CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004431
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Platelet-derived growth factor receptor alpha 
Protein Synonyms/Alias
 PDGF-R-alpha; PDGFR-alpha; 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; PDGFR-2; CD140a 
Gene Name
 PDGFRA 
Gene Synonyms/Alias
 PDGFR2; RHEPDGFRA 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
606LGSGAFGKVVEGTAYubiquitination[1, 2]
852HDSNYVSKGSTFLPVubiquitination[2]
971KIHLDFLKSDHPAVAubiquitination[2]
1036PEEEDLGKRNRHSSQubiquitination[2]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 
Functional Description
 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 Ca(2+) 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. 
Sequence Annotation
 DOMAIN 24 113 Ig-like C2-type 1.
 DOMAIN 117 201 Ig-like C2-type 2.
 DOMAIN 202 306 Ig-like C2-type 3.
 DOMAIN 319 410 Ig-like C2-type 4.
 DOMAIN 414 517 Ig-like C2-type 5.
 DOMAIN 593 954 Protein kinase.
 NP_BIND 599 607 ATP (By similarity).
 ACT_SITE 818 818 Proton acceptor (By similarity).
 BINDING 627 627 ATP (By similarity).
 MOD_RES 555 555 Phosphotyrosine.
 MOD_RES 572 572 Phosphotyrosine; by autocatalysis.
 MOD_RES 574 574 Phosphotyrosine; by autocatalysis.
 MOD_RES 582 582 Phosphotyrosine.
 MOD_RES 720 720 Phosphotyrosine; by autocatalysis.
 MOD_RES 731 731 Phosphotyrosine; by autocatalysis.
 MOD_RES 742 742 Phosphotyrosine; by autocatalysis.
 MOD_RES 754 754 Phosphotyrosine; by autocatalysis.
 MOD_RES 762 762 Phosphotyrosine; by autocatalysis.
 MOD_RES 768 768 Phosphotyrosine; by autocatalysis.
 MOD_RES 849 849 Phosphotyrosine; by autocatalysis (By
 MOD_RES 944 944 Phosphotyrosine.
 MOD_RES 958 958 Phosphotyrosine.
 MOD_RES 962 962 Phosphotyrosine.
 MOD_RES 988 988 Phosphotyrosine; by autocatalysis.
 MOD_RES 993 993 Phosphotyrosine.
 MOD_RES 1018 1018 Phosphotyrosine; by autocatalysis.
 CARBOHYD 42 42 N-linked (GlcNAc...) (Potential).
 CARBOHYD 76 76 N-linked (GlcNAc...) (Potential).
 CARBOHYD 103 103 N-linked (GlcNAc...) (Potential).
 CARBOHYD 179 179 N-linked (GlcNAc...) (Potential).
 CARBOHYD 353 353 N-linked (GlcNAc...) (Potential).
 CARBOHYD 359 359 N-linked (GlcNAc...) (Potential).
 CARBOHYD 458 458 N-linked (GlcNAc...) (Potential).
 CARBOHYD 468 468 N-linked (GlcNAc...) (Potential).
 DISULFID 49 100 By similarity.
 DISULFID 150 189 By similarity.
 DISULFID 235 290 By similarity.
 DISULFID 435 501 By similarity.  
Keyword
 3D-structure; Alternative splicing; ATP-binding; Cell membrane; Chemotaxis; Complete proteome; Developmental protein; Disulfide bond; Glycoprotein; Host-virus interaction; Immunoglobulin domain; Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Polymorphism; Proto-oncogene; Receptor; Reference proteome; Repeat; Signal; Transferase; Transmembrane; Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1089 AA 
Protein Sequence
MGTSHPAFLV LGCLLTGLSL ILCQLSLPSI LPNENEKVVQ LNSSFSLRCF GESEVSWQYP 60
MSEEESSDVE IRNEENNSGL FVTVLEVSSA SAAHTGLYTC YYNHTQTEEN ELEGRHIYIY 120
VPDPDVAFVP LGMTDYLVIV EDDDSAIIPC RTTDPETPVT LHNSEGVVPA SYDSRQGFNG 180
TFTVGPYICE ATVKGKKFQT IPFNVYALKA TSELDLEMEA LKTVYKSGET IVVTCAVFNN 240
EVVDLQWTYP GEVKGKGITM LEEIKVPSIK LVYTLTVPEA TVKDSGDYEC AARQATREVK 300
EMKKVTISVH EKGFIEIKPT FSQLEAVNLH EVKHFVVEVR AYPPPRISWL KNNLTLIENL 360
TEITTDVEKI QEIRYRSKLK LIRAKEEDSG HYTIVAQNED AVKSYTFELL TQVPSSILDL 420
VDDHHGSTGG QTVRCTAEGT PLPDIEWMIC KDIKKCNNET SWTILANNVS NIITEIHSRD 480
RSTVEGRVTF AKVEETIAVR CLAKNLLGAE NRELKLVAPT LRSELTVAAA VLVLLVIVII 540
SLIVLVVIWK QKPRYEIRWR VIESISPDGH EYIYVDPMQL PYDSRWEFPR DGLVLGRVLG 600
SGAFGKVVEG TAYGLSRSQP VMKVAVKMLK PTARSSEKQA LMSELKIMTH LGPHLNIVNL 660
LGACTKSGPI YIITEYCFYG DLVNYLHKNR DSFLSHHPEK PKKELDIFGL NPADESTRSY 720
VILSFENNGD YMDMKQADTT QYVPMLERKE VSKYSDIQRS LYDRPASYKK KSMLDSEVKN 780
LLSDDNSEGL TLLDLLSFTY QVARGMEFLA SKNCVHRDLA ARNVLLAQGK IVKICDFGLA 840
RDIMHDSNYV SKGSTFLPVK WMAPESIFDN LYTTLSDVWS YGILLWEIFS LGGTPYPGMM 900
VDSTFYNKIK SGYRMAKPDH ATSEVYEIMV KCWNSEPEKR PSFYHLSEIV ENLLPGQYKK 960
SYEKIHLDFL KSDHPAVARM RVDSDNAYIG VTYKNEEDKL KDWEGGLDEQ RLSADSGYII 1020
PLPDIDPVPE EEDLGKRNRH SSQTSEESAI ETGSSSSTFI KREDETIEDI DMMDDIGIDS 1080
SDLVEDSFL 1089 
Gene Ontology
 GO:0005737; C:cytoplasm; ISS:UniProtKB.
 GO:0009897; C:external side of plasma membrane; IEA:Compara.
 GO:0005887; C:integral to plasma membrane; IDA:BHF-UCL.
 GO:0005634; C:nucleus; ISS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0005018; F:platelet-derived growth factor alpha-receptor activity; IDA:UniProtKB.
 GO:0048407; F:platelet-derived growth factor binding; IDA:UniProtKB.
 GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
 GO:0005021; F:vascular endothelial growth factor-activated receptor activity; IDA:BHF-UCL.
 GO:0030325; P:adrenal gland development; IEA:Compara.
 GO:0055003; P:cardiac myofibril assembly; ISS:UniProtKB.
 GO:0060326; P:cell chemotaxis; IMP:UniProtKB.
 GO:0071230; P:cellular response to amino acid stimulus; IEA:Compara.
 GO:0007204; P:elevation of cytosolic calcium ion concentration; IMP:UniProtKB.
 GO:0048701; P:embryonic cranial skeleton morphogenesis; ISS:UniProtKB.
 GO:0048557; P:embryonic digestive tract morphogenesis; ISS:UniProtKB.
 GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
 GO:0008210; P:estrogen metabolic process; IEA:Compara.
 GO:0030198; P:extracellular matrix organization; IEA:Compara.
 GO:0060325; P:face morphogenesis; IEA:Compara.
 GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
 GO:0001701; P:in utero embryonic development; IEA:Compara.
 GO:0045087; P:innate immune response; TAS:Reactome.
 GO:0033327; P:Leydig cell differentiation; IEA:Compara.
 GO:0030324; P:lung development; IEA:Compara.
 GO:0001553; P:luteinization; ISS:UniProtKB.
 GO:0030539; P:male genitalia development; IEA:Compara.
 GO:0072277; P:metanephric glomerular capillary formation; ISS:UniProtKB.
 GO:0010544; P:negative regulation of platelet activation; IDA:UniProtKB.
 GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
 GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Compara.
 GO:0060021; P:palate development; IEA:Compara.
 GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
 GO:0048015; P:phosphatidylinositol-mediated signaling; IMP:UniProtKB.
 GO:0070527; P:platelet aggregation; IMP:UniProtKB.
 GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
 GO:0038091; P:positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway; IDA:BHF-UCL.
 GO:0045740; P:positive regulation of DNA replication; IDA:BHF-UCL.
 GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
 GO:0048146; P:positive regulation of fibroblast proliferation; IDA:BHF-UCL.
 GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IMP:UniProtKB.
 GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase cascade; TAS:UniProtKB.
 GO:0010863; P:positive regulation of phospholipase C activity; IMP:UniProtKB.
 GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
 GO:2000249; P:regulation of actin cytoskeleton reorganization; TAS:UniProtKB.
 GO:0050920; P:regulation of chemotaxis; IMP:UniProtKB.
 GO:2000739; P:regulation of mesenchymal stem cell differentiation; IMP:UniProtKB.
 GO:0061298; P:retina vasculature development in camera-type eye; ISS:UniProtKB.
 GO:0023019; P:signal transduction involved in regulation of gene expression; IEA:Compara.
 GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IEA:InterPro.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
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. 
Pfam
 PF07679; I-set
 PF07714; Pkinase_Tyr 
SMART
 SM00409; IG
 SM00408; IGc2
 SM00219; TyrKc 
PROSITE
 PS50835; IG_LIKE
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00109; PROTEIN_KINASE_TYR
 PS00240; RECEPTOR_TYR_KIN_III 
PRINTS
 PR01832; VEGFRECEPTOR.