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Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor) (CD140 antigen-like family member B) (Platelet-derived growth factor receptor 1) (PDGFR-1) (CD antigen CD140b)

 PGFRB_HUMAN             Reviewed;        1106 AA.
P09619; B5A957; Q8N5L4;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
17-JUN-2020, entry version 242.
RecName: Full=Platelet-derived growth factor receptor beta;
Short=PDGF-R-beta;
Short=PDGFR-beta;
EC=2.7.10.1;
AltName: Full=Beta platelet-derived growth factor receptor;
AltName: Full=Beta-type platelet-derived growth factor receptor;
AltName: Full=CD140 antigen-like family member B;
AltName: Full=Platelet-derived growth factor receptor 1;
Short=PDGFR-1;
AltName: CD_antigen=CD140b;
Flags: Precursor;
Name=PDGFRB; Synonyms=PDGFR, PDGFR1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION AS PDGFB RECEPTOR,
SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, AND INTERACTION WITH PDGFB.
PubMed=2835772; DOI=10.1073/pnas.85.10.3435;
Gronwald R.G.K., Grant F.J., Haldeman B.A., Hart C.E., O'Hara P.J.,
Hagen F.S., Ross R., Bowen-Pope D.F., Murray M.J.;
"Cloning and expression of a cDNA coding for the human platelet-derived
growth factor receptor: evidence for more than one receptor class.";
Proc. Natl. Acad. Sci. U.S.A. 85:3435-3439(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION AS PDGFB RECEPTOR,
SUBCELLULAR LOCATION, GLYCOSYLATION, AUTOPHOSPHORYLATION, AND INTERACTION
WITH PDGFA AND PDGFB.
PubMed=2850496; DOI=10.1128/mcb.8.8.3476;
Claesson-Welsh L., Eriksson A., Moren A., Severinsson L., Ek B.,
Oestman A., Betsholtz C., Heldin C.-H.;
"cDNA cloning and expression of a human platelet-derived growth factor
(PDGF) receptor specific for B-chain-containing PDGF molecules.";
Mol. Cell. Biol. 8:3476-3486(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
PubMed=18593464; DOI=10.1186/ar2447;
Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D.,
Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.;
"Novel splice variants derived from the receptor tyrosine kinase
superfamily are potential therapeutics for rheumatoid arthritis.";
Arthritis Res. Ther. 10:R73-R73(2008).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PHE-180.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 548-569.
PubMed=9285559; DOI=10.1038/sj.onc.1201267;
Chi K.D., McPhee R.A., Wagner A.S., Dietz J.J., Pantazis P., Goustin A.S.;
"Integration of proviral DNA into the PDGF beta-receptor gene in HTLV-I-
infected T-cells results in a novel tyrosine kinase product with
transforming activity.";
Oncogene 15:1051-1057(1997).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 559-1106 (ISOFORM 1), AND CHROMOSOMAL
TRANSLOCATION WITH CEP85L.
PubMed=21938754; DOI=10.1002/gcc.20930;
Chmielecki J., Peifer M., Viale A., Hutchinson K., Giltnane J., Socci N.D.,
Hollis C.J., Dean R.S., Yenamandra A., Jagasia M., Kim A.S., Dave U.P.,
Thomas R.K., Pao W.;
"Systematic screen for tyrosine kinase rearrangements identifies a novel
C6orf204-PDGFRB fusion in a patient with recurrent T-ALL and an associated
myeloproliferative neoplasm.";
Genes Chromosomes Cancer 51:54-65(2012).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1046-1106.
PubMed=2846185; DOI=10.1016/0092-8674(88)90224-3;
Roberts W.M., Look A.T., Roussel M.F., Sherr C.J.;
"Tandem linkage of human CSF-1 receptor (c-fms) and PDGF receptor genes.";
Cell 55:655-661(1988).
[9]
PROTEIN SEQUENCE OF 33-47.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally verified
cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[10]
PHOSPHORYLATION AT TYR-751 AND TYR-857.
PubMed=2550144; DOI=10.1016/0092-8674(89)90510-2;
Kazlauskas A., Cooper J.A.;
"Autophosphorylation of the PDGF receptor in the kinase insert region
regulates interactions with cell proteins.";
Cell 58:1121-1133(1989).
[11]
FUNCTION AS PDGFB RECEPTOR IN CELL PROLIFERATION AND CHEMOTAXIS, AND
SUBCELLULAR LOCATION.
PubMed=2554309; DOI=10.1073/pnas.86.21.8314;
Matsui T., Pierce J.H., Fleming T.P., Greenberger J.S., LaRochelle W.J.,
Ruggiero M., Aaronson S.A.;
"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.";
Proc. Natl. Acad. Sci. U.S.A. 86:8314-8318(1989).
[12]
FUNCTION IN CELL PROLIFERATION; ACTIVATION OF PLCG1 AND IN PHOSPHORYLATION
OF PLCG1 AND RASA1/GAP, AND MUTAGENESIS OF TYR-751 AND TYR-857.
PubMed=1653029; DOI=10.1091/mbc.2.6.413;
Kazlauskas A., Durden D.L., Cooper J.A.;
"Functions of the major tyrosine phosphorylation site of the PDGF receptor
beta subunit.";
Cell Regul. 2:413-425(1991).
[13]
INTERACTION WITH PDGFRA; PDGFA AND PDGFB, FUNCTION AS RECEPTOR FOR PDGFA
AND PDGFB, AND PHOSPHORYLATION AT TYR-857 AND TYR-751.
PubMed=1709159;
Kelly J.D., Haldeman B.A., Grant F.J., Murray M.J., Seifert R.A.,
Bowen-Pope D.F., Cooper J.A., Kazlauskas A.;
"Platelet-derived growth factor (PDGF) stimulates PDGF receptor subunit
dimerization and intersubunit trans-phosphorylation.";
J. Biol. Chem. 266:8987-8992(1991).
[14]
FUNCTION AS RECEPTOR FOR PDGFA AND PDGFB, SUBCELLULAR LOCATION, CATALYTIC
ACTIVITY, AND MUTAGENESIS OF LYS-634.
PubMed=1846866; DOI=10.1083/jcb.112.3.469;
Sorkin A., Westermark B., Heldin C.H., Claesson-Welsh L.;
"Effect of receptor kinase inactivation on the rate of internalization and
degradation of PDGF and the PDGF beta-receptor.";
J. Cell Biol. 112:469-478(1991).
[15]
FUNCTION IN ACTIVATION OF PHOSPHATIDYLINOSITOL 3-KINASE ACTIVITY,
INTERACTION WITH PIK3R1 AND RASA1, PHOSPHORYLATION AT TYR-740; TYR-751;
TYR-771 AND TYR-857, AND MUTAGENESIS OF LYS-634; TYR-716; TYR-740; TYR-751;
TYR-763; TYR-771; TYR-775; TYR-778 AND TYR-857.
PubMed=1314164; DOI=10.1002/j.1460-2075.1992.tb05182.x;
Kashishian A., Kazlauskas A., Cooper J.A.;
"Phosphorylation sites in the PDGF receptor with different specificities
for binding GAP and PI3 kinase in vivo.";
EMBO J. 11:1373-1382(1992).
[16]
FUNCTION AS PDGFB RECEPTOR IN CELL PROLIFERATION AND PHOSPHORYLATION OF
PLCG1, INTERACTION WITH PLCG1, PHOSPHORYLATION AT TYR-1009 AND TYR-1021,
AND MUTAGENESIS OF TYR-1009 AND TYR-1021.
PubMed=1396585; DOI=10.1002/j.1460-2075.1992.tb05484.x;
Ronnstrand L., Mori S., Arridsson A.K., Eriksson A., Wernstedt C.,
Hellman U., Claesson-Welsh L., Heldin C.H.;
"Identification of two C-terminal autophosphorylation sites in the PDGF
beta-receptor: involvement in the interaction with phospholipase C-gamma.";
EMBO J. 11:3911-3919(1992).
[17]
UBIQUITINATION, AND DEGRADATION.
PubMed=1313434;
Mori S., Heldin C.H., Claesson-Welsh L.;
"Ligand-induced polyubiquitination of the platelet-derived growth factor
beta-receptor.";
J. Biol. Chem. 267:6429-6434(1992).
[18]
INTERACTION WITH PIK3R1 AND RASA1, AND MUTAGENESIS OF TYR-740; TYR-751 AND
TYR-771.
PubMed=1375321; DOI=10.1128/mcb.12.6.2534;
Kazlauskas A., Kashishian A., Cooper J.A., Valius M.;
"GTPase-activating protein and phosphatidylinositol 3-kinase bind to
distinct regions of the platelet-derived growth factor receptor beta
subunit.";
Mol. Cell. Biol. 12:2534-2544(1992).
[19]
FUNCTION AS PDGFB RECEPTOR IN CELL PROLIFERATION, PHOSPHORYLATION AT
TYR-579 AND TYR-581; INTERACTION WITH SRC, CATALYTIC ACTIVITY, AND
MUTAGENESIS OF TYR-579 AND TYR-581.
PubMed=7685273; DOI=10.1002/j.1460-2075.1993.tb05879.x;
Mori S., Ronnstrand L., Yokote K., Engstrom A., Courtneidge S.A.,
Claesson-Welsh L., Heldin C.H.;
"Identification of two juxtamembrane autophosphorylation sites in the PDGF
beta-receptor; involvement in the interaction with Src family tyrosine
kinases.";
EMBO J. 12:2257-2264(1993).
[20]
INTERACTION WITH DGFA AND PDGFB.
PubMed=7679113;
Fretto L.J., Snape A.J., Tomlinson J.E., Seroogy J.J., Wolf D.L.,
LaRochelle W.J., Giese N.A.;
"Mechanism of platelet-derived growth factor (PDGF) AA, AB, and BB binding
to alpha and beta PDGF receptor.";
J. Biol. Chem. 268:3625-3631(1993).
[21]
FUNCTION IN PHOSPHORYLATION AND ACTIVATION OF PTPN11, INTERACTION WITH
PTPN11; PIK3R1; PLCG1 AND RASA1, AND MUTAGENESIS OF TYR-1009.
PubMed=7691811;
Lechleider R.J., Sugimoto S., Bennett A.M., Kashishian A.S., Cooper J.A.,
Shoelson S.E., Walsh C.T., Neel B.G.;
"Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by
its binding site, phosphotyrosine 1009, on the human platelet-derived
growth factor receptor.";
J. Biol. Chem. 268:21478-21481(1993).
[22]
INTERACTION WITH NCK1 AND PIK3R1, FUNCTION IN PHOSPHORYLATION OF NCK1, AND
MUTAGENESIS OF TYR-751.
PubMed=7692233; DOI=10.1128/mcb.13.11.6889;
Nishimura R., Li W., Kashishian A., Mondino A., Zhou M., Cooper J.,
Schlessinger J.;
"Two signaling molecules share a phosphotyrosine-containing binding site in
the platelet-derived growth factor receptor.";
Mol. Cell. Biol. 13:6889-6896(1993).
[23]
INTERACTION WITH SHB.
PubMed=8302579;
Welsh M., Mares J., Karlsson T., Lavergne C., Breant B., Claesson-Welsh L.;
"Shb is a ubiquitously expressed Src homology 2 protein.";
Oncogene 9:19-27(1994).
[24]
INTERACTION WITH GRB7.
PubMed=8940081; DOI=10.1074/jbc.271.48.30942;
Yokote K., Margolis B., Heldin C.H., Claesson-Welsh L.;
"Grb7 is a downstream signaling component of platelet-derived growth factor
alpha- and beta-receptors.";
J. Biol. Chem. 271:30942-30949(1996).
[25]
CHROMOSOMAL TRANSLOCATION WITH TRIP11.
PubMed=9373237;
Abe A., Emi N., Tanimoto M., Terasaki H., Marunouchi T., Saito H.;
"Fusion of the platelet-derived growth factor receptor beta to a novel gene
CEV14 in acute myelogenous leukemia after clonal evolution.";
Blood 90:4271-4277(1997).
[26]
INTERACTION WITH GRB10, AND MUTAGENESIS OF TYR-579; TYR-581; TYR-716;
TYR-740; TYR-751; TYR-771; TYR-857; TYR-1009 AND TYR-1021.
PubMed=10454568; DOI=10.1128/mcb.19.9.6217;
Wang J., Dai H., Yousaf N., Moussaif M., Deng Y., Boufelliga A.,
Swamy O.R., Leone M.E., Riedel H.;
"Grb10, a positive, stimulatory signaling adapter in platelet-derived
growth factor BB-, insulin-like growth factor I-, and insulin-mediated
mitogenesis.";
Mol. Cell. Biol. 19:6217-6228(1999).
[27]
INTERACTION WITH SH2B2/APS.
PubMed=9989826; DOI=10.1038/sj.onc.1202326;
Yokouchi M., Wakioka T., Sakamoto H., Yasukawa H., Ohtsuka S., Sasaki A.,
Ohtsubo M., Valius M., Inoue A., Komiya S., Yoshimura A.;
"APS, an adaptor protein containing PH and SH2 domains, is associated with
the PDGF receptor and c-Cbl and inhibits PDGF-induced mitogenesis.";
Oncogene 18:759-767(1999).
[28]
PHOSPHORYLATION AT TYR-562; TYR-751; TYR-763; TYR-771; TYR-775; TYR-778;
TYR-857; TYR-1009 AND TYR-1021, AND DEPHOSPHORYLATION AT TYR-751; TYR-857;
TYR-1009 AND TYR-1021 BY PTPRJ.
PubMed=10821867; DOI=10.1074/jbc.275.21.16219;
Kovalenko M., Denner K., Sandstrom J., Persson C., Gross S., Jandt E.,
Vilella R., Bohmer F., Ostman A.;
"Site-selective dephosphorylation of the platelet-derived growth factor
beta-receptor by the receptor-like protein-tyrosine phosphatase DEP-1.";
J. Biol. Chem. 275:16219-16226(2000).
[29]
INTERACTION WITH PIK3C2B.
PubMed=10805725; DOI=10.1128/mcb.20.11.3817-3830.2000;
Arcaro A., Zvelebil M.J., Wallasch C., Ullrich A., Waterfield M.D.,
Domin J.;
"Class II phosphoinositide 3-kinases are downstream targets of activated
polypeptide growth factor receptors.";
Mol. Cell. Biol. 20:3817-3830(2000).
[30]
FUNCTION AS A RECEPTOR FOR PDGFC, AND INTERACTION WITH PDGFC.
PubMed=11297552; DOI=10.1074/jbc.m101056200;
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.;
"Platelet-derived growth factor C (PDGF-C), a novel growth factor that
binds to PDGF alpha and beta receptor.";
J. Biol. Chem. 276:27406-27414(2001).
[31]
FUNCTION AS A RECEPTOR FOR PDGFD.
PubMed=11331881; DOI=10.1038/35074588;
Bergsten E., Uutela M., Li X., Pietras K., Oestman A., Heldin C.-H.,
Alitalo K., Eriksson U.;
"PDGF-D is a specific, protease-activated ligand for the PDGF beta-
receptor.";
Nat. Cell Biol. 3:512-516(2001).
[32]
CHROMOSOMAL TRANSLOCATION WITH ETV6.
PubMed=12181402; DOI=10.1056/nejmoa020150;
Apperley J.F., Gardembas M., Melo J.V., Russell-Jones R., Bain B.J.,
Baxter E.J., Chase A., Chessells J.M., Colombat M., Dearden C.E.,
Dimitrijevic S., Mahon F.-X., Marin D., Nikolova Z., Olavarria E.,
Silberman S., Schultheis B., Cross N.C.P., Goldman J.M.;
"Response to imatinib mesylate in patients with chronic myeloproliferative
diseases with rearrangements of the platelet-derived growth factor receptor
beta.";
N. Engl. J. Med. 347:481-487(2002).
[33]
CHROMOSOMAL TRANSLOCATION WITH PDE4DIP.
PubMed=12907457; DOI=10.1182/blood-2003-04-1150;
Wilkinson K., Velloso E.R.P., Lopes L.F., Lee C., Aster J.C., Shipp M.A.,
Aguiar R.C.T.;
"Cloning of the t(1;5)(q23;q33) in a myeloproliferative disorder associated
with eosinophilia: involvement of PDGFRB and response to imatinib.";
Blood 102:4187-4190(2003).
[34]
CHROMOSOMAL TRANSLOCATION WITH SPECC1.
PubMed=15087372; DOI=10.1158/0008-5472.can-03-4026;
Morerio C., Acquila M., Rosanda C., Rapella A., Dufour C., Locatelli F.,
Maserati E., Pasquali F., Panarello C.;
"HCMOGT-1 is a novel fusion partner to PDGFRB in juvenile myelomonocytic
leukemia with t(5;17)(q33;p11.2).";
Cancer Res. 64:2649-2651(2004).
[35]
CHROMOSOMAL TRANSLOCATION WITH TP53BP1, AND ACTIVITY REGULATION.
PubMed=15492236; DOI=10.1158/0008-5472.can-04-2005;
Grand F.H., Burgstaller S., Kuhr T., Baxter E.J., Webersinke G., Thaler J.,
Chase A.J., Cross N.C.;
"p53-Binding protein 1 is fused to the platelet-derived growth factor
receptor beta in a patient with a t(5;15)(q33;q22) and an imatinib-
responsive eosinophilic myeloproliferative disorder.";
Cancer Res. 64:7216-7219(2004).
[36]
PHOSPHORYLATION AT TYR-579; TYR-751; TYR-771 AND TYR-1021, AND
DEPHOSPHORYLATION AT TYR-579 AND TYR-1021 BY PTPN2.
PubMed=14966296; DOI=10.1128/mcb.24.5.2190-2201.2004;
Persson C., Saevenhed C., Bourdeau A., Tremblay M.L., Markova B.,
Boehmer F.D., Haj F.G., Neel B.G., Elson A., Heldin C.H., Roennstrand L.,
Ostman A., Hellberg C.;
"Site-selective regulation of platelet-derived growth factor beta receptor
tyrosine phosphorylation by T-cell protein tyrosine phosphatase.";
Mol. Cell. Biol. 24:2190-2201(2004).
[37]
PHOSPHORYLATION AT TYR-579; TYR-581; TYR-716; TYR-740; TYR-771; TYR-857;
TYR-1009 AND TYR-1021.
PubMed=15902258; DOI=10.1038/nature03587;
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.;
"Regulation of PDGF signalling and vascular remodelling by peroxiredoxin
II.";
Nature 435:347-353(2005).
[38]
INTERACTION WITH CBL, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-1021, AND
UBIQUITINATION.
PubMed=17620338; DOI=10.1074/jbc.m701797200;
Reddi A.L., Ying G., Duan L., Chen G., Dimri M., Douillard P., Druker B.J.,
Naramura M., Band V., Band H.;
"Binding of Cbl to a phospholipase Cgamma1-docking site on platelet-derived
growth factor receptor beta provides a dual mechanism of negative
regulation.";
J. Biol. Chem. 282:29336-29347(2007).
[39]
FUNCTION AS PDGFD RECEPTOR.
PubMed=21098708; DOI=10.1158/0008-5472.can-10-0511;
Ustach C.V., Huang W., Conley-LaComb M.K., Lin C.Y., Che M., Abrams J.,
Kim H.R.;
"A novel signaling axis of matriptase/PDGF-D/ss-PDGFR in human prostate
cancer.";
Cancer Res. 70:9631-9640(2010).
[40]
FUNCTION IN PHOSPHORYLATION OF CBL; STAM; PDCD6IP/ALIX; PLCG1 AND PTPN11,
CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF LYS-634 AND TYR-857.
PubMed=20494825; DOI=10.1016/j.cellsig.2010.05.004;
Wardega P., Heldin C.H., Lennartsson J.;
"Mutation of tyrosine residue 857 in the PDGF beta-receptor affects cell
proliferation but not migration.";
Cell. Signal. 22:1363-1368(2010).
[41]
FUNCTION.
PubMed=20529858; DOI=10.1074/jbc.m110.102566;
Mendelson K., Swendeman S., Saftig P., Blobel C.P.;
"Stimulation of platelet-derived growth factor receptor beta (PDGFRbeta)
activates ADAM17 and promotes metalloproteinase-dependent cross-talk
between the PDGFRbeta and epidermal growth factor receptor (EGFR) signaling
pathways.";
J. Biol. Chem. 285:25024-25032(2010).
[42]
FUNCTION IN SMOOTH MUSCLE CELL PROLIFERATION AND MIGRATION.
PubMed=21733313; DOI=10.1017/s0007114511002571;
Kim H.J., Cha B.Y., Choi B., Lim J.S., Woo J.T., Kim J.S.;
"Glyceollins inhibit platelet-derived growth factor-mediated human arterial
smooth muscle cell proliferation and migration.";
Br. J. Nutr. 107:24-35(2012).
[43]
INTERACTION WITH SHC1 AND GRB2, AND FUNCTION IN PHOSPHORYLATION OF SHC1.
PubMed=8195171;
Yokote K., Mori S., Hansen K., McGlade J., Pawson T., Heldin C.H.,
Claesson-Welsh L.;
"Direct interaction between Shc and the platelet-derived growth factor
beta-receptor.";
J. Biol. Chem. 269:15337-15343(1994).
[44]
FUNCTION IN SMOOTH MUSCLE CELL MIGRATION AND NEOINTIMA FORMATION AFTER
BLOOD VESSEL INJURY, AND MUTAGENESIS OF TYR-740; TYR-751 AND TYR-1021.
PubMed=21679854; DOI=10.1016/j.jacc.2011.02.037;
Caglayan E., Vantler M., Leppanen O., Gerhardt F., Mustafov L.,
Ten Freyhaus H., Kappert K., Odenthal M., Zimmermann W.H., Tallquist M.D.,
Rosenkranz S.;
"Disruption of platelet-derived growth factor-dependent
phosphatidylinositol 3-kinase and phospholipase Cgamma 1 activity abolishes
vascular smooth muscle cell proliferation and migration and attenuates
neointima formation in vivo.";
J. Am. Coll. Cardiol. 57:2527-2538(2011).
[45]
INVOLVEMENT IN PENTT, VARIANT PENTT ALA-665, AND CHARACTERIZATION OF
VARIANT PENTT ALA-665.
PubMed=26279204; DOI=10.1016/j.ajhg.2015.07.009;
Johnston J.J., Sanchez-Contreras M.Y., Keppler-Noreuil K.M., Sapp J.,
Crenshaw M., Finch N.A., Cormier-Daire V., Rademakers R., Sybert V.P.,
Biesecker L.G.;
"A point mutation in PDGFRB causes autosomal-dominant Penttinen syndrome.";
Am. J. Hum. Genet. 97:465-474(2015).
[46]
INVOLVEMENT IN KOGS, AND VARIANT KOGS ARG-584.
PubMed=25454926; DOI=10.1016/j.jpeds.2014.10.015;
Takenouchi T., Yamaguchi Y., Tanikawa A., Kosaki R., Okano H., Kosaki K.;
"Novel overgrowth syndrome phenotype due to recurrent de novo PDGFRB
mutation.";
J. Pediatr. 166:483-486(2015).
[47]
CHARACTERIZATION OF VARIANTS IBGC4 PRO-658; TRP-987 AND VAL-1071, AND
FUNCTION.
PubMed=26599395; DOI=10.1371/journal.pone.0143407;
Vanlandewijck M., Lebouvier T., Andaloussi Maee M., Nahar K., Hornemann S.,
Kenkel D., Cunha S.I., Lennartsson J., Boss A., Heldin C.H., Keller A.,
Betsholtz C.;
"Functional characterization of germline mutations in PDGFB and PDGFRB in
primary familial brain calcification.";
PLoS ONE 10:E0143407-E0143407(2015).
[48]
REVIEW ON SIGNALING AND AUTOPHOSPHORYLATION.
PubMed=9739761; DOI=10.1016/s0304-419x(98)00015-8;
Heldin C.H., Ostman A., Ronnstrand L.;
"Signal transduction via platelet-derived growth factor receptors.";
Biochim. Biophys. Acta 1378:F79-113(1998).
[49]
REVIEW.
PubMed=15207817; DOI=10.1016/j.cytogfr.2004.03.002;
Ostman A.;
"PDGF receptors-mediators of autocrine tumor growth and regulators of tumor
vasculature and stroma.";
Cytokine Growth Factor Rev. 15:275-286(2004).
[50]
REVIEW.
PubMed=17419949; DOI=10.1016/s0065-230x(06)97011-0;
Ostman A., Heldin C.H.;
"PDGF receptors as targets in tumor treatment.";
Adv. Cancer Res. 97:247-274(2007).
[51]
REVIEW ON FUNCTION; LIGANDS; ROLE IN DEVELOPMENT AND DISEASE AND ACTIVATION
OF SIGNALING PATHWAYS.
PubMed=18483217; DOI=10.1101/gad.1653708;
Andrae J., Gallini R., Betsholtz C.;
"Role of platelet-derived growth factors in physiology and medicine.";
Genes Dev. 22:1276-1312(2008).
[52]
X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 751-755 IN COMPLEX WITH PIK3R1,
AND COMPARISON WITH NMR ANALYSIS.
PubMed=11567151; DOI=10.1107/s0907444901012434;
Pauptit R.A., Dennis C.A., Derbyshire D.J., Breeze A.L., Weston S.A.,
Rowsell S., Murshudov G.N.;
"NMR trial models: experiences with the colicin immunity protein Im7 and
the p85alpha C-terminal SH2-peptide complex.";
Acta Crystallogr. D 57:1397-1404(2001).
[53]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1102-1106 IN COMPLEX WITH
SLC9A3R1, AND INTERACTION WITH SLC9A3R1.
PubMed=11882663; DOI=10.1074/jbc.m201507200;
Karthikeyan S., Leung T., Ladias J.A.A.;
"Structural determinants of the Na+/H+ exchanger regulatory factor
interaction with the beta 2 adrenergic and platelet-derived growth factor
receptors.";
J. Biol. Chem. 277:18973-18978(2002).
[54]
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.
PubMed=20534510; DOI=10.1073/pnas.1000806107;
Shim A.H., Liu H., Focia P.J., Chen X., Lin P.C., He X.;
"Structures of a platelet-derived growth factor/propeptide complex and a
platelet-derived growth factor/receptor complex.";
Proc. Natl. Acad. Sci. U.S.A. 107:11307-11312(2010).
[55]
VARIANTS [LARGE SCALE ANALYSIS] PHE-29; LYS-282; LYS-485; HIS-589; TYR-718
AND ILE-882.
PubMed=17344846; DOI=10.1038/nature05610;
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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[56]
VARIANT IMF1 THR-660.
PubMed=23731542; DOI=10.1016/j.ajhg.2013.04.024;
Martignetti J.A., Tian L., Li D., Ramirez M.C., Camacho-Vanegas O.,
Camacho S.C., Guo Y., Zand D.J., Bernstein A.M., Masur S.K., Kim C.E.,
Otieno F.G., Hou C., Abdel-Magid N., Tweddale B., Metry D., Fournet J.C.,
Papp E., McPherson E.W., Zabel C., Vaksmann G., Morisot C., Keating B.,
Sleiman P.M., Cleveland J.A., Everman D.B., Zackai E., Hakonarson H.;
"Mutations in PDGFRB cause autosomal-dominant infantile myofibromatosis.";
Am. J. Hum. Genet. 92:1001-1007(2013).
[57]
VARIANT IMF1 CYS-561.
PubMed=23731537; DOI=10.1016/j.ajhg.2013.04.026;
Cheung Y.H., Gayden T., Campeau P.M., Leduc C.A., Russo D., Nguyen V.H.,
Guo J., Qi M., Guan Y., Albrecht S., Moroz B., Eldin K.W., Lu J.T.,
Schwartzentruber J., Malkin D., Berghuis A.M., Emil S., Gibbs R.A.,
Burk D.L., Vanstone M., Lee B.H., Orchard D., Boycott K.M., Chung W.K.,
Jabado N.;
"A recurrent PDGFRB mutation causes familial infantile myofibromatosis.";
Am. J. Hum. Genet. 92:996-1000(2013).
[58]
VARIANTS IBGC4 PRO-658; TRP-987 AND VAL-1071.
PubMed=24065723; DOI=10.1093/brain/awt255;
French IBGC Study Group;
Nicolas G., Pottier C., Charbonnier C., Guyant-Marechal L., Le Ber I.,
Pariente J., Labauge P., Ayrignac X., Defebvre L., Maltete D.,
Martinaud O., Lefaucheur R., Guillin O., Wallon D., Chaumette B.,
Rondepierre P., Derache N., Fromager G., Schaeffer S., Krystkowiak P.,
Verny C., Jurici S., Sauvee M., Verin M., Lebouvier T., Rouaud O.,
Thauvin-Robinet C., Rousseau S., Rovelet-Lecrux A., Frebourg T.,
Campion D., Hannequin D.;
"Phenotypic spectrum of probable and genetically-confirmed idiopathic basal
ganglia calcification.";
Brain 136:3395-3407(2013).
[59]
VARIANTS IBGC4 PRO-658 AND TRP-987.
PubMed=23255827; DOI=10.1212/wnl.0b013e31827ccf34;
Nicolas G., Pottier C., Maltete D., Coutant S., Rovelet-Lecrux A.,
Legallic S., Rousseau S., Vaschalde Y., Guyant-Marechal L., Augustin J.,
Martinaud O., Defebvre L., Krystkowiak P., Pariente J., Clanet M.,
Labauge P., Ayrignac X., Lefaucheur R., Le Ber I., Frebourg T.,
Hannequin D., Campion D.;
"Mutation of the PDGFRB gene as a cause of idiopathic basal ganglia
calcification.";
Neurology 80:181-187(2013).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:11297552, ECO:0000269|PubMed:11331881,
ECO:0000269|PubMed:1314164, ECO:0000269|PubMed:1396585,
ECO:0000269|PubMed:1653029, ECO:0000269|PubMed:1709159,
ECO:0000269|PubMed:1846866, ECO:0000269|PubMed:20494825,
ECO:0000269|PubMed:20529858, ECO:0000269|PubMed:21098708,
ECO:0000269|PubMed:21679854, ECO:0000269|PubMed:21733313,
ECO:0000269|PubMed:2554309, ECO:0000269|PubMed:26599395,
ECO:0000269|PubMed:2835772, ECO:0000269|PubMed:2850496,
ECO:0000269|PubMed:7685273, ECO:0000269|PubMed:7691811,
ECO:0000269|PubMed:7692233, ECO:0000269|PubMed:8195171}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
Evidence={ECO:0000255|PROSITE-ProRule:PRU10028,
ECO:0000269|PubMed:1846866, ECO:0000269|PubMed:20494825,
ECO:0000269|PubMed:7685273};
-!- ACTIVITY REGULATION: Present in an inactive conformation in the absence
of bound ligand. Binding of PDGFB and/or PDGFD leads to dimerization
and activation by autophosphorylation on tyrosine residues. Inhibited
by imatinib. {ECO:0000269|PubMed:15492236}.
-!- SUBUNIT: Interacts with homodimeric PDGFB and PDGFD, and with
heterodimers formed by PDGFA and PDGFB. May also interact with
homodimeric PDGFC. Monomer in the absence of bound ligand. Interaction
with homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or
homodimeric PDGFD, leads to receptor dimerization, where both PDGFRA
homodimers and heterodimers with PDGFRB are observed. Interacts with
SH2B2/APS. Interacts directly (tyrosine phosphorylated) with SHB.
Interacts (tyrosine phosphorylated) with PIK3R1 and RASA1. Interacts
(tyrosine phosphorylated) with CBL. Interacts (tyrosine phosphorylated)
with SRC and SRC family kinases. Interacts (tyrosine phosphorylated)
with PIK3C2B, maybe indirectly. Interacts (tyrosine phosphorylated)
with SHC1, GRB7, GRB10 and NCK1. Interaction with GRB2 is mediated by
SHC1. Interacts (via C-terminus) with SLC9A3R1.
{ECO:0000269|PubMed:10454568, ECO:0000269|PubMed:10805725,
ECO:0000269|PubMed:11297552, ECO:0000269|PubMed:11567151,
ECO:0000269|PubMed:11882663, ECO:0000269|PubMed:1314164,
ECO:0000269|PubMed:1375321, ECO:0000269|PubMed:1396585,
ECO:0000269|PubMed:1709159, ECO:0000269|PubMed:17620338,
ECO:0000269|PubMed:20534510, ECO:0000269|PubMed:2835772,
ECO:0000269|PubMed:2850496, ECO:0000269|PubMed:7679113,
ECO:0000269|PubMed:7691811, ECO:0000269|PubMed:7692233,
ECO:0000269|PubMed:8195171, ECO:0000269|PubMed:8302579,
ECO:0000269|PubMed:8940081, ECO:0000269|PubMed:9989826}.
-!- INTERACTION:
P09619; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-641237, EBI-742887;
P09619; P06241: FYN; NbExp=3; IntAct=EBI-641237, EBI-515315;
P09619; Q14451: GRB7; NbExp=4; IntAct=EBI-641237, EBI-970191;
P09619; P14778: IL1R1; NbExp=2; IntAct=EBI-641237, EBI-525905;
P09619; P35968: KDR; NbExp=2; IntAct=EBI-641237, EBI-1005487;
P09619; Q53G59: KLHL12; NbExp=6; IntAct=EBI-641237, EBI-740929;
P09619; Q5T749: KPRP; NbExp=3; IntAct=EBI-641237, EBI-10981970;
P09619; Q15323: KRT31; NbExp=3; IntAct=EBI-641237, EBI-948001;
P09619; O76011: KRT34; NbExp=3; IntAct=EBI-641237, EBI-1047093;
P09619; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-641237, EBI-10172052;
P09619; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-641237, EBI-11953334;
P09619; O94898: LRIG2; NbExp=3; IntAct=EBI-641237, EBI-2830372;
P09619; O75581: LRP6; NbExp=3; IntAct=EBI-641237, EBI-910915;
P09619; P01127: PDGFB; NbExp=16; IntAct=EBI-641237, EBI-1554925;
P09619; P16234: PDGFRA; NbExp=2; IntAct=EBI-641237, EBI-2861522;
P09619; P27986: PIK3R1; NbExp=19; IntAct=EBI-641237, EBI-79464;
P09619; P19174: PLCG1; NbExp=6; IntAct=EBI-641237, EBI-79387;
P09619; P60484: PTEN; NbExp=3; IntAct=EBI-641237, EBI-696162;
P09619; P18031: PTPN1; NbExp=3; IntAct=EBI-641237, EBI-968788;
P09619; Q06124: PTPN11; NbExp=8; IntAct=EBI-641237, EBI-297779;
P09619; Q05209: PTPN12; NbExp=3; IntAct=EBI-641237, EBI-2266035;
P09619; Q12913: PTPRJ; NbExp=4; IntAct=EBI-641237, EBI-2264500;
P09619; P04049: RAF1; NbExp=2; IntAct=EBI-641237, EBI-365996;
P09619; P20936: RASA1; NbExp=3; IntAct=EBI-641237, EBI-1026476;
P09619; Q13239: SLA; NbExp=4; IntAct=EBI-641237, EBI-726214;
P09619; O14745: SLC9A3R1; NbExp=5; IntAct=EBI-641237, EBI-349787;
P09619; Q15654: TRIP6; NbExp=3; IntAct=EBI-641237, EBI-742327;
P09619; P0CK45: E5; Xeno; NbExp=2; IntAct=EBI-641237, EBI-7015490;
P09619; P35918: Kdr; Xeno; NbExp=4; IntAct=EBI-641237, EBI-1555005;
P09619; P23727: PIK3R1; Xeno; NbExp=6; IntAct=EBI-641237, EBI-520244;
P09619; P08487: PLCG1; Xeno; NbExp=3; IntAct=EBI-641237, EBI-8013886;
P09619; P41499: Ptpn11; Xeno; NbExp=4; IntAct=EBI-641237, EBI-7180604;
P09619; P25020: V-SRC; Xeno; NbExp=4; IntAct=EBI-641237, EBI-8636140;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein. Cytoplasmic vesicle. Lysosome lumen. Note=After ligand
binding, the autophosphorylated receptor is ubiquitinated and
internalized, leading to its degradation.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P09619-1; Sequence=Displayed;
Name=2;
IsoId=P09619-2; Sequence=VSP_056008, VSP_056009;
-!- PTM: 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-579, and to a lesser degree, at Tyr-581, is
important for interaction with SRC family kinases. Phosphorylation at
Tyr-740 and Tyr-751 is important for interaction with PIK3R1.
Phosphorylation at Tyr-751 is important for interaction with NCK1.
Phosphorylation at Tyr-771 and Tyr-857 is important for interaction
with RASA1/GAP. Phosphorylation at Tyr-857 is important for efficient
phosphorylation of PLCG1 and PTPN11, resulting in increased
phosphorylation of AKT1, MAPK1/ERK2 and/or MAPK3/ERK1, PDCD6IP/ALIX and
STAM, and in increased cell proliferation. Phosphorylation at Tyr-1009
is important for interaction with PTPN11. Phosphorylation at Tyr-1009
and Tyr-1021 is important for interaction with PLCG1. Phosphorylation
at Tyr-1021 is important for interaction with CBL; PLCG1 and CBL
compete for the same binding site. Dephosphorylated by PTPRJ at Tyr-
751, Tyr-857, Tyr-1009 and Tyr-1021. Dephosphorylated by PTPN2 at Tyr-
579 and Tyr-1021. {ECO:0000269|PubMed:10821867,
ECO:0000269|PubMed:1314164, ECO:0000269|PubMed:1396585,
ECO:0000269|PubMed:14966296, ECO:0000269|PubMed:15902258,
ECO:0000269|PubMed:1709159, ECO:0000269|PubMed:2550144,
ECO:0000269|PubMed:7685273}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:20534510,
ECO:0000269|PubMed:2850496}.
-!- PTM: Ubiquitinated. After autophosphorylation, the receptor is
polyubiquitinated, leading to its degradation.
{ECO:0000269|PubMed:1313434, ECO:0000269|PubMed:17620338}.
-!- 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).
-!- DISEASE: Myeloproliferative disorder chronic with eosinophilia (MPE)
[MIM:131440]: A hematologic disorder characterized by malignant
eosinophils proliferation. Note=The gene represented in this entry may
be involved in disease pathogenesis. Chromosomal aberrations involving
PDGFRB have been found in many instances of chronic myeloproliferative
disorder with eosinophilia. Translocation t(5;12) with ETV6 on
chromosome 12 creating an PDGFRB-ETV6 fusion protein (PubMed:12181402).
Translocation t(5;15)(q33;q22) with TP53BP1 creating a PDGFRB-TP53BP1
fusion protein (PubMed:15492236). Translocation t(1;5)(q23;q33) that
forms a PDE4DIP-PDGFRB fusion protein (PubMed:12907457). Translocation
t(5;6)(q33-34;q23) with CEP85L that fuses the 5'-end of CEP85L (isoform
4) to the 3'-end of PDGFRB (PubMed:21938754).
{ECO:0000269|PubMed:12181402, ECO:0000269|PubMed:12907457,
ECO:0000269|PubMed:15492236, ECO:0000269|PubMed:21938754}.
-!- DISEASE: Leukemia, acute myelogenous (AML) [MIM:601626]: A subtype of
acute leukemia, a cancer of the white blood cells. AML is a malignant
disease of bone marrow characterized by maturational arrest of
hematopoietic precursors at an early stage of development. Clonal
expansion of myeloid blasts occurs in bone marrow, blood, and other
tissue. Myelogenous leukemias develop from changes in cells that
normally produce neutrophils, basophils, eosinophils and monocytes.
Note=The gene represented in this entry may be involved in disease
pathogenesis. A chromosomal aberration involving PDGFRB has been found
in a patient with AML. Translocation t(5;14)(q33;q32) with TRIP11
(PubMed:9373237). {ECO:0000269|PubMed:9373237}.
-!- DISEASE: Leukemia, juvenile myelomonocytic (JMML) [MIM:607785]: An
aggressive pediatric myelodysplastic syndrome/myeloproliferative
disorder characterized by malignant transformation in the hematopoietic
stem cell compartment with proliferation of differentiated progeny.
Patients have splenomegaly, enlarged lymph nodes, rashes, and
hemorrhages. Note=The gene represented in this entry may be involved in
disease pathogenesis. A chromosomal aberration involving PDGFRB has
been found in a patient with JMML. Translocation t(5;17)(q33;p11.2)
with SPECC1 (PubMed:15087372). {ECO:0000269|PubMed:15087372}.
-!- DISEASE: Basal ganglia calcification, idiopathic, 4 (IBGC4)
[MIM:615007]: A form of basal ganglia calcification, an autosomal
dominant condition characterized by symmetric calcification in the
basal ganglia and other brain regions. Affected individuals can either
be asymptomatic or show a wide spectrum of neuropsychiatric symptoms,
including parkinsonism, dystonia, tremor, ataxia, dementia, psychosis,
seizures, and chronic headache. Serum levels of calcium, phosphate,
alkaline phosphatase and parathyroid hormone are normal. The
neuropathological hallmark of the disease is vascular and pericapillary
calcification, mainly of calcium phosphate, in the affected brain
areas. {ECO:0000269|PubMed:23255827, ECO:0000269|PubMed:24065723,
ECO:0000269|PubMed:26599395}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- DISEASE: Myofibromatosis, infantile 1 (IMF1) [MIM:228550]: A rare
mesenchymal disorder characterized by the development of benign tumors
in the skin, striated muscles, bones, and, more rarely, visceral
organs. Subcutaneous or soft tissue nodules commonly involve the skin
of the head, neck, and trunk. Skeletal and muscular lesions occur in
about half of the patients. Lesions may be solitary or multicentric,
and they may be present at birth or become apparent in early infancy or
occasionally in adult life. Visceral lesions are associated with high
morbidity and mortality. {ECO:0000269|PubMed:23731537,
ECO:0000269|PubMed:23731542}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- DISEASE: Kosaki overgrowth syndrome (KOGS) [MIM:616592]: A syndrome
characterized by somatic overgrowth, distinctive facial features,
hyperelastic and fragile skin, and progressive neurologic deterioration
with white matter lesions on brain imaging.
{ECO:0000269|PubMed:25454926}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- DISEASE: Premature aging syndrome, Penttinen type (PENTT) [MIM:601812]:
A syndrome characterized by a prematurely aged appearance with
lipoatrophy, epidermal and dermal atrophy along with hypertrophic
lesions that resemble scars, thin hair, proptosis, underdeveloped
cheekbones, and marked acro-osteolysis. {ECO:0000269|PubMed:26279204}.
Note=The disease is caused by mutations affecting the gene represented
in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. CSF-1/PDGF receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PDGFRBID21ch5q32.html";
---------------------------------------------------------------------------
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EMBL; J03278; AAA60049.1; -; mRNA.
EMBL; M21616; AAA36427.1; -; mRNA.
EMBL; EU826595; ACF47631.1; -; mRNA.
EMBL; AC005895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC011382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC032224; AAH32224.1; -; mRNA.
EMBL; U33172; AAC51675.1; -; Genomic_DNA.
CCDS; CCDS4303.1; -. [P09619-1]
PIR; A28206; PFHUGB.
RefSeq; NP_002600.1; NM_002609.3. [P09619-1]
RefSeq; XP_011535960.1; XM_011537658.1.
RefSeq; XP_011535961.1; XM_011537659.1.
PDB; 1GQ5; X-ray; 2.20 A; A=1102-1106.
PDB; 1H9O; X-ray; 1.79 A; B=751-755.
PDB; 1LWP; Model; -; A=600-962.
PDB; 1SHA; X-ray; 1.50 A; B=751-755.
PDB; 2IUI; X-ray; 2.40 A; C/D=748-758.
PDB; 2L6W; NMR; -; A/B=526-563.
PDB; 2PLD; NMR; -; B=1018-1029.
PDB; 2PLE; NMR; -; B=1018-1029.
PDB; 3MJG; X-ray; 2.30 A; X/Y=33-314.
PDBsum; 1GQ5; -.
PDBsum; 1H9O; -.
PDBsum; 1LWP; -.
PDBsum; 1SHA; -.
PDBsum; 2IUI; -.
PDBsum; 2L6W; -.
PDBsum; 2PLD; -.
PDBsum; 2PLE; -.
PDBsum; 3MJG; -.
SMR; P09619; -.
BioGRID; 111185; 92.
ComplexPortal; CPX-2882; PDGF receptor beta - PDGF-BB complex.
ComplexPortal; CPX-2883; PDGF receptor alpha-beta - PDGF-BB complex.
ComplexPortal; CPX-2886; PDGF receptor beta - PDGF-AB complex.
ComplexPortal; CPX-2888; PDGF receptor alpha-beta - PDGF-CC complex.
ComplexPortal; CPX-2889; PDGF receptor beta - PDGF-DD complex.
ComplexPortal; CPX-2890; PDGF receptor alpha-beta - PDGF-DD complex.
ComplexPortal; CPX-2891; PDGF receptor beta - PDGF-CC complex.
ComplexPortal; CPX-2892; PDGF receptor alpha-beta - PDGF-AB complex.
CORUM; P09619; -.
DIP; DIP-558N; -.
IntAct; P09619; 200.
MINT; P09619; -.
STRING; 9606.ENSP00000261799; -.
BindingDB; P09619; -.
ChEMBL; CHEMBL1913; -.
DrugBank; DB00102; Becaplermin.
DrugBank; DB01254; Dasatinib.
DrugBank; DB12147; Erdafitinib.
DrugBank; DB10770; Foreskin fibroblast (neonatal).
DrugBank; DB12010; Fostamatinib.
DrugBank; DB00619; Imatinib.
DrugBank; DB06595; Midostaurin.
DrugBank; DB09079; Nintedanib.
DrugBank; DB06589; Pazopanib.
DrugBank; DB12978; Pexidartinib.
DrugBank; DB09221; Polaprezinc.
DrugBank; DB08896; Regorafenib.
DrugBank; DB00398; Sorafenib.
DrugBank; DB01268; Sunitinib.
DrugBank; DB09283; Trapidil.
DrugBank; DB05146; XL820.
DrugBank; DB05014; XL999.
DrugCentral; P09619; -.
GuidetoPHARMACOLOGY; 1804; -.
GlyConnect; 1967; -.
iPTMnet; P09619; -.
PhosphoSitePlus; P09619; -.
BioMuta; PDGFRB; -.
DMDM; 129890; -.
EPD; P09619; -.
jPOST; P09619; -.
MassIVE; P09619; -.
MaxQB; P09619; -.
PaxDb; P09619; -.
PeptideAtlas; P09619; -.
PRIDE; P09619; -.
ProteomicsDB; 52253; -. [P09619-1]
ABCD; P09619; 1 sequenced antibody.
Antibodypedia; 3424; 2035 antibodies.
DNASU; 5159; -.
Ensembl; ENST00000261799; ENSP00000261799; ENSG00000113721. [P09619-1]
GeneID; 5159; -.
KEGG; hsa:5159; -.
UCSC; uc003lro.4; human. [P09619-1]
CTD; 5159; -.
DisGeNET; 5159; -.
EuPathDB; HostDB:ENSG00000113721.13; -.
GeneCards; PDGFRB; -.
GeneReviews; PDGFRB; -.
HGNC; HGNC:8804; PDGFRB.
HPA; ENSG00000113721; Low tissue specificity.
MalaCards; PDGFRB; -.
MIM; 131440; phenotype.
MIM; 173410; gene.
MIM; 228550; phenotype.
MIM; 601626; phenotype.
MIM; 601812; phenotype.
MIM; 607785; phenotype.
MIM; 615007; phenotype.
MIM; 616592; phenotype.
neXtProt; NX_P09619; -.
OpenTargets; ENSG00000113721; -.
Orphanet; 363665; Acroosteolysis-keloid-like lesions-premature aging syndrome.
Orphanet; 1980; Bilateral striopallidodentate calcinosis.
Orphanet; 98823; Chronic myelomonocytic leukemia.
Orphanet; 86830; Chronic myeloproliferative disease, unclassifiable.
Orphanet; 2591; Infantile myofibromatosis.
Orphanet; 168950; Myeloid/lymphoid neoplasm associated with PDGFRB rearrangement.
Orphanet; 314950; Primary hypereosinophilic syndrome.
Orphanet; 477831; Skeletal overgrowth-craniofacial dysmorphism-hyperelastic skin-white matter lesions syndrome.
PharmGKB; PA33148; -.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00940000157138; -.
HOGENOM; CLU_000288_49_0_1; -.
InParanoid; P09619; -.
KO; K05089; -.
OMA; TYVCNVS; -.
OrthoDB; 269253at2759; -.
PhylomeDB; P09619; -.
TreeFam; TF325768; -.
BRENDA; 2.7.10.1; 2681.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-186763; Downstream signal transduction.
Reactome; R-HSA-186797; Signaling by PDGF.
Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
SignaLink; P09619; -.
SIGNOR; P09619; -.
BioGRID-ORCS; 5159; 9 hits in 816 CRISPR screens.
ChiTaRS; PDGFRB; human.
EvolutionaryTrace; P09619; -.
GeneWiki; PDGFRB; -.
GenomeRNAi; 5159; -.
Pharos; P09619; Tclin.
PRO; PR:P09619; -.
Proteomes; UP000005640; Chromosome 5.
RNAct; P09619; protein.
Bgee; ENSG00000113721; Expressed in ectocervix and 214 other tissues.
ExpressionAtlas; P09619; baseline and differential.
Genevisible; P09619; HS.
GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:UniProtKB.
GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:BHF-UCL.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043235; C:receptor complex; IBA:GO_Central.
GO; GO:0001726; C:ruffle; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0019838; F:growth factor binding; IBA:GO_Central.
GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IEA:Ensembl.
GO; GO:0004992; F:platelet activating factor receptor activity; TAS:ProtInc.
GO; GO:0005019; F:platelet-derived growth factor beta-receptor activity; IDA:UniProtKB.
GO; GO:0048407; F:platelet-derived growth factor binding; IDA:UniProtKB.
GO; GO:0005161; F:platelet-derived growth factor receptor binding; IPI:BHF-UCL.
GO; GO:0005017; F:platelet-derived growth factor-activated receptor activity; IBA:GO_Central.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0038085; F:vascular endothelial growth factor binding; IPI:BHF-UCL.
GO; GO:0030325; P:adrenal gland development; IEA:Ensembl.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0035909; P:aorta morphogenesis; ISS:BHF-UCL.
GO; GO:0055003; P:cardiac myofibril assembly; ISS:UniProtKB.
GO; GO:0060326; P:cell chemotaxis; IDA:UniProtKB.
GO; GO:0016477; P:cell migration; IMP:UniProtKB.
GO; GO:0060981; P:cell migration involved in coronary angiogenesis; ISS:UniProtKB.
GO; GO:0035441; P:cell migration involved in vasculogenesis; ISS:UniProtKB.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0048568; P:embryonic organ development; IEA:Ensembl.
GO; GO:0006024; P:glycosaminoglycan biosynthetic process; IEA:Ensembl.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IBA:GO_Central.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0048839; P:inner ear development; IEA:Ensembl.
GO; GO:0060437; P:lung growth; IEA:Ensembl.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0072278; P:metanephric comma-shaped body morphogenesis; IEA:Ensembl.
GO; GO:0072277; P:metanephric glomerular capillary formation; ISS:UniProtKB.
GO; GO:0072262; P:metanephric glomerular mesangial cell proliferation involved in metanephros development; ISS:UniProtKB.
GO; GO:0035789; P:metanephric mesenchymal cell migration; IEA:Ensembl.
GO; GO:0072075; P:metanephric mesenchyme development; IEA:Ensembl.
GO; GO:0072284; P:metanephric S-shaped body morphogenesis; IEA:Ensembl.
GO; GO:0007275; P:multicellular organism development; IBA:GO_Central.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0046488; P:phosphatidylinositol metabolic process; IMP:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IMP:UniProtKB.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IDA:UniProtKB.
GO; GO:0035791; P:platelet-derived growth factor receptor-beta signaling pathway; IMP:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
GO; GO:0090280; P:positive regulation of calcium ion import; ISS:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IDA:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
GO; GO:0038091; P:positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0050921; P:positive regulation of chemotaxis; ISS:UniProtKB.
GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IEA:Ensembl.
GO; GO:2000573; P:positive regulation of DNA biosynthetic process; ISS:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
GO; GO:2000491; P:positive regulation of hepatic stellate cell activation; IEA:Ensembl.
GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:UniProtKB.
GO; GO:0035793; P:positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway; ISS:UniProtKB.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISS:UniProtKB.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IDA:UniProtKB.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
GO; GO:0010863; P:positive regulation of phospholipase C activity; IDA:UniProtKB.
GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IDA:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; TAS:Reactome.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISS:UniProtKB.
GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IEA:Ensembl.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IMP:UniProtKB.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:BHF-UCL.
GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
GO; GO:0106096; P:response to ceramide; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
GO; GO:0034405; P:response to fluid shear stress; IEA:Ensembl.
GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl.
GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
GO; GO:0061298; P:retina vasculature development in camera-type eye; ISS:UniProtKB.
GO; GO:0097178; P:ruffle assembly; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
GO; GO:0048705; P:skeletal system morphogenesis; IEA:Ensembl.
GO; GO:0071670; P:smooth muscle cell chemotaxis; ISS:BHF-UCL.
GO; GO:0048745; P:smooth muscle tissue development; IEA:Ensembl.
GO; GO:0001894; P:tissue homeostasis; IEA:Ensembl.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 5.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013151; Immunoglobulin.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR027288; PGFRB.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
Pfam; PF07679; I-set; 1.
Pfam; PF00047; ig; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
PIRSF; PIRSF500948; Beta-PDGF_receptor; 1.
SMART; SM00409; IG; 3.
SMART; SM00408; IGc2; 3.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF48726; SSF48726; 3.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50835; IG_LIKE; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell membrane; Chemotaxis;
Chromosomal rearrangement; Cytoplasmic vesicle; Developmental protein;
Direct protein sequencing; Disease mutation; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Kinase; Lysosome; Membrane; Nucleotide-binding;
Phosphoprotein; Polymorphism; Proto-oncogene; Receptor; Reference proteome;
Repeat; Signal; Transferase; Transmembrane; Transmembrane helix;
Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1..32
/evidence="ECO:0000269|PubMed:15340161"
CHAIN 33..1106
/note="Platelet-derived growth factor receptor beta"
/id="PRO_0000016757"
TOPO_DOM 33..532
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 533..553
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 554..1106
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 33..120
/note="Ig-like C2-type 1"
DOMAIN 129..210
/note="Ig-like C2-type 2"
DOMAIN 214..309
/note="Ig-like C2-type 3"
DOMAIN 331..403
/note="Ig-like C2-type 4"
DOMAIN 416..524
/note="Ig-like C2-type 5"
DOMAIN 600..962
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 606..614
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
ACT_SITE 826
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10028"
BINDING 634
/note="ATP"
/evidence="ECO:0000305"
SITE 527..528
/note="Breakpoint for insertion to form PDE4DIP-PDGFRB
fusion protein"
SITE 527..528
/note="Breakpoint for translocation to form TRIP11-PDGFRB"
SITE 558..559
/note="Breakpoint for translocation to form the CEP85L-
PDGFRB fusion protein"
MOD_RES 562
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000269|PubMed:10821867"
MOD_RES 579
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000269|PubMed:14966296,
ECO:0000269|PubMed:15902258, ECO:0000269|PubMed:7685273"
MOD_RES 581
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000269|PubMed:15902258,
ECO:0000269|PubMed:7685273"
MOD_RES 686
/note="Phosphotyrosine; by ABL1 and ABL2"
/evidence="ECO:0000250|UniProtKB:P05622"
MOD_RES 716
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000269|PubMed:15902258"
MOD_RES 740
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000269|PubMed:1314164,
ECO:0000269|PubMed:15902258"
MOD_RES 751
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000269|PubMed:10821867,
ECO:0000269|PubMed:1314164, ECO:0000269|PubMed:14966296,
ECO:0000269|PubMed:1709159, ECO:0000269|PubMed:2550144"
MOD_RES 763
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000269|PubMed:10821867"
MOD_RES 771
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000269|PubMed:10821867,
ECO:0000269|PubMed:1314164, ECO:0000269|PubMed:14966296,
ECO:0000269|PubMed:15902258"
MOD_RES 775
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000269|PubMed:10821867"
MOD_RES 778
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000269|PubMed:10821867"
MOD_RES 857
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000269|PubMed:10821867,
ECO:0000269|PubMed:1314164, ECO:0000269|PubMed:15902258,
ECO:0000269|PubMed:1709159, ECO:0000269|PubMed:2550144"
MOD_RES 934
/note="Phosphotyrosine; by ABL1 and ABL2"
/evidence="ECO:0000250|UniProtKB:P05622"
MOD_RES 970
/note="Phosphotyrosine; by ABL1 and ABL2"
/evidence="ECO:0000250|UniProtKB:P05622"
MOD_RES 1009
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000269|PubMed:10821867,
ECO:0000269|PubMed:1396585, ECO:0000269|PubMed:15902258"
MOD_RES 1021
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000269|PubMed:10821867,
ECO:0000269|PubMed:1396585, ECO:0000269|PubMed:14966296,
ECO:0000269|PubMed:15902258"
CARBOHYD 45
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 89
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:20534510"
CARBOHYD 103
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:20534510"
CARBOHYD 215
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:20534510"
CARBOHYD 230
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:20534510"
CARBOHYD 292
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:20534510"
CARBOHYD 307
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:20534510"
CARBOHYD 354
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 371
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 468
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 479
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 54..100
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:20534510"
DISULFID 149..190
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:20534510"
DISULFID 235..291
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:20534510"
DISULFID 436..508
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
VAR_SEQ 311..336
/note="VESGYVRLLGEVGTLQFAELHRSRTL -> RAATCGSWERWAHYNLLSCIGA
GHCR (in isoform 2)"
/evidence="ECO:0000303|PubMed:18593464"
/id="VSP_056008"
VAR_SEQ 337..1106
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:18593464"
/id="VSP_056009"
VARIANT 29
/note="I -> F (in dbSNP:rs17110944)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_034377"
VARIANT 180
/note="S -> F (in dbSNP:rs17853027)"
/evidence="ECO:0000269|PubMed:15489334"
/id="VAR_035125"
VARIANT 282
/note="E -> K (in dbSNP:rs34586048)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_042027"
VARIANT 345
/note="P -> S (in dbSNP:rs2229558)"
/id="VAR_049717"
VARIANT 485
/note="E -> K (in dbSNP:rs41287110)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_042028"
VARIANT 561
/note="R -> C (in IMF1; dbSNP:rs367543286)"
/evidence="ECO:0000269|PubMed:23731537"
/id="VAR_069925"
VARIANT 584
/note="P -> R (in KOGS; dbSNP:rs863224946)"
/evidence="ECO:0000269|PubMed:25454926"
/id="VAR_075865"
VARIANT 589
/note="Y -> H (in a gastric adenocarcinoma sample; somatic
mutation)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_042029"
VARIANT 658
/note="L -> P (in IBGC4; no effect on protein abundance;
loss of PDGF beta receptor activity; dbSNP:rs397509381)"
/evidence="ECO:0000269|PubMed:23255827,
ECO:0000269|PubMed:24065723, ECO:0000269|PubMed:26599395"
/id="VAR_069320"
VARIANT 660
/note="P -> T (in IMF1; dbSNP:rs144050370)"
/evidence="ECO:0000269|PubMed:23731542"
/id="VAR_069926"
VARIANT 665
/note="V -> A (in PENTT; gain of function in protein
tyrosine kinase activity; shows ligand-independent
constitutive signaling; dbSNP:rs1554108211)"
/evidence="ECO:0000269|PubMed:26279204"
/id="VAR_075866"
VARIANT 718
/note="N -> Y (in dbSNP:rs35322465)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_042030"
VARIANT 882
/note="T -> I (in a breast infiltrating ductal carcinoma
sample; somatic mutation)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_042031"
VARIANT 987
/note="R -> W (in IBGC4; decreased protein abundance; no
effect on receptor activity; decreased PDGF signaling
pathway; dbSNP:rs397509382)"
/evidence="ECO:0000269|PubMed:23255827,
ECO:0000269|PubMed:24065723, ECO:0000269|PubMed:26599395"
/id="VAR_069321"
VARIANT 1071
/note="E -> V (in IBGC4; no effect on protein abundance; no
effect on receptor activity; decreased PDGF signaling
pathway)"
/evidence="ECO:0000269|PubMed:24065723,
ECO:0000269|PubMed:26599395"
/id="VAR_075395"
MUTAGEN 579
/note="Y->F: Loss of kinase activity; when associated with
F-581. Strongly reduces interaction with SRC family
kinases. No effect on interaction with GRB10."
/evidence="ECO:0000269|PubMed:10454568,
ECO:0000269|PubMed:7685273"
MUTAGEN 581
/note="Y->F: Loss of kinase activity; when associated with
F-579. No effect on interaction with GRB10."
/evidence="ECO:0000269|PubMed:10454568,
ECO:0000269|PubMed:7685273"
MUTAGEN 634
/note="K->A,R: Loss of kinase activity. Abolishes
interaction with RASA1. No effect on phosphatidylinositol
3-kinase activity."
/evidence="ECO:0000269|PubMed:1314164,
ECO:0000269|PubMed:1846866, ECO:0000269|PubMed:20494825"
MUTAGEN 716
/note="Y->F: No effect neither on interaction with GRB10
and RASA1 nor on phosphatidylinositol 3-kinase activity."
/evidence="ECO:0000269|PubMed:10454568,
ECO:0000269|PubMed:1314164"
MUTAGEN 740
/note="Y->F: Strongly reduces up-regulation of cell
proliferation; when associated with F-751. Strongly
decreases phosphatidylinositol 3-kinase activity. No effect
on interaction with GRB10 and RASA1."
/evidence="ECO:0000269|PubMed:10454568,
ECO:0000269|PubMed:1314164, ECO:0000269|PubMed:1375321,
ECO:0000269|PubMed:21679854"
MUTAGEN 751
/note="Y->F: Strongly reduces up-regulation of cell
proliferation; when associated with F-740. Abolishes
phosphatidylinositol 3-kinase activity and interaction with
NCK1, and slightly reduces interaction with RASA1. No
effect on interaction with GRB10."
/evidence="ECO:0000269|PubMed:10454568,
ECO:0000269|PubMed:1314164, ECO:0000269|PubMed:1375321,
ECO:0000269|PubMed:1653029, ECO:0000269|PubMed:21679854,
ECO:0000269|PubMed:7692233"
MUTAGEN 763
/note="Y->F: No effect on interaction with RASA1 and on
phosphatidylinositol 3-kinase activity."
/evidence="ECO:0000269|PubMed:1314164"
MUTAGEN 771
/note="Y->F: Loss of interaction with GRB10. Abolishes
interaction with RASA1. No effect on phosphatidylinositol
3-kinase activity."
/evidence="ECO:0000269|PubMed:10454568,
ECO:0000269|PubMed:1314164, ECO:0000269|PubMed:1375321"
MUTAGEN 775
/note="Y->F: No effect on interaction with RASA1 and on
phosphatidylinositol 3-kinase activity."
/evidence="ECO:0000269|PubMed:1314164"
MUTAGEN 778
/note="Y->F: Strongly reduces expression levels."
/evidence="ECO:0000269|PubMed:1314164"
MUTAGEN 857
/note="Y->F: Reduces kinase activity. No effect on
interaction with GRB10. Abolishes interaction with RASA1.
No effect on phosphatidylinositol 3-kinase activity."
/evidence="ECO:0000269|PubMed:10454568,
ECO:0000269|PubMed:1314164, ECO:0000269|PubMed:1653029,
ECO:0000269|PubMed:20494825"
MUTAGEN 1009
/note="Y->F: No effect on interaction with GRB10. Abolishes
interaction with PLCG1; when associated with F-1021."
/evidence="ECO:0000269|PubMed:10454568,
ECO:0000269|PubMed:1396585, ECO:0000269|PubMed:7691811"
MUTAGEN 1021
/note="Y->F: Strongly reduces up-regulation of cell
proliferation. Abolishes interaction with PLCG1; when
associated with F-1009. No effect on interaction with
GRB10."
/evidence="ECO:0000269|PubMed:10454568,
ECO:0000269|PubMed:1396585, ECO:0000269|PubMed:17620338,
ECO:0000269|PubMed:21679854"
CONFLICT 241
/note="E -> D (in Ref. 2; AAA36427)"
/evidence="ECO:0000305"
STRAND 40..43
/evidence="ECO:0000244|PDB:3MJG"
STRAND 50..58
/evidence="ECO:0000244|PDB:3MJG"
STRAND 61..64
/evidence="ECO:0000244|PDB:3MJG"
STRAND 70..75
/evidence="ECO:0000244|PDB:3MJG"
STRAND 81..87
/evidence="ECO:0000244|PDB:3MJG"
HELIX 92..94
/evidence="ECO:0000244|PDB:3MJG"
STRAND 96..101
/evidence="ECO:0000244|PDB:3MJG"
STRAND 114..119
/evidence="ECO:0000244|PDB:3MJG"
HELIX 132..135
/evidence="ECO:0000244|PDB:3MJG"
STRAND 136..141
/evidence="ECO:0000244|PDB:3MJG"
STRAND 145..147
/evidence="ECO:0000244|PDB:3MJG"
STRAND 158..164
/evidence="ECO:0000244|PDB:3MJG"
TURN 175..177
/evidence="ECO:0000244|PDB:3MJG"
STRAND 178..181
/evidence="ECO:0000244|PDB:3MJG"
STRAND 185..194
/evidence="ECO:0000244|PDB:3MJG"
STRAND 197..200
/evidence="ECO:0000244|PDB:3MJG"
STRAND 204..208
/evidence="ECO:0000244|PDB:3MJG"
STRAND 217..221
/evidence="ECO:0000244|PDB:3MJG"
STRAND 223..226
/evidence="ECO:0000244|PDB:3MJG"
STRAND 231..239
/evidence="ECO:0000244|PDB:3MJG"
STRAND 241..248
/evidence="ECO:0000244|PDB:3MJG"
STRAND 252..255
/evidence="ECO:0000244|PDB:3MJG"
STRAND 261..265
/evidence="ECO:0000244|PDB:3MJG"
TURN 267..270
/evidence="ECO:0000244|PDB:3MJG"
STRAND 271..280
/evidence="ECO:0000244|PDB:3MJG"
STRAND 287..295
/evidence="ECO:0000244|PDB:3MJG"
TURN 296..299
/evidence="ECO:0000244|PDB:3MJG"
STRAND 300..311
/evidence="ECO:0000244|PDB:3MJG"
HELIX 530..556
/evidence="ECO:0000244|PDB:2L6W"
SEQUENCE 1106 AA; 123968 MW; 038C15E531D6E89D CRC64;
MRLPGAMPAL ALKGELLLLS LLLLLEPQIS QGLVVTPPGP ELVLNVSSTF VLTCSGSAPV
VWERMSQEPP QEMAKAQDGT FSSVLTLTNL TGLDTGEYFC THNDSRGLET DERKRLYIFV
PDPTVGFLPN DAEELFIFLT EITEITIPCR VTDPQLVVTL HEKKGDVALP VPYDHQRGFS
GIFEDRSYIC KTTIGDREVD SDAYYVYRLQ VSSINVSVNA VQTVVRQGEN ITLMCIVIGN
EVVNFEWTYP RKESGRLVEP VTDFLLDMPY HIRSILHIPS AELEDSGTYT CNVTESVNDH
QDEKAINITV VESGYVRLLG EVGTLQFAEL HRSRTLQVVF EAYPPPTVLW FKDNRTLGDS
SAGEIALSTR NVSETRYVSE LTLVRVKVAE AGHYTMRAFH EDAEVQLSFQ LQINVPVRVL
ELSESHPDSG EQTVRCRGRG MPQPNIIWSA CRDLKRCPRE LPPTLLGNSS EEESQLETNV
TYWEEEQEFE VVSTLRLQHV DRPLSVRCTL RNAVGQDTQE VIVVPHSLPF KVVVISAILA
LVVLTIISLI ILIMLWQKKP RYEIRWKVIE SVSSDGHEYI YVDPMQLPYD STWELPRDQL
VLGRTLGSGA FGQVVEATAH GLSHSQATMK VAVKMLKSTA RSSEKQALMS ELKIMSHLGP
HLNVVNLLGA CTKGGPIYII TEYCRYGDLV DYLHRNKHTF LQHHSDKRRP PSAELYSNAL
PVGLPLPSHV SLTGESDGGY MDMSKDESVD YVPMLDMKGD VKYADIESSN YMAPYDNYVP
SAPERTCRAT LINESPVLSY MDLVGFSYQV ANGMEFLASK NCVHRDLAAR NVLICEGKLV
KICDFGLARD IMRDSNYISK GSTFLPLKWM APESIFNSLY TTLSDVWSFG ILLWEIFTLG
GTPYPELPMN EQFYNAIKRG YRMAQPAHAS DEIYEIMQKC WEEKFEIRPP FSQLVLLLER
LLGEGYKKKY QQVDEEFLRS DHPAILRSQA RLPGFHGLRS PLDTSSVLYT AVQPNEGDND
YIIPLPDPKP EVADEGPLEG SPSLASSTLN EVNTSSTISC DSPLEPQDEP EPEPQLELQV
EPEPELEQLP DSGCPAPRAE AEDSFL


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Related Genes :
[Pdgfrb Pdgfr Pdgfr1] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor) (CD140 antigen-like family member B) (Platelet-derived growth factor receptor 1) (PDGFR-1) (CD antigen CD140b)
[PDGFRB PDGFR PDGFR1] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor) (CD140 antigen-like family member B) (Platelet-derived growth factor receptor 1) (PDGFR-1) (CD antigen CD140b)
[Pdgfrb Pdgfr Pdgfr1] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor) (CD140 antigen-like family member B) (Platelet-derived growth factor receptor 1) (PDGFR-1) (CD antigen CD140b)
[PDGFRB PDGFR PDGFR1] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor) (CD140 antigen-like family member B) (Platelet-derived growth factor receptor 1) (PDGFR-1) (CD antigen CD140b)
[PDGFRA PDGFR2 RHEPDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (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) (CD antigen CD140a)
[Pdgfra] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor) (CD140 antigen-like family member A) (Platelet-derived growth factor alpha receptor) (CD antigen CD140a)
[Pdgfra] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor) (CD140 antigen-like family member A) (Platelet-derived growth factor alpha receptor) (CD antigen CD140a)
[pdgfra] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[pdgfrb] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor)
[I79_024441] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[pdgfra] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFRA GW7_00400] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[Pdgfra rCG_57147] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)
[PDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor)

Bibliography :