PGFRB_HUMAN - dbPTM
PGFRB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PGFRB_HUMAN
UniProt AC P09619
Protein Name Platelet-derived growth factor receptor beta
Gene Name PDGFRB
Organism Homo sapiens (Human).
Sequence Length 1106
Subcellular Localization Cell membrane
Single-pass type I membrane protein. Cytoplasmic vesicle. Lysosome lumen. After ligand binding, the autophosphorylated receptor is ubiquitinated and internalized, leading to its degradation.
Protein Description Tyrosine-protein kinase that acts as cell-surface receptor for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA and PDGFB, and plays an essential role in the regulation of embryonic development, cell proliferation, survival, differentiation, chemotaxis and migration. Plays an essential role in blood vessel development by promoting proliferation, migration and recruitment of pericytes and smooth muscle cells to endothelial cells. Plays a role in the migration of vascular smooth muscle cells and the formation of neointima at vascular injury sites. Required for normal development of the cardiovascular system. Required for normal recruitment of pericytes (mesangial cells) in the kidney glomerulus, and for normal formation of a branched network of capillaries in kidney glomeruli. Promotes rearrangement of the actin cytoskeleton and the formation of membrane ruffles. Binding of its cognate ligands - homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFD -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 PLCG1, PIK3R1, PTPN11, RASA1/GAP, CBL, SHC1 and NCK1. 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. Phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leads to the activation of the AKT1 signaling pathway. Phosphorylation of SHC1, or of the C-terminus of PTPN11, creates a binding site for GRB2, resulting in the activation of HRAS, RAF1 and down-stream MAP kinases, including MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation and activation of SRC family kinases. Promotes phosphorylation of PDCD6IP/ALIX and STAM. 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 MRLPGAMPALALKGELLLLSLLLLLEPQISQGLVVTPPGPELVLNVSSTFVLTCSGSAPVVWERMSQEPPQEMAKAQDGTFSSVLTLTNLTGLDTGEYFCTHNDSRGLETDERKRLYIFVPDPTVGFLPNDAEELFIFLTEITEITIPCRVTDPQLVVTLHEKKGDVALPVPYDHQRGFSGIFEDRSYICKTTIGDREVDSDAYYVYRLQVSSINVSVNAVQTVVRQGENITLMCIVIGNEVVNFEWTYPRKESGRLVEPVTDFLLDMPYHIRSILHIPSAELEDSGTYTCNVTESVNDHQDEKAINITVVESGYVRLLGEVGTLQFAELHRSRTLQVVFEAYPPPTVLWFKDNRTLGDSSAGEIALSTRNVSETRYVSELTLVRVKVAEAGHYTMRAFHEDAEVQLSFQLQINVPVRVLELSESHPDSGEQTVRCRGRGMPQPNIIWSACRDLKRCPRELPPTLLGNSSEEESQLETNVTYWEEEQEFEVVSTLRLQHVDRPLSVRCTLRNAVGQDTQEVIVVPHSLPFKVVVISAILALVVLTIISLIILIMLWQKKPRYEIRWKVIESVSSDGHEYIYVDPMQLPYDSTWELPRDQLVLGRTLGSGAFGQVVEATAHGLSHSQATMKVAVKMLKSTARSSEKQALMSELKIMSHLGPHLNVVNLLGACTKGGPIYIITEYCRYGDLVDYLHRNKHTFLQHHSDKRRPPSAELYSNALPVGLPLPSHVSLTGESDGGYMDMSKDESVDYVPMLDMKGDVKYADIESSNYMAPYDNYVPSAPERTCRATLINESPVLSYMDLVGFSYQVANGMEFLASKNCVHRDLAARNVLICEGKLVKICDFGLARDIMRDSNYISKGSTFLPLKWMAPESIFNSLYTTLSDVWSFGILLWEIFTLGGTPYPELPMNEQFYNAIKRGYRMAQPAHASDEIYEIMQKCWEEKFEIRPPFSQLVLLLERLLGEGYKKKYQQVDEEFLRSDHPAILRSQARLPGFHGLRSPLDTSSVLYTAVQPNEGDNDYIIPLPDPKPEVADEGPLEGSPSLASSTLNEVNTSSTISCDSPLEPQDEPEPEPQLELQVEPEPELEQLPDSGCPAPRAEAEDSFL
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
45N-linked_GlycosylationPGPELVLNVSSTFVL
CCCCEEEEECCEEEE		24.93UniProtKB CARBOHYD
89N-linked_GlycosylationSSVLTLTNLTGLDTG
CEEEEEECCCCCCCC		38.4220534510
103N-linked_GlycosylationGEYFCTHNDSRGLET
CCEEECCCCCCCCCC		30.6920534510
212PhosphorylationYVYRLQVSSINVSVN
EEEEEEEEEEEEEEE		16.73-
213PhosphorylationVYRLQVSSINVSVNA
EEEEEEEEEEEEEEE		21.23-
215N-linked_GlycosylationRLQVSSINVSVNAVQ
EEEEEEEEEEEEEHH		23.2020534510
223PhosphorylationVSVNAVQTVVRQGEN
EEEEEHHHHHHCCCC		17.8624719451
230N-linked_GlycosylationTVVRQGENITLMCIV
HHHHCCCCEEEEEEE		39.0920534510
292N-linked_GlycosylationDSGTYTCNVTESVND
CCCEEEEECCCCCCC		35.6320534510
307N-linked_GlycosylationHQDEKAINITVVESG
CCCCEEEEEEEEECC		28.8320534510
354N-linked_GlycosylationTVLWFKDNRTLGDSS
EEEEEECCCCCCCCC		39.15UniProtKB CARBOHYD
371N-linked_GlycosylationEIALSTRNVSETRYV
CEEEEECCCCCCEEE		41.58UniProtKB CARBOHYD
377PhosphorylationRNVSETRYVSELTLV
CCCCCCEEEEEEEEE		18.7525690035
468N-linked_GlycosylationLPPTLLGNSSEEESQ
CCCCCCCCCCHHHHH		42.19UniProtKB CARBOHYD
479N-linked_GlycosylationEESQLETNVTYWEEE
HHHHCCCCCCCCCCH		18.11UniProtKB CARBOHYD
562PhosphorylationLWQKKPRYEIRWKVI
HHHCCCCCEEEEEEE		25.0010821867
562DephosphorylationLWQKKPRYEIRWKVI
HHHCCCCCEEEEEEE		25.0012062403
571PhosphorylationIRWKVIESVSSDGHE
EEEEEEEEECCCCCE		19.0426356563
573PhosphorylationWKVIESVSSDGHEYI
EEEEEEECCCCCEEE		31.8026356563
574PhosphorylationKVIESVSSDGHEYIY
EEEEEECCCCCEEEE		45.5226356563
579PhosphorylationVSSDGHEYIYVDPMQ
ECCCCCEEEEECCCC		7.5915902258
579DephosphorylationVSSDGHEYIYVDPMQ
ECCCCCEEEEECCCC		7.5914966296
581PhosphorylationSDGHEYIYVDPMQLP
CCCCEEEEECCCCCC		9.6315902258
589PhosphorylationVDPMQLPYDSTWELP
ECCCCCCCCCCCCCC		30.99-
605PhosphorylationDQLVLGRTLGSGAFG
HHEEEEEEECCCHHH		33.40-
608PhosphorylationVLGRTLGSGAFGQVV
EEEEEECCCHHHHHH		30.02-
639PhosphorylationAVKMLKSTARSSEKQ
HHHHHHHHCCCHHHH		25.2222798277
642PhosphorylationMLKSTARSSEKQALM
HHHHHCCCHHHHHHH		40.1422798277
643PhosphorylationLKSTARSSEKQALMS
HHHHCCCHHHHHHHH		43.1722798277
645UbiquitinationSTARSSEKQALMSEL
HHCCCHHHHHHHHHH		42.70-
672PhosphorylationVNLLGACTKGGPIYI
HHHHHHHCCCCCEEE		31.9922210691
678PhosphorylationCTKGGPIYIITEYCR
HCCCCCEEEEECCCC		6.8724927040
683PhosphorylationPIYIITEYCRYGDLV
CEEEEECCCCCHHHH		3.5827259358
686PhosphorylationIITEYCRYGDLVDYL
EEECCCCCHHHHHHH		16.0725884760
692PhosphorylationRYGDLVDYLHRNKHT
CCHHHHHHHHHCCCC		9.2725884760
705PhosphorylationHTFLQHHSDKRRPPS
CCHHHCCCCCCCCCC		42.5823909892
707UbiquitinationFLQHHSDKRRPPSAE
HHHCCCCCCCCCCHH		54.0121139048
712PhosphorylationSDKRRPPSAELYSNA
CCCCCCCCHHHHCCC		36.7426657352
716PhosphorylationRPPSAELYSNALPVG
CCCCHHHHCCCCCCC		7.4415902258
717PhosphorylationPPSAELYSNALPVGL
CCCHHHHCCCCCCCC		28.4025884760
740PhosphorylationTGESDGGYMDMSKDE
ECCCCCCCCCCCCCC		8.7515902258
740DephosphorylationTGESDGGYMDMSKDE
ECCCCCCCCCCCCCC		8.7512681492
748PhosphorylationMDMSKDESVDYVPML
CCCCCCCCCCEEEEE		30.3522199227
751DephosphorylationSKDESVDYVPMLDMK
CCCCCCCEEEEECCC		12.3312681492
751PhosphorylationSKDESVDYVPMLDMK
CCCCCCCEEEEECCC		12.331314164
763PhosphorylationDMKGDVKYADIESSN
CCCCCEEEEECCCCC		14.89N.N.
768PhosphorylationVKYADIESSNYMAPY
EEEEECCCCCCEECC		24.9826356563
769PhosphorylationKYADIESSNYMAPYD
EEEECCCCCCEECCC		21.1326356563
771DephosphorylationADIESSNYMAPYDNY
EECCCCCCEECCCCC		9.157545675
771PhosphorylationADIESSNYMAPYDNY
EECCCCCCEECCCCC		9.1515902258
775PhosphorylationSSNYMAPYDNYVPSA
CCCCEECCCCCCCCC		13.7910821867
778PhosphorylationYMAPYDNYVPSAPER
CEECCCCCCCCCCCC		15.7310821867
857DephosphorylationDIMRDSNYISKGSTF
HHHHCCCCCCCCCCC		15.5512062403
857PhosphorylationDIMRDSNYISKGSTF
HHHHCCCCCCCCCCC		15.5515902258
921PhosphorylationYNAIKRGYRMAQPAH
HHHHHHCCCCCCCCC		10.97-
930PhosphorylationMAQPAHASDEIYEIM
CCCCCCCCHHHHHHH		26.38-
934PhosphorylationAHASDEIYEIMQKCW
CCCCHHHHHHHHHHH		9.4319275932
970PhosphorylationGEGYKKKYQQVDEEF
CCHHHHHHHHHCHHH		17.0419275932
1009DephosphorylationLDTSSVLYTAVQPNE
CCCCCCEEEEECCCC		7.187688466
1009PhosphorylationLDTSSVLYTAVQPNE
CCCCCCEEEEECCCC		7.1815902258
1021PhosphorylationPNEGDNDYIIPLPDP
CCCCCCCEEEECCCC		13.6515902258
1021DephosphorylationPNEGDNDYIIPLPDP
CCCCCCCEEEECCCC		13.6512062403
1104PhosphorylationPRAEAEDSFL-----
CCHHHHHHCC-----		21.6915271984
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
562YPhosphorylationKinasePGFRBP09619
PhosphoELM
579YPhosphorylationKinasePGFRBP09619
PhosphoELM
581YPhosphorylationKinasePGFRBP09619
PhosphoELM
589YPhosphorylationKinasePDGFRBP09619
GPS
686YPhosphorylationKinaseABLP00519
PSP
686YPhosphorylationKinaseABL-FAMILY-GPS
686YPhosphorylationKinaseARGP42684
PSP
712SPhosphorylationKinasePKG2Q13237
PSP
716YPhosphorylationKinasePDGFRBP09619
GPS
740YPhosphorylationKinasePGFRBP09619
PhosphoELM
751YPhosphorylationKinasePDGFR_GROUP-PhosphoELM
751YPhosphorylationKinasePDGFR-FAMILY-GPS
751YPhosphorylationKinasePGFRBP09619
PhosphoELM
763YPhosphorylationKinasePGFRBP09619
PhosphoELM
771YPhosphorylationKinasePGFRBP09619
PhosphoELM
775YPhosphorylationKinasePGFRBP09619
PhosphoELM
778YPhosphorylationKinasePGFRBP09619
PhosphoELM
857YPhosphorylationKinasePGFRBP09619
PhosphoELM
857YPhosphorylationKinasePDGFR_GROUP-PhosphoELM
857YPhosphorylationKinasePDGFR-FAMILY-GPS
934YPhosphorylationKinaseABLP00519
PSP
934YPhosphorylationKinaseABL2P42684
Uniprot
934YPhosphorylationKinaseABL-FAMILY-GPS
970YPhosphorylationKinaseABLP00519
PSP
970YPhosphorylationKinaseABL-FAMILY-GPS
970YPhosphorylationKinaseABL2P42684
Uniprot
1009YPhosphorylationKinasePGFRBP09619
PhosphoELM
1021YPhosphorylationKinasePGFRBP09619
PhosphoELM
1104SPhosphorylationKinaseGRK2P21146
PSP
1104SPhosphorylationKinaseARBK1P25098
PhosphoELM
-KUbiquitinationE3 ubiquitin ligaseCBLP22681
PMID:10347229
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PGFRB_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 PGFRB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KR412_HUMANKRTAP4-12physical
16189514
PTN11_HUMANPTPN11physical
11266449
PGFRB_HUMANPDGFRBphysical
7523122
PLCG1_HUMANPLCG1physical
8443409
NHRF1_HUMANSLC9A3R1physical
11046132
PGFRB_HUMANPDGFRBphysical
11046132
SHC1_HUMANSHC1physical
8195171
P85A_HUMANPIK3R1physical
10697503
RASA1_HUMANRASA1physical
10697503
ARBK1_HUMANADRBK1physical
12381737
MFGM_HUMANMFGE8physical
21868707
ETV6_HUMANETV6physical
22262849
IRF8_HUMANIRF8physical
22262849
P85A_HUMANPIK3R1physical
15377662
PLCG1_HUMANPLCG1physical
22974441
VAV_HUMANVAV1physical
22974441
TRIP6_HUMANTRIP6physical
25416956
KLH12_HUMANKLHL12physical
25416956
PDGFB_HUMANPDGFBphysical
20577048
ACK1_HUMANTNK2physical
25257795
MYO1E_HUMANMYO1Ephysical
26496610
BCLF1_HUMANBCLAF1physical
26496610
ZZEF1_HUMANZZEF1physical
26496610
FGD6_HUMANFGD6physical
26496610
FOXK1_HUMANFOXK1physical
26496610
P55G_HUMANPIK3R3physical
25241761
PTEN_HUMANPTENphysical
25241761
STA5A_HUMANSTAT5Aphysical
25241761
STAT3_HUMANSTAT3physical
25241761
CBLB_HUMANCBLBphysical
27048651
DEP1A_HUMANDEPDC1physical
28514442
ATR_HUMANATRphysical
28514442
FOXK2_HUMANFOXK2physical
28514442
ANKL2_HUMANANKLE2physical
28514442
FOXK1_HUMANFOXK1physical
28514442
AVR2B_HUMANACVR2Bphysical
28514442
UBB_HUMANUBBphysical
28514442
PGFRA_HUMANPDGFRAphysical
28514442
ABCD4_HUMANABCD4physical
28514442
NOP9_HUMANNOP9physical
28514442
FND3A_HUMANFNDC3Aphysical
28514442
HUS1_HUMANHUS1physical
28514442
TYW1_HUMANTYW1physical
28514442
CGRF1_HUMANCGRRF1physical
28514442
HELLS_HUMANHELLSphysical
28514442
PDE3B_HUMANPDE3Bphysical
28514442
P85A_HUMANPIK3R1physical
28514442
BMR1A_HUMANBMPR1Aphysical
28514442
CNEP1_HUMANCTDNEP1physical
28514442
PPM1L_HUMANPPM1Lphysical
28065597
TPTE_HUMANTPTEphysical
28065597
Drug and Disease Associations
Kegg Disease
H00042 Glioma
OMIM Disease
Note=A chromosomal aberration involving PDGFRB is found in a form of chronic myelomonocytic leukemia (CMML). Translocation t(5
12)(q33
p13) with EVT6/TEL. It is characterized by abnormal clonal myeloid proliferation and by progression to acute myelogenous leukemia (AML).
131440
601626Leukemia, acute myelogenous (AML)
607785Leukemia, juvenile myelomonocytic (JMML)
615007Basal ganglia calcification, idiopathic, 4 (IBGC4)
228550Myofibromatosis, infantile 1 (IMF1)
Kegg Drug
D01441 Imatinib mesilate (JAN); Imatinib mesylate (USAN); Gleevec (TN); Glivec (TN)
D03065 Becaplermin (USAN/INN); Regranex (TN)
D03218 Axitinib (JAN/USAN); Inlyta (TN)
D03658 Dasatinib (INN)
D05029 Midostaurin (USAN/INN)
D05380 Pazopanib hydrochloride (JAN/USAN); Votrient (TN)
D06005 Tandutinib (USAN/INN)
D06272 Sorafenib tosilate (JAN); Sorafenib tosylate (USAN); Nexavar (TN)
D06285 Vatalanib (USAN/INN)
D06402 Sunitinib malate (JAN/USAN); Sutent (TN)
D06413 Nilotinib hydrochloride hydrate (JAN); Tasigna (TN)
D06414 Dasatinib hydrate (JAN); Dasatinib (USAN); Sprycel (TN)
D06678 Motesanib; AMG 706
D08066 Imatinib (INN); Glamox (TN)
D08503 Toceranib (USAN)
D08524 Sorafenib (USAN/INN)
D08544 Toceranib phosphate (USAN)
D08552 Sunitinib (INN)
D08881 Cediranib (USAN/INN)
D08883 Cediranib maleate (JAN/USAN)
D08907 Dovitinib lactate (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)
D10062 Cabozantinib (USAN)
D10095 Cabozantinib s-malate (USAN); Cometriq (TN)
D10102 Crenolanib (USAN)
D10103 Crenolanib besylate (USAN)
D10137 Regorafenib hydrate (JAN); Stivarga (TN)
D10138 Regorafenib (USAN/INN)
D10396 Nintedanib esylate (USAN)
D10423 Ilorasertib (USAN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PGFRB_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Structures of a platelet-derived growth factor/propeptide complex anda platelet-derived growth factor/receptor complex.";
Shim A.H., Liu H., Focia P.J., Chen X., Lin P.C., He X.;
Proc. Natl. Acad. Sci. U.S.A. 107:11307-11312(2010).
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 33-314 IN COMPLEX WITH PDGFB,SUBUNIT, GLYCOSYLATION AT ASN-45; ASN-89; ASN-103; ASN-215; ASN-230;ASN-292 AND ASN-307, AND DISULFIDE BONDS.
Phosphorylation
ReferencePubMed
"Regulation of PDGF signalling and vascular remodelling byperoxiredoxin II.";
Choi M.H., Lee I.K., Kim G.W., Kim B.U., Han Y.H., Yu D.Y., Park H.S.,Kim K.Y., Lee J.S., Choi C., Bae Y.S., Lee B.I., Rhee S.G., Kang S.W.;
Nature 435:347-353(2005).
Cited for: AUTOPHOSPHORYLATION AT TYR-579; TYR-581; TYR-716; TYR-740; TYR-771;TYR-857; TYR-1009 AND TYR-1021.
"Site-selective dephosphorylation of the platelet-derived growthfactor beta-receptor by the receptor-like protein-tyrosine phosphataseDEP-1.";
Kovalenko M., Denner K., Sandstrom J., Persson C., Gross S., Jandt E.,Vilella R., Bohmer F., Ostman A.;
J. Biol. Chem. 275:16219-16226(2000).
Cited for: AUTOPHOSPHORYLATION AT TYR-562; TYR-751; TYR-763; TYR-771; TYR-775;TYR-778; TYR-857; TYR-1009 AND TYR-1021, AND DEPHOSPHORYLATION BYPTPRJ AT TYR-751; TYR-857; TYR-1009 AND TYR-1021.
"Identification of two juxtamembrane autophosphorylation sites in thePDGF beta-receptor; involvement in the interaction with Src familytyrosine kinases.";
Mori S., Ronnstrand L., Yokote K., Engstrom A., Courtneidge S.A.,Claesson-Welsh L., Heldin C.H.;
EMBO J. 12:2257-2264(1993).
Cited for: FUNCTION AS PDGFB RECEPTOR IN CELL PROLIFERATION, PHOSPHORYLATION ATTYR-579 AND TYR-581; INTERACTION WITH SRC, CATALYTIC ACTIVITY, ANDMUTAGENESIS OF TYR-579 AND TYR-581.
"Identification of two C-terminal autophosphorylation sites in thePDGF beta-receptor: involvement in the interaction with phospholipaseC-gamma.";
Ronnstrand L., Mori S., Arridsson A.K., Eriksson A., Wernstedt C.,Hellman U., Claesson-Welsh L., Heldin C.H.;
EMBO J. 11:3911-3919(1992).
Cited for: FUNCTION AS PDGFB RECEPTOR IN CELL PROLIFERATION AND PHOSPHORYLATIONOF PLCG1, INTERACTION WITH PLCG1, PHOSPHORYLATION AT TYR-1009 ANDTYR-1021, AND MUTAGENESIS OF TYR-1009 AND TYR-1021.
"Phosphorylation sites in the PDGF receptor with differentspecificities for binding GAP and PI3 kinase in vivo.";
Kashishian A., Kazlauskas A., Cooper J.A.;
EMBO J. 11:1373-1382(1992).
Cited for: FUNCTION IN PHOSPHORYLATION OF PIK3R1 AND RASA1/GAP AND IN ACTIVATIONOF PHOSPHATIDYLINOSITOL 3-KINASE, INTERACTION WITH PIK3R1 ANDRASA1/GAP, PHOSPHORYLATION AT TYR-740; TYR-751; TYR-771 AND TYR-857,AND MUTAGENESIS OF MET-635; TYR-740; TYR-751; TYR-771; TYR-778 ANDTYR-857.
"Platelet-derived growth factor (PDGF) stimulates PDGF receptorsubunit 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).
Cited for: INTERACTION WITH PDGFRA; PDGFA AND PDGFB, FUNCTION AS RECEPTOR FORPDGFA AND PDGFB, AND PHOSPHORYLATION AT TYR-857 AND TYR-751.
"Autophosphorylation of the PDGF receptor in the kinase insert regionregulates interactions with cell proteins.";
Kazlauskas A., Cooper J.A.;
Cell 58:1121-1133(1989).
Cited for: PHOSPHORYLATION AT TYR-751 AND TYR-857.

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