PGFRA_HUMAN - dbPTM
PGFRA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PGFRA_HUMAN
UniProt AC P16234
Protein Name Platelet-derived growth factor receptor alpha
Gene Name PDGFRA
Organism Homo sapiens (Human).
Sequence Length 1089
Subcellular Localization Cell membrane
Single-pass type I membrane protein . The activated receptor is rapidly internalized and degraded.
Protein 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..
Protein Sequence MGTSHPAFLVLGCLLTGLSLILCQLSLPSILPNENEKVVQLNSSFSLRCFGESEVSWQYPMSEEESSDVEIRNEENNSGLFVTVLEVSSASAAHTGLYTCYYNHTQTEENELEGRHIYIYVPDPDVAFVPLGMTDYLVIVEDDDSAIIPCRTTDPETPVTLHNSEGVVPASYDSRQGFNGTFTVGPYICEATVKGKKFQTIPFNVYALKATSELDLEMEALKTVYKSGETIVVTCAVFNNEVVDLQWTYPGEVKGKGITMLEEIKVPSIKLVYTLTVPEATVKDSGDYECAARQATREVKEMKKVTISVHEKGFIEIKPTFSQLEAVNLHEVKHFVVEVRAYPPPRISWLKNNLTLIENLTEITTDVEKIQEIRYRSKLKLIRAKEEDSGHYTIVAQNEDAVKSYTFELLTQVPSSILDLVDDHHGSTGGQTVRCTAEGTPLPDIEWMICKDIKKCNNETSWTILANNVSNIITEIHSRDRSTVEGRVTFAKVEETIAVRCLAKNLLGAENRELKLVAPTLRSELTVAAAVLVLLVIVIISLIVLVVIWKQKPRYEIRWRVIESISPDGHEYIYVDPMQLPYDSRWEFPRDGLVLGRVLGSGAFGKVVEGTAYGLSRSQPVMKVAVKMLKPTARSSEKQALMSELKIMTHLGPHLNIVNLLGACTKSGPIYIITEYCFYGDLVNYLHKNRDSFLSHHPEKPKKELDIFGLNPADESTRSYVILSFENNGDYMDMKQADTTQYVPMLERKEVSKYSDIQRSLYDRPASYKKKSMLDSEVKNLLSDDNSEGLTLLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDIMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGTPYPGMMVDSTFYNKIKSGYRMAKPDHATSEVYEIMVKCWNSEPEKRPSFYHLSEIVENLLPGQYKKSYEKIHLDFLKSDHPAVARMRVDSDNAYIGVTYKNEEDKLKDWEGGLDEQRLSADSGYIIPLPDIDPVPEEEDLGKRNRHSSQTSEESAIETGSSSSTFIKREDETIEDIDMMDDIGIDSSDLVEDSFL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
42N-linked_GlycosylationNEKVVQLNSSFSLRC
CCCEEECCCCEEEEE		20.65UniProtKB CARBOHYD
44PhosphorylationKVVQLNSSFSLRCFG
CEEECCCCEEEEEEC		20.1324719451
46PhosphorylationVQLNSSFSLRCFGES
EECCCCEEEEEECCC		19.4924719451
76N-linked_GlycosylationVEIRNEENNSGLFVT
CEEECCCCCCCEEEE		41.61UniProtKB CARBOHYD
78PhosphorylationIRNEENNSGLFVTVL
EECCCCCCCEEEEEE		48.7529759185
103N-linked_GlycosylationGLYTCYYNHTQTEEN
CEEEEEECCCCCCCC		12.78UniProtKB CARBOHYD
179N-linked_GlycosylationYDSRQGFNGTFTVGP
CCCCCCCCCEEEECC		56.25UniProtKB CARBOHYD
183PhosphorylationQGFNGTFTVGPYICE
CCCCCEEEECCEEEE		25.1329759185
187PhosphorylationGTFTVGPYICEATVK
CEEEECCEEEEEEEC		16.5729759185
192PhosphorylationGPYICEATVKGKKFQ
CCEEEEEEECCCCEE		10.6429759185
308PhosphorylationEMKKVTISVHEKGFI
HHHCEEEEEECCCEE		14.2026503514
353N-linked_GlycosylationRISWLKNNLTLIENL
CCHHHHHCEEHHHHH		32.58UniProtKB CARBOHYD
359N-linked_GlycosylationNNLTLIENLTEITTD
HCEEHHHHHHHCCCC		45.31UniProtKB CARBOHYD
378MethylationQEIRYRSKLKLIRAK
HHHHHHHCEEEEEEE		40.41-
458N-linked_GlycosylationKDIKKCNNETSWTIL
CCHHHCCCCCCEEEE		64.49UniProtKB CARBOHYD
468N-linked_GlycosylationSWTILANNVSNIITE
CEEEEECHHHHHHHH		32.74UniProtKB CARBOHYD
555PhosphorylationIWKQKPRYEIRWRVI
HHHCCCCCEEEEEEE		25.00-
566PhosphorylationWRVIESISPDGHEYI
EEEEEECCCCCCEEE		26.64-
572PhosphorylationISPDGHEYIYVDPMQ
CCCCCCEEEEECCCC		7.5921082442
574PhosphorylationPDGHEYIYVDPMQLP
CCCCEEEEECCCCCC		9.6326356563
582PhosphorylationVDPMQLPYDSRWEFP
ECCCCCCCCCCCCCC		34.8326356563
584PhosphorylationPMQLPYDSRWEFPRD
CCCCCCCCCCCCCCC		33.19-
606UbiquitinationLGSGAFGKVVEGTAY
ECCCCCCCEEECCCC		36.3323000965
611PhosphorylationFGKVVEGTAYGLSRS
CCCEEECCCCCCCCC		11.8224719451
613PhosphorylationKVVEGTAYGLSRSQP
CEEECCCCCCCCCCC		20.5925884760
616PhosphorylationEGTAYGLSRSQPVMK
ECCCCCCCCCCCHHH		26.0629083192
618PhosphorylationTAYGLSRSQPVMKVA
CCCCCCCCCCHHHHH		35.1529083192
619UbiquitinationAYGLSRSQPVMKVAV
CCCCCCCCCHHHHHH		33.2323000965
631UbiquitinationVAVKMLKPTARSSEK
HHHHHHCCCCCCHHH		27.5923000965
638UbiquitinationPTARSSEKQALMSEL
CCCCCHHHHHHHHHH		42.70-
716PhosphorylationGLNPADESTRSYVIL
CCCCCCCCCCEEEEE		29.66-
717PhosphorylationLNPADESTRSYVILS
CCCCCCCCCEEEEEE		22.91-
720PhosphorylationADESTRSYVILSFEN
CCCCCCEEEEEEECC		6.5510837138
731PhosphorylationSFENNGDYMDMKQAD
EECCCCCCCCHHHCC		9.0925884760
739PhosphorylationMDMKQADTTQYVPML
CCHHHCCCCCCCCCH		20.8626356563
740PhosphorylationDMKQADTTQYVPMLE
CHHHCCCCCCCCCHH		20.6026356563
742PhosphorylationKQADTTQYVPMLERK
HHCCCCCCCCCHHHH		12.3921082442
752PhosphorylationMLERKEVSKYSDIQR
CHHHHHHHCCHHHHH		27.2826356563
754PhosphorylationERKEVSKYSDIQRSL
HHHHHHCCHHHHHHH		12.227523122
755PhosphorylationRKEVSKYSDIQRSLY
HHHHHCCHHHHHHHC		31.7925884760
760PhosphorylationKYSDIQRSLYDRPAS
CCHHHHHHHCCCCCH		18.2025884760
762PhosphorylationSDIQRSLYDRPASYK
HHHHHHHCCCCCHHC		15.919546424
767PhosphorylationSLYDRPASYKKKSML
HHCCCCCHHCCHHHC		39.9228355574
768PhosphorylationLYDRPASYKKKSMLD
HCCCCCHHCCHHHCH		29.0021082442
847PhosphorylationARDIMHDSNYVSKGS
HHHHHCCCCCCCCCC		18.5122322096
849PhosphorylationDIMHDSNYVSKGSTF
HHHCCCCCCCCCCCC		15.2822322096
851PhosphorylationMHDSNYVSKGSTFLP
HCCCCCCCCCCCCCC		22.4218452278
852UbiquitinationHDSNYVSKGSTFLPV
CCCCCCCCCCCCCCE		47.0023503661
865UbiquitinationPVKWMAPESIFDNLY
CEEECCCHHHHHHHC		47.1023503661
877UbiquitinationNLYTTLSDVWSYGIL
HHCHHHHHHHHHHHH		49.3623503661
926PhosphorylationDHATSEVYEIMVKCW
CCCCHHHHHHHHHHH		8.8324961811
935PhosphorylationIMVKCWNSEPEKRPS
HHHHHHCCCCCCCCC		29.99-
944PhosphorylationPEKRPSFYHLSEIVE
CCCCCCCCCHHHHHH		13.2422817900
958PhosphorylationENLLPGQYKKSYEKI
HHHCCCCCHHCCEEE		26.7122817900
962PhosphorylationPGQYKKSYEKIHLDF
CCCCHHCCEEEEHHH		30.0722817900
971UbiquitinationKIHLDFLKSDHPAVA
EEEHHHHHCCCCCEE		54.5623503661
984UbiquitinationVARMRVDSDNAYIGV
EEEEEECCCCCEEEE		29.8823503661
984PhosphorylationVARMRVDSDNAYIGV
EEEEEECCCCCEEEE		29.8824961811
988PhosphorylationRVDSDNAYIGVTYKN
EECCCCCEEEEEEEC		12.4021082442
992PhosphorylationDNAYIGVTYKNEEDK
CCCEEEEEEECHHHH		24.4624961811
993PhosphorylationNAYIGVTYKNEEDKL
CCEEEEEEECHHHHC		14.9210837138
996UbiquitinationIGVTYKNEEDKLKDW
EEEEEECHHHHCCCC		64.5223503661
1013PhosphorylationGLDEQRLSADSGYII
CCCCCEECCCCCEEE		32.0224961811
1016PhosphorylationEQRLSADSGYIIPLP
CCEECCCCCEEEECC		32.9626356563
1018PhosphorylationRLSADSGYIIPLPDI
EECCCCCEEEECCCC		10.3021215800
1036UbiquitinationPEEEDLGKRNRHSSQ
CCHHHCCCCCCCCCC		54.5223503661
1041PhosphorylationLGKRNRHSSQTSEES
CCCCCCCCCCCCCHH		22.3926657352
1042PhosphorylationGKRNRHSSQTSEESA
CCCCCCCCCCCCHHH		31.2126657352
1044PhosphorylationRNRHSSQTSEESAIE
CCCCCCCCCCHHHHH		39.8026657352
1045PhosphorylationNRHSSQTSEESAIET
CCCCCCCCCHHHHHC		31.5626699800
1048PhosphorylationSSQTSEESAIETGSS
CCCCCCHHHHHCCCC		30.4123312004
1049UbiquitinationSQTSEESAIETGSSS
CCCCCHHHHHCCCCC		13.6023503661
1061UbiquitinationSSSSTFIKREDETIE
CCCCCEEECCCCCCC		45.6123503661
1080PhosphorylationMDDIGIDSSDLVEDS
CCCCCCCHHHHHCCC		24.67-
1081PhosphorylationDDIGIDSSDLVEDSF
CCCCCCHHHHHCCCC		31.08-
1087PhosphorylationSSDLVEDSFL-----
HHHHHCCCCC-----		18.23-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
572YPhosphorylationKinasePDGFRAP16234
PSP
574YPhosphorylationKinasePDGFRAP16234
PSP
720YPhosphorylationKinasePDGFRAP16234
GPS
731YPhosphorylationKinasePDGFRAP16234
GPS
742YPhosphorylationKinasePDGFRAP16234
GPS
754YPhosphorylationKinasePDGFRAP16234
GPS
754YPhosphorylationKinasePDGFRBP09619
PSP
762YPhosphorylationKinasePDGFRAP16234
GPS
768YPhosphorylationKinasePDGFRAP16234
GPS
988YPhosphorylationKinasePGFRAP16234
PhosphoELM
1018YPhosphorylationKinasePGFRAP16234
PhosphoELM
-KUbiquitinationE3 ubiquitin ligaseCBLP22681
PMID:10347229
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:20804422
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PGFRA_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PGFRA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PDGFA_HUMANPDGFAphysical
2544881
PDGFB_HUMANPDGFBphysical
2544881
PDGFC_HUMANPDGFCphysical
11297552
PGFRB_HUMANPDGFRBphysical
7523122
PGFRA_HUMANPDGFRAphysical
7523122
PGFRB_HUMANPDGFRBphysical
2542288
CRKL_HUMANCRKLphysical
9546424
CRK_HUMANCRKphysical
9546424
GRB2_HUMANGRB2physical
8943348
PGFRA_HUMANPDGFRAphysical
7535778
PLCG1_HUMANPLCG1physical
7535778
NHRF1_HUMANSLC9A3R1physical
11046132
PGFRA_HUMANPDGFRAphysical
11046132
GRB2_HUMANGRB2physical
21596750
P85A_HUMANPIK3R1physical
17452978
KIT_HUMANKITphysical
17452978
ULBP2_HUMANULBP2physical
21988832
TGFR2_HUMANTGFBR2physical
21988832
KASH5_HUMANCCDC155physical
25416956
CLUS_HUMANCLUphysical
26496610
DSG2_HUMANDSG2physical
26496610
H33_HUMANH3F3Aphysical
26496610
MYO1C_HUMANMYO1Cphysical
26496610
NRDC_HUMANNRD1physical
26496610
TFR1_HUMANTFRCphysical
26496610
TNK1_HUMANTNK1physical
26496610
FARP1_HUMANFARP1physical
26496610
FLOT1_HUMANFLOT1physical
26496610
RNPS1_HUMANRNPS1physical
26496610
SCFD1_HUMANSCFD1physical
26496610
PPIL2_HUMANPPIL2physical
26496610
PACN3_HUMANPACSIN3physical
26496610
WDR74_HUMANWDR74physical
26496610
PKRI1_HUMANPRKRIP1physical
26496610
RFIP1_HUMANRAB11FIP1physical
26496610
MAK16_HUMANMAK16physical
26496610
PHLB2_HUMANPHLDB2physical
26496610
P85A_HUMANPIK3R1physical
25241761
PLCG1_HUMANPLCG1physical
25241761
STAT3_HUMANSTAT3physical
25241761
P85A_MOUSEPik3r1physical
21393858
TOP1_HUMANTOP1genetic
28319113
VHL_HUMANVHLgenetic
28319113
RIR2_HUMANRRM2genetic
28319113
PDGFB_HUMANPDGFBphysical
9677323
PGFRA_HUMANPDGFRAphysical
9677323
PGFRA_HUMANPDGFRAphysical
15767546
PDGFA_HUMANPDGFAphysical
15767546
PDGFB_HUMANPDGFBphysical
15767546
PTN11_HUMANPTPN11physical
8959326
RASA1_HUMANRASA1physical
7682895
PLCG1_HUMANPLCG1physical
7682895
PK3CA_HUMANPIK3CAphysical
7682895
PGFRA_HUMANPDGFRAphysical
7682895
Drug and Disease Associations
Kegg Disease
H00042 Glioma
OMIM Disease
0000269|PubMedNote=A chromosomal aberration involving PDGFRA is found in some cases of hypereosinophilic syndrome. Interstitial chromosomal deletion del(4)(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. {ECO
606764
Kegg Drug
D01441 Imatinib mesilate (JAN); Imatinib mesylate (USAN); Gleevec (TN); Glivec (TN)
D05380 Pazopanib hydrochloride (JAN/USAN); Votrient (TN)
D06402 Sunitinib malate (JAN/USAN); Sutent (TN)
D06413 Nilotinib hydrochloride hydrate (JAN); Tasigna (TN)
D06678 Motesanib; AMG 706
D08066 Imatinib (INN); Glamox (TN)
D08503 Toceranib (USAN)
D08544 Toceranib phosphate (USAN)
D08552 Sunitinib (INN)
D08881 Cediranib (USAN/INN)
D08883 Cediranib maleate (JAN/USAN)
D08947 Motesanib phosphate (JAN); Motesanib diphosphate (USAN)
D08953 Nilotinib (USAN/INN)
D09635 Linifanib (USAN/INN)
D09919 Lenvatinib (USAN/INN)
D09920 Lenvatinib mesilate (JAN); Lenvatinib mesylate (USAN)
D09939 Olaratumab (USAN/INN)
D10062 Cabozantinib (USAN)
D10095 Cabozantinib s-malate (USAN); Cometriq (TN)
D10102 Crenolanib (USAN)
D10103 Crenolanib besylate (USAN)
D10396 Nintedanib esylate (USAN)
D10411 Tovetumab (USAN)
D10423 Ilorasertib (USAN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PGFRA_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-762; TYR-768; TYR-849AND TYR-1018, AND MASS SPECTROMETRY.
"Shf, a Shb-like adapter protein, is involved in PDGF-alpha-receptorregulation of apoptosis.";
Lindholm C.K., Frantz J.D., Shoelson S.E., Welsh M.;
Biochem. Biophys. Res. Commun. 278:537-543(2000).
Cited for: INTERACTION WITH SHF, AND PROBABLE PHOSPHORYLATION AT TYR-720.
"Phosphorylation of tyrosine 720 in the platelet-derived growth factoralpha receptor is required for binding of Grb2 and SHP-2 but not foractivation of Ras or cell proliferation.";
Bazenet C.E., Gelderloos J.A., Kazlauskas A.;
Mol. Cell. Biol. 16:6926-6936(1996).
Cited for: FUNCTION IN PHOSPHORYLATION OF PTPN11; ACTIVATION OF HRAS ANDREGULATION OF CELL PROLIFERATION, PHOSPHORYLATION AT TYR-720,INTERACTION WITH GRB2; PTPN11; PLCG1 AND PIK3R1, AUTOPHOSPHORYLATION,AND MUTAGENESIS OF TYR-720.

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