PGFRB_HUMAN
ID PGFRB_HUMAN Reviewed; 1106 AA.
AC P09619; B5A957; Q8N5L4;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 252.
DE RecName: Full=Platelet-derived growth factor receptor beta;
DE Short=PDGF-R-beta;
DE Short=PDGFR-beta;
DE EC=2.7.10.1;
DE AltName: Full=Beta platelet-derived growth factor receptor;
DE AltName: Full=Beta-type platelet-derived growth factor receptor;
DE AltName: Full=CD140 antigen-like family member B;
DE AltName: Full=Platelet-derived growth factor receptor 1;
DE Short=PDGFR-1;
DE AltName: CD_antigen=CD140b;
DE Flags: Precursor;
GN Name=PDGFRB; Synonyms=PDGFR, PDGFR1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION AS PDGFB RECEPTOR,
RP SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, AND INTERACTION WITH PDGFB.
RX PubMed=2835772; DOI=10.1073/pnas.85.10.3435;
RA Gronwald R.G.K., Grant F.J., Haldeman B.A., Hart C.E., O'Hara P.J.,
RA Hagen F.S., Ross R., Bowen-Pope D.F., Murray M.J.;
RT "Cloning and expression of a cDNA coding for the human platelet-derived
RT growth factor receptor: evidence for more than one receptor class.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:3435-3439(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION AS PDGFB RECEPTOR,
RP SUBCELLULAR LOCATION, GLYCOSYLATION, AUTOPHOSPHORYLATION, AND INTERACTION
RP WITH PDGFA AND PDGFB.
RX PubMed=2850496; DOI=10.1128/mcb.8.8.3476-3486.1988;
RA Claesson-Welsh L., Eriksson A., Moren A., Severinsson L., Ek B.,
RA Oestman A., Betsholtz C., Heldin C.-H.;
RT "cDNA cloning and expression of a human platelet-derived growth factor
RT (PDGF) receptor specific for B-chain-containing PDGF molecules.";
RL Mol. Cell. Biol. 8:3476-3486(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
RX PubMed=18593464; DOI=10.1186/ar2447;
RA Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D.,
RA Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.;
RT "Novel splice variants derived from the receptor tyrosine kinase
RT superfamily are potential therapeutics for rheumatoid arthritis.";
RL Arthritis Res. Ther. 10:R73-R73(2008).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PHE-180.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 548-569.
RX PubMed=9285559; DOI=10.1038/sj.onc.1201267;
RA Chi K.D., McPhee R.A., Wagner A.S., Dietz J.J., Pantazis P., Goustin A.S.;
RT "Integration of proviral DNA into the PDGF beta-receptor gene in HTLV-I-
RT infected T-cells results in a novel tyrosine kinase product with
RT transforming activity.";
RL Oncogene 15:1051-1057(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 559-1106 (ISOFORM 1), AND CHROMOSOMAL
RP TRANSLOCATION WITH CEP85L.
RX PubMed=21938754; DOI=10.1002/gcc.20930;
RA Chmielecki J., Peifer M., Viale A., Hutchinson K., Giltnane J., Socci N.D.,
RA Hollis C.J., Dean R.S., Yenamandra A., Jagasia M., Kim A.S., Dave U.P.,
RA Thomas R.K., Pao W.;
RT "Systematic screen for tyrosine kinase rearrangements identifies a novel
RT C6orf204-PDGFRB fusion in a patient with recurrent T-ALL and an associated
RT myeloproliferative neoplasm.";
RL Genes Chromosomes Cancer 51:54-65(2012).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1046-1106.
RX PubMed=2846185; DOI=10.1016/0092-8674(88)90224-3;
RA Roberts W.M., Look A.T., Roussel M.F., Sherr C.J.;
RT "Tandem linkage of human CSF-1 receptor (c-fms) and PDGF receptor genes.";
RL Cell 55:655-661(1988).
RN [9]
RP PROTEIN SEQUENCE OF 33-47.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [10]
RP PHOSPHORYLATION AT TYR-751 AND TYR-857.
RX PubMed=2550144; DOI=10.1016/0092-8674(89)90510-2;
RA Kazlauskas A., Cooper J.A.;
RT "Autophosphorylation of the PDGF receptor in the kinase insert region
RT regulates interactions with cell proteins.";
RL Cell 58:1121-1133(1989).
RN [11]
RP FUNCTION AS PDGFB RECEPTOR IN CELL PROLIFERATION AND CHEMOTAXIS, AND
RP SUBCELLULAR LOCATION.
RX PubMed=2554309; DOI=10.1073/pnas.86.21.8314;
RA Matsui T., Pierce J.H., Fleming T.P., Greenberger J.S., LaRochelle W.J.,
RA Ruggiero M., Aaronson S.A.;
RT "Independent expression of human alpha or beta platelet-derived growth
RT factor receptor cDNAs in a naive hematopoietic cell leads to functional
RT coupling with mitogenic and chemotactic signaling pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:8314-8318(1989).
RN [12]
RP FUNCTION IN CELL PROLIFERATION; ACTIVATION OF PLCG1 AND IN PHOSPHORYLATION
RP OF PLCG1 AND RASA1/GAP, AND MUTAGENESIS OF TYR-751 AND TYR-857.
RX PubMed=1653029; DOI=10.1091/mbc.2.6.413;
RA Kazlauskas A., Durden D.L., Cooper J.A.;
RT "Functions of the major tyrosine phosphorylation site of the PDGF receptor
RT beta subunit.";
RL Cell Regul. 2:413-425(1991).
RN [13]
RP INTERACTION WITH PDGFRA; PDGFA AND PDGFB, FUNCTION AS RECEPTOR FOR PDGFA
RP AND PDGFB, AND PHOSPHORYLATION AT TYR-857 AND TYR-751.
RX PubMed=1709159; DOI=10.1016/s0021-9258(18)31541-2;
RA Kelly J.D., Haldeman B.A., Grant F.J., Murray M.J., Seifert R.A.,
RA Bowen-Pope D.F., Cooper J.A., Kazlauskas A.;
RT "Platelet-derived growth factor (PDGF) stimulates PDGF receptor subunit
RT dimerization and intersubunit trans-phosphorylation.";
RL J. Biol. Chem. 266:8987-8992(1991).
RN [14]
RP FUNCTION AS RECEPTOR FOR PDGFA AND PDGFB, SUBCELLULAR LOCATION, CATALYTIC
RP ACTIVITY, AND MUTAGENESIS OF LYS-634.
RX PubMed=1846866; DOI=10.1083/jcb.112.3.469;
RA Sorkin A., Westermark B., Heldin C.H., Claesson-Welsh L.;
RT "Effect of receptor kinase inactivation on the rate of internalization and
RT degradation of PDGF and the PDGF beta-receptor.";
RL J. Cell Biol. 112:469-478(1991).
RN [15]
RP FUNCTION IN ACTIVATION OF PHOSPHATIDYLINOSITOL 3-KINASE ACTIVITY,
RP INTERACTION WITH PIK3R1 AND RASA1, PHOSPHORYLATION AT TYR-740; TYR-751;
RP TYR-771 AND TYR-857, AND MUTAGENESIS OF LYS-634; TYR-716; TYR-740; TYR-751;
RP TYR-763; TYR-771; TYR-775; TYR-778 AND TYR-857.
RX PubMed=1314164; DOI=10.1002/j.1460-2075.1992.tb05182.x;
RA Kashishian A., Kazlauskas A., Cooper J.A.;
RT "Phosphorylation sites in the PDGF receptor with different specificities
RT for binding GAP and PI3 kinase in vivo.";
RL EMBO J. 11:1373-1382(1992).
RN [16]
RP FUNCTION AS PDGFB RECEPTOR IN CELL PROLIFERATION AND PHOSPHORYLATION OF
RP PLCG1, INTERACTION WITH PLCG1, PHOSPHORYLATION AT TYR-1009 AND TYR-1021,
RP AND MUTAGENESIS OF TYR-1009 AND TYR-1021.
RX PubMed=1396585; DOI=10.1002/j.1460-2075.1992.tb05484.x;
RA Ronnstrand L., Mori S., Arridsson A.K., Eriksson A., Wernstedt C.,
RA Hellman U., Claesson-Welsh L., Heldin C.H.;
RT "Identification of two C-terminal autophosphorylation sites in the PDGF
RT beta-receptor: involvement in the interaction with phospholipase C-gamma.";
RL EMBO J. 11:3911-3919(1992).
RN [17]
RP UBIQUITINATION, AND DEGRADATION.
RX PubMed=1313434; DOI=10.1016/s0021-9258(18)42714-7;
RA Mori S., Heldin C.H., Claesson-Welsh L.;
RT "Ligand-induced polyubiquitination of the platelet-derived growth factor
RT beta-receptor.";
RL J. Biol. Chem. 267:6429-6434(1992).
RN [18]
RP INTERACTION WITH PIK3R1 AND RASA1, AND MUTAGENESIS OF TYR-740; TYR-751 AND
RP TYR-771.
RX PubMed=1375321; DOI=10.1128/mcb.12.6.2534-2544.1992;
RA Kazlauskas A., Kashishian A., Cooper J.A., Valius M.;
RT "GTPase-activating protein and phosphatidylinositol 3-kinase bind to
RT distinct regions of the platelet-derived growth factor receptor beta
RT subunit.";
RL Mol. Cell. Biol. 12:2534-2544(1992).
RN [19]
RP FUNCTION AS PDGFB RECEPTOR IN CELL PROLIFERATION, PHOSPHORYLATION AT
RP TYR-579 AND TYR-581; INTERACTION WITH SRC, CATALYTIC ACTIVITY, AND
RP MUTAGENESIS OF TYR-579 AND TYR-581.
RX PubMed=7685273; DOI=10.1002/j.1460-2075.1993.tb05879.x;
RA Mori S., Ronnstrand L., Yokote K., Engstrom A., Courtneidge S.A.,
RA Claesson-Welsh L., Heldin C.H.;
RT "Identification of two juxtamembrane autophosphorylation sites in the PDGF
RT beta-receptor; involvement in the interaction with Src family tyrosine
RT kinases.";
RL EMBO J. 12:2257-2264(1993).
RN [20]
RP INTERACTION WITH DGFA AND PDGFB.
RX PubMed=7679113; DOI=10.1016/s0021-9258(18)53739-x;
RA Fretto L.J., Snape A.J., Tomlinson J.E., Seroogy J.J., Wolf D.L.,
RA LaRochelle W.J., Giese N.A.;
RT "Mechanism of platelet-derived growth factor (PDGF) AA, AB, and BB binding
RT to alpha and beta PDGF receptor.";
RL J. Biol. Chem. 268:3625-3631(1993).
RN [21]
RP FUNCTION IN PHOSPHORYLATION AND ACTIVATION OF PTPN11, INTERACTION WITH
RP PTPN11; PIK3R1; PLCG1 AND RASA1, AND MUTAGENESIS OF TYR-1009.
RX PubMed=7691811; DOI=10.1016/s0021-9258(20)80562-6;
RA Lechleider R.J., Sugimoto S., Bennett A.M., Kashishian A.S., Cooper J.A.,
RA Shoelson S.E., Walsh C.T., Neel B.G.;
RT "Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by
RT its binding site, phosphotyrosine 1009, on the human platelet-derived
RT growth factor receptor.";
RL J. Biol. Chem. 268:21478-21481(1993).
RN [22]
RP INTERACTION WITH NCK1 AND PIK3R1, FUNCTION IN PHOSPHORYLATION OF NCK1, AND
RP MUTAGENESIS OF TYR-751.
RX PubMed=7692233; DOI=10.1128/mcb.13.11.6889-6896.1993;
RA Nishimura R., Li W., Kashishian A., Mondino A., Zhou M., Cooper J.,
RA Schlessinger J.;
RT "Two signaling molecules share a phosphotyrosine-containing binding site in
RT the platelet-derived growth factor receptor.";
RL Mol. Cell. Biol. 13:6889-6896(1993).
RN [23]
RP INTERACTION WITH SHB.
RX PubMed=8302579;
RA Welsh M., Mares J., Karlsson T., Lavergne C., Breant B., Claesson-Welsh L.;
RT "Shb is a ubiquitously expressed Src homology 2 protein.";
RL Oncogene 9:19-27(1994).
RN [24]
RP INTERACTION WITH GRB7.
RX PubMed=8940081; DOI=10.1074/jbc.271.48.30942;
RA Yokote K., Margolis B., Heldin C.H., Claesson-Welsh L.;
RT "Grb7 is a downstream signaling component of platelet-derived growth factor
RT alpha- and beta-receptors.";
RL J. Biol. Chem. 271:30942-30949(1996).
RN [25]
RP CHROMOSOMAL TRANSLOCATION WITH TRIP11.
RX PubMed=9373237;
RA Abe A., Emi N., Tanimoto M., Terasaki H., Marunouchi T., Saito H.;
RT "Fusion of the platelet-derived growth factor receptor beta to a novel gene
RT CEV14 in acute myelogenous leukemia after clonal evolution.";
RL Blood 90:4271-4277(1997).
RN [26]
RP INTERACTION WITH GRB10, AND MUTAGENESIS OF TYR-579; TYR-581; TYR-716;
RP TYR-740; TYR-751; TYR-771; TYR-857; TYR-1009 AND TYR-1021.
RX PubMed=10454568; DOI=10.1128/mcb.19.9.6217;
RA Wang J., Dai H., Yousaf N., Moussaif M., Deng Y., Boufelliga A.,
RA Swamy O.R., Leone M.E., Riedel H.;
RT "Grb10, a positive, stimulatory signaling adapter in platelet-derived
RT growth factor BB-, insulin-like growth factor I-, and insulin-mediated
RT mitogenesis.";
RL Mol. Cell. Biol. 19:6217-6228(1999).
RN [27]
RP INTERACTION WITH SH2B2/APS.
RX PubMed=9989826; DOI=10.1038/sj.onc.1202326;
RA Yokouchi M., Wakioka T., Sakamoto H., Yasukawa H., Ohtsuka S., Sasaki A.,
RA Ohtsubo M., Valius M., Inoue A., Komiya S., Yoshimura A.;
RT "APS, an adaptor protein containing PH and SH2 domains, is associated with
RT the PDGF receptor and c-Cbl and inhibits PDGF-induced mitogenesis.";
RL Oncogene 18:759-767(1999).
RN [28]
RP PHOSPHORYLATION AT TYR-562; TYR-751; TYR-763; TYR-771; TYR-775; TYR-778;
RP TYR-857; TYR-1009 AND TYR-1021, AND DEPHOSPHORYLATION AT TYR-751; TYR-857;
RP TYR-1009 AND TYR-1021 BY PTPRJ.
RX PubMed=10821867; DOI=10.1074/jbc.275.21.16219;
RA Kovalenko M., Denner K., Sandstrom J., Persson C., Gross S., Jandt E.,
RA Vilella R., Bohmer F., Ostman A.;
RT "Site-selective dephosphorylation of the platelet-derived growth factor
RT beta-receptor by the receptor-like protein-tyrosine phosphatase DEP-1.";
RL J. Biol. Chem. 275:16219-16226(2000).
RN [29]
RP INTERACTION WITH PIK3C2B.
RX PubMed=10805725; DOI=10.1128/mcb.20.11.3817-3830.2000;
RA Arcaro A., Zvelebil M.J., Wallasch C., Ullrich A., Waterfield M.D.,
RA Domin J.;
RT "Class II phosphoinositide 3-kinases are downstream targets of activated
RT polypeptide growth factor receptors.";
RL Mol. Cell. Biol. 20:3817-3830(2000).
RN [30]
RP FUNCTION AS A RECEPTOR FOR PDGFC, AND INTERACTION WITH PDGFC.
RX PubMed=11297552; DOI=10.1074/jbc.m101056200;
RA Gilbertson D.G., Duff M.E., West J.W., Kelly J.D., Sheppard P.O.,
RA Hofstrand P.D., Gao Z., Shoemaker K., Bukowski T.R., Moore M.,
RA Feldhaus A.L., Humes J.M., Palmer T.E., Hart C.E.;
RT "Platelet-derived growth factor C (PDGF-C), a novel growth factor that
RT binds to PDGF alpha and beta receptor.";
RL J. Biol. Chem. 276:27406-27414(2001).
RN [31]
RP FUNCTION AS A RECEPTOR FOR PDGFD.
RX PubMed=11331881; DOI=10.1038/35074588;
RA Bergsten E., Uutela M., Li X., Pietras K., Oestman A., Heldin C.-H.,
RA Alitalo K., Eriksson U.;
RT "PDGF-D is a specific, protease-activated ligand for the PDGF beta-
RT receptor.";
RL Nat. Cell Biol. 3:512-516(2001).
RN [32]
RP CHROMOSOMAL TRANSLOCATION WITH ETV6.
RX PubMed=12181402; DOI=10.1056/nejmoa020150;
RA Apperley J.F., Gardembas M., Melo J.V., Russell-Jones R., Bain B.J.,
RA Baxter E.J., Chase A., Chessells J.M., Colombat M., Dearden C.E.,
RA Dimitrijevic S., Mahon F.-X., Marin D., Nikolova Z., Olavarria E.,
RA Silberman S., Schultheis B., Cross N.C.P., Goldman J.M.;
RT "Response to imatinib mesylate in patients with chronic myeloproliferative
RT diseases with rearrangements of the platelet-derived growth factor receptor
RT beta.";
RL N. Engl. J. Med. 347:481-487(2002).
RN [33]
RP CHROMOSOMAL TRANSLOCATION WITH PDE4DIP.
RX PubMed=12907457; DOI=10.1182/blood-2003-04-1150;
RA Wilkinson K., Velloso E.R.P., Lopes L.F., Lee C., Aster J.C., Shipp M.A.,
RA Aguiar R.C.T.;
RT "Cloning of the t(1;5)(q23;q33) in a myeloproliferative disorder associated
RT with eosinophilia: involvement of PDGFRB and response to imatinib.";
RL Blood 102:4187-4190(2003).
RN [34]
RP CHROMOSOMAL TRANSLOCATION WITH SPECC1.
RX PubMed=15087372; DOI=10.1158/0008-5472.can-03-4026;
RA Morerio C., Acquila M., Rosanda C., Rapella A., Dufour C., Locatelli F.,
RA Maserati E., Pasquali F., Panarello C.;
RT "HCMOGT-1 is a novel fusion partner to PDGFRB in juvenile myelomonocytic
RT leukemia with t(5;17)(q33;p11.2).";
RL Cancer Res. 64:2649-2651(2004).
RN [35]
RP CHROMOSOMAL TRANSLOCATION WITH TP53BP1, AND ACTIVITY REGULATION.
RX PubMed=15492236; DOI=10.1158/0008-5472.can-04-2005;
RA Grand F.H., Burgstaller S., Kuhr T., Baxter E.J., Webersinke G., Thaler J.,
RA Chase A.J., Cross N.C.;
RT "p53-Binding protein 1 is fused to the platelet-derived growth factor
RT receptor beta in a patient with a t(5;15)(q33;q22) and an imatinib-
RT responsive eosinophilic myeloproliferative disorder.";
RL Cancer Res. 64:7216-7219(2004).
RN [36]
RP PHOSPHORYLATION AT TYR-579; TYR-751; TYR-771 AND TYR-1021, AND
RP DEPHOSPHORYLATION AT TYR-579 AND TYR-1021 BY PTPN2.
RX PubMed=14966296; DOI=10.1128/mcb.24.5.2190-2201.2004;
RA Persson C., Saevenhed C., Bourdeau A., Tremblay M.L., Markova B.,
RA Boehmer F.D., Haj F.G., Neel B.G., Elson A., Heldin C.H., Roennstrand L.,
RA Ostman A., Hellberg C.;
RT "Site-selective regulation of platelet-derived growth factor beta receptor
RT tyrosine phosphorylation by T-cell protein tyrosine phosphatase.";
RL Mol. Cell. Biol. 24:2190-2201(2004).
RN [37]
RP PHOSPHORYLATION AT TYR-579; TYR-581; TYR-716; TYR-740; TYR-771; TYR-857;
RP TYR-1009 AND TYR-1021.
RX PubMed=15902258; DOI=10.1038/nature03587;
RA Choi M.H., Lee I.K., Kim G.W., Kim B.U., Han Y.H., Yu D.Y., Park H.S.,
RA Kim K.Y., Lee J.S., Choi C., Bae Y.S., Lee B.I., Rhee S.G., Kang S.W.;
RT "Regulation of PDGF signalling and vascular remodelling by peroxiredoxin
RT II.";
RL Nature 435:347-353(2005).
RN [38]
RP INTERACTION WITH CBL, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-1021, AND
RP UBIQUITINATION.
RX PubMed=17620338; DOI=10.1074/jbc.m701797200;
RA Reddi A.L., Ying G., Duan L., Chen G., Dimri M., Douillard P., Druker B.J.,
RA Naramura M., Band V., Band H.;
RT "Binding of Cbl to a phospholipase Cgamma1-docking site on platelet-derived
RT growth factor receptor beta provides a dual mechanism of negative
RT regulation.";
RL J. Biol. Chem. 282:29336-29347(2007).
RN [39]
RP FUNCTION AS PDGFD RECEPTOR.
RX PubMed=21098708; DOI=10.1158/0008-5472.can-10-0511;
RA Ustach C.V., Huang W., Conley-LaComb M.K., Lin C.Y., Che M., Abrams J.,
RA Kim H.R.;
RT "A novel signaling axis of matriptase/PDGF-D/ss-PDGFR in human prostate
RT cancer.";
RL Cancer Res. 70:9631-9640(2010).
RN [40]
RP FUNCTION IN PHOSPHORYLATION OF CBL; STAM; PDCD6IP/ALIX; PLCG1 AND PTPN11,
RP CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF LYS-634 AND TYR-857.
RX PubMed=20494825; DOI=10.1016/j.cellsig.2010.05.004;
RA Wardega P., Heldin C.H., Lennartsson J.;
RT "Mutation of tyrosine residue 857 in the PDGF beta-receptor affects cell
RT proliferation but not migration.";
RL Cell. Signal. 22:1363-1368(2010).
RN [41]
RP FUNCTION.
RX PubMed=20529858; DOI=10.1074/jbc.m110.102566;
RA Mendelson K., Swendeman S., Saftig P., Blobel C.P.;
RT "Stimulation of platelet-derived growth factor receptor beta (PDGFRbeta)
RT activates ADAM17 and promotes metalloproteinase-dependent cross-talk
RT between the PDGFRbeta and epidermal growth factor receptor (EGFR) signaling
RT pathways.";
RL J. Biol. Chem. 285:25024-25032(2010).
RN [42]
RP FUNCTION IN SMOOTH MUSCLE CELL PROLIFERATION AND MIGRATION.
RX PubMed=21733313; DOI=10.1017/s0007114511002571;
RA Kim H.J., Cha B.Y., Choi B., Lim J.S., Woo J.T., Kim J.S.;
RT "Glyceollins inhibit platelet-derived growth factor-mediated human arterial
RT smooth muscle cell proliferation and migration.";
RL Br. J. Nutr. 107:24-35(2012).
RN [43]
RP INTERACTION WITH SHC1 AND GRB2, AND FUNCTION IN PHOSPHORYLATION OF SHC1.
RX PubMed=8195171; DOI=10.1016/s0021-9258(17)36611-5;
RA Yokote K., Mori S., Hansen K., McGlade J., Pawson T., Heldin C.H.,
RA Claesson-Welsh L.;
RT "Direct interaction between Shc and the platelet-derived growth factor
RT beta-receptor.";
RL J. Biol. Chem. 269:15337-15343(1994).
RN [44]
RP FUNCTION IN SMOOTH MUSCLE CELL MIGRATION AND NEOINTIMA FORMATION AFTER
RP BLOOD VESSEL INJURY, AND MUTAGENESIS OF TYR-740; TYR-751 AND TYR-1021.
RX PubMed=21679854; DOI=10.1016/j.jacc.2011.02.037;
RA Caglayan E., Vantler M., Leppanen O., Gerhardt F., Mustafov L.,
RA Ten Freyhaus H., Kappert K., Odenthal M., Zimmermann W.H., Tallquist M.D.,
RA Rosenkranz S.;
RT "Disruption of platelet-derived growth factor-dependent
RT phosphatidylinositol 3-kinase and phospholipase Cgamma 1 activity abolishes
RT vascular smooth muscle cell proliferation and migration and attenuates
RT neointima formation in vivo.";
RL J. Am. Coll. Cardiol. 57:2527-2538(2011).
RN [45]
RP INVOLVEMENT IN PENTT, VARIANT PENTT ALA-665, AND CHARACTERIZATION OF
RP VARIANT PENTT ALA-665.
RX PubMed=26279204; DOI=10.1016/j.ajhg.2015.07.009;
RA Johnston J.J., Sanchez-Contreras M.Y., Keppler-Noreuil K.M., Sapp J.,
RA Crenshaw M., Finch N.A., Cormier-Daire V., Rademakers R., Sybert V.P.,
RA Biesecker L.G.;
RT "A point mutation in PDGFRB causes autosomal-dominant Penttinen syndrome.";
RL Am. J. Hum. Genet. 97:465-474(2015).
RN [46]
RP INVOLVEMENT IN KOGS, AND VARIANT KOGS ARG-584.
RX PubMed=25454926; DOI=10.1016/j.jpeds.2014.10.015;
RA Takenouchi T., Yamaguchi Y., Tanikawa A., Kosaki R., Okano H., Kosaki K.;
RT "Novel overgrowth syndrome phenotype due to recurrent de novo PDGFRB
RT mutation.";
RL J. Pediatr. 166:483-486(2015).
RN [47]
RP CHARACTERIZATION OF VARIANTS IBGC4 PRO-658; TRP-987 AND VAL-1071, AND
RP FUNCTION.
RX PubMed=26599395; DOI=10.1371/journal.pone.0143407;
RA Vanlandewijck M., Lebouvier T., Andaloussi Maee M., Nahar K., Hornemann S.,
RA Kenkel D., Cunha S.I., Lennartsson J., Boss A., Heldin C.H., Keller A.,
RA Betsholtz C.;
RT "Functional characterization of germline mutations in PDGFB and PDGFRB in
RT primary familial brain calcification.";
RL PLoS ONE 10:E0143407-E0143407(2015).
RN [48]
RP REVIEW ON SIGNALING AND AUTOPHOSPHORYLATION.
RX PubMed=9739761; DOI=10.1016/s0304-419x(98)00015-8;
RA Heldin C.H., Ostman A., Ronnstrand L.;
RT "Signal transduction via platelet-derived growth factor receptors.";
RL Biochim. Biophys. Acta 1378:F79-113(1998).
RN [49]
RP REVIEW.
RX PubMed=15207817; DOI=10.1016/j.cytogfr.2004.03.002;
RA Ostman A.;
RT "PDGF receptors-mediators of autocrine tumor growth and regulators of tumor
RT vasculature and stroma.";
RL Cytokine Growth Factor Rev. 15:275-286(2004).
RN [50]
RP REVIEW.
RX PubMed=17419949; DOI=10.1016/s0065-230x(06)97011-0;
RA Ostman A., Heldin C.H.;
RT "PDGF receptors as targets in tumor treatment.";
RL Adv. Cancer Res. 97:247-274(2007).
RN [51]
RP REVIEW ON FUNCTION; LIGANDS; ROLE IN DEVELOPMENT AND DISEASE AND ACTIVATION
RP OF SIGNALING PATHWAYS.
RX PubMed=18483217; DOI=10.1101/gad.1653708;
RA Andrae J., Gallini R., Betsholtz C.;
RT "Role of platelet-derived growth factors in physiology and medicine.";
RL Genes Dev. 22:1276-1312(2008).
RN [52]
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 751-755 IN COMPLEX WITH PIK3R1,
RP AND COMPARISON WITH NMR ANALYSIS.
RX PubMed=11567151; DOI=10.1107/s0907444901012434;
RA Pauptit R.A., Dennis C.A., Derbyshire D.J., Breeze A.L., Weston S.A.,
RA Rowsell S., Murshudov G.N.;
RT "NMR trial models: experiences with the colicin immunity protein Im7 and
RT the p85alpha C-terminal SH2-peptide complex.";
RL Acta Crystallogr. D 57:1397-1404(2001).
RN [53]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1102-1106 IN COMPLEX WITH
RP SLC9A3R1, AND INTERACTION WITH SLC9A3R1.
RX PubMed=11882663; DOI=10.1074/jbc.m201507200;
RA Karthikeyan S., Leung T., Ladias J.A.A.;
RT "Structural determinants of the Na+/H+ exchanger regulatory factor
RT interaction with the beta 2 adrenergic and platelet-derived growth factor
RT receptors.";
RL J. Biol. Chem. 277:18973-18978(2002).
RN [54]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 33-314 IN COMPLEX WITH PDGFB,
RP SUBUNIT, GLYCOSYLATION AT ASN-45; ASN-89; ASN-103; ASN-215; ASN-230;
RP ASN-292 AND ASN-307, AND DISULFIDE BONDS.
RX PubMed=20534510; DOI=10.1073/pnas.1000806107;
RA Shim A.H., Liu H., Focia P.J., Chen X., Lin P.C., He X.;
RT "Structures of a platelet-derived growth factor/propeptide complex and a
RT platelet-derived growth factor/receptor complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11307-11312(2010).
RN [55]
RP VARIANTS [LARGE SCALE ANALYSIS] PHE-29; LYS-282; LYS-485; HIS-589; TYR-718
RP AND ILE-882.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
RN [56]
RP VARIANT IMF1 THR-660.
RX PubMed=23731542; DOI=10.1016/j.ajhg.2013.04.024;
RA Martignetti J.A., Tian L., Li D., Ramirez M.C., Camacho-Vanegas O.,
RA Camacho S.C., Guo Y., Zand D.J., Bernstein A.M., Masur S.K., Kim C.E.,
RA Otieno F.G., Hou C., Abdel-Magid N., Tweddale B., Metry D., Fournet J.C.,
RA Papp E., McPherson E.W., Zabel C., Vaksmann G., Morisot C., Keating B.,
RA Sleiman P.M., Cleveland J.A., Everman D.B., Zackai E., Hakonarson H.;
RT "Mutations in PDGFRB cause autosomal-dominant infantile myofibromatosis.";
RL Am. J. Hum. Genet. 92:1001-1007(2013).
RN [57]
RP VARIANT IMF1 CYS-561.
RX PubMed=23731537; DOI=10.1016/j.ajhg.2013.04.026;
RA Cheung Y.H., Gayden T., Campeau P.M., Leduc C.A., Russo D., Nguyen V.H.,
RA Guo J., Qi M., Guan Y., Albrecht S., Moroz B., Eldin K.W., Lu J.T.,
RA Schwartzentruber J., Malkin D., Berghuis A.M., Emil S., Gibbs R.A.,
RA Burk D.L., Vanstone M., Lee B.H., Orchard D., Boycott K.M., Chung W.K.,
RA Jabado N.;
RT "A recurrent PDGFRB mutation causes familial infantile myofibromatosis.";
RL Am. J. Hum. Genet. 92:996-1000(2013).
RN [58]
RP VARIANTS IBGC4 PRO-658; TRP-987 AND VAL-1071.
RX PubMed=24065723; DOI=10.1093/brain/awt255;
RG French IBGC Study Group;
RA Nicolas G., Pottier C., Charbonnier C., Guyant-Marechal L., Le Ber I.,
RA Pariente J., Labauge P., Ayrignac X., Defebvre L., Maltete D.,
RA Martinaud O., Lefaucheur R., Guillin O., Wallon D., Chaumette B.,
RA Rondepierre P., Derache N., Fromager G., Schaeffer S., Krystkowiak P.,
RA Verny C., Jurici S., Sauvee M., Verin M., Lebouvier T., Rouaud O.,
RA Thauvin-Robinet C., Rousseau S., Rovelet-Lecrux A., Frebourg T.,
RA Campion D., Hannequin D.;
RT "Phenotypic spectrum of probable and genetically-confirmed idiopathic basal
RT ganglia calcification.";
RL Brain 136:3395-3407(2013).
RN [59]
RP VARIANTS IBGC4 PRO-658 AND TRP-987.
RX PubMed=23255827; DOI=10.1212/wnl.0b013e31827ccf34;
RA Nicolas G., Pottier C., Maltete D., Coutant S., Rovelet-Lecrux A.,
RA Legallic S., Rousseau S., Vaschalde Y., Guyant-Marechal L., Augustin J.,
RA Martinaud O., Defebvre L., Krystkowiak P., Pariente J., Clanet M.,
RA Labauge P., Ayrignac X., Lefaucheur R., Le Ber I., Frebourg T.,
RA Hannequin D., Campion D.;
RT "Mutation of the PDGFRB gene as a cause of idiopathic basal ganglia
RT calcification.";
RL Neurology 80:181-187(2013).
CC -!- FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor
CC for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA
CC and PDGFB, and plays an essential role in the regulation of embryonic
CC development, cell proliferation, survival, differentiation, chemotaxis
CC and migration. Plays an essential role in blood vessel development by
CC promoting proliferation, migration and recruitment of pericytes and
CC smooth muscle cells to endothelial cells. Plays a role in the migration
CC of vascular smooth muscle cells and the formation of neointima at
CC vascular injury sites. Required for normal development of the
CC cardiovascular system. Required for normal recruitment of pericytes
CC (mesangial cells) in the kidney glomerulus, and for normal formation of
CC a branched network of capillaries in kidney glomeruli. Promotes
CC rearrangement of the actin cytoskeleton and the formation of membrane
CC ruffles. Binding of its cognate ligands - homodimeric PDGFB,
CC heterodimers formed by PDGFA and PDGFB or homodimeric PDGFD -leads to
CC the activation of several signaling cascades; the response depends on
CC the nature of the bound ligand and is modulated by the formation of
CC heterodimers between PDGFRA and PDGFRB. Phosphorylates PLCG1, PIK3R1,
CC PTPN11, RASA1/GAP, CBL, SHC1 and NCK1. Activation of PLCG1 leads to the
CC production of the cellular signaling molecules diacylglycerol and
CC inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca(2+) and the
CC activation of protein kinase C. Phosphorylation of PIK3R1, the
CC regulatory subunit of phosphatidylinositol 3-kinase, leads to the
CC activation of the AKT1 signaling pathway. Phosphorylation of SHC1, or
CC of the C-terminus of PTPN11, creates a binding site for GRB2, resulting
CC in the activation of HRAS, RAF1 and down-stream MAP kinases, including
CC MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation and activation
CC of SRC family kinases. Promotes phosphorylation of PDCD6IP/ALIX and
CC STAM. Receptor signaling is down-regulated by protein phosphatases that
CC dephosphorylate the receptor and its down-stream effectors, and by
CC rapid internalization of the activated receptor.
CC {ECO:0000269|PubMed:11297552, ECO:0000269|PubMed:11331881,
CC ECO:0000269|PubMed:1314164, ECO:0000269|PubMed:1396585,
CC ECO:0000269|PubMed:1653029, ECO:0000269|PubMed:1709159,
CC ECO:0000269|PubMed:1846866, ECO:0000269|PubMed:20494825,
CC ECO:0000269|PubMed:20529858, ECO:0000269|PubMed:21098708,
CC ECO:0000269|PubMed:21679854, ECO:0000269|PubMed:21733313,
CC ECO:0000269|PubMed:2554309, ECO:0000269|PubMed:26599395,
CC ECO:0000269|PubMed:2835772, ECO:0000269|PubMed:2850496,
CC ECO:0000269|PubMed:7685273, ECO:0000269|PubMed:7691811,
CC ECO:0000269|PubMed:7692233, ECO:0000269|PubMed:8195171}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028,
CC ECO:0000269|PubMed:1846866, ECO:0000269|PubMed:20494825,
CC ECO:0000269|PubMed:7685273};
CC -!- ACTIVITY REGULATION: Present in an inactive conformation in the absence
CC of bound ligand. Binding of PDGFB and/or PDGFD leads to dimerization
CC and activation by autophosphorylation on tyrosine residues. Inhibited
CC by imatinib. {ECO:0000269|PubMed:15492236}.
CC -!- SUBUNIT: Interacts with homodimeric PDGFB and PDGFD, and with
CC heterodimers formed by PDGFA and PDGFB. May also interact with
CC homodimeric PDGFC. Monomer in the absence of bound ligand. Interaction
CC with homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or
CC homodimeric PDGFD, leads to receptor dimerization, where both PDGFRA
CC homodimers and heterodimers with PDGFRB are observed. Interacts with
CC SH2B2/APS. Interacts directly (tyrosine phosphorylated) with SHB.
CC Interacts (tyrosine phosphorylated) with PIK3R1 and RASA1. Interacts
CC (tyrosine phosphorylated) with CBL. Interacts (tyrosine phosphorylated)
CC with SRC and SRC family kinases. Interacts (tyrosine phosphorylated)
CC with PIK3C2B, maybe indirectly. Interacts (tyrosine phosphorylated)
CC with SHC1, GRB7, GRB10 and NCK1. Interaction with GRB2 is mediated by
CC SHC1. Interacts (via C-terminus) with SLC9A3R1.
CC {ECO:0000269|PubMed:10454568, ECO:0000269|PubMed:10805725,
CC ECO:0000269|PubMed:11297552, ECO:0000269|PubMed:11567151,
CC ECO:0000269|PubMed:11882663, ECO:0000269|PubMed:1314164,
CC ECO:0000269|PubMed:1375321, ECO:0000269|PubMed:1396585,
CC ECO:0000269|PubMed:1709159, ECO:0000269|PubMed:17620338,
CC ECO:0000269|PubMed:20534510, ECO:0000269|PubMed:2835772,
CC ECO:0000269|PubMed:2850496, ECO:0000269|PubMed:7679113,
CC ECO:0000269|PubMed:7691811, ECO:0000269|PubMed:7692233,
CC ECO:0000269|PubMed:8195171, ECO:0000269|PubMed:8302579,
CC ECO:0000269|PubMed:8940081, ECO:0000269|PubMed:9989826}.
CC -!- INTERACTION:
CC P09619; P05067: APP; NbExp=3; IntAct=EBI-641237, EBI-77613;
CC P09619; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-641237, EBI-742887;
CC P09619; P06241: FYN; NbExp=3; IntAct=EBI-641237, EBI-515315;
CC P09619; Q14451: GRB7; NbExp=4; IntAct=EBI-641237, EBI-970191;
CC P09619; P14778: IL1R1; NbExp=2; IntAct=EBI-641237, EBI-525905;
CC P09619; P35968: KDR; NbExp=2; IntAct=EBI-641237, EBI-1005487;
CC P09619; Q53G59: KLHL12; NbExp=6; IntAct=EBI-641237, EBI-740929;
CC P09619; Q5T749: KPRP; NbExp=3; IntAct=EBI-641237, EBI-10981970;
CC P09619; Q15323: KRT31; NbExp=3; IntAct=EBI-641237, EBI-948001;
CC P09619; O76011: KRT34; NbExp=3; IntAct=EBI-641237, EBI-1047093;
CC P09619; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-641237, EBI-10172052;
CC P09619; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-641237, EBI-11953334;
CC P09619; O94898: LRIG2; NbExp=3; IntAct=EBI-641237, EBI-2830372;
CC P09619; O75581: LRP6; NbExp=3; IntAct=EBI-641237, EBI-910915;
CC P09619; P01127: PDGFB; NbExp=16; IntAct=EBI-641237, EBI-1554925;
CC P09619; P27986: PIK3R1; NbExp=19; IntAct=EBI-641237, EBI-79464;
CC P09619; P19174: PLCG1; NbExp=6; IntAct=EBI-641237, EBI-79387;
CC P09619; P60484: PTEN; NbExp=3; IntAct=EBI-641237, EBI-696162;
CC P09619; P18031: PTPN1; NbExp=3; IntAct=EBI-641237, EBI-968788;
CC P09619; Q06124: PTPN11; NbExp=8; IntAct=EBI-641237, EBI-297779;
CC P09619; Q05209: PTPN12; NbExp=3; IntAct=EBI-641237, EBI-2266035;
CC P09619; Q12913: PTPRJ; NbExp=4; IntAct=EBI-641237, EBI-2264500;
CC P09619; P20936: RASA1; NbExp=3; IntAct=EBI-641237, EBI-1026476;
CC P09619; Q13239: SLA; NbExp=4; IntAct=EBI-641237, EBI-726214;
CC P09619; O14745: SLC9A3R1; NbExp=5; IntAct=EBI-641237, EBI-349787;
CC P09619; Q15654: TRIP6; NbExp=3; IntAct=EBI-641237, EBI-742327;
CC P09619; P0CK45: E5; Xeno; NbExp=2; IntAct=EBI-641237, EBI-7015490;
CC P09619; P35918: Kdr; Xeno; NbExp=4; IntAct=EBI-641237, EBI-1555005;
CC P09619; P23727: PIK3R1; Xeno; NbExp=6; IntAct=EBI-641237, EBI-520244;
CC P09619; P08487: PLCG1; Xeno; NbExp=3; IntAct=EBI-641237, EBI-8013886;
CC P09619; P41499: Ptpn11; Xeno; NbExp=4; IntAct=EBI-641237, EBI-7180604;
CC P09619; P25020: V-SRC; Xeno; NbExp=4; IntAct=EBI-641237, EBI-8636140;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Cytoplasmic vesicle. Lysosome lumen. Note=After ligand
CC binding, the autophosphorylated receptor is ubiquitinated and
CC internalized, leading to its degradation.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P09619-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P09619-2; Sequence=VSP_056008, VSP_056009;
CC -!- PTM: Autophosphorylated on tyrosine residues upon ligand binding.
CC Autophosphorylation occurs in trans, i.e. one subunit of the dimeric
CC receptor phosphorylates tyrosine residues on the other subunit.
CC Phosphorylation at Tyr-579, and to a lesser degree, at Tyr-581, is
CC important for interaction with SRC family kinases. Phosphorylation at
CC Tyr-740 and Tyr-751 is important for interaction with PIK3R1.
CC Phosphorylation at Tyr-751 is important for interaction with NCK1.
CC Phosphorylation at Tyr-771 and Tyr-857 is important for interaction
CC with RASA1/GAP. Phosphorylation at Tyr-857 is important for efficient
CC phosphorylation of PLCG1 and PTPN11, resulting in increased
CC phosphorylation of AKT1, MAPK1/ERK2 and/or MAPK3/ERK1, PDCD6IP/ALIX and
CC STAM, and in increased cell proliferation. Phosphorylation at Tyr-1009
CC is important for interaction with PTPN11. Phosphorylation at Tyr-1009
CC and Tyr-1021 is important for interaction with PLCG1. Phosphorylation
CC at Tyr-1021 is important for interaction with CBL; PLCG1 and CBL
CC compete for the same binding site. Dephosphorylated by PTPRJ at Tyr-
CC 751, Tyr-857, Tyr-1009 and Tyr-1021. Dephosphorylated by PTPN2 at Tyr-
CC 579 and Tyr-1021. {ECO:0000269|PubMed:10821867,
CC ECO:0000269|PubMed:1314164, ECO:0000269|PubMed:1396585,
CC ECO:0000269|PubMed:14966296, ECO:0000269|PubMed:15902258,
CC ECO:0000269|PubMed:1709159, ECO:0000269|PubMed:2550144,
CC ECO:0000269|PubMed:7685273}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:20534510,
CC ECO:0000269|PubMed:2850496}.
CC -!- PTM: Ubiquitinated. After autophosphorylation, the receptor is
CC polyubiquitinated, leading to its degradation.
CC {ECO:0000269|PubMed:1313434, ECO:0000269|PubMed:17620338}.
CC -!- DISEASE: Note=A chromosomal aberration involving PDGFRB is found in a
CC form of chronic myelomonocytic leukemia (CMML). Translocation
CC t(5;12)(q33;p13) with EVT6/TEL. It is characterized by abnormal clonal
CC myeloid proliferation and by progression to acute myelogenous leukemia
CC (AML).
CC -!- DISEASE: Myeloproliferative disorder chronic with eosinophilia (MPE)
CC [MIM:131440]: A hematologic disorder characterized by malignant
CC eosinophils proliferation. Note=The gene represented in this entry may
CC be involved in disease pathogenesis. Chromosomal aberrations involving
CC PDGFRB have been found in many instances of chronic myeloproliferative
CC disorder with eosinophilia. Translocation t(5;12) with ETV6 on
CC chromosome 12 creating an PDGFRB-ETV6 fusion protein (PubMed:12181402).
CC Translocation t(5;15)(q33;q22) with TP53BP1 creating a PDGFRB-TP53BP1
CC fusion protein (PubMed:15492236). Translocation t(1;5)(q23;q33) that
CC forms a PDE4DIP-PDGFRB fusion protein (PubMed:12907457). Translocation
CC t(5;6)(q33-34;q23) with CEP85L that fuses the 5'-end of CEP85L (isoform
CC 4) to the 3'-end of PDGFRB (PubMed:21938754).
CC {ECO:0000269|PubMed:12181402, ECO:0000269|PubMed:12907457,
CC ECO:0000269|PubMed:15492236, ECO:0000269|PubMed:21938754}.
CC -!- DISEASE: Leukemia, acute myelogenous (AML) [MIM:601626]: A subtype of
CC acute leukemia, a cancer of the white blood cells. AML is a malignant
CC disease of bone marrow characterized by maturational arrest of
CC hematopoietic precursors at an early stage of development. Clonal
CC expansion of myeloid blasts occurs in bone marrow, blood, and other
CC tissue. Myelogenous leukemias develop from changes in cells that
CC normally produce neutrophils, basophils, eosinophils and monocytes.
CC Note=The gene represented in this entry may be involved in disease
CC pathogenesis. A chromosomal aberration involving PDGFRB has been found
CC in a patient with AML. Translocation t(5;14)(q33;q32) with TRIP11
CC (PubMed:9373237). {ECO:0000269|PubMed:9373237}.
CC -!- DISEASE: Leukemia, juvenile myelomonocytic (JMML) [MIM:607785]: An
CC aggressive pediatric myelodysplastic syndrome/myeloproliferative
CC disorder characterized by malignant transformation in the hematopoietic
CC stem cell compartment with proliferation of differentiated progeny.
CC Patients have splenomegaly, enlarged lymph nodes, rashes, and
CC hemorrhages. Note=The gene represented in this entry may be involved in
CC disease pathogenesis. A chromosomal aberration involving PDGFRB has
CC been found in a patient with JMML. Translocation t(5;17)(q33;p11.2)
CC with SPECC1 (PubMed:15087372). {ECO:0000269|PubMed:15087372}.
CC -!- DISEASE: Basal ganglia calcification, idiopathic, 4 (IBGC4)
CC [MIM:615007]: A form of basal ganglia calcification, an autosomal
CC dominant condition characterized by symmetric calcification in the
CC basal ganglia and other brain regions. Affected individuals can either
CC be asymptomatic or show a wide spectrum of neuropsychiatric symptoms,
CC including parkinsonism, dystonia, tremor, ataxia, dementia, psychosis,
CC seizures, and chronic headache. Serum levels of calcium, phosphate,
CC alkaline phosphatase and parathyroid hormone are normal. The
CC neuropathological hallmark of the disease is vascular and pericapillary
CC calcification, mainly of calcium phosphate, in the affected brain
CC areas. {ECO:0000269|PubMed:23255827, ECO:0000269|PubMed:24065723,
CC ECO:0000269|PubMed:26599395}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Myofibromatosis, infantile 1 (IMF1) [MIM:228550]: A rare
CC mesenchymal disorder characterized by the development of benign tumors
CC in the skin, striated muscles, bones, and, more rarely, visceral
CC organs. Subcutaneous or soft tissue nodules commonly involve the skin
CC of the head, neck, and trunk. Skeletal and muscular lesions occur in
CC about half of the patients. Lesions may be solitary or multicentric,
CC and they may be present at birth or become apparent in early infancy or
CC occasionally in adult life. Visceral lesions are associated with high
CC morbidity and mortality. {ECO:0000269|PubMed:23731537,
CC ECO:0000269|PubMed:23731542}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Kosaki overgrowth syndrome (KOGS) [MIM:616592]: A syndrome
CC characterized by somatic overgrowth, distinctive facial features,
CC hyperelastic and fragile skin, and progressive neurologic deterioration
CC with white matter lesions on brain imaging.
CC {ECO:0000269|PubMed:25454926}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Premature aging syndrome, Penttinen type (PENTT) [MIM:601812]:
CC A syndrome characterized by a prematurely aged appearance with
CC lipoatrophy, epidermal and dermal atrophy along with hypertrophic
CC lesions that resemble scars, thin hair, proptosis, underdeveloped
CC cheekbones, and marked acro-osteolysis. {ECO:0000269|PubMed:26279204}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. CSF-1/PDGF receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PDGFRBID21ch5q32.html";
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DR EMBL; J03278; AAA60049.1; -; mRNA.
DR EMBL; M21616; AAA36427.1; -; mRNA.
DR EMBL; EU826595; ACF47631.1; -; mRNA.
DR EMBL; AC005895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032224; AAH32224.1; -; mRNA.
DR EMBL; U33172; AAC51675.1; -; Genomic_DNA.
DR CCDS; CCDS4303.1; -. [P09619-1]
DR PIR; A28206; PFHUGB.
DR RefSeq; NP_002600.1; NM_002609.3. [P09619-1]
DR RefSeq; XP_011535960.1; XM_011537658.1.
DR RefSeq; XP_011535961.1; XM_011537659.1.
DR PDB; 1GQ5; X-ray; 2.20 A; A=1102-1106.
DR PDB; 1H9O; X-ray; 1.79 A; B=751-755.
DR PDB; 1SHA; X-ray; 1.50 A; B=751-755.
DR PDB; 2IUI; X-ray; 2.40 A; C/D=748-758.
DR PDB; 2L6W; NMR; -; A/B=526-563.
DR PDB; 2PLD; NMR; -; B=1018-1029.
DR PDB; 2PLE; NMR; -; B=1018-1029.
DR PDB; 3MJG; X-ray; 2.30 A; X/Y=33-314.
DR PDBsum; 1GQ5; -.
DR PDBsum; 1H9O; -.
DR PDBsum; 1SHA; -.
DR PDBsum; 2IUI; -.
DR PDBsum; 2L6W; -.
DR PDBsum; 2PLD; -.
DR PDBsum; 2PLE; -.
DR PDBsum; 3MJG; -.
DR AlphaFoldDB; P09619; -.
DR BMRB; P09619; -.
DR SMR; P09619; -.
DR BioGRID; 111185; 120.
DR ComplexPortal; CPX-2882; PDGF receptor beta - PDGF-BB complex.
DR ComplexPortal; CPX-2883; PDGF receptor alpha-beta - PDGF-BB complex.
DR ComplexPortal; CPX-2886; PDGF receptor beta - PDGF-AB complex.
DR ComplexPortal; CPX-2888; PDGF receptor alpha-beta - PDGF-CC complex.
DR ComplexPortal; CPX-2889; PDGF receptor beta - PDGF-DD complex.
DR ComplexPortal; CPX-2890; PDGF receptor alpha-beta - PDGF-DD complex.
DR ComplexPortal; CPX-2891; PDGF receptor beta - PDGF-CC complex.
DR ComplexPortal; CPX-2892; PDGF receptor alpha-beta - PDGF-AB complex.
DR CORUM; P09619; -.
DR DIP; DIP-558N; -.
DR IntAct; P09619; 201.
DR MINT; P09619; -.
DR STRING; 9606.ENSP00000261799; -.
DR BindingDB; P09619; -.
DR ChEMBL; CHEMBL1913; -.
DR DrugBank; DB00102; Becaplermin.
DR DrugBank; DB01254; Dasatinib.
DR DrugBank; DB12147; Erdafitinib.
DR DrugBank; DB10770; Foreskin fibroblast (neonatal).
DR DrugBank; DB12010; Fostamatinib.
DR DrugBank; DB00619; Imatinib.
DR DrugBank; DB06595; Midostaurin.
DR DrugBank; DB09079; Nintedanib.
DR DrugBank; DB06589; Pazopanib.
DR DrugBank; DB12978; Pexidartinib.
DR DrugBank; DB09221; Polaprezinc.
DR DrugBank; DB15822; Pralsetinib.
DR DrugBank; DB08896; Regorafenib.
DR DrugBank; DB14840; Ripretinib.
DR DrugBank; DB00398; Sorafenib.
DR DrugBank; DB01268; Sunitinib.
DR DrugBank; DB11800; Tivozanib.
DR DrugBank; DB09283; Trapidil.
DR DrugBank; DB05146; XL820.
DR DrugBank; DB05014; XL999.
DR DrugCentral; P09619; -.
DR GuidetoPHARMACOLOGY; 1804; -.
DR TCDB; 8.A.23.1.37; the basigin (basigin) family.
DR GlyConnect; 1967; 4 N-Linked glycans (3 sites).
DR GlyGen; P09619; 11 sites, 4 N-linked glycans (3 sites).
DR iPTMnet; P09619; -.
DR PhosphoSitePlus; P09619; -.
DR BioMuta; PDGFRB; -.
DR DMDM; 129890; -.
DR CPTAC; CPTAC-1630; -.
DR EPD; P09619; -.
DR jPOST; P09619; -.
DR MassIVE; P09619; -.
DR MaxQB; P09619; -.
DR PaxDb; P09619; -.
DR PeptideAtlas; P09619; -.
DR PRIDE; P09619; -.
DR ProteomicsDB; 52253; -. [P09619-1]
DR ABCD; P09619; 4 sequenced antibodies.
DR Antibodypedia; 3424; 2229 antibodies from 49 providers.
DR DNASU; 5159; -.
DR Ensembl; ENST00000261799.9; ENSP00000261799.4; ENSG00000113721.14. [P09619-1]
DR GeneID; 5159; -.
DR KEGG; hsa:5159; -.
DR MANE-Select; ENST00000261799.9; ENSP00000261799.4; NM_002609.4; NP_002600.1.
DR UCSC; uc003lro.4; human. [P09619-1]
DR CTD; 5159; -.
DR DisGeNET; 5159; -.
DR GeneCards; PDGFRB; -.
DR GeneReviews; PDGFRB; -.
DR HGNC; HGNC:8804; PDGFRB.
DR HPA; ENSG00000113721; Low tissue specificity.
DR MalaCards; PDGFRB; -.
DR MIM; 131440; phenotype.
DR MIM; 173410; gene.
DR MIM; 228550; phenotype.
DR MIM; 601626; phenotype.
DR MIM; 601812; phenotype.
DR MIM; 607785; phenotype.
DR MIM; 615007; phenotype.
DR MIM; 616592; phenotype.
DR neXtProt; NX_P09619; -.
DR OpenTargets; ENSG00000113721; -.
DR Orphanet; 363665; Acroosteolysis-keloid-like lesions-premature aging syndrome.
DR Orphanet; 1980; Bilateral striopallidodentate calcinosis.
DR Orphanet; 98823; Chronic myelomonocytic leukemia.
DR Orphanet; 86830; Chronic myeloproliferative disease, unclassifiable.
DR Orphanet; 2591; Infantile myofibromatosis.
DR Orphanet; 477831; Kosaki overgrowth syndrome.
DR Orphanet; 168950; Myeloid/lymphoid neoplasm associated with PDGFRB rearrangement.
DR Orphanet; 314950; Primary hypereosinophilic syndrome.
DR PharmGKB; PA33148; -.
DR VEuPathDB; HostDB:ENSG00000113721; -.
DR eggNOG; KOG0200; Eukaryota.
DR GeneTree; ENSGT00940000157138; -.
DR HOGENOM; CLU_000288_49_0_1; -.
DR InParanoid; P09619; -.
DR OMA; PQPGCQE; -.
DR OrthoDB; 269253at2759; -.
DR PhylomeDB; P09619; -.
DR TreeFam; TF325768; -.
DR BRENDA; 2.7.10.1; 2681.
DR PathwayCommons; P09619; -.
DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-HSA-186763; Downstream signal transduction.
DR Reactome; R-HSA-186797; Signaling by PDGF.
DR Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR SignaLink; P09619; -.
DR SIGNOR; P09619; -.
DR BioGRID-ORCS; 5159; 16 hits in 1107 CRISPR screens.
DR ChiTaRS; PDGFRB; human.
DR EvolutionaryTrace; P09619; -.
DR GeneWiki; PDGFRB; -.
DR GenomeRNAi; 5159; -.
DR Pharos; P09619; Tclin.
DR PRO; PR:P09619; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P09619; protein.
DR Bgee; ENSG00000113721; Expressed in stromal cell of endometrium and 180 other tissues.
DR ExpressionAtlas; P09619; baseline and differential.
DR Genevisible; P09619; HS.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0019838; F:growth factor binding; IBA:GO_Central.
DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IEA:Ensembl.
DR GO; GO:0004992; F:platelet activating factor receptor activity; TAS:ProtInc.
DR GO; GO:0005019; F:platelet-derived growth factor beta-receptor activity; IDA:UniProtKB.
DR GO; GO:0048407; F:platelet-derived growth factor binding; IDA:UniProtKB.
DR GO; GO:0005017; F:platelet-derived growth factor receptor activity; TAS:ProtInc.
DR GO; GO:0005161; F:platelet-derived growth factor receptor binding; IPI:BHF-UCL.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0038085; F:vascular endothelial growth factor binding; IPI:BHF-UCL.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
DR GO; GO:0035909; P:aorta morphogenesis; ISS:BHF-UCL.
DR GO; GO:0055003; P:cardiac myofibril assembly; ISS:UniProtKB.
DR GO; GO:0060326; P:cell chemotaxis; IDA:UniProtKB.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0060981; P:cell migration involved in coronary angiogenesis; ISS:UniProtKB.
DR GO; GO:0035441; P:cell migration involved in vasculogenesis; ISS:UniProtKB.
DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; IEA:Ensembl.
DR GO; GO:0048839; P:inner ear development; IEA:Ensembl.
DR GO; GO:0060437; P:lung growth; IEA:Ensembl.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0072278; P:metanephric comma-shaped body morphogenesis; IEA:Ensembl.
DR GO; GO:0072277; P:metanephric glomerular capillary formation; ISS:UniProtKB.
DR GO; GO:0072262; P:metanephric glomerular mesangial cell proliferation involved in metanephros development; ISS:UniProtKB.
DR GO; GO:0035789; P:metanephric mesenchymal cell migration; IEA:Ensembl.
DR GO; GO:0072075; P:metanephric mesenchyme development; IEA:Ensembl.
DR GO; GO:0072284; P:metanephric S-shaped body morphogenesis; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IMP:UniProtKB.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IMP:UniProtKB.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0035791; P:platelet-derived growth factor receptor-beta signaling pathway; IMP:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0090280; P:positive regulation of calcium ion import; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0038091; P:positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0050921; P:positive regulation of chemotaxis; ISS:UniProtKB.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IEA:Ensembl.
DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; ISS:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:2000491; P:positive regulation of hepatic stellate cell activation; IEA:Ensembl.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:UniProtKB.
DR GO; GO:0035793; P:positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway; ISS:UniProtKB.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISS:UniProtKB.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IDA:UniProtKB.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
DR GO; GO:0010863; P:positive regulation of phospholipase C activity; IDA:UniProtKB.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IDA:UniProtKB.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISS:UniProtKB.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IEA:Ensembl.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IMP:UniProtKB.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:BHF-UCL.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR GO; GO:0034405; P:response to fluid shear stress; IEA:Ensembl.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl.
DR GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR GO; GO:0061298; P:retina vasculature development in camera-type eye; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
DR GO; GO:0071670; P:smooth muscle cell chemotaxis; ISS:BHF-UCL.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027288; PGFRB.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF500948; Beta-PDGF_receptor; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 3.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cell membrane; Chemotaxis;
KW Chromosomal rearrangement; Cytoplasmic vesicle; Developmental protein;
KW Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Kinase; Lysosome; Membrane; Nucleotide-binding;
KW Phosphoprotein; Proto-oncogene; Receptor; Reference proteome; Repeat;
KW Signal; Transferase; Transmembrane; Transmembrane helix;
KW Tyrosine-protein kinase; Ubl conjugation.
FT SIGNAL 1..32
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 33..1106
FT /note="Platelet-derived growth factor receptor beta"
FT /id="PRO_0000016757"
FT TOPO_DOM 33..532
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 533..553
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 554..1106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 33..120
FT /note="Ig-like C2-type 1"
FT DOMAIN 129..210
FT /note="Ig-like C2-type 2"
FT DOMAIN 214..309
FT /note="Ig-like C2-type 3"
FT DOMAIN 331..403
FT /note="Ig-like C2-type 4"
FT DOMAIN 416..524
FT /note="Ig-like C2-type 5"
FT DOMAIN 600..962
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1019..1106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1063
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1080
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 826
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 606..614
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 634
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT SITE 527..528
FT /note="Breakpoint for insertion to form PDE4DIP-PDGFRB
FT fusion protein"
FT SITE 527..528
FT /note="Breakpoint for translocation to form TRIP11-PDGFRB"
FT SITE 558..559
FT /note="Breakpoint for translocation to form the CEP85L-
FT PDGFRB fusion protein"
FT MOD_RES 562
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:10821867"
FT MOD_RES 579
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:14966296,
FT ECO:0000269|PubMed:15902258, ECO:0000269|PubMed:7685273"
FT MOD_RES 581
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:15902258,
FT ECO:0000269|PubMed:7685273"
FT MOD_RES 686
FT /note="Phosphotyrosine; by ABL1 and ABL2"
FT /evidence="ECO:0000250|UniProtKB:P05622"
FT MOD_RES 716
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:15902258"
FT MOD_RES 740
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:1314164,
FT ECO:0000269|PubMed:15902258"
FT MOD_RES 751
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:10821867,
FT ECO:0000269|PubMed:1314164, ECO:0000269|PubMed:14966296,
FT ECO:0000269|PubMed:1709159, ECO:0000269|PubMed:2550144"
FT MOD_RES 763
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:10821867"
FT MOD_RES 771
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:10821867,
FT ECO:0000269|PubMed:1314164, ECO:0000269|PubMed:14966296,
FT ECO:0000269|PubMed:15902258"
FT MOD_RES 775
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:10821867"
FT MOD_RES 778
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:10821867"
FT MOD_RES 857
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:10821867,
FT ECO:0000269|PubMed:1314164, ECO:0000269|PubMed:15902258,
FT ECO:0000269|PubMed:1709159, ECO:0000269|PubMed:2550144"
FT MOD_RES 934
FT /note="Phosphotyrosine; by ABL1 and ABL2"
FT /evidence="ECO:0000250|UniProtKB:P05622"
FT MOD_RES 970
FT /note="Phosphotyrosine; by ABL1 and ABL2"
FT /evidence="ECO:0000250|UniProtKB:P05622"
FT MOD_RES 1009
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:10821867,
FT ECO:0000269|PubMed:1396585, ECO:0000269|PubMed:15902258"
FT MOD_RES 1021
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:10821867,
FT ECO:0000269|PubMed:1396585, ECO:0000269|PubMed:14966296,
FT ECO:0000269|PubMed:15902258"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20534510"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20534510"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20534510"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20534510"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20534510"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20534510"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:20534510"
FT DISULFID 149..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:20534510"
FT DISULFID 235..291
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:20534510"
FT DISULFID 436..508
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 311..336
FT /note="VESGYVRLLGEVGTLQFAELHRSRTL -> RAATCGSWERWAHYNLLSCIGA
FT GHCR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:18593464"
FT /id="VSP_056008"
FT VAR_SEQ 337..1106
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:18593464"
FT /id="VSP_056009"
FT VARIANT 29
FT /note="I -> F (in dbSNP:rs17110944)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_034377"
FT VARIANT 180
FT /note="S -> F (in dbSNP:rs17853027)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_035125"
FT VARIANT 282
FT /note="E -> K (in dbSNP:rs34586048)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042027"
FT VARIANT 345
FT /note="P -> S (in dbSNP:rs2229558)"
FT /id="VAR_049717"
FT VARIANT 485
FT /note="E -> K (in dbSNP:rs41287110)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042028"
FT VARIANT 561
FT /note="R -> C (in IMF1; dbSNP:rs367543286)"
FT /evidence="ECO:0000269|PubMed:23731537"
FT /id="VAR_069925"
FT VARIANT 584
FT /note="P -> R (in KOGS; dbSNP:rs863224946)"
FT /evidence="ECO:0000269|PubMed:25454926"
FT /id="VAR_075865"
FT VARIANT 589
FT /note="Y -> H (in a gastric adenocarcinoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042029"
FT VARIANT 658
FT /note="L -> P (in IBGC4; no effect on protein abundance;
FT loss of PDGF beta receptor activity; dbSNP:rs397509381)"
FT /evidence="ECO:0000269|PubMed:23255827,
FT ECO:0000269|PubMed:24065723, ECO:0000269|PubMed:26599395"
FT /id="VAR_069320"
FT VARIANT 660
FT /note="P -> T (in IMF1; dbSNP:rs144050370)"
FT /evidence="ECO:0000269|PubMed:23731542"
FT /id="VAR_069926"
FT VARIANT 665
FT /note="V -> A (in PENTT; gain of function in protein
FT tyrosine kinase activity; shows ligand-independent
FT constitutive signaling; dbSNP:rs1554108211)"
FT /evidence="ECO:0000269|PubMed:26279204"
FT /id="VAR_075866"
FT VARIANT 718
FT /note="N -> Y (in dbSNP:rs35322465)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042030"
FT VARIANT 882
FT /note="T -> I (in a breast infiltrating ductal carcinoma
FT sample; somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042031"
FT VARIANT 987
FT /note="R -> W (in IBGC4; decreased protein abundance; no
FT effect on receptor activity; decreased PDGF signaling
FT pathway; dbSNP:rs397509382)"
FT /evidence="ECO:0000269|PubMed:23255827,
FT ECO:0000269|PubMed:24065723, ECO:0000269|PubMed:26599395"
FT /id="VAR_069321"
FT VARIANT 1071
FT /note="E -> V (in IBGC4; no effect on protein abundance; no
FT effect on receptor activity; decreased PDGF signaling
FT pathway)"
FT /evidence="ECO:0000269|PubMed:24065723,
FT ECO:0000269|PubMed:26599395"
FT /id="VAR_075395"
FT MUTAGEN 579
FT /note="Y->F: Loss of kinase activity; when associated with
FT F-581. Strongly reduces interaction with SRC family
FT kinases. No effect on interaction with GRB10."
FT /evidence="ECO:0000269|PubMed:10454568,
FT ECO:0000269|PubMed:7685273"
FT MUTAGEN 581
FT /note="Y->F: Loss of kinase activity; when associated with
FT F-579. No effect on interaction with GRB10."
FT /evidence="ECO:0000269|PubMed:10454568,
FT ECO:0000269|PubMed:7685273"
FT MUTAGEN 634
FT /note="K->A,R: Loss of kinase activity. Abolishes
FT interaction with RASA1. No effect on phosphatidylinositol
FT 3-kinase activity."
FT /evidence="ECO:0000269|PubMed:1314164,
FT ECO:0000269|PubMed:1846866, ECO:0000269|PubMed:20494825"
FT MUTAGEN 716
FT /note="Y->F: No effect neither on interaction with GRB10
FT and RASA1 nor on phosphatidylinositol 3-kinase activity."
FT /evidence="ECO:0000269|PubMed:10454568,
FT ECO:0000269|PubMed:1314164"
FT MUTAGEN 740
FT /note="Y->F: Strongly reduces up-regulation of cell
FT proliferation; when associated with F-751. Strongly
FT decreases phosphatidylinositol 3-kinase activity. No effect
FT on interaction with GRB10 and RASA1."
FT /evidence="ECO:0000269|PubMed:10454568,
FT ECO:0000269|PubMed:1314164, ECO:0000269|PubMed:1375321,
FT ECO:0000269|PubMed:21679854"
FT MUTAGEN 751
FT /note="Y->F: Strongly reduces up-regulation of cell
FT proliferation; when associated with F-740. Abolishes
FT phosphatidylinositol 3-kinase activity and interaction with
FT NCK1, and slightly reduces interaction with RASA1. No
FT effect on interaction with GRB10."
FT /evidence="ECO:0000269|PubMed:10454568,
FT ECO:0000269|PubMed:1314164, ECO:0000269|PubMed:1375321,
FT ECO:0000269|PubMed:1653029, ECO:0000269|PubMed:21679854,
FT ECO:0000269|PubMed:7692233"
FT MUTAGEN 763
FT /note="Y->F: No effect on interaction with RASA1 and on
FT phosphatidylinositol 3-kinase activity."
FT /evidence="ECO:0000269|PubMed:1314164"
FT MUTAGEN 771
FT /note="Y->F: Loss of interaction with GRB10. Abolishes
FT interaction with RASA1. No effect on phosphatidylinositol
FT 3-kinase activity."
FT /evidence="ECO:0000269|PubMed:10454568,
FT ECO:0000269|PubMed:1314164, ECO:0000269|PubMed:1375321"
FT MUTAGEN 775
FT /note="Y->F: No effect on interaction with RASA1 and on
FT phosphatidylinositol 3-kinase activity."
FT /evidence="ECO:0000269|PubMed:1314164"
FT MUTAGEN 778
FT /note="Y->F: Strongly reduces expression levels."
FT /evidence="ECO:0000269|PubMed:1314164"
FT MUTAGEN 857
FT /note="Y->F: Reduces kinase activity. No effect on
FT interaction with GRB10. Abolishes interaction with RASA1.
FT No effect on phosphatidylinositol 3-kinase activity."
FT /evidence="ECO:0000269|PubMed:10454568,
FT ECO:0000269|PubMed:1314164, ECO:0000269|PubMed:1653029,
FT ECO:0000269|PubMed:20494825"
FT MUTAGEN 1009
FT /note="Y->F: No effect on interaction with GRB10. Abolishes
FT interaction with PLCG1; when associated with F-1021."
FT /evidence="ECO:0000269|PubMed:10454568,
FT ECO:0000269|PubMed:1396585, ECO:0000269|PubMed:7691811"
FT MUTAGEN 1021
FT /note="Y->F: Strongly reduces up-regulation of cell
FT proliferation. Abolishes interaction with PLCG1; when
FT associated with F-1009. No effect on interaction with
FT GRB10."
FT /evidence="ECO:0000269|PubMed:10454568,
FT ECO:0000269|PubMed:1396585, ECO:0000269|PubMed:17620338,
FT ECO:0000269|PubMed:21679854"
FT CONFLICT 241
FT /note="E -> D (in Ref. 2; AAA36427)"
FT /evidence="ECO:0000305"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:3MJG"
FT STRAND 50..58
FT /evidence="ECO:0007829|PDB:3MJG"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:3MJG"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:3MJG"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:3MJG"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:3MJG"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:3MJG"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:3MJG"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:3MJG"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:3MJG"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:3MJG"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:3MJG"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:3MJG"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:3MJG"
FT STRAND 185..194
FT /evidence="ECO:0007829|PDB:3MJG"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:3MJG"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:3MJG"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:3MJG"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:3MJG"
FT STRAND 231..239
FT /evidence="ECO:0007829|PDB:3MJG"
FT STRAND 241..248
FT /evidence="ECO:0007829|PDB:3MJG"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:3MJG"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:3MJG"
FT TURN 267..270
FT /evidence="ECO:0007829|PDB:3MJG"
FT STRAND 271..280
FT /evidence="ECO:0007829|PDB:3MJG"
FT STRAND 287..295
FT /evidence="ECO:0007829|PDB:3MJG"
FT TURN 296..299
FT /evidence="ECO:0007829|PDB:3MJG"
FT STRAND 300..311
FT /evidence="ECO:0007829|PDB:3MJG"
FT HELIX 530..556
FT /evidence="ECO:0007829|PDB:2L6W"
SQ 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
