ID PGFRA_HUMAN Reviewed; 1089 AA. AC P16234; B2RE69; E9PBH0; Q6P4H5; Q96KZ7; Q9UD28; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 27-MAR-2024, entry version 245. DE RecName: Full=Platelet-derived growth factor receptor alpha; DE Short=PDGF-R-alpha; DE Short=PDGFR-alpha; DE EC=2.7.10.1; DE AltName: Full=Alpha platelet-derived growth factor receptor; DE AltName: Full=Alpha-type platelet-derived growth factor receptor; DE AltName: Full=CD140 antigen-like family member A; DE AltName: Full=CD140a antigen; DE AltName: Full=Platelet-derived growth factor alpha receptor; DE AltName: Full=Platelet-derived growth factor receptor 2; DE Short=PDGFR-2; DE AltName: CD_antigen=CD140a; DE Flags: Precursor; GN Name=PDGFRA; Synonyms=PDGFR2, RHEPDGFRA; 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), AND INTERACTION WITH PDGFA AND RP PDGFB. RC TISSUE=Foreskin; RX PubMed=2544881; DOI=10.1073/pnas.86.13.4917; RA Claesson-Welsh L., Eriksson A., Westermark B., Heldin C.H.; RT "cDNA cloning and expression of the human A-type platelet-derived growth RT factor (PDGF) receptor establishes structural similarity to the B-type PDGF RT receptor."; RL Proc. Natl. Acad. Sci. U.S.A. 86:4917-4921(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AUTOPHOSPHORYLATION, TISSUE RP SPECIFICITY, AND INTERACTION WITH PDGFA AND PDGFB. RC TISSUE=Brain; RX PubMed=2536956; DOI=10.1126/science.2536956; RA Matsui T., Heidaran M., Miki T., Popescu N., la Rochelle W., Kraus M., RA Pierce J., Aaronson S.; RT "Isolation of a novel receptor cDNA establishes the existence of two PDGF RT receptor genes."; RL Science 243:800-804(1989). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Blood; RX PubMed=8586421; DOI=10.1006/geno.1995.9883; RA Kawagishi J., Ku T.; RT "Structure, organization, and transcription units of the human alpha- RT platelet-derived growth factor receptor gene, PDGFRA."; RL Genomics 30:224-232(1995). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PRO-478. RC TISSUE=Lung, and Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT RP PRO-478. RC TISSUE=Placenta; 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 [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 579-1089, DISEASE, AND IDENTIFICATION BY MASS RP SPECTROMETRY OF FIP1L1-PDGFRA FUSION PROTEIN. RC TISSUE=Eosinophil; RX PubMed=12808148; DOI=10.1073/pnas.0932698100; RA Griffin J.H., Leung J., Bruner R.J., Caligiuri M.A., Briesewitz R.; RT "Discovery of a fusion kinase in EOL-1 cells and idiopathic RT hypereosinophilic syndrome."; RL Proc. Natl. Acad. Sci. U.S.A. 100:7830-7835(2003). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 823-876, AND TISSUE SPECIFICITY. RC TISSUE=Colon tumor; RX PubMed=7896447; DOI=10.1002/ijc.2910600611; RA Craven R.J., Xu L.H., Weiner T.M., Fridell Y.-W., Dent G.A., Srivastava S., RA Varnum B., Liu E.T., Cance W.G.; RT "Receptor tyrosine kinases expressed in metastatic colon cancer."; RL Int. J. Cancer 60:791-797(1995). RN [9] RP FUNCTION AS PDGFA AND PDGFB RECEPTOR IN CELL PROLIFERATION AND CHEMOTAXIS, RP AND 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 [10] RP INTERACTION WITH PLCG1 AND SRC. RX PubMed=2173144; DOI=10.1126/science.2173144; RA Anderson D., Koch C.A., Grey L., Ellis C., Moran M.F., Pawson T.; RT "Binding of SH2 domains of phospholipase C gamma 1, GAP, and Src to RT activated growth factor receptors."; RL Science 250:979-982(1990). RN [11] RP INTERACTION WITH PDGFRA; PDGFA AND PDGFB, FUNCTION AS RECEPTOR FOR PDGFA RP AND PDGFB, AND AUTOPHOSPHORYLATION. 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 [12] RP FUNCTION AS PDGFB RECEPTOR IN CHEMOTAXIS; CELL PROLIFERATION; RP PHOSPHORYLATION OF PLCG1; ACTIVATION OF PHOSPHATIDYLINOSITOL 3-KINASE AND RP REGULATION OF PHOSPHATIDYLINOSITOL METABOLISM, INTERACTION WITH PIK3R, RP PHOSPHORYLATION AT TYR-731 AND TYR-742, AND MUTAGENESIS OF TYR-731 AND RP TYR-742. RX PubMed=1646396; DOI=10.1128/mcb.11.7.3780-3785.1991; RA Yu J.C., Heidaran M.A., Pierce J.H., Gutkind J.S., Lombardi D., RA Ruggiero M., Aaronson S.A.; RT "Tyrosine mutations within the alpha platelet-derived growth factor RT receptor kinase insert domain abrogate receptor-associated RT phosphatidylinositol-3 kinase activity without affecting mitogenic or RT chemotactic signal transduction."; RL Mol. Cell. Biol. 11:3780-3785(1991). RN [13] RP INTERACTION WITH PDGFA 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 [14] RP FUNCTION AS PDGFA RECEPTOR IN REGULATION OF PLATELET ACTIVATION, RP SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, AND TISSUE SPECIFICITY. RX PubMed=8188664; DOI=10.1016/s0021-9258(17)36728-5; RA Vassbotn F.S., Havnen O.K., Heldin C.H., Holmsen H.; RT "Negative feedback regulation of human platelets via autocrine activation RT of the platelet-derived growth factor alpha-receptor."; RL J. Biol. Chem. 269:13874-13879(1994). RN [15] RP PHOSPHORYLATION AT TYR-988 AND TYR-1018, AND INTERACTION WITH PLCG1. RX PubMed=7535778; DOI=10.1074/jbc.270.13.7773; RA Eriksson A., Naanberg E., Roennstrand L., Engstroem U., Hellman U., RA Rupp E., Carpenter G., Heldin C.H., Claesson-Welsh L.; RT "Demonstration of functionally different interactions between phospholipase RT C-gamma and the two types of platelet-derived growth factor receptors."; RL J. Biol. Chem. 270:7773-7781(1995). RN [16] RP FUNCTION IN PROMOTING CHEMOTAXIS. RX PubMed=8760137; DOI=10.1152/ajplung.1996.271.1.l93; RA Osornio-Vargas A.R., Lindroos P.M., Coin P.G., Badgett A., RA Hernandez-Rodriguez N.A., Bonner J.C.; RT "Maximal PDGF-induced lung fibroblast chemotaxis requires PDGF receptor- RT alpha."; RL Am. J. Physiol. 271:L93-L99(1996). RN [17] RP PHOSPHORYLATION AT TYR-768. RX PubMed=8617789; DOI=10.1074/jbc.271.9.5101; RA Yokote K., Mori S., Siegbahn A., Ronnstrand L., Wernstedt C., Heldin C.H., RA Claesson-Welsh L.; RT "Structural determinants in the platelet-derived growth factor alpha- RT receptor implicated in modulation of chemotaxis."; RL J. Biol. Chem. 271:5101-5111(1996). RN [18] RP INTERACTION WITH GRB7 AND PIK3R1. 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 [19] RP FUNCTION IN PHOSPHORYLATION OF PTPN11; ACTIVATION OF HRAS AND REGULATION OF RP CELL PROLIFERATION, PHOSPHORYLATION AT TYR-720, INTERACTION WITH GRB2; RP PTPN11; PLCG1 AND PIK3R1, AUTOPHOSPHORYLATION, AND MUTAGENESIS OF TYR-720. RX PubMed=8943348; DOI=10.1128/mcb.16.12.6926; RA Bazenet C.E., Gelderloos J.A., Kazlauskas A.; RT "Phosphorylation of tyrosine 720 in the platelet-derived growth factor RT alpha receptor is required for binding of Grb2 and SHP-2 but not for RT activation of Ras or cell proliferation."; RL Mol. Cell. Biol. 16:6926-6936(1996). RN [20] RP INTERACTION WITH CRK, PHOSPHORYLATION AT TYR-762, AND MUTAGENESIS OF RP TYR-762. RX PubMed=10733900; DOI=10.1006/bbrc.2000.2374; RA Matsumoto T., Yokote K., Take A., Takemoto M., Asaumi S., Hashimoto Y., RA Matsuda M., Saito Y., Mori S.; RT "Differential interaction of CrkII adaptor protein with platelet-derived RT growth factor alpha- and beta-receptors is determined by its internal RT tyrosine phosphorylation."; RL Biochem. Biophys. Res. Commun. 270:28-33(2000). RN [21] RP INTERACTION WITH SHF, AND PHOSPHORYLATION AT TYR-720. RX PubMed=11095946; DOI=10.1006/bbrc.2000.3847; RA Lindholm C.K., Frantz J.D., Shoelson S.E., Welsh M.; RT "Shf, a Shb-like adapter protein, is involved in PDGF-alpha-receptor RT regulation of apoptosis."; RL Biochem. Biophys. Res. Commun. 278:537-543(2000). RN [22] RP FUNCTION IN PLATELET ACTIVATION. RX PubMed=10947961; DOI=10.1042/bj3500469; RA Selheim F., Fukami M.H., Holmsen H., Vassbotn F.S.; RT "Platelet-derived-growth-factor-induced signalling in human platelets: RT phosphoinositide-3-kinase-dependent inhibition of platelet activation."; RL Biochem. J. 350:469-475(2000). RN [23] RP FUNCTION IN ACTIVATION OF MAPK1/ERK2 AND/OR MAPK3/ERK1, DEGRADATION, RP PHOSPHORYLATION AT TYR-572 AND TYR-574, AND MUTAGENESIS OF TYR-572 AND RP TYR-574. RX PubMed=10734113; DOI=10.1074/jbc.275.13.9620; RA Rosenkranz S., Ikuno Y., Leong F.L., Klinghoffer R.A., Miyake S., Band H., RA Kazlauskas A.; RT "Src family kinases negatively regulate platelet-derived growth factor RT alpha receptor-dependent signaling and disease progression."; RL J. Biol. Chem. 275:9620-9627(2000). RN [24] 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 [25] RP SUBCELLULAR LOCATION, INTERACTION WITH SRC, AND MUTAGENESIS OF TYR-572 AND RP TYR-574. RX PubMed=14644164; DOI=10.1016/j.yexcr.2003.08.001; RA Avrov K., Kazlauskas A.; RT "The role of c-Src in platelet-derived growth factor alpha receptor RT internalization."; RL Exp. Cell Res. 291:426-434(2003). RN [26] RP INVOLVEMENT IN HES. RX PubMed=12660384; DOI=10.1056/nejmoa025217; RA Cools J., DeAngelo D.J., Gotlib J., Stover E.H., Legare R.D., Cortes J., RA Kutok J., Clark J., Galinsky I., Griffin J.D., Cross N.C., Tefferi A., RA Malone J., Alam R., Schrier S.L., Schmid J., Rose M., Vandenberghe P., RA Verhoef G., Boogaerts M., Wlodarska I., Kantarjian H., Marynen P., RA Coutre S.E., Stone R., Gilliland D.G.; RT "A tyrosine kinase created by fusion of the PDGFRA and FIP1L1 genes as a RT therapeutic target of imatinib in idiopathic hypereosinophilic syndrome."; RL N. Engl. J. Med. 348:1201-1214(2003). RN [27] RP FUNCTION IN PHOSPHORYLATION OF AKT1; MAP KINASES; STAT1 AND STAT3, RP INVOLVEMENT IN GIST, VARIANTS ASP-561; VAL-842; 842-ASP--HIS-845 DEL AND RP 845-HIS--PRO-448 DEL, AND CHARACTERIZATION OF VARIANTS ASP-561; VAL-842; RP 842-ASP--HIS-845 DEL AND 845-HIS--PRO-448 DEL. RX PubMed=12522257; DOI=10.1126/science.1079666; RA Heinrich M.C., Corless C.L., Duensing A., McGreevey L., Chen C.J., RA Joseph N., Singer S., Griffith D.J., Haley A., Town A., Demetri G.D., RA Fletcher C.D., Fletcher J.A.; RT "PDGFRA activating mutations in gastrointestinal stromal tumors."; RL Science 299:708-710(2003). RN [28] RP INVOLVEMENT IN GIST, VARIANTS ASP-561; LYS-659; TYR-842; VAL-842; RP 842-ASP--HIS-845 DEL; 845-HIS--PRO-448 DEL AND CYS-849, CHARACTERIZATION OF RP VARIANTS ASP-561; LYS-659; TYR-842; VAL-842; 842-ASP--HIS-845 DEL; RP 845-HIS--PRO-448 DEL AND CYS-849, AND ACTIVITY REGULATION. RX PubMed=15928335; DOI=10.1200/jco.2005.14.068; RA Corless C.L., Schroeder A., Griffith D., Town A., McGreevey L., Harrell P., RA Shiraga S., Bainbridge T., Morich J., Heinrich M.C.; RT "PDGFRA mutations in gastrointestinal stromal tumors: frequency, spectrum RT and in vitro sensitivity to imatinib."; RL J. Clin. Oncol. 23:5357-5364(2005). RN [29] RP FUNCTION IN CELL SURVIVAL. RX PubMed=17141222; DOI=10.1016/j.febslet.2006.11.034; RA Vantler M., Huntgeburth M., Caglayan E., Ten Freyhaus H., Schnabel P., RA Rosenkranz S.; RT "PI3-kinase/Akt-dependent antiapoptotic signaling by the PDGF alpha RT receptor is negatively regulated by Src family kinases."; RL FEBS Lett. 580:6769-6776(2006). RN [30] RP PHOSPHORYLATION AT TYR-754. RX PubMed=17604334; DOI=10.1158/1535-7163.mct-06-0720; RA Stock P., Monga D., Tan X., Micsenyi A., Loizos N., Monga S.P.; RT "Platelet-derived growth factor receptor-alpha: a novel therapeutic target RT in human hepatocellular cancer."; RL Mol. Cancer Ther. 6:1932-1941(2007). RN [31] RP INTERACTION WITH HHV-5 GB (MICROBIAL INFECTION). RX PubMed=20660204; DOI=10.1128/jvi.00710-10; RA Feire A.L., Roy R.M., Manley K., Compton T.; RT "The glycoprotein B disintegrin-like domain binds beta 1 integrin to RT mediate cytomegalovirus entry."; RL J. Virol. 84:10026-10037(2010). RN [32] RP FUNCTION IN PHOSPHORYLATION OF STAT 5A AND/OR STAT5B, ROLE IN RP HYPEREOSINOPHILIC SYNDROME, VARIANTS GLY-481; PRO-507; MET-562; ARG-570; RP GLN-650; SER-659; PRO-705; GLY-748 AND SER-849, CHARACTERIZATION OF RP VARIANTS GLY-481; PRO-507; MET-562; ARG-570; GLN-650; SER-659; PRO-705; RP GLY-748 AND SER-849, AND ACTIVITY REGULATION. RX PubMed=21224473; DOI=10.1182/blood-2010-05-286757; RA Elling C., Erben P., Walz C., Frickenhaus M., Schemionek M., Stehling M., RA Serve H., Cross N.C., Hochhaus A., Hofmann W.K., Berdel W.E., RA Muller-Tidow C., Reiter A., Koschmieder S.; RT "Novel imatinib-sensitive PDGFRA-activating point mutations in RT hypereosinophilic syndrome induce growth factor independence and leukemia- RT like disease."; RL Blood 117:2935-2943(2011). RN [33] RP FUNCTION IN CELL DIFFERENTIATION, AND UBIQUITINATION. RX PubMed=21596750; DOI=10.1074/jbc.m110.197525; RA Severe N., Miraoui H., Marie P.J.; RT "The Casitas B lineage lymphoma (Cbl) mutant G306E enhances osteogenic RT differentiation in human mesenchymal stromal cells in part by decreased RT Cbl-mediated platelet-derived growth factor receptor alpha and fibroblast RT growth factor receptor 2 ubiquitination."; RL J. Biol. Chem. 286:24443-24450(2011). RN [34] RP ROLE IN DISEASE, CHARACTERIZATION OF VARIANT VAL-842, AND ACTIVITY RP REGULATION. RX PubMed=20972453; DOI=10.1038/onc.2010.476; RA von Bubnoff N., Gorantla S.P., Engh R.A., Oliveira T.M., Thone S., RA Aberg E., Peschel C., Duyster J.; RT "The low frequency of clinical resistance to PDGFR inhibitors in myeloid RT neoplasms with abnormalities of PDGFRA might be related to the limited RT repertoire of possible PDGFRA kinase domain mutations in vitro."; RL Oncogene 30:933-943(2011). RN [35] 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 [36] RP REVIEW ON ROLE IN DISEASE AND ACTIVITY REGULATION. 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 [37] RP REVIEW ON ROLE IN DISEASE AND ACTIVITY REGULATION. 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 [38] RP REVIEW ON FUNCTION IN DEVELOPMENT AND DISEASE; LIGANDS AND SIGNALING RP 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 [39] RP INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEINS GH; GL AND GO (MICROBIAL RP INFECTION). RX PubMed=28403202; DOI=10.1371/journal.ppat.1006281; RA Wu Y., Prager A., Boos S., Resch M., Brizic I., Mach M., Wildner S., RA Scrivano L., Adler B.; RT "Human cytomegalovirus glycoprotein complex gH/gL/gO uses PDGFR-alpha as a RT key for entry."; RL PLoS Pathog. 13:E1006281-E1006281(2017). RN [40] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1185-1189 IN COMPLEX WITH NHERF1 RP AND PDGFRB. 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 [41] {ECO:0007744|PDB:7LBF} RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) OF 1-524, AND INTERACTION RP WITH HUMAN CYTOMEGALOVIRUS PROTEINS GH; GL AND GO (MICROBIAL INFECTION). RX PubMed=33626330; DOI=10.1016/j.cell.2021.01.036; RA Kschonsak M., Rouge L., Arthur C.P., Hoangdung H., Patel N., Kim I., RA Johnson M.C., Kraft E., Rohou A.L., Gill A., Martinez-Martin N., RA Payandeh J., Ciferri C.; RT "Structures of HCMV Trimer reveal the basis for receptor recognition and RT cell entry."; RL Cell 184:1232-1244(2021). RN [42] RP INVOLVEMENT IN GISTPS, AND VARIANT GISTPS TYR-846. RX PubMed=14699510; DOI=10.1053/j.gastro.2003.10.079; RA Chompret A., Kannengiesser C., Barrois M., Terrier P., Dahan P., Tursz T., RA Lenoir G.M., Bressac-De Paillerets B.; RT "PDGFRA germline mutation in a family with multiple cases of RT gastrointestinal stromal tumor."; RL Gastroenterology 126:318-321(2004). RN [43] RP VARIANT GISTPS CYS-555, CHARACTERIZATION OF VARIANT GISTPS CYS-555, AND RP FUNCTION. RX PubMed=17087943; DOI=10.1053/j.gastro.2006.07.002; RA de Raedt T., Cools J., Debiec-Rychter M., Brems H., Mentens N., Sciot R., RA Himpens J., de Wever I., Schoeffski P., Marynen P., Legius E.; RT "Intestinal neurofibromatosis is a subtype of familial GIST and results RT from a dominant activating mutation in PDGFRA."; RL Gastroenterology 131:1907-1912(2006). RN [44] RP VARIANTS [LARGE SCALE ANALYSIS] ASP-79; ASP-426; PRO-478; CYS-764; ARG-829; RP LYS-996 AND ASN-1071. 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 [45] RP VARIANT GISTPS LEU-653. RX PubMed=25975287; DOI=10.1038/modpathol.2015.56; RA Ricci R., Martini M., Cenci T., Carbone A., Lanza P., Biondi A., Rindi G., RA Cassano A., Larghi A., Persiani R., Larocca L.M.; RT "PDGFRA-mutant syndrome."; RL Mod. Pathol. 28:954-964(2015). CC -!- FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor CC for PDGFA, PDGFB and PDGFC and plays an essential role in the CC regulation of embryonic development, cell proliferation, survival and CC chemotaxis. Depending on the context, promotes or inhibits cell CC proliferation and cell migration. Plays an important role in the CC differentiation of bone marrow-derived mesenchymal stem cells. Required CC for normal skeleton development and cephalic closure during embryonic CC development. Required for normal development of the mucosa lining the CC gastrointestinal tract, and for recruitment of mesenchymal cells and CC normal development of intestinal villi. Plays a role in cell migration CC and chemotaxis in wound healing. Plays a role in platelet activation, CC secretion of agonists from platelet granules, and in thrombin-induced CC platelet aggregation. Binding of its cognate ligands - homodimeric CC PDGFA, homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or CC homodimeric PDGFC -leads to the activation of several signaling CC cascades; the response depends on the nature of the bound ligand and is CC modulated by the formation of heterodimers between PDGFRA and PDGFRB. CC Phosphorylates PIK3R1, PLCG1, and PTPN11. Activation of PLCG1 leads to CC the 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. Phosphorylates PIK3R1, the regulatory CC subunit of phosphatidylinositol 3-kinase, and thereby mediates CC activation of the AKT1 signaling pathway. Mediates activation of HRAS CC and of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes CC activation of STAT family members STAT1, STAT3 and STAT5A and/or CC STAT5B. Receptor signaling is down-regulated by protein phosphatases CC that dephosphorylate the receptor and its down-stream effectors, and by CC rapid internalization of the activated receptor. CC {ECO:0000269|PubMed:10734113, ECO:0000269|PubMed:10947961, CC ECO:0000269|PubMed:11297552, ECO:0000269|PubMed:12522257, CC ECO:0000269|PubMed:1646396, ECO:0000269|PubMed:17087943, CC ECO:0000269|PubMed:1709159, ECO:0000269|PubMed:17141222, CC ECO:0000269|PubMed:20972453, ECO:0000269|PubMed:21224473, CC ECO:0000269|PubMed:21596750, ECO:0000269|PubMed:2554309, CC ECO:0000269|PubMed:8188664, ECO:0000269|PubMed:8760137, CC ECO:0000269|PubMed:8943348}. 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 -!- ACTIVITY REGULATION: Present in an inactive conformation in the absence CC of bound ligand. Binding of PDGFA and/or PDGFB leads to dimerization CC and activation by autophosphorylation on tyrosine residues. Inhibited CC by imatinib, nilotinib and sorafenib. {ECO:0000269|PubMed:15928335, CC ECO:0000269|PubMed:20972453, ECO:0000269|PubMed:21224473}. CC -!- SUBUNIT: Interacts with homodimeric PDGFA, PDGFB and PDGFC, and with CC heterodimers formed by PDGFA and PDGFB. Monomer in the absence of bound CC ligand. Interaction with dimeric PDGFA, PDGFB and/or PDGFC leads to CC receptor dimerization, where both PDGFRA homodimers and heterodimers CC with PDGFRB are observed. Interacts (tyrosine phosphorylated) with SHB CC (via SH2 domain) (By similarity). Interacts (tyrosine phosphorylated) CC with SHF (via SH2 domain). Interacts (tyrosine phosphorylated) with SRC CC (via SH2 domain). Interacts (tyrosine phosphorylated) with PIK3R1. CC Interacts (tyrosine phosphorylated) with PLCG1 (via SH2 domain). CC Interacts (tyrosine phosphorylated) with CRK, GRB2 and GRB7. CC {ECO:0000250, ECO:0000269|PubMed:10733900, ECO:0000269|PubMed:11095946, CC ECO:0000269|PubMed:11297552, ECO:0000269|PubMed:11882663, CC ECO:0000269|PubMed:14644164, ECO:0000269|PubMed:1646396, CC ECO:0000269|PubMed:1709159, ECO:0000269|PubMed:2173144, CC ECO:0000269|PubMed:2536956, ECO:0000269|PubMed:2544881, CC ECO:0000269|PubMed:7535778, ECO:0000269|PubMed:7679113, CC ECO:0000269|PubMed:8940081, ECO:0000269|PubMed:8943348}. CC -!- SUBUNIT: (Microbial infection) Interacts with human CC cytomegalovirus/HHV-5 envelope glycoprotein B/gB. Interacts also with CC the trimeric complex gH-gL-gO. Trimer-PDGFRA interaction has an CC inhibitory effect on PDGFRA signaling (PubMed:33626330). CC {ECO:0000269|PubMed:20660204, ECO:0000269|PubMed:28403202, CC ECO:0000269|PubMed:33626330}. CC -!- INTERACTION: CC P16234; P46108: CRK; NbExp=4; IntAct=EBI-2861522, EBI-886; CC P16234; P46109: CRKL; NbExp=3; IntAct=EBI-2861522, EBI-910; CC P16234; P00533: EGFR; NbExp=4; IntAct=EBI-2861522, EBI-297353; CC P16234; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-2861522, EBI-749265; CC P16234; P04085: PDGFA; NbExp=6; IntAct=EBI-2861522, EBI-2881386; CC P16234; P01127: PDGFB; NbExp=11; IntAct=EBI-2861522, EBI-1554925; CC P16234; Q9NRA1: PDGFC; NbExp=3; IntAct=EBI-2861522, EBI-8833587; CC P16234; P31947: SFN; NbExp=2; IntAct=EBI-2861522, EBI-476295; CC P16234; P62258: YWHAE; NbExp=2; IntAct=EBI-2861522, EBI-356498; CC P16234-1; Q9NRA1-1: PDGFC; NbExp=2; IntAct=EBI-15499330, EBI-15499301; CC P16234-1; A8T7D5: UL55; Xeno; NbExp=2; IntAct=EBI-15499330, EBI-15722055; CC P16234-2; P05067: APP; NbExp=3; IntAct=EBI-13380852, EBI-77613; CC P16234-2; Q8IY26: PLPP6; NbExp=3; IntAct=EBI-13380852, EBI-11721828; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14644164, CC ECO:0000269|PubMed:2554309, ECO:0000269|PubMed:8188664}; Single-pass CC type I membrane protein {ECO:0000269|PubMed:14644164, CC ECO:0000269|PubMed:2554309, ECO:0000269|PubMed:8188664}. Cell CC projection, cilium {ECO:0000250|UniProtKB:P26618}. Golgi apparatus CC {ECO:0000250|UniProtKB:P26618}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P16234-1; Sequence=Displayed; CC Name=2; CC IsoId=P16234-2; Sequence=VSP_007833, VSP_007834; CC Name=3; CC IsoId=P16234-3; Sequence=VSP_042015, VSP_042016; CC -!- TISSUE SPECIFICITY: Detected in platelets (at protein level). Widely CC expressed. Detected in brain, fibroblasts, smooth muscle, heart, and CC embryo. Expressed in primary and metastatic colon tumors and in normal CC colon tissue. {ECO:0000269|PubMed:2536956, ECO:0000269|PubMed:7896447, CC ECO:0000269|PubMed:8188664}. CC -!- PTM: N-glycosylated. CC -!- PTM: Ubiquitinated, leading to its internalization and degradation. CC {ECO:0000305|PubMed:21596750}. 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-731 and Tyr-742 is important for interaction CC with PIK3R1. Phosphorylation at Tyr-720 and Tyr-754 is important for CC interaction with PTPN11. Phosphorylation at Tyr-762 is important for CC interaction with CRK. Phosphorylation at Tyr-572 and Tyr-574 is CC important for interaction with SRC and SRC family members. CC Phosphorylation at Tyr-988 and Tyr-1018 is important for interaction CC with PLCG1. {ECO:0000269|PubMed:10733900, ECO:0000269|PubMed:10734113, CC ECO:0000269|PubMed:11095946, ECO:0000269|PubMed:1646396, CC ECO:0000269|PubMed:7535778, ECO:0000269|PubMed:8943348}. CC -!- DISEASE: Note=A chromosomal aberration involving PDGFRA is found in CC some cases of hypereosinophilic syndrome. Interstitial chromosomal CC deletion del(4)(q12q12) causes the fusion of FIP1L1 and PDGFRA (FIP1L1- CC PDGFRA). Mutations that cause overexpression and/or constitutive CC activation of PDGFRA may be a cause of hypereosinophilic syndrome. CC {ECO:0000269|PubMed:12808148}. CC -!- DISEASE: Gastrointestinal stromal tumor (GIST) [MIM:606764]: Common CC mesenchymal neoplasms arising in the gastrointestinal tract, most often CC in the stomach. They are histologically, immunohistochemically, and CC genetically different from typical leiomyomas, leiomyosarcomas, and CC schwannomas. Most GISTs are composed of a fairly uniform population of CC spindle-shaped cells. Some tumors are dominated by epithelioid cells or CC contain a mixture of spindle and epithelioid morphologies. Primary CC GISTs in the gastrointestinal tract commonly metastasize in the omentum CC and mesenteries, often as multiple nodules. However, primary tumors may CC also occur outside of the gastrointestinal tract, in other intra- CC abdominal locations, especially in the omentum and mesentery. CC {ECO:0000269|PubMed:12522257, ECO:0000269|PubMed:15928335}. Note=The CC gene represented in this entry may be involved in disease pathogenesis. CC Mutations causing PDGFRA constitutive activation have been found in CC gastrointestinal stromal tumors lacking KIT mutations CC (PubMed:12522257). {ECO:0000269|PubMed:12522257}. CC -!- DISEASE: GIST-plus syndrome (GISTPS) [MIM:175510]: A disorder CC characterized by multiple mesenchymal tumors of the gastrointestinal CC tract, including gastrointestinal stromal tumor, inflammatory fibroid CC polyps, and fibroid tumors. Additional features are coarse facies and CC skin, broad hands and feet, and premature tooth loss. GISTPS is an CC autosomal dominant disease with incomplete penetrance. Gastrointestinal CC stromal tumor and inflammatory fibroid polyps may also occur in CC isolation. {ECO:0000269|PubMed:14699510, ECO:0000269|PubMed:17087943, CC ECO:0000269|PubMed:25975287}. Note=The disease is caused by variants CC affecting the gene represented 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 -!- SEQUENCE CAUTION: CC Sequence=AAP69563.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; 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; M22734; AAA60048.1; -; mRNA. DR EMBL; M21574; AAA96715.1; -; mRNA. DR EMBL; D50017; BAA08742.1; -; Genomic_DNA. DR EMBL; AK316578; BAG38166.1; -; mRNA. DR EMBL; AC098587; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC138779; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC015186; AAH15186.1; -; mRNA. DR EMBL; BC063414; AAH63414.1; -; mRNA. DR EMBL; AY229892; AAP69563.1; ALT_INIT; mRNA. DR CCDS; CCDS3495.1; -. [P16234-1] DR PIR; A40162; PFHUGA. DR RefSeq; NP_001334758.1; NM_001347829.1. [P16234-1] DR RefSeq; NP_006197.1; NM_006206.5. [P16234-1] DR RefSeq; XP_005265800.1; XM_005265743.1. [P16234-1] DR PDB; 1GQ5; X-ray; 2.20 A; -. DR PDB; 5GRN; X-ray; 1.77 A; A=550-973. DR PDB; 5K5X; X-ray; 2.17 A; A=550-973. DR PDB; 6A32; X-ray; 1.87 A; A=550-973. DR PDB; 6JOI; X-ray; 3.10 A; A=550-973. DR PDB; 6JOJ; X-ray; 2.60 A; A=550-973. DR PDB; 6JOK; X-ray; 3.80 A; A=550-973. DR PDB; 6JOL; X-ray; 1.90 A; A=550-973. DR PDB; 7LBF; EM; 2.80 A; D=1-524. DR PDB; 7RAM; EM; 3.43 A; D=1-524. DR PDBsum; 1GQ5; -. DR PDBsum; 5GRN; -. DR PDBsum; 5K5X; -. DR PDBsum; 6A32; -. DR PDBsum; 6JOI; -. DR PDBsum; 6JOJ; -. DR PDBsum; 6JOK; -. DR PDBsum; 6JOL; -. DR PDBsum; 7LBF; -. DR PDBsum; 7RAM; -. DR AlphaFoldDB; P16234; -. DR EMDB; EMD-23253; -. DR EMDB; EMD-24369; -. DR EMDB; EMD-27408; -. DR EMDB; EMD-27410; -. DR EMDB; EMD-27411; -. DR EMDB; EMD-27495; -. DR EMDB; EMD-27496; -. DR SMR; P16234; -. DR BioGRID; 111182; 389. DR ComplexPortal; CPX-2881; PDGF receptor alpha - PDGF-AA complex. DR ComplexPortal; CPX-2883; PDGF receptor alpha-beta - PDGF-BB complex. DR ComplexPortal; CPX-2884; PDGF receptor alpha - PDGF-BB complex. DR ComplexPortal; CPX-2885; PDGF receptor alpha - PDGF-AB complex. DR ComplexPortal; CPX-2887; PDGF receptor alpha - PDGF-CC complex. DR ComplexPortal; CPX-2888; PDGF receptor alpha-beta - PDGF-CC complex. DR ComplexPortal; CPX-2890; PDGF receptor alpha-beta - PDGF-DD complex. DR ComplexPortal; CPX-2892; PDGF receptor alpha-beta - PDGF-AB complex. DR CORUM; P16234; -. DR DIP; DIP-5736N; -. DR IntAct; P16234; 125. DR MINT; P16234; -. DR STRING; 9606.ENSP00000257290; -. DR BindingDB; P16234; -. DR ChEMBL; CHEMBL2007; -. DR DrugBank; DB12742; Amuvatinib. DR DrugBank; DB00102; Becaplermin. DR DrugBank; DB12147; Erdafitinib. DR DrugBank; DB10772; Foreskin keratinocyte (neonatal). DR DrugBank; DB12010; Fostamatinib. DR DrugBank; DB00619; Imatinib. DR DrugBank; DB09078; Lenvatinib. DR DrugBank; DB06595; Midostaurin. DR DrugBank; DB09079; Nintedanib. DR DrugBank; DB06043; Olaratumab. DR DrugBank; DB06589; Pazopanib. DR DrugBank; DB08901; Ponatinib. DR DrugBank; DB08896; Regorafenib. DR DrugBank; DB14840; Ripretinib. DR DrugBank; DB01268; Sunitinib. DR DrugBank; DB11800; Tivozanib. DR DrugBank; DB05146; XL820. DR DrugCentral; P16234; -. DR GuidetoPHARMACOLOGY; 1803; -. DR GlyCosmos; P16234; 8 sites, No reported glycans. DR GlyGen; P16234; 8 sites. DR iPTMnet; P16234; -. DR PhosphoSitePlus; P16234; -. DR BioMuta; PDGFRA; -. DR DMDM; 129892; -. DR CPTAC; CPTAC-1767; -. DR CPTAC; CPTAC-3115; -. DR CPTAC; CPTAC-3116; -. DR jPOST; P16234; -. DR MassIVE; P16234; -. DR MaxQB; P16234; -. DR PaxDb; 9606-ENSP00000257290; -. DR PeptideAtlas; P16234; -. DR ProteomicsDB; 53328; -. [P16234-1] DR ProteomicsDB; 53329; -. [P16234-2] DR ProteomicsDB; 53330; -. [P16234-3] DR ABCD; P16234; 32 sequenced antibodies. DR Antibodypedia; 1381; 2547 antibodies from 46 providers. DR DNASU; 5156; -. DR Ensembl; ENST00000257290.10; ENSP00000257290.5; ENSG00000134853.12. [P16234-1] DR Ensembl; ENST00000508170.5; ENSP00000425648.1; ENSG00000134853.12. [P16234-2] DR Ensembl; ENST00000509490.5; ENSP00000424218.1; ENSG00000134853.12. [P16234-3] DR GeneID; 5156; -. DR KEGG; hsa:5156; -. DR MANE-Select; ENST00000257290.10; ENSP00000257290.5; NM_006206.6; NP_006197.1. DR UCSC; uc003hal.4; human. [P16234-1] DR AGR; HGNC:8803; -. DR CTD; 5156; -. DR DisGeNET; 5156; -. DR GeneCards; PDGFRA; -. DR HGNC; HGNC:8803; PDGFRA. DR HPA; ENSG00000134853; Tissue enhanced (ovary). DR MalaCards; PDGFRA; -. DR MIM; 173490; gene. DR MIM; 175510; phenotype. DR MIM; 606764; phenotype. DR MIM; 607685; phenotype. DR neXtProt; NX_P16234; -. DR OpenTargets; ENSG00000134853; -. DR Orphanet; 585877; B-lymphoblastic leukemia/lymphoma with recurrent genetic abnormality. DR Orphanet; 168940; Chronic eosinophilic leukemia. DR Orphanet; 199306; Cleft lip/palate. DR Orphanet; 44890; Gastrointestinal stromal tumor. DR Orphanet; 168947; Myeloid/lymphoid neoplasm associated with PDGFRA rearrangement. DR Orphanet; 314950; Primary hypereosinophilic syndrome. DR PharmGKB; PA33147; -. DR VEuPathDB; HostDB:ENSG00000134853; -. DR eggNOG; KOG0200; Eukaryota. DR GeneTree; ENSGT00940000156021; -. DR HOGENOM; CLU_000288_49_0_1; -. DR InParanoid; P16234; -. DR OMA; PGLILCQ; -. DR OrthoDB; 1614410at2759; -. DR PhylomeDB; P16234; -. DR TreeFam; TF325768; -. DR BRENDA; 2.7.10.1; 2681. DR PathwayCommons; P16234; -. 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 Reactome; R-HSA-9673767; Signaling by PDGFRA transmembrane, juxtamembrane and kinase domain mutants. DR Reactome; R-HSA-9673770; Signaling by PDGFRA extracellular domain mutants. DR Reactome; R-HSA-9674396; Imatinib-resistant PDGFR mutants. DR Reactome; R-HSA-9674401; Sunitinib-resistant PDGFR mutants. DR Reactome; R-HSA-9674403; Regorafenib-resistant PDGFR mutants. DR Reactome; R-HSA-9674404; Sorafenib-resistant PDGFR mutants. DR Reactome; R-HSA-9674428; PDGFR mutants bind TKIs. DR SignaLink; P16234; -. DR SIGNOR; P16234; -. DR BioGRID-ORCS; 5156; 40 hits in 1185 CRISPR screens. DR ChiTaRS; PDGFRA; human. DR EvolutionaryTrace; P16234; -. DR GeneWiki; PDGFRA; -. DR GenomeRNAi; 5156; -. DR Pharos; P16234; Tclin. DR PRO; PR:P16234; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; P16234; Protein. DR Bgee; ENSG00000134853; Expressed in tibia and 207 other cell types or tissues. DR ExpressionAtlas; P16234; baseline and differential. DR GO; GO:0030054; C:cell junction; IDA:HPA. DR GO; GO:0005929; C:cilium; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl. DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005902; C:microvillus; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0032991; C:protein-containing complex; IDA:MGI. DR GO; GO:0043235; C:receptor complex; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005018; F:platelet-derived growth factor alpha-receptor activity; IDA:UniProtKB. DR GO; GO:0048407; F:platelet-derived growth factor binding; IDA:UniProtKB. DR GO; GO:0005161; F:platelet-derived growth factor receptor binding; IPI:BHF-UCL. DR GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL. DR GO; GO:0004672; F:protein kinase activity; IDA:MGI. DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl. DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IDA:UniProtKB. DR GO; GO:0038085; F:vascular endothelial growth factor binding; IPI:BHF-UCL. DR GO; GO:0005021; F:vascular endothelial growth factor receptor activity; IDA:BHF-UCL. DR GO; GO:0030325; P:adrenal gland development; IEA:Ensembl. DR GO; GO:0055003; P:cardiac myofibril assembly; ISS:UniProtKB. DR GO; GO:0001775; P:cell activation; TAS:BHF-UCL. DR GO; GO:0060326; P:cell chemotaxis; IMP:UniProtKB. DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl. DR GO; GO:0034614; P:cellular response to reactive oxygen species; IDA:MGI. DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; ISS:UniProtKB. DR GO; GO:0048557; P:embryonic digestive tract morphogenesis; ISS:UniProtKB. DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; ISS:UniProtKB. DR GO; GO:0008210; P:estrogen metabolic process; IEA:Ensembl. DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl. DR GO; GO:0060325; P:face morphogenesis; IEA:Ensembl. DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl. DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl. DR GO; GO:0033327; P:Leydig cell differentiation; IEA:Ensembl. DR GO; GO:0030324; P:lung development; IEA:Ensembl. DR GO; GO:0001553; P:luteinization; ISS:UniProtKB. DR GO; GO:0030539; P:male genitalia development; IEA:Ensembl. DR GO; GO:0072277; P:metanephric glomerular capillary formation; ISS:UniProtKB. DR GO; GO:0010544; P:negative regulation of platelet activation; IDA:UniProtKB. DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl. DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB. DR GO; GO:0070527; P:platelet aggregation; IMP:UniProtKB. DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IDA:BHF-UCL. DR GO; GO:0035790; P:platelet-derived growth factor receptor-alpha signaling pathway; IMP: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; IDA:BHF-UCL. 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; IMP: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; IDA:BHF-UCL. DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IMP:UniProtKB. DR GO; GO:0010863; P:positive regulation of phospholipase C activity; IMP:UniProtKB. DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB. DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; TAS:UniProtKB. DR GO; GO:2000739; P:regulation of mesenchymal stem cell differentiation; IMP:UniProtKB. DR GO; GO:0061298; P:retina vasculature development in camera-type eye; ISS:UniProtKB. DR GO; GO:0060021; P:roof of mouth development; IEA:Ensembl. DR GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IEA:Ensembl. DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central. DR GO; GO:0050872; P:white fat cell differentiation; IEA:Ensembl. DR GO; GO:0042060; P:wound healing; ISS:UniProtKB. DR CDD; cd05859; Ig4_PDGFR; 1. DR CDD; cd05861; IgI_PDGFR-alphabeta; 1. DR CDD; cd05105; PTKc_PDGFR_alpha; 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; IPR013098; Ig_I-set. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR027290; PDGFRA. 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:SF52; PLATELET-DERIVED GROWTH FACTOR RECEPTOR ALPHA; 1. DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1. DR Pfam; PF07679; I-set; 2. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR PIRSF; PIRSF500950; Alpha-PDGF_receptor; 1. DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 1. DR PRINTS; PR01832; VEGFRECEPTOR. DR SMART; SM00409; IG; 4. DR SMART; SM00408; IGc2; 3. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00219; TyrKc; 1. DR SUPFAM; SSF48726; Immunoglobulin; 4. 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; P16234; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Cell membrane; KW Cell projection; Chemotaxis; Developmental protein; Disease variant; KW Disulfide bond; Glycoprotein; Golgi apparatus; Host-virus interaction; KW Immunoglobulin domain; Kinase; 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..23 FT CHAIN 24..1089 FT /note="Platelet-derived growth factor receptor alpha" FT /id="PRO_0000016760" FT TOPO_DOM 24..528 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 529..549 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 550..1089 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 24..113 FT /note="Ig-like C2-type 1" FT DOMAIN 117..201 FT /note="Ig-like C2-type 2" FT DOMAIN 202..306 FT /note="Ig-like C2-type 3" FT DOMAIN 319..410 FT /note="Ig-like C2-type 4" FT DOMAIN 414..517 FT /note="Ig-like C2-type 5" FT DOMAIN 593..954 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 1018..1089 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1029..1044 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1045..1060 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 818 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10028" FT BINDING 599..607 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 627 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT SITE 578..579 FT /note="Breakpoint for interstitial deletion to form the FT FIP1L1-PDGFRA fusion protein" FT MOD_RES 572 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:10734113" FT MOD_RES 574 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:10734113" FT MOD_RES 720 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:11095946, FT ECO:0000269|PubMed:8943348" FT MOD_RES 731 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:1646396" FT MOD_RES 742 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:1646396" FT MOD_RES 754 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:17604334" FT MOD_RES 762 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:10733900" FT MOD_RES 768 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:8617789" FT MOD_RES 849 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250" FT MOD_RES 988 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:7535778" FT MOD_RES 1018 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:7535778" FT CARBOHYD 42 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 76 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 103 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 179 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 353 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 359 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 458 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 468 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 49..100 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 150..189 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 235..290 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 435..501 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT VAR_SEQ 210..218 FT /note="ATSELDLEM -> GTCIISFLL (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_007833" FT VAR_SEQ 219..1089 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_007834" FT VAR_SEQ 720..743 FT /note="YVILSFENNGDYMDMKQADTTQYV -> SGQGCLSSGTLQELSVDLQARGPC FT (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_042015" FT VAR_SEQ 744..1089 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_042016" FT VARIANT 79 FT /note="G -> D (in dbSNP:rs36035373)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042032" FT VARIANT 426 FT /note="G -> D (in dbSNP:rs55865821)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042033" FT VARIANT 478 FT /note="S -> P (in dbSNP:rs35597368)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17344846" FT /id="VAR_034378" FT VARIANT 481 FT /note="R -> G (in a hypereosinophilic syndrome sample; does FT not lead to constitutive kinase activation)" FT /evidence="ECO:0000269|PubMed:21224473" FT /id="VAR_066460" FT VARIANT 507 FT /note="L -> P (in a hypereosinophilic syndrome sample; does FT not lead to constitutive kinase activation)" FT /evidence="ECO:0000269|PubMed:21224473" FT /id="VAR_066461" FT VARIANT 555 FT /note="Y -> C (in GISTPS; increased platelet-derived growth FT factor alpha-receptor activity; constitutively activated FT kinase; dbSNP:rs121908589)" FT /evidence="ECO:0000269|PubMed:17087943" FT /id="VAR_083158" FT VARIANT 561 FT /note="V -> D (in a GIST sample; constitutively activated FT kinase; dbSNP:rs121908586)" FT /evidence="ECO:0000269|PubMed:12522257, FT ECO:0000269|PubMed:15928335" FT /id="VAR_066462" FT VARIANT 562 FT /note="I -> M (in a hypereosinophilic syndrome sample; does FT not lead to constitutive kinase activation)" FT /evidence="ECO:0000269|PubMed:21224473" FT /id="VAR_066463" FT VARIANT 570 FT /note="H -> R (in a hypereosinophilic syndrome sample; does FT not lead to constitutive kinase activation)" FT /evidence="ECO:0000269|PubMed:21224473" FT /id="VAR_066464" FT VARIANT 650 FT /note="H -> Q (in a hypereosinophilic syndrome sample; FT constitutively activated kinase)" FT /evidence="ECO:0000269|PubMed:21224473" FT /id="VAR_066465" FT VARIANT 653 FT /note="P -> L (in GISTPS; uncertain significance)" FT /evidence="ECO:0000269|PubMed:25975287" FT /id="VAR_083159" FT VARIANT 659 FT /note="N -> K (in GIST sample; constitutively activated FT kinase; dbSNP:rs1057519700)" FT /evidence="ECO:0000269|PubMed:15928335" FT /id="VAR_066466" FT VARIANT 659 FT /note="N -> S (in a hypereosinophilic syndrome sample; FT constitutively activated kinase)" FT /evidence="ECO:0000269|PubMed:21224473" FT /id="VAR_066467" FT VARIANT 705 FT /note="L -> P (in a hypereosinophilic syndrome sample; does FT not lead to constitutive kinase activation)" FT /evidence="ECO:0000269|PubMed:21224473" FT /id="VAR_066468" FT VARIANT 748 FT /note="R -> G (in a hypereosinophilic syndrome sample; FT constitutively activated kinase)" FT /evidence="ECO:0000269|PubMed:21224473" FT /id="VAR_066469" FT VARIANT 764 FT /note="R -> C (in dbSNP:rs34392012)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042034" FT VARIANT 829 FT /note="G -> R (in a glioblastoma multiforme sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042035" FT VARIANT 842..845 FT /note="Missing (in a GIST sample; constitutively activated FT kinase)" FT /evidence="ECO:0000269|PubMed:12522257, FT ECO:0000269|PubMed:15928335" FT /id="VAR_066470" FT VARIANT 842 FT /note="D -> V (in a GIST sample; imatinib resistant, FT constitutively activated kinase; dbSNP:rs121908585)" FT /evidence="ECO:0000269|PubMed:12522257, FT ECO:0000269|PubMed:15928335, ECO:0000269|PubMed:20972453" FT /id="VAR_066471" FT VARIANT 842 FT /note="D -> Y (in a GIST sample; imatinib sensitive, FT constitutively activated kinase; dbSNP:rs121913265)" FT /evidence="ECO:0000269|PubMed:15928335" FT /id="VAR_066472" FT VARIANT 845..848 FT /note="Missing (in a GIST sample; constitutively activated FT kinase)" FT /evidence="ECO:0000269|PubMed:12522257, FT ECO:0000269|PubMed:15928335" FT /id="VAR_066473" FT VARIANT 846 FT /note="D -> Y (in GISTPS; uncertain significance; FT dbSNP:rs121908588)" FT /evidence="ECO:0000269|PubMed:14699510" FT /id="VAR_083160" FT VARIANT 849 FT /note="Y -> C (in GIST)" FT /evidence="ECO:0000269|PubMed:15928335" FT /id="VAR_066474" FT VARIANT 849 FT /note="Y -> S (in a hypereosinophilic syndrome sample; FT constitutively activated kinase)" FT /evidence="ECO:0000269|PubMed:21224473" FT /id="VAR_066475" FT VARIANT 996 FT /note="E -> K (in a metastatic melanoma sample; somatic FT mutation; dbSNP:rs779173667)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042036" FT VARIANT 1071 FT /note="D -> N (in a lung neuroendocrine carcinoma sample; FT somatic mutation; dbSNP:rs376544204)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_042037" FT MUTAGEN 572 FT /note="Y->F: Abolishes interaction with SRC-family members FT and impairs internalization of the activated receptor; when FT associated with F-574." FT /evidence="ECO:0000269|PubMed:10734113, FT ECO:0000269|PubMed:14644164" FT MUTAGEN 574 FT /note="Y->F: Abolishes interaction with SRC-family members FT and impairs internalization of the activated receptor; when FT associated with F-572." FT /evidence="ECO:0000269|PubMed:10734113, FT ECO:0000269|PubMed:14644164" FT MUTAGEN 720 FT /note="Y->F: Strongly reduced interaction with PTPN11 and FT GRB2." FT /evidence="ECO:0000269|PubMed:8943348" FT MUTAGEN 731 FT /note="Y->F: No effect on autophosphorylation and FT phosphorylation of PLCG1. Abolishes activation of FT phosphatidylinositol 3-kinase." FT /evidence="ECO:0000269|PubMed:1646396" FT MUTAGEN 742 FT /note="Y->F: No effect on autophosphorylation and FT phosphorylation of PLCG1. Abolishes activation of FT phosphatidylinositol 3-kinase." FT /evidence="ECO:0000269|PubMed:1646396" FT MUTAGEN 762 FT /note="Y->F: Abolishes interaction with CRK." FT /evidence="ECO:0000269|PubMed:10733900" FT STRAND 29..32 FT /evidence="ECO:0007829|PDB:7LBF" FT STRAND 35..38 FT /evidence="ECO:0007829|PDB:7LBF" FT STRAND 41..43 FT /evidence="ECO:0007829|PDB:7LBF" FT STRAND 46..53 FT /evidence="ECO:0007829|PDB:7LBF" FT STRAND 55..58 FT /evidence="ECO:0007829|PDB:7LBF" FT TURN 62..65 FT /evidence="ECO:0007829|PDB:7RAM" FT STRAND 67..69 FT /evidence="ECO:0007829|PDB:7RAM" FT STRAND 70..72 FT /evidence="ECO:0007829|PDB:7LBF" FT STRAND 80..86 FT /evidence="ECO:0007829|PDB:7LBF" FT HELIX 92..94 FT /evidence="ECO:0007829|PDB:7LBF" FT STRAND 96..102 FT /evidence="ECO:0007829|PDB:7LBF" FT HELIX 103..105 FT /evidence="ECO:0007829|PDB:7LBF" FT STRAND 107..111 FT /evidence="ECO:0007829|PDB:7LBF" FT STRAND 114..120 FT /evidence="ECO:0007829|PDB:7LBF" FT STRAND 124..128 FT /evidence="ECO:0007829|PDB:7RAM" FT STRAND 133..141 FT /evidence="ECO:0007829|PDB:7LBF" FT STRAND 144..148 FT /evidence="ECO:0007829|PDB:7LBF" FT STRAND 152..156 FT /evidence="ECO:0007829|PDB:7LBF" FT STRAND 159..167 FT /evidence="ECO:0007829|PDB:7LBF" FT STRAND 171..173 FT /evidence="ECO:0007829|PDB:7LBF" FT TURN 174..176 FT /evidence="ECO:0007829|PDB:7LBF" FT STRAND 177..181 FT /evidence="ECO:0007829|PDB:7LBF" FT STRAND 184..192 FT /evidence="ECO:0007829|PDB:7LBF" FT STRAND 197..199 FT /evidence="ECO:0007829|PDB:7LBF" FT STRAND 203..208 FT /evidence="ECO:0007829|PDB:7LBF" FT STRAND 216..219 FT /evidence="ECO:0007829|PDB:7LBF" FT STRAND 224..226 FT /evidence="ECO:0007829|PDB:7LBF" FT STRAND 231..237 FT /evidence="ECO:0007829|PDB:7LBF" FT STRAND 239..241 FT /evidence="ECO:0007829|PDB:7LBF" FT STRAND 246..248 FT /evidence="ECO:0007829|PDB:7LBF" FT HELIX 252..254 FT /evidence="ECO:0007829|PDB:7LBF" FT STRAND 258..264 FT /evidence="ECO:0007829|PDB:7LBF" FT STRAND 266..268 FT /evidence="ECO:0007829|PDB:7LBF" FT STRAND 270..279 FT /evidence="ECO:0007829|PDB:7LBF" FT STRAND 286..292 FT /evidence="ECO:0007829|PDB:7LBF" FT STRAND 301..306 FT /evidence="ECO:0007829|PDB:7LBF" FT STRAND 308..310 FT /evidence="ECO:0007829|PDB:7LBF" FT STRAND 560..565 FT /evidence="ECO:0007829|PDB:6A32" FT STRAND 567..570 FT /evidence="ECO:0007829|PDB:6A32" FT STRAND 572..574 FT /evidence="ECO:0007829|PDB:6A32" FT HELIX 577..579 FT /evidence="ECO:0007829|PDB:6A32" FT HELIX 584..586 FT /evidence="ECO:0007829|PDB:6JOL" FT HELIX 590..592 FT /evidence="ECO:0007829|PDB:5GRN" FT STRAND 593..601 FT /evidence="ECO:0007829|PDB:5GRN" FT STRAND 603..614 FT /evidence="ECO:0007829|PDB:5GRN" FT STRAND 616..618 FT /evidence="ECO:0007829|PDB:5GRN" FT STRAND 620..629 FT /evidence="ECO:0007829|PDB:5GRN" FT HELIX 635..651 FT /evidence="ECO:0007829|PDB:5GRN" FT STRAND 660..664 FT /evidence="ECO:0007829|PDB:5GRN" FT STRAND 666..669 FT /evidence="ECO:0007829|PDB:5GRN" FT STRAND 671..675 FT /evidence="ECO:0007829|PDB:5GRN" FT STRAND 678..681 FT /evidence="ECO:0007829|PDB:6JOJ" FT HELIX 682..688 FT /evidence="ECO:0007829|PDB:5GRN" FT HELIX 690..696 FT /evidence="ECO:0007829|PDB:6A32" FT HELIX 769..774 FT /evidence="ECO:0007829|PDB:6A32" FT HELIX 778..781 FT /evidence="ECO:0007829|PDB:5K5X" FT HELIX 792..811 FT /evidence="ECO:0007829|PDB:5GRN" FT HELIX 821..823 FT /evidence="ECO:0007829|PDB:5GRN" FT STRAND 824..827 FT /evidence="ECO:0007829|PDB:5GRN" FT TURN 828..830 FT /evidence="ECO:0007829|PDB:5GRN" FT STRAND 831..834 FT /evidence="ECO:0007829|PDB:5GRN" FT HELIX 838..840 FT /evidence="ECO:0007829|PDB:5GRN" FT HELIX 843..845 FT /evidence="ECO:0007829|PDB:5GRN" FT STRAND 849..851 FT /evidence="ECO:0007829|PDB:5GRN" FT STRAND 853..857 FT /evidence="ECO:0007829|PDB:5GRN" FT HELIX 859..861 FT /evidence="ECO:0007829|PDB:5GRN" FT HELIX 864..869 FT /evidence="ECO:0007829|PDB:5GRN" FT HELIX 874..889 FT /evidence="ECO:0007829|PDB:5GRN" FT HELIX 903..910 FT /evidence="ECO:0007829|PDB:5GRN" FT HELIX 923..932 FT /evidence="ECO:0007829|PDB:5GRN" FT HELIX 937..939 FT /evidence="ECO:0007829|PDB:5GRN" FT HELIX 943..953 FT /evidence="ECO:0007829|PDB:5GRN" FT HELIX 956..971 FT /evidence="ECO:0007829|PDB:6A32" SQ SEQUENCE 1089 AA; 122670 MW; 5E3FB9940ACD1BE8 CRC64; MGTSHPAFLV LGCLLTGLSL ILCQLSLPSI LPNENEKVVQ LNSSFSLRCF GESEVSWQYP MSEEESSDVE IRNEENNSGL FVTVLEVSSA SAAHTGLYTC YYNHTQTEEN ELEGRHIYIY VPDPDVAFVP LGMTDYLVIV EDDDSAIIPC RTTDPETPVT LHNSEGVVPA SYDSRQGFNG TFTVGPYICE ATVKGKKFQT IPFNVYALKA TSELDLEMEA LKTVYKSGET IVVTCAVFNN EVVDLQWTYP GEVKGKGITM LEEIKVPSIK LVYTLTVPEA TVKDSGDYEC AARQATREVK EMKKVTISVH EKGFIEIKPT FSQLEAVNLH EVKHFVVEVR AYPPPRISWL KNNLTLIENL TEITTDVEKI QEIRYRSKLK LIRAKEEDSG HYTIVAQNED AVKSYTFELL TQVPSSILDL VDDHHGSTGG QTVRCTAEGT PLPDIEWMIC KDIKKCNNET SWTILANNVS NIITEIHSRD RSTVEGRVTF AKVEETIAVR CLAKNLLGAE NRELKLVAPT LRSELTVAAA VLVLLVIVII SLIVLVVIWK QKPRYEIRWR VIESISPDGH EYIYVDPMQL PYDSRWEFPR DGLVLGRVLG SGAFGKVVEG TAYGLSRSQP VMKVAVKMLK PTARSSEKQA LMSELKIMTH LGPHLNIVNL LGACTKSGPI YIITEYCFYG DLVNYLHKNR DSFLSHHPEK PKKELDIFGL NPADESTRSY VILSFENNGD YMDMKQADTT QYVPMLERKE VSKYSDIQRS LYDRPASYKK KSMLDSEVKN LLSDDNSEGL TLLDLLSFTY QVARGMEFLA SKNCVHRDLA ARNVLLAQGK IVKICDFGLA RDIMHDSNYV SKGSTFLPVK WMAPESIFDN LYTTLSDVWS YGILLWEIFS LGGTPYPGMM VDSTFYNKIK SGYRMAKPDH ATSEVYEIMV KCWNSEPEKR PSFYHLSEIV ENLLPGQYKK SYEKIHLDFL KSDHPAVARM RVDSDNAYIG VTYKNEEDKL KDWEGGLDEQ RLSADSGYII PLPDIDPVPE EEDLGKRNRH SSQTSEESAI ETGSSSSTFI KREDETIEDI DMMDDIGIDS SDLVEDSFL //