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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.
30-AUG-2017, entry version 216.
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;
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;
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;
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;
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 ENZYME 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: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:1846866,
ECO:0000269|PubMed:20494825, ECO:0000269|PubMed:7685273}.
-!- ENZYME 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:
P0CK45:E5 (xeno); NbExp=2; IntAct=EBI-641237, EBI-7015490;
P06241:FYN; NbExp=3; IntAct=EBI-641237, EBI-515315;
Q14451:GRB7; NbExp=4; IntAct=EBI-641237, EBI-970191;
Q53G59:KLHL12; NbExp=5; IntAct=EBI-641237, EBI-740929;
P01127:PDGFB; NbExp=13; IntAct=EBI-641237, EBI-1554925;
P23727:PIK3R1 (xeno); NbExp=6; IntAct=EBI-641237, EBI-520244;
P27986:PIK3R1; NbExp=19; IntAct=EBI-641237, EBI-79464;
P08487:PLCG1 (xeno); NbExp=3; IntAct=EBI-641237, EBI-8013886;
P19174:PLCG1; NbExp=5; IntAct=EBI-641237, EBI-79387;
P60484:PTEN; NbExp=3; IntAct=EBI-641237, EBI-696162;
P18031:PTPN1; NbExp=3; IntAct=EBI-641237, EBI-968788;
Q06124:PTPN11; NbExp=8; IntAct=EBI-641237, EBI-297779;
Q05209:PTPN12; NbExp=3; IntAct=EBI-641237, EBI-2266035;
Q12913:PTPRJ; NbExp=4; IntAct=EBI-641237, EBI-2264500;
P04049:RAF1; NbExp=2; IntAct=EBI-641237, EBI-365996;
P20936:RASA1; NbExp=3; IntAct=EBI-641237, EBI-1026476;
Q13239:SLA; NbExp=4; IntAct=EBI-641237, EBI-726214;
O14745:SLC9A3R1; NbExp=5; IntAct=EBI-641237, EBI-349787;
Q15654:TRIP6; NbExp=3; IntAct=EBI-641237, EBI-742327;
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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Distributed under the Creative Commons Attribution-NoDerivs License
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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. [P09619-1]
RefSeq; XP_011535961.1; XM_011537659.1. [P09619-1]
UniGene; Hs.509067; -.
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; 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; 2L6W; -.
PDBsum; 2PLD; -.
PDBsum; 2PLE; -.
PDBsum; 3MJG; -.
ProteinModelPortal; P09619; -.
SMR; P09619; -.
BioGrid; 111185; 73.
DIP; DIP-558N; -.
IntAct; P09619; 81.
MINT; MINT-148093; -.
STRING; 9606.ENSP00000261799; -.
BindingDB; P09619; -.
ChEMBL; CHEMBL1913; -.
DrugBank; DB00102; Becaplermin.
DrugBank; DB01254; Dasatinib.
DrugBank; DB00619; Imatinib.
DrugBank; DB06589; Pazopanib.
DrugBank; DB08896; Regorafenib.
DrugBank; DB00398; Sorafenib.
DrugBank; DB01268; Sunitinib.
DrugBank; DB05146; XL820.
DrugBank; DB05014; XL999.
GuidetoPHARMACOLOGY; 1804; -.
iPTMnet; P09619; -.
PhosphoSitePlus; P09619; -.
BioMuta; PDGFRB; -.
DMDM; 129890; -.
EPD; P09619; -.
MaxQB; P09619; -.
PaxDb; P09619; -.
PeptideAtlas; P09619; -.
PRIDE; P09619; -.
DNASU; 5159; -.
Ensembl; ENST00000261799; ENSP00000261799; ENSG00000113721. [P09619-1]
GeneID; 5159; -.
KEGG; hsa:5159; -.
UCSC; uc003lro.4; human. [P09619-1]
CTD; 5159; -.
DisGeNET; 5159; -.
GeneCards; PDGFRB; -.
GeneReviews; PDGFRB; -.
HGNC; HGNC:8804; PDGFRB.
HPA; CAB003842; -.
HPA; CAB018144; -.
HPA; HPA028499; -.
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; 1980; Bilateral striopallidodentate calcinosis.
Orphanet; 98823; Chronic myelomonocytic leukemia.
Orphanet; 2591; Infantile myofibromatosis.
Orphanet; 168950; Myeloid neoplasm associated with PDGFRB rearrangement.
Orphanet; 314950; Primary hypereosinophilic syndrome.
Orphanet; 86830; Unclassified chronic myeloproliferative disease.
PharmGKB; PA33148; -.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118923; -.
HOGENOM; HOG000112009; -.
HOVERGEN; HBG004335; -.
InParanoid; P09619; -.
KO; K05089; -.
OMA; APYDNYV; -.
OrthoDB; EOG091G01TL; -.
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; -.
ChiTaRS; PDGFRB; human.
EvolutionaryTrace; P09619; -.
GeneWiki; PDGFRB; -.
GenomeRNAi; 5159; -.
PRO; PR:P09619; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000113721; -.
CleanEx; HS_PDGFRB; -.
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:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IEA:Ensembl.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; TAS:Reactome.
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; TAS:ProtInc.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
GO; GO:0038085; F:vascular endothelial growth factor binding; IPI:BHF-UCL.
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:0006024; P:glycosaminoglycan biosynthetic process; 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:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:2000587; P:negative regulation of platelet-derived growth factor receptor-beta signaling pathway; TAS:Reactome.
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 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: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: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:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; TAS:Reactome.
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:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl.
GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
GO; GO:0061298; P:retina vasculature development in camera-type eye; ISS:UniProtKB.
GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
GO; GO:0071670; P:smooth muscle cell chemotaxis; ISS:BHF-UCL.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 5.
InterPro; IPR007110; Ig-like_dom.
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.
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; 2.
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; Complete proteome;
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 {ECO:0000269|PubMed:15340161}.
CHAIN 33 1106 Platelet-derived growth factor receptor
beta.
/FTId=PRO_0000016757.
TOPO_DOM 33 532 Extracellular. {ECO:0000255}.
TRANSMEM 533 553 Helical. {ECO:0000255}.
TOPO_DOM 554 1106 Cytoplasmic. {ECO:0000255}.
DOMAIN 33 120 Ig-like C2-type 1.
DOMAIN 129 210 Ig-like C2-type 2.
DOMAIN 214 309 Ig-like C2-type 3.
DOMAIN 331 403 Ig-like C2-type 4.
DOMAIN 416 524 Ig-like C2-type 5.
DOMAIN 600 962 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 606 614 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 826 826 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 634 634 ATP. {ECO:0000305}.
SITE 527 528 Breakpoint for insertion to form PDE4DIP-
PDGFRB fusion protein.
SITE 527 528 Breakpoint for translocation to form
TRIP11-PDGFRB.
SITE 558 559 Breakpoint for translocation to form the
CEP85L-PDGFRB fusion protein.
MOD_RES 562 562 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:10821867}.
MOD_RES 579 579 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:14966296,
ECO:0000269|PubMed:15902258,
ECO:0000269|PubMed:7685273}.
MOD_RES 581 581 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:15902258,
ECO:0000269|PubMed:7685273}.
MOD_RES 686 686 Phosphotyrosine; by ABL1 and ABL2.
{ECO:0000250|UniProtKB:P05622}.
MOD_RES 716 716 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:15902258}.
MOD_RES 740 740 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:1314164,
ECO:0000269|PubMed:15902258}.
MOD_RES 751 751 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:10821867,
ECO:0000269|PubMed:1314164,
ECO:0000269|PubMed:14966296,
ECO:0000269|PubMed:1709159,
ECO:0000269|PubMed:2550144}.
MOD_RES 763 763 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:10821867}.
MOD_RES 771 771 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:10821867,
ECO:0000269|PubMed:1314164,
ECO:0000269|PubMed:14966296,
ECO:0000269|PubMed:15902258}.
MOD_RES 775 775 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:10821867}.
MOD_RES 778 778 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:10821867}.
MOD_RES 857 857 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:10821867,
ECO:0000269|PubMed:1314164,
ECO:0000269|PubMed:15902258,
ECO:0000269|PubMed:1709159,
ECO:0000269|PubMed:2550144}.
MOD_RES 934 934 Phosphotyrosine; by ABL1 and ABL2.
{ECO:0000250|UniProtKB:P05622}.
MOD_RES 970 970 Phosphotyrosine; by ABL1 and ABL2.
{ECO:0000250|UniProtKB:P05622}.
MOD_RES 1009 1009 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:10821867,
ECO:0000269|PubMed:1396585,
ECO:0000269|PubMed:15902258}.
MOD_RES 1021 1021 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:10821867,
ECO:0000269|PubMed:1396585,
ECO:0000269|PubMed:14966296,
ECO:0000269|PubMed:15902258}.
CARBOHYD 45 45 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 89 89 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20534510}.
CARBOHYD 103 103 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20534510}.
CARBOHYD 215 215 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20534510}.
CARBOHYD 230 230 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20534510}.
CARBOHYD 292 292 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20534510}.
CARBOHYD 307 307 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20534510}.
CARBOHYD 354 354 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 371 371 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 468 468 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 479 479 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 54 100 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:20534510}.
DISULFID 149 190 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:20534510}.
DISULFID 235 291 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:20534510}.
DISULFID 436 508 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 311 336 VESGYVRLLGEVGTLQFAELHRSRTL -> RAATCGSWERW
AHYNLLSCIGAGHCR (in isoform 2).
{ECO:0000303|PubMed:18593464}.
/FTId=VSP_056008.
VAR_SEQ 337 1106 Missing (in isoform 2).
{ECO:0000303|PubMed:18593464}.
/FTId=VSP_056009.
VARIANT 29 29 I -> F (in dbSNP:rs17110944).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_034377.
VARIANT 180 180 S -> F (in dbSNP:rs17853027).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_035125.
VARIANT 282 282 E -> K (in dbSNP:rs34586048).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042027.
VARIANT 345 345 P -> S (in dbSNP:rs2229558).
/FTId=VAR_049717.
VARIANT 485 485 E -> K (in dbSNP:rs41287110).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042028.
VARIANT 561 561 R -> C (in IMF1; dbSNP:rs367543286).
{ECO:0000269|PubMed:23731537}.
/FTId=VAR_069925.
VARIANT 584 584 P -> R (in KOGS; dbSNP:rs863224946).
{ECO:0000269|PubMed:25454926}.
/FTId=VAR_075865.
VARIANT 589 589 Y -> H (in a gastric adenocarcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042029.
VARIANT 658 658 L -> P (in IBGC4; no effect on protein
abundance; loss of PDGF beta receptor
activity; dbSNP:rs397509381).
{ECO:0000269|PubMed:23255827,
ECO:0000269|PubMed:24065723,
ECO:0000269|PubMed:26599395}.
/FTId=VAR_069320.
VARIANT 660 660 P -> T (in IMF1; dbSNP:rs144050370).
{ECO:0000269|PubMed:23731542}.
/FTId=VAR_069926.
VARIANT 665 665 V -> A (in PENTT; gain of function in
protein tyrosine kinase activity; shows
ligand-independent constitutive
signaling).
{ECO:0000269|PubMed:26279204}.
/FTId=VAR_075866.
VARIANT 718 718 N -> Y (in dbSNP:rs35322465).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042030.
VARIANT 882 882 T -> I (in a breast infiltrating ductal
carcinoma sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042031.
VARIANT 987 987 R -> W (in IBGC4; decreased protein
abundance; no effect on receptor
activity; decreased PDGF signaling
pathway; dbSNP:rs397509382).
{ECO:0000269|PubMed:23255827,
ECO:0000269|PubMed:24065723,
ECO:0000269|PubMed:26599395}.
/FTId=VAR_069321.
VARIANT 1071 1071 E -> V (in IBGC4; no effect on protein
abundance; no effect on receptor
activity; decreased PDGF signaling
pathway). {ECO:0000269|PubMed:24065723,
ECO:0000269|PubMed:26599395}.
/FTId=VAR_075395.
MUTAGEN 579 579 Y->F: Loss of kinase activity; when
associated with F-581. Strongly reduces
interaction with SRC family kinases. No
effect on interaction with GRB10.
{ECO:0000269|PubMed:10454568,
ECO:0000269|PubMed:7685273}.
MUTAGEN 581 581 Y->F: Loss of kinase activity; when
associated with F-579. No effect on
interaction with GRB10.
{ECO:0000269|PubMed:10454568,
ECO:0000269|PubMed:7685273}.
MUTAGEN 634 634 K->A,R: Loss of kinase activity.
Abolishes interaction with RASA1. No
effect on phosphatidylinositol 3-kinase
activity. {ECO:0000269|PubMed:1314164,
ECO:0000269|PubMed:1846866,
ECO:0000269|PubMed:20494825}.
MUTAGEN 716 716 Y->F: No effect neither on interaction
with GRB10 and RASA1 nor on
phosphatidylinositol 3-kinase activity.
{ECO:0000269|PubMed:10454568,
ECO:0000269|PubMed:1314164}.
MUTAGEN 740 740 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. {ECO:0000269|PubMed:10454568,
ECO:0000269|PubMed:1314164,
ECO:0000269|PubMed:1375321,
ECO:0000269|PubMed:21679854}.
MUTAGEN 751 751 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. {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 763 763 Y->F: No effect on interaction with RASA1
and on phosphatidylinositol 3-kinase
activity. {ECO:0000269|PubMed:1314164}.
MUTAGEN 771 771 Y->F: Loss of interaction with GRB10.
Abolishes interaction with RASA1. No
effect on phosphatidylinositol 3-kinase
activity. {ECO:0000269|PubMed:10454568,
ECO:0000269|PubMed:1314164,
ECO:0000269|PubMed:1375321}.
MUTAGEN 775 775 Y->F: No effect on interaction with RASA1
and on phosphatidylinositol 3-kinase
activity. {ECO:0000269|PubMed:1314164}.
MUTAGEN 778 778 Y->F: Strongly reduces expression levels.
{ECO:0000269|PubMed:1314164}.
MUTAGEN 857 857 Y->F: Reduces kinase activity. No effect
on interaction with GRB10. Abolishes
interaction with RASA1. No effect on
phosphatidylinositol 3-kinase activity.
{ECO:0000269|PubMed:10454568,
ECO:0000269|PubMed:1314164,
ECO:0000269|PubMed:1653029,
ECO:0000269|PubMed:20494825}.
MUTAGEN 1009 1009 Y->F: No effect on interaction with
GRB10. Abolishes interaction with PLCG1;
when associated with F-1021.
{ECO:0000269|PubMed:10454568,
ECO:0000269|PubMed:1396585,
ECO:0000269|PubMed:7691811}.
MUTAGEN 1021 1021 Y->F: Strongly reduces up-regulation of
cell proliferation. Abolishes interaction
with PLCG1; when associated with F-1009.
No effect on interaction with GRB10.
{ECO:0000269|PubMed:10454568,
ECO:0000269|PubMed:1396585,
ECO:0000269|PubMed:17620338,
ECO:0000269|PubMed:21679854}.
CONFLICT 241 241 E -> D (in Ref. 2; AAA36427).
{ECO:0000305}.
STRAND 40 43 {ECO:0000244|PDB:3MJG}.
STRAND 50 58 {ECO:0000244|PDB:3MJG}.
STRAND 61 64 {ECO:0000244|PDB:3MJG}.
STRAND 70 75 {ECO:0000244|PDB:3MJG}.
STRAND 81 87 {ECO:0000244|PDB:3MJG}.
HELIX 92 94 {ECO:0000244|PDB:3MJG}.
STRAND 96 101 {ECO:0000244|PDB:3MJG}.
STRAND 114 119 {ECO:0000244|PDB:3MJG}.
HELIX 132 135 {ECO:0000244|PDB:3MJG}.
STRAND 136 141 {ECO:0000244|PDB:3MJG}.
STRAND 145 147 {ECO:0000244|PDB:3MJG}.
STRAND 158 164 {ECO:0000244|PDB:3MJG}.
TURN 175 177 {ECO:0000244|PDB:3MJG}.
STRAND 178 181 {ECO:0000244|PDB:3MJG}.
STRAND 185 194 {ECO:0000244|PDB:3MJG}.
STRAND 197 200 {ECO:0000244|PDB:3MJG}.
STRAND 204 208 {ECO:0000244|PDB:3MJG}.
STRAND 217 221 {ECO:0000244|PDB:3MJG}.
STRAND 223 226 {ECO:0000244|PDB:3MJG}.
STRAND 231 239 {ECO:0000244|PDB:3MJG}.
STRAND 241 248 {ECO:0000244|PDB:3MJG}.
STRAND 252 255 {ECO:0000244|PDB:3MJG}.
STRAND 261 265 {ECO:0000244|PDB:3MJG}.
TURN 267 270 {ECO:0000244|PDB:3MJG}.
STRAND 271 280 {ECO:0000244|PDB:3MJG}.
STRAND 287 295 {ECO:0000244|PDB:3MJG}.
TURN 296 299 {ECO:0000244|PDB:3MJG}.
STRAND 300 311 {ECO:0000244|PDB:3MJG}.
HELIX 530 556 {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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