGFRA_HUMAN

Accession

Primary (citable) accession number: P16234
Secondary accession number(s): B2RE69 , E9PBH0, Q6P4H5, Q96KZ7, Q9UD28

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	May 1, 2013
This is version 153 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.