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 27-MAR-2024, entry version 261. 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 NHERF1, RP AND INTERACTION WITH NHERF1. 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 a 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 NHERF1. 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; O14745: NHERF1; NbExp=5; IntAct=EBI-641237, EBI-349787; CC P09619; P01127: PDGFB; NbExp=16; IntAct=EBI-641237, EBI-1554925; CC P09619; P27986: PIK3R1; NbExp=20; IntAct=EBI-641237, EBI-79464; CC P09619; P19174: PLCG1; NbExp=7; 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; 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="https://atlasgeneticsoncology.org/gene/21/PDGFRB"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-6426; -. DR SMR; P09619; -. DR BioGRID; 111185; 205. 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; 284. 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 GlyCosmos; P09619; 11 sites, 4 glycans. 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 CPTAC; CPTAC-3063; -. DR EPD; P09619; -. DR jPOST; P09619; -. DR MassIVE; P09619; -. DR MaxQB; P09619; -. DR PaxDb; 9606-ENSP00000261799; -. DR PeptideAtlas; P09619; -. DR ProteomicsDB; 52253; -. [P09619-1] DR Pumba; P09619; -. DR ABCD; P09619; 4 sequenced antibodies. DR Antibodypedia; 3424; 2490 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 AGR; HGNC:8804; -. 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; VHKSRTI; -. DR OrthoDB; 1614410at2759; -. 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; 18 hits in 1194 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 182 other cell types or tissues. DR ExpressionAtlas; P09619; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB. 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:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. 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; IDA:UniProtKB. 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: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:0004672; F:protein kinase activity; IDA:UniProtKB. 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:0038085; F:vascular endothelial growth factor binding; IPI:BHF-UCL. 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: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: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:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB. DR GO; GO:0046488; P:phosphatidylinositol metabolic process; 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:0090280; P:positive regulation of calcium ion import; ISS:UniProtKB. DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IMP: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: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: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:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IDA: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: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: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 CDD; cd00096; Ig; 1. DR CDD; cd05859; Ig4_PDGFR; 1. DR CDD; cd05861; IgI_PDGFR-alphabeta; 1. DR CDD; cd05107; PTKc_PDGFR_beta; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 5. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. 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 PANTHER; PTHR24416:SF53; PLATELET-DERIVED GROWTH FACTOR RECEPTOR BETA; 1. DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1. DR Pfam; PF00047; ig; 1. DR Pfam; PF13927; Ig_3; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR PIRSF; PIRSF500948; Beta-PDGF_receptor; 1. DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 1. DR PRINTS; PR01832; VEGFRECEPTOR. DR SMART; SM00409; IG; 3. DR SMART; SM00408; IGc2; 3. DR SMART; SM00219; TyrKc; 1. DR SUPFAM; SSF48726; Immunoglobulin; 3. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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. DR Genevisible; P09619; HS. 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 //