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Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor) (CD140 antigen-like family member A) (CD140a antigen) (Platelet-derived growth factor alpha receptor) (Platelet-derived growth factor receptor 2) (PDGFR-2) (CD antigen CD140a)

 PGFRA_HUMAN             Reviewed;        1089 AA.
P16234; B2RE69; E9PBH0; Q6P4H5; Q96KZ7; Q9UD28;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
25-OCT-2017, entry version 201.
RecName: Full=Platelet-derived growth factor receptor alpha;
Short=PDGF-R-alpha;
Short=PDGFR-alpha;
EC=2.7.10.1;
AltName: Full=Alpha platelet-derived growth factor receptor;
AltName: Full=Alpha-type platelet-derived growth factor receptor;
AltName: Full=CD140 antigen-like family member A;
AltName: Full=CD140a antigen;
AltName: Full=Platelet-derived growth factor alpha receptor;
AltName: Full=Platelet-derived growth factor receptor 2;
Short=PDGFR-2;
AltName: CD_antigen=CD140a;
Flags: Precursor;
Name=PDGFRA; Synonyms=PDGFR2, RHEPDGFRA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH PDGFA AND
PDGFB.
TISSUE=Foreskin;
PubMed=2544881; DOI=10.1073/pnas.86.13.4917;
Claesson-Welsh L., Eriksson A., Westermark B., Heldin C.H.;
"cDNA cloning and expression of the human A-type platelet-derived
growth factor (PDGF) receptor establishes structural similarity to the
B-type PDGF receptor.";
Proc. Natl. Acad. Sci. U.S.A. 86:4917-4921(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AUTOPHOSPHORYLATION, TISSUE
SPECIFICITY, AND INTERACTION WITH PDGFA AND PDGFB.
TISSUE=Brain;
PubMed=2536956; DOI=10.1126/science.2536956;
Matsui T., Heidaran M., Miki T., Popescu N., la Rochelle W., Kraus M.,
Pierce J., Aaronson S.;
"Isolation of a novel receptor cDNA establishes the existence of two
PDGF receptor genes.";
Science 243:800-804(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Blood;
PubMed=8586421; DOI=10.1006/geno.1995.9883;
Kawagishi J., Ku T.;
"Structure, organization, and transcription units of the human alpha-
platelet-derived growth factor receptor gene, PDGFRA.";
Genomics 30:224-232(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
PRO-478.
TISSUE=Lung, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
PRO-478.
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 579-1089, DISEASE, AND IDENTIFICATION BY
MASS SPECTROMETRY OF FIP1L1-PDGFRA FUSION PROTEIN.
TISSUE=Eosinophil;
PubMed=12808148; DOI=10.1073/pnas.0932698100;
Griffin J.H., Leung J., Bruner R.J., Caligiuri M.A., Briesewitz R.;
"Discovery of a fusion kinase in EOL-1 cells and idiopathic
hypereosinophilic syndrome.";
Proc. Natl. Acad. Sci. U.S.A. 100:7830-7835(2003).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 823-876, AND TISSUE SPECIFICITY.
TISSUE=Colon tumor;
PubMed=7896447; DOI=10.1002/ijc.2910600611;
Craven R.J., Xu L.H., Weiner T.M., Fridell Y.-W., Dent G.A.,
Srivastava S., Varnum B., Liu E.T., Cance W.G.;
"Receptor tyrosine kinases expressed in metastatic colon cancer.";
Int. J. Cancer 60:791-797(1995).
[9]
FUNCTION AS PDGFA AND PDGFB RECEPTOR IN CELL PROLIFERATION AND
CHEMOTAXIS, AND SUBCELLULAR LOCATION.
PubMed=2554309; DOI=10.1073/pnas.86.21.8314;
Matsui T., Pierce J.H., Fleming T.P., Greenberger J.S.,
LaRochelle W.J., Ruggiero M., Aaronson S.A.;
"Independent expression of human alpha or beta platelet-derived growth
factor receptor cDNAs in a naive hematopoietic cell leads to
functional coupling with mitogenic and chemotactic signaling
pathways.";
Proc. Natl. Acad. Sci. U.S.A. 86:8314-8318(1989).
[10]
INTERACTION WITH PLCG1 AND SRC.
PubMed=2173144; DOI=10.1126/science.2173144;
Anderson D., Koch C.A., Grey L., Ellis C., Moran M.F., Pawson T.;
"Binding of SH2 domains of phospholipase C gamma 1, GAP, and Src to
activated growth factor receptors.";
Science 250:979-982(1990).
[11]
INTERACTION WITH PDGFRA; PDGFA AND PDGFB, FUNCTION AS RECEPTOR FOR
PDGFA AND PDGFB, AND AUTOPHOSPHORYLATION.
PubMed=1709159;
Kelly J.D., Haldeman B.A., Grant F.J., Murray M.J., Seifert R.A.,
Bowen-Pope D.F., Cooper J.A., Kazlauskas A.;
"Platelet-derived growth factor (PDGF) stimulates PDGF receptor
subunit dimerization and intersubunit trans-phosphorylation.";
J. Biol. Chem. 266:8987-8992(1991).
[12]
FUNCTION AS PDGFB RECEPTOR IN CHEMOTAXIS; CELL PROLIFERATION;
PHOSPHORYLATION OF PLCG1; ACTIVATION OF PHOSPHATIDYLINOSITOL 3-KINASE
AND REGULATION OF PHOSPHATIDYLINOSITOL METABOLISM, INTERACTION WITH
PIK3R, PHOSPHORYLATION AT TYR-731 AND TYR-742, AND MUTAGENESIS OF
TYR-731 AND TYR-742.
PubMed=1646396; DOI=10.1128/MCB.11.7.3780;
Yu J.C., Heidaran M.A., Pierce J.H., Gutkind J.S., Lombardi D.,
Ruggiero M., Aaronson S.A.;
"Tyrosine mutations within the alpha platelet-derived growth factor
receptor kinase insert domain abrogate receptor-associated
phosphatidylinositol-3 kinase activity without affecting mitogenic or
chemotactic signal transduction.";
Mol. Cell. Biol. 11:3780-3785(1991).
[13]
INTERACTION WITH PDGFA AND PDGFB.
PubMed=7679113;
Fretto L.J., Snape A.J., Tomlinson J.E., Seroogy J.J., Wolf D.L.,
LaRochelle W.J., Giese N.A.;
"Mechanism of platelet-derived growth factor (PDGF) AA, AB, and BB
binding to alpha and beta PDGF receptor.";
J. Biol. Chem. 268:3625-3631(1993).
[14]
FUNCTION AS PDGFA RECEPTOR IN REGULATION OF PLATELET ACTIVATION,
SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, AND TISSUE SPECIFICITY.
PubMed=8188664;
Vassbotn F.S., Havnen O.K., Heldin C.H., Holmsen H.;
"Negative feedback regulation of human platelets via autocrine
activation of the platelet-derived growth factor alpha-receptor.";
J. Biol. Chem. 269:13874-13879(1994).
[15]
PHOSPHORYLATION AT TYR-988 AND TYR-1018, AND INTERACTION WITH PLCG1.
PubMed=7535778; DOI=10.1074/jbc.270.13.7773;
Eriksson A., Naanberg E., Roennstrand L., Engstroem U., Hellman U.,
Rupp E., Carpenter G., Heldin C.H., Claesson-Welsh L.;
"Demonstration of functionally different interactions between
phospholipase C-gamma and the two types of platelet-derived growth
factor receptors.";
J. Biol. Chem. 270:7773-7781(1995).
[16]
FUNCTION IN PROMOTING CHEMOTAXIS.
PubMed=8760137;
Osornio-Vargas A.R., Lindroos P.M., Coin P.G., Badgett A.,
Hernandez-Rodriguez N.A., Bonner J.C.;
"Maximal PDGF-induced lung fibroblast chemotaxis requires PDGF
receptor-alpha.";
Am. J. Physiol. 271:L93-L99(1996).
[17]
PHOSPHORYLATION AT TYR-768.
PubMed=8617789; DOI=10.1074/jbc.271.9.5101;
Yokote K., Mori S., Siegbahn A., Ronnstrand L., Wernstedt C.,
Heldin C.H., Claesson-Welsh L.;
"Structural determinants in the platelet-derived growth factor alpha-
receptor implicated in modulation of chemotaxis.";
J. Biol. Chem. 271:5101-5111(1996).
[18]
INTERACTION WITH GRB7 AND PIK3R1.
PubMed=8940081; DOI=10.1074/jbc.271.48.30942;
Yokote K., Margolis B., Heldin C.H., Claesson-Welsh L.;
"Grb7 is a downstream signaling component of platelet-derived growth
factor alpha- and beta-receptors.";
J. Biol. Chem. 271:30942-30949(1996).
[19]
FUNCTION IN PHOSPHORYLATION OF PTPN11; ACTIVATION OF HRAS AND
REGULATION OF CELL PROLIFERATION, PHOSPHORYLATION AT TYR-720,
INTERACTION WITH GRB2; PTPN11; PLCG1 AND PIK3R1, AUTOPHOSPHORYLATION,
AND MUTAGENESIS OF TYR-720.
PubMed=8943348; DOI=10.1128/MCB.16.12.6926;
Bazenet C.E., Gelderloos J.A., Kazlauskas A.;
"Phosphorylation of tyrosine 720 in the platelet-derived growth factor
alpha receptor is required for binding of Grb2 and SHP-2 but not for
activation of Ras or cell proliferation.";
Mol. Cell. Biol. 16:6926-6936(1996).
[20]
INTERACTION WITH CRK, PHOSPHORYLATION AT TYR-762, AND MUTAGENESIS OF
TYR-762.
PubMed=10733900; DOI=10.1006/bbrc.2000.2374;
Matsumoto T., Yokote K., Take A., Takemoto M., Asaumi S.,
Hashimoto Y., Matsuda M., Saito Y., Mori S.;
"Differential interaction of CrkII adaptor protein with platelet-
derived growth factor alpha- and beta-receptors is determined by its
internal tyrosine phosphorylation.";
Biochem. Biophys. Res. Commun. 270:28-33(2000).
[21]
INTERACTION WITH SHF, AND PHOSPHORYLATION AT TYR-720.
PubMed=11095946; DOI=10.1006/bbrc.2000.3847;
Lindholm C.K., Frantz J.D., Shoelson S.E., Welsh M.;
"Shf, a Shb-like adapter protein, is involved in PDGF-alpha-receptor
regulation of apoptosis.";
Biochem. Biophys. Res. Commun. 278:537-543(2000).
[22]
FUNCTION IN PLATELET ACTIVATION.
PubMed=10947961; DOI=10.1042/bj3500469;
Selheim F., Fukami M.H., Holmsen H., Vassbotn F.S.;
"Platelet-derived-growth-factor-induced signalling in human platelets:
phosphoinositide-3-kinase-dependent inhibition of platelet
activation.";
Biochem. J. 350:469-475(2000).
[23]
FUNCTION IN ACTIVATION OF MAPK1/ERK2 AND/OR MAPK3/ERK1, DEGRADATION,
PHOSPHORYLATION AT TYR-572 AND TYR-574, AND MUTAGENESIS OF TYR-572 AND
TYR-574.
PubMed=10734113; DOI=10.1074/jbc.275.13.9620;
Rosenkranz S., Ikuno Y., Leong F.L., Klinghoffer R.A., Miyake S.,
Band H., Kazlauskas A.;
"Src family kinases negatively regulate platelet-derived growth factor
alpha receptor-dependent signaling and disease progression.";
J. Biol. Chem. 275:9620-9627(2000).
[24]
FUNCTION AS A RECEPTOR FOR PDGFC, AND INTERACTION WITH PDGFC.
PubMed=11297552; DOI=10.1074/jbc.M101056200;
Gilbertson D.G., Duff M.E., West J.W., Kelly J.D., Sheppard P.O.,
Hofstrand P.D., Gao Z., Shoemaker K., Bukowski T.R., Moore M.,
Feldhaus A.L., Humes J.M., Palmer T.E., Hart C.E.;
"Platelet-derived growth factor C (PDGF-C), a novel growth factor that
binds to PDGF alpha and beta receptor.";
J. Biol. Chem. 276:27406-27414(2001).
[25]
SUBCELLULAR LOCATION, INTERACTION WITH SRC, AND MUTAGENESIS OF TYR-572
AND TYR-574.
PubMed=14644164; DOI=10.1016/j.yexcr.2003.08.001;
Avrov K., Kazlauskas A.;
"The role of c-Src in platelet-derived growth factor alpha receptor
internalization.";
Exp. Cell Res. 291:426-434(2003).
[26]
INVOLVEMENT IN HES.
PubMed=12660384; DOI=10.1056/NEJMoa025217;
Cools J., DeAngelo D.J., Gotlib J., Stover E.H., Legare R.D.,
Cortes J., Kutok J., Clark J., Galinsky I., Griffin J.D., Cross N.C.,
Tefferi A., Malone J., Alam R., Schrier S.L., Schmid J., Rose M.,
Vandenberghe P., Verhoef G., Boogaerts M., Wlodarska I.,
Kantarjian H., Marynen P., Coutre S.E., Stone R., Gilliland D.G.;
"A tyrosine kinase created by fusion of the PDGFRA and FIP1L1 genes as
a therapeutic target of imatinib in idiopathic hypereosinophilic
syndrome.";
N. Engl. J. Med. 348:1201-1214(2003).
[27]
FUNCTION IN PHOSPHORYLATION OF AKT1; MAP KINASES; STAT1 AND STAT3,
INVOLVEMENT IN GIST, VARIANTS ASP-561; VAL-842; 842-ASP--HIS-845 DEL
AND 845-HIS--PRO-448 DEL, AND CHARACTERIZATION OF VARIANTS ASP-561;
VAL-842; 842-ASP--HIS-845 DEL AND 845-HIS--PRO-448 DEL.
PubMed=12522257; DOI=10.1126/science.1079666;
Heinrich M.C., Corless C.L., Duensing A., McGreevey L., Chen C.J.,
Joseph N., Singer S., Griffith D.J., Haley A., Town A., Demetri G.D.,
Fletcher C.D., Fletcher J.A.;
"PDGFRA activating mutations in gastrointestinal stromal tumors.";
Science 299:708-710(2003).
[28]
INVOLVEMENT IN GIST, VARIANTS ASP-561; LYS-659; TYR-842; VAL-842;
842-ASP--HIS-845 DEL 845-HIS--PRO-448 DEL AND CYS-849,
CHARACTERIZATION OF VARIANTS ASP-561; LYS-659; TYR-842; VAL-842;
842-ASP--HIS-845 DEL 845-HIS--PRO-448 DEL AND CYS-849, AND ENZYME
REGULATION.
PubMed=15928335; DOI=10.1200/JCO.2005.14.068;
Corless C.L., Schroeder A., Griffith D., Town A., McGreevey L.,
Harrell P., Shiraga S., Bainbridge T., Morich J., Heinrich M.C.;
"PDGFRA mutations in gastrointestinal stromal tumors: frequency,
spectrum and in vitro sensitivity to imatinib.";
J. Clin. Oncol. 23:5357-5364(2005).
[29]
FUNCTION IN CELL SURVIVAL.
PubMed=17141222; DOI=10.1016/j.febslet.2006.11.034;
Vantler M., Huntgeburth M., Caglayan E., Ten Freyhaus H., Schnabel P.,
Rosenkranz S.;
"PI3-kinase/Akt-dependent antiapoptotic signaling by the PDGF alpha
receptor is negatively regulated by Src family kinases.";
FEBS Lett. 580:6769-6776(2006).
[30]
PHOSPHORYLATION AT TYR-754.
PubMed=17604334; DOI=10.1158/1535-7163.MCT-06-0720;
Stock P., Monga D., Tan X., Micsenyi A., Loizos N., Monga S.P.;
"Platelet-derived growth factor receptor-alpha: a novel therapeutic
target in human hepatocellular cancer.";
Mol. Cancer Ther. 6:1932-1941(2007).
[31]
INTERACTION WITH HHV-5 GB.
PubMed=20660204; DOI=10.1128/JVI.00710-10;
Feire A.L., Roy R.M., Manley K., Compton T.;
"The glycoprotein B disintegrin-like domain binds beta 1 integrin to
mediate cytomegalovirus entry.";
J. Virol. 84:10026-10037(2010).
[32]
FUNCTION IN PHOSPHORYLATION OF STAT 5A AND/OR STAT5B, ROLE IN
HYPEREOSINOPHILIC SYNDROME, VARIANTS GLY-481; PRO-507; MET-562;
ARG-570; GLN-650; SER-659; PRO-705; GLY-748 AND SER-849,
CHARACTERIZATION OF VARIANTS GLY-481; PRO-507; MET-562; ARG-570;
GLN-650; SER-659; PRO-705; GLY-748 AND SER-849, AND ENZYME REGULATION.
PubMed=21224473; DOI=10.1182/blood-2010-05-286757;
Elling C., Erben P., Walz C., Frickenhaus M., Schemionek M.,
Stehling M., Serve H., Cross N.C., Hochhaus A., Hofmann W.K.,
Berdel W.E., Muller-Tidow C., Reiter A., Koschmieder S.;
"Novel imatinib-sensitive PDGFRA-activating point mutations in
hypereosinophilic syndrome induce growth factor independence and
leukemia-like disease.";
Blood 117:2935-2943(2011).
[33]
FUNCTION IN CELL DIFFERENTIATION, AND UBIQUITINATION.
PubMed=21596750; DOI=10.1074/jbc.M110.197525;
Severe N., Miraoui H., Marie P.J.;
"The Casitas B lineage lymphoma (Cbl) mutant G306E enhances osteogenic
differentiation in human mesenchymal stromal cells in part by
decreased Cbl-mediated platelet-derived growth factor receptor alpha
and fibroblast growth factor receptor 2 ubiquitination.";
J. Biol. Chem. 286:24443-24450(2011).
[34]
ROLE IN DISEASE, CHARACTERIZATION OF VARIANT VAL-842, AND ENZYME
REGULATION.
PubMed=20972453; DOI=10.1038/onc.2010.476;
von Bubnoff N., Gorantla S.P., Engh R.A., Oliveira T.M., Thone S.,
Aberg E., Peschel C., Duyster J.;
"The low frequency of clinical resistance to PDGFR inhibitors in
myeloid neoplasms with abnormalities of PDGFRA might be related to the
limited repertoire of possible PDGFRA kinase domain mutations in
vitro.";
Oncogene 30:933-943(2011).
[35]
REVIEW ON SIGNALING AND AUTOPHOSPHORYLATION.
PubMed=9739761; DOI=10.1016/S0304-419X(98)00015-8;
Heldin C.H., Ostman A., Ronnstrand L.;
"Signal transduction via platelet-derived growth factor receptors.";
Biochim. Biophys. Acta 1378:F79-113(1998).
[36]
REVIEW ON ROLE IN DISEASE AND ENZYME REGULATION.
PubMed=15207817; DOI=10.1016/j.cytogfr.2004.03.002;
Ostman A.;
"PDGF receptors-mediators of autocrine tumor growth and regulators of
tumor vasculature and stroma.";
Cytokine Growth Factor Rev. 15:275-286(2004).
[37]
REVIEW ON ROLE IN DISEASE AND ENZYME REGULATION.
PubMed=17419949; DOI=10.1016/S0065-230X(06)97011-0;
Ostman A., Heldin C.H.;
"PDGF receptors as targets in tumor treatment.";
Adv. Cancer Res. 97:247-274(2007).
[38]
REVIEW ON FUNCTION IN DEVELOPMENT AND DISEASE; LIGANDS AND SIGNALING
PATHWAYS.
PubMed=18483217; DOI=10.1101/gad.1653708;
Andrae J., Gallini R., Betsholtz C.;
"Role of platelet-derived growth factors in physiology and medicine.";
Genes Dev. 22:1276-1312(2008).
[39]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1185-1189 IN COMPLEX WITH
SLC9A3R1 AND PDGFRB.
PubMed=11882663; DOI=10.1074/jbc.M201507200;
Karthikeyan S., Leung T., Ladias J.A.A.;
"Structural determinants of the Na+/H+ exchanger regulatory factor
interaction with the beta 2 adrenergic and platelet-derived growth
factor receptors.";
J. Biol. Chem. 277:18973-18978(2002).
[40]
VARIANTS [LARGE SCALE ANALYSIS] ASP-79; ASP-426; PRO-478; CYS-764;
ARG-829; LYS-996 AND ASN-1071.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Tyrosine-protein kinase that acts as a cell-surface
receptor for PDGFA, PDGFB and PDGFC and plays an essential role in
the regulation of embryonic development, cell proliferation,
survival and chemotaxis. Depending on the context, promotes or
inhibits cell proliferation and cell migration. Plays an important
role in the differentiation of bone marrow-derived mesenchymal
stem cells. Required for normal skeleton development and cephalic
closure during embryonic development. Required for normal
development of the mucosa lining the gastrointestinal tract, and
for recruitment of mesenchymal cells and normal development of
intestinal villi. Plays a role in cell migration and chemotaxis in
wound healing. Plays a role in platelet activation, secretion of
agonists from platelet granules, and in thrombin-induced platelet
aggregation. Binding of its cognate ligands - homodimeric PDGFA,
homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or
homodimeric PDGFC -leads to the activation of several signaling
cascades; the response depends on the nature of the bound ligand
and is modulated by the formation of heterodimers between PDGFRA
and PDGFRB. Phosphorylates PIK3R1, PLCG1, and PTPN11. Activation
of PLCG1 leads to the production of the cellular signaling
molecules diacylglycerol and inositol 1,4,5-trisphosphate,
mobilization of cytosolic Ca(2+) and the activation of protein
kinase C. Phosphorylates PIK3R1, the regulatory subunit of
phosphatidylinositol 3-kinase, and thereby mediates activation of
the AKT1 signaling pathway. Mediates activation of HRAS and of the
MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of
STAT family members STAT1, STAT3 and STAT5A and/or STAT5B.
Receptor signaling is down-regulated by protein phosphatases that
dephosphorylate the receptor and its down-stream effectors, and by
rapid internalization of the activated receptor.
{ECO:0000269|PubMed:10734113, ECO:0000269|PubMed:10947961,
ECO:0000269|PubMed:11297552, ECO:0000269|PubMed:12522257,
ECO:0000269|PubMed:1646396, ECO:0000269|PubMed:1709159,
ECO:0000269|PubMed:17141222, ECO:0000269|PubMed:20972453,
ECO:0000269|PubMed:21224473, ECO:0000269|PubMed:21596750,
ECO:0000269|PubMed:2554309, ECO:0000269|PubMed:8188664,
ECO:0000269|PubMed:8760137, ECO:0000269|PubMed:8943348}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ENZYME REGULATION: Present in an inactive conformation in the
absence of bound ligand. Binding of PDGFA and/or PDGFB leads to
dimerization and activation by autophosphorylation on tyrosine
residues. Inhibited by imatinib, nilotinib and sorafenib.
{ECO:0000269|PubMed:15928335, ECO:0000269|PubMed:20972453,
ECO:0000269|PubMed:21224473}.
-!- SUBUNIT: Interacts with homodimeric PDGFA, PDGFB and PDGFC, and
with heterodimers formed by PDGFA and PDGFB. Monomer in the
absence of bound ligand. Interaction with dimeric PDGFA, PDGFB
and/or PDGFC leads to receptor dimerization, where both PDGFRA
homodimers and heterodimers with PDGFRB are observed. Interacts
(tyrosine phosphorylated) with SHB (via SH2 domain) (By
similarity). Interacts (tyrosine phosphorylated) with SHF (via SH2
domain). Interacts (tyrosine phosphorylated) with SRC (via SH2
domain). Interacts (tyrosine phosphorylated) with PIK3R1.
Interacts (tyrosine phosphorylated) with PLCG1 (via SH2 domain).
Interacts (tyrosine phosphorylated) with CRK, GRB2 and GRB7.
Interacts with human cytomegalovirus/HHV-5 envelop glycoprotein
B/gB. {ECO:0000250, ECO:0000269|PubMed:10733900,
ECO:0000269|PubMed:11095946, ECO:0000269|PubMed:11297552,
ECO:0000269|PubMed:11882663, ECO:0000269|PubMed:14644164,
ECO:0000269|PubMed:1646396, ECO:0000269|PubMed:1709159,
ECO:0000269|PubMed:20660204, ECO:0000269|PubMed:2173144,
ECO:0000269|PubMed:2536956, ECO:0000269|PubMed:2544881,
ECO:0000269|PubMed:7535778, ECO:0000269|PubMed:7679113,
ECO:0000269|PubMed:8940081, ECO:0000269|PubMed:8943348}.
-!- INTERACTION:
Q8N6L0:CCDC155; NbExp=3; IntAct=EBI-2861522, EBI-749265;
P46108:CRK; NbExp=4; IntAct=EBI-2861522, EBI-886;
P46109:CRKL; NbExp=3; IntAct=EBI-2861522, EBI-910;
P00533:EGFR; NbExp=3; IntAct=EBI-2861522, EBI-297353;
P04085:PDGFA; NbExp=6; IntAct=EBI-2861522, EBI-2881386;
P01127:PDGFB; NbExp=11; IntAct=EBI-2861522, EBI-1554925;
Q9NRA1:PDGFC; NbExp=2; IntAct=EBI-2861522, EBI-8833587;
Q9NRA1-1:PDGFC; NbExp=2; IntAct=EBI-15499330, EBI-15499301;
A8T7D5:UL55 (xeno); NbExp=2; IntAct=EBI-15499330, EBI-15722055;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14644164,
ECO:0000269|PubMed:2554309, ECO:0000269|PubMed:8188664}; Single-
pass type I membrane protein {ECO:0000269|PubMed:14644164,
ECO:0000269|PubMed:2554309, ECO:0000269|PubMed:8188664}. Note=The
activated receptor is rapidly internalized and degraded.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P16234-1; Sequence=Displayed;
Name=2;
IsoId=P16234-2; Sequence=VSP_007833, VSP_007834;
Note=No experimental confirmation available.;
Name=3;
IsoId=P16234-3; Sequence=VSP_042015, VSP_042016;
-!- TISSUE SPECIFICITY: Detected in platelets (at protein level).
Widely expressed. Detected in brain, fibroblasts, smooth muscle,
heart, and embryo. Expressed in primary and metastatic colon
tumors and in normal colon tissue. {ECO:0000269|PubMed:2536956,
ECO:0000269|PubMed:7896447, ECO:0000269|PubMed:8188664}.
-!- PTM: N-glycosylated.
-!- PTM: Ubiquitinated, leading to its degradation.
{ECO:0000305|PubMed:21596750}.
-!- PTM: Autophosphorylated on tyrosine residues upon ligand binding.
Autophosphorylation occurs in trans, i.e. one subunit of the
dimeric receptor phosphorylates tyrosine residues on the other
subunit. Phosphorylation at Tyr-731 and Tyr-742 is important for
interaction with PIK3R1. Phosphorylation at Tyr-720 and Tyr-754 is
important for interaction with PTPN11. Phosphorylation at Tyr-762
is important for interaction with CRK. Phosphorylation at Tyr-572
and Tyr-574 is important for interaction with SRC and SRC family
members. Phosphorylation at Tyr-988 and Tyr-1018 is important for
interaction with PLCG1. {ECO:0000269|PubMed:10733900,
ECO:0000269|PubMed:10734113, ECO:0000269|PubMed:11095946,
ECO:0000269|PubMed:1646396, ECO:0000269|PubMed:7535778,
ECO:0000269|PubMed:8943348}.
-!- DISEASE: Note=A chromosomal aberration involving PDGFRA is found
in some cases of hypereosinophilic syndrome. Interstitial
chromosomal deletion del(4)(q12q12) causes the fusion of FIP1L1
and PDGFRA (FIP1L1-PDGFRA). Mutations that cause overexpression
and/or constitutive activation of PDGFRA may be a cause of
hypereosinophilic syndrome. {ECO:0000269|PubMed:12808148}.
-!- DISEASE: Gastrointestinal stromal tumor (GIST) [MIM:606764]:
Common mesenchymal neoplasms arising in the gastrointestinal
tract, most often in the stomach. They are histologically,
immunohistochemically, and genetically different from typical
leiomyomas, leiomyosarcomas, and schwannomas. Most GISTs are
composed of a fairly uniform population of spindle-shaped cells.
Some tumors are dominated by epithelioid cells or contain a
mixture of spindle and epithelioid morphologies. Primary GISTs in
the gastrointestinal tract commonly metastasize in the omentum and
mesenteries, often as multiple nodules. However, primary tumors
may also occur outside of the gastrointestinal tract, in other
intra-abdominal locations, especially in the omentum and
mesentery. {ECO:0000269|PubMed:12522257,
ECO:0000269|PubMed:15928335}. Note=The gene represented in this
entry may be involved in disease pathogenesis. Mutations causing
PDGFRA constitutive activation have been found in gastrointestinal
stromal tumors lacking KIT mutations (PubMed:12522257).
{ECO:0000269|PubMed:12522257}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. CSF-1/PDGF receptor subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=AAP69563.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M22734; AAA60048.1; -; mRNA.
EMBL; M21574; AAA96715.1; -; mRNA.
EMBL; D50017; BAA08742.1; -; Genomic_DNA.
EMBL; AK316578; BAG38166.1; -; mRNA.
EMBL; AC098587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC138779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC015186; AAH15186.1; -; mRNA.
EMBL; BC063414; AAH63414.1; -; mRNA.
EMBL; AY229892; AAP69563.1; ALT_INIT; mRNA.
CCDS; CCDS3495.1; -. [P16234-1]
PIR; A40162; PFHUGA.
RefSeq; NP_001334758.1; NM_001347829.1. [P16234-1]
RefSeq; NP_006197.1; NM_006206.5. [P16234-1]
RefSeq; XP_005265800.1; XM_005265743.1. [P16234-1]
UniGene; Hs.74615; -.
PDB; 1GQ5; X-ray; 2.20 A; -.
PDB; 5GRN; X-ray; 1.77 A; A=550-973.
PDB; 5K5X; X-ray; 2.17 A; A=550-973.
PDBsum; 1GQ5; -.
PDBsum; 5GRN; -.
PDBsum; 5K5X; -.
ProteinModelPortal; P16234; -.
SMR; P16234; -.
BioGrid; 111182; 60.
CORUM; P16234; -.
DIP; DIP-5736N; -.
IntAct; P16234; 39.
MINT; MINT-4529366; -.
STRING; 9606.ENSP00000257290; -.
BindingDB; P16234; -.
ChEMBL; CHEMBL2007; -.
DrugBank; DB00102; Becaplermin.
DrugBank; DB00619; Imatinib.
DrugBank; DB05216; MP470.
DrugBank; DB06043; Olaratumab.
DrugBank; DB06589; Pazopanib.
DrugBank; DB08901; Ponatinib.
DrugBank; DB08896; Regorafenib.
DrugBank; DB01268; Sunitinib.
DrugBank; DB05146; XL820.
GuidetoPHARMACOLOGY; 1803; -.
iPTMnet; P16234; -.
PhosphoSitePlus; P16234; -.
BioMuta; PDGFRA; -.
DMDM; 129892; -.
MaxQB; P16234; -.
PaxDb; P16234; -.
PeptideAtlas; P16234; -.
PRIDE; P16234; -.
DNASU; 5156; -.
Ensembl; ENST00000257290; ENSP00000257290; ENSG00000134853. [P16234-1]
Ensembl; ENST00000508170; ENSP00000425648; ENSG00000134853. [P16234-2]
Ensembl; ENST00000509490; ENSP00000424218; ENSG00000134853. [P16234-3]
GeneID; 5156; -.
KEGG; hsa:5156; -.
UCSC; uc003hal.4; human. [P16234-1]
CTD; 5156; -.
DisGeNET; 5156; -.
EuPathDB; HostDB:ENSG00000134853.11; -.
GeneCards; PDGFRA; -.
HGNC; HGNC:8803; PDGFRA.
HPA; CAB018143; -.
HPA; HPA004947; -.
MalaCards; PDGFRA; -.
MIM; 173490; gene.
MIM; 606764; phenotype.
MIM; 607685; phenotype.
neXtProt; NX_P16234; -.
OpenTargets; ENSG00000134853; -.
Orphanet; 44890; Gastrointestinal stromal tumor.
Orphanet; 168947; Myeloid neoplasm associated with PDGFRA rearrangement.
Orphanet; 99860; Precursor B-cell acute lymphoblastic leukemia.
Orphanet; 314950; Primary hypereosinophilic syndrome.
PharmGKB; PA33147; -.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118923; -.
HOGENOM; HOG000112009; -.
HOVERGEN; HBG004335; -.
InParanoid; P16234; -.
KO; K04363; -.
OMA; CKDIKKC; -.
OrthoDB; EOG091G01TL; -.
PhylomeDB; P16234; -.
TreeFam; TF325768; -.
BRENDA; 2.7.10.1; 2681.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-186763; Downstream signal transduction.
Reactome; R-HSA-186797; Signaling by PDGF.
Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
SignaLink; P16234; -.
SIGNOR; P16234; -.
ChiTaRS; PDGFRA; human.
EvolutionaryTrace; P16234; -.
GeneWiki; PDGFRA; -.
GenomeRNAi; 5156; -.
PRO; PR:P16234; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000134853; -.
CleanEx; HS_PDGFRA; -.
ExpressionAtlas; P16234; baseline and differential.
Genevisible; P16234; HS.
GO; GO:0030054; C:cell junction; IDA:HPA.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; IDA:BHF-UCL.
GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005902; C:microvillus; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0043234; C:protein complex; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; TAS:Reactome.
GO; GO:0005018; F:platelet-derived growth factor alpha-receptor activity; IDA:UniProtKB.
GO; GO:0048407; F:platelet-derived growth factor binding; IDA:UniProtKB.
GO; GO:0005161; F:platelet-derived growth factor receptor binding; IPI:BHF-UCL.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0038085; F:vascular endothelial growth factor binding; IPI:BHF-UCL.
GO; GO:0005021; F:vascular endothelial growth factor-activated receptor activity; IDA:BHF-UCL.
GO; GO:0030325; P:adrenal gland development; IEA:Ensembl.
GO; GO:0055003; P:cardiac myofibril assembly; ISS:UniProtKB.
GO; GO:0001775; P:cell activation; TAS:BHF-UCL.
GO; GO:0060326; P:cell chemotaxis; IMP:UniProtKB.
GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
GO; GO:0034614; P:cellular response to reactive oxygen species; IDA:MGI.
GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; ISS:UniProtKB.
GO; GO:0048557; P:embryonic digestive tract morphogenesis; ISS:UniProtKB.
GO; GO:0048704; P:embryonic skeletal system morphogenesis; ISS:UniProtKB.
GO; GO:0008210; P:estrogen metabolic process; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
GO; GO:0060325; P:face morphogenesis; IEA:Ensembl.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
GO; GO:0033327; P:Leydig cell differentiation; IEA:Ensembl.
GO; GO:0030324; P:lung development; IEA:Ensembl.
GO; GO:0001553; P:luteinization; ISS:UniProtKB.
GO; GO:0030539; P:male genitalia development; IEA:Ensembl.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0072277; P:metanephric glomerular capillary formation; ISS:UniProtKB.
GO; GO:0010544; P:negative regulation of platelet activation; IDA:UniProtKB.
GO; GO:2000587; P:negative regulation of platelet-derived growth factor receptor-beta signaling pathway; TAS:Reactome.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
GO; GO:0060021; P:palate development; IEA:Ensembl.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IMP:UniProtKB.
GO; GO:0070527; P:platelet aggregation; IMP:UniProtKB.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0035790; P:platelet-derived growth factor receptor-alpha signaling pathway; IMP:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IDA:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0038091; P:positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:UniProtKB.
GO; GO:0045740; P:positive regulation of DNA replication; IDA:BHF-UCL.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:BHF-UCL.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IMP:UniProtKB.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; TAS:UniProtKB.
GO; GO:0010863; P:positive regulation of phospholipase C activity; IMP:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; TAS:UniProtKB.
GO; GO:0050920; P:regulation of chemotaxis; IMP:UniProtKB.
GO; GO:2000739; P:regulation of mesenchymal stem cell differentiation; IMP:UniProtKB.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; TAS:Reactome.
GO; GO:0061298; P:retina vasculature development in camera-type eye; ISS:UniProtKB.
GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IEA:Ensembl.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
GO; GO:0042060; P:wound healing; ISS:UniProtKB.
Gene3D; 2.60.40.10; -; 6.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR027290; PDGFRA.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
Pfam; PF07679; I-set; 2.
Pfam; PF07714; Pkinase_Tyr; 1.
PIRSF; PIRSF500950; Alpha-PDGF_receptor; 1.
SMART; SM00409; IG; 4.
SMART; SM00408; IGc2; 3.
SMART; SM00220; S_TKc; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF48726; SSF48726; 4.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS50835; IG_LIKE; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell membrane;
Chemotaxis; Complete proteome; Developmental protein; Disulfide bond;
Glycoprotein; Host-virus interaction; Immunoglobulin domain; Kinase;
Membrane; Nucleotide-binding; Phosphoprotein; Polymorphism;
Proto-oncogene; Receptor; Reference proteome; Repeat; Signal;
Transferase; Transmembrane; Transmembrane helix;
Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1 23
CHAIN 24 1089 Platelet-derived growth factor receptor
alpha.
/FTId=PRO_0000016760.
TOPO_DOM 24 528 Extracellular. {ECO:0000255}.
TRANSMEM 529 549 Helical. {ECO:0000255}.
TOPO_DOM 550 1089 Cytoplasmic. {ECO:0000255}.
DOMAIN 24 113 Ig-like C2-type 1.
DOMAIN 117 201 Ig-like C2-type 2.
DOMAIN 202 306 Ig-like C2-type 3.
DOMAIN 319 410 Ig-like C2-type 4.
DOMAIN 414 517 Ig-like C2-type 5.
DOMAIN 593 954 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 599 607 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COMPBIAS 1041 1087 Ser-rich.
ACT_SITE 818 818 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 627 627 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 578 579 Breakpoint for interstitial deletion to
form the FIP1L1-PDGFRA fusion protein.
MOD_RES 572 572 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:10734113}.
MOD_RES 574 574 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:10734113}.
MOD_RES 720 720 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:11095946,
ECO:0000269|PubMed:8943348}.
MOD_RES 731 731 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:1646396}.
MOD_RES 742 742 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:1646396}.
MOD_RES 754 754 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:17604334}.
MOD_RES 762 762 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:10733900}.
MOD_RES 768 768 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:8617789}.
MOD_RES 849 849 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
MOD_RES 988 988 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:7535778}.
MOD_RES 1018 1018 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:7535778}.
CARBOHYD 42 42 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 76 76 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 103 103 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 179 179 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 353 353 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 359 359 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 458 458 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 468 468 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 49 100 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 150 189 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 235 290 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 435 501 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 210 218 ATSELDLEM -> GTCIISFLL (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_007833.
VAR_SEQ 219 1089 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_007834.
VAR_SEQ 720 743 YVILSFENNGDYMDMKQADTTQYV -> SGQGCLSSGTLQE
LSVDLQARGPC (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_042015.
VAR_SEQ 744 1089 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_042016.
VARIANT 79 79 G -> D (in dbSNP:rs36035373).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042032.
VARIANT 426 426 G -> D (in dbSNP:rs55865821).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042033.
VARIANT 478 478 S -> P (in dbSNP:rs35597368).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_034378.
VARIANT 481 481 R -> G (in a hypereosinophilic syndrome
sample; does not lead to constitutive
kinase activation).
{ECO:0000269|PubMed:21224473}.
/FTId=VAR_066460.
VARIANT 507 507 L -> P (in a hypereosinophilic syndrome
sample; does not lead to constitutive
kinase activation).
{ECO:0000269|PubMed:21224473}.
/FTId=VAR_066461.
VARIANT 561 561 V -> D (in a GIST sample; constitutively
activated kinase; dbSNP:rs121908586).
{ECO:0000269|PubMed:12522257,
ECO:0000269|PubMed:15928335}.
/FTId=VAR_066462.
VARIANT 562 562 I -> M (in a hypereosinophilic syndrome
sample; does not lead to constitutive
kinase activation).
{ECO:0000269|PubMed:21224473}.
/FTId=VAR_066463.
VARIANT 570 570 H -> R (in a hypereosinophilic syndrome
sample; does not lead to constitutive
kinase activation).
{ECO:0000269|PubMed:21224473}.
/FTId=VAR_066464.
VARIANT 650 650 H -> Q (in a hypereosinophilic syndrome
sample; constitutively activated kinase).
{ECO:0000269|PubMed:21224473}.
/FTId=VAR_066465.
VARIANT 659 659 N -> K (in GIST sample; constitutively
activated kinase).
{ECO:0000269|PubMed:15928335}.
/FTId=VAR_066466.
VARIANT 659 659 N -> S (in a hypereosinophilic syndrome
sample; constitutively activated kinase).
{ECO:0000269|PubMed:21224473}.
/FTId=VAR_066467.
VARIANT 705 705 L -> P (in a hypereosinophilic syndrome
sample; does not lead to constitutive
kinase activation).
{ECO:0000269|PubMed:21224473}.
/FTId=VAR_066468.
VARIANT 748 748 R -> G (in a hypereosinophilic syndrome
sample; constitutively activated kinase).
{ECO:0000269|PubMed:21224473}.
/FTId=VAR_066469.
VARIANT 764 764 R -> C (in dbSNP:rs34392012).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042034.
VARIANT 829 829 G -> R (in a glioblastoma multiforme
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042035.
VARIANT 842 845 Missing (in a GIST sample; constitutively
activated kinase).
{ECO:0000269|PubMed:12522257,
ECO:0000269|PubMed:15928335}.
/FTId=VAR_066470.
VARIANT 842 842 D -> V (in a GIST sample; imatinib
resistant, constitutively activated
kinase; dbSNP:rs121908585).
{ECO:0000269|PubMed:12522257,
ECO:0000269|PubMed:15928335,
ECO:0000269|PubMed:20972453}.
/FTId=VAR_066471.
VARIANT 842 842 D -> Y (in a GIST sample; imatinib
sensitive, constitutively activated
kinase; dbSNP:rs121913265).
{ECO:0000269|PubMed:15928335}.
/FTId=VAR_066472.
VARIANT 845 848 Missing (in a GIST sample; constitutively
activated kinase).
{ECO:0000269|PubMed:12522257,
ECO:0000269|PubMed:15928335}.
/FTId=VAR_066473.
VARIANT 849 849 Y -> C (in GIST).
{ECO:0000269|PubMed:15928335}.
/FTId=VAR_066474.
VARIANT 849 849 Y -> S (in a hypereosinophilic syndrome
sample; constitutively activated kinase).
{ECO:0000269|PubMed:21224473}.
/FTId=VAR_066475.
VARIANT 996 996 E -> K (in a metastatic melanoma sample;
somatic mutation; dbSNP:rs779173667).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042036.
VARIANT 1071 1071 D -> N (in a lung neuroendocrine
carcinoma sample; somatic mutation;
dbSNP:rs376544204).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042037.
MUTAGEN 572 572 Y->F: Abolishes interaction with SRC-
family members and impairs
internalization of the activated
receptor; when associated with F-574.
{ECO:0000269|PubMed:10734113,
ECO:0000269|PubMed:14644164}.
MUTAGEN 574 574 Y->F: Abolishes interaction with SRC-
family members and impairs
internalization of the activated
receptor; when associated with F-572.
{ECO:0000269|PubMed:10734113,
ECO:0000269|PubMed:14644164}.
MUTAGEN 720 720 Y->F: Strongly reduced interaction with
PTPN11 and GRB2.
{ECO:0000269|PubMed:8943348}.
MUTAGEN 731 731 Y->F: No effect on autophosphorylation
and phosphorylation of PLCG1. Abolishes
activation of phosphatidylinositol 3-
kinase. {ECO:0000269|PubMed:1646396}.
MUTAGEN 742 742 Y->F: No effect on autophosphorylation
and phosphorylation of PLCG1. Abolishes
activation of phosphatidylinositol 3-
kinase. {ECO:0000269|PubMed:1646396}.
MUTAGEN 762 762 Y->F: Abolishes interaction with CRK.
{ECO:0000269|PubMed:10733900}.
STRAND 560 565 {ECO:0000244|PDB:5K5X}.
STRAND 572 574 {ECO:0000244|PDB:5K5X}.
HELIX 577 579 {ECO:0000244|PDB:5K5X}.
HELIX 584 586 {ECO:0000244|PDB:5K5X}.
HELIX 590 592 {ECO:0000244|PDB:5K5X}.
STRAND 593 601 {ECO:0000244|PDB:5K5X}.
STRAND 603 615 {ECO:0000244|PDB:5K5X}.
STRAND 620 629 {ECO:0000244|PDB:5K5X}.
HELIX 635 651 {ECO:0000244|PDB:5K5X}.
STRAND 660 664 {ECO:0000244|PDB:5K5X}.
STRAND 666 669 {ECO:0000244|PDB:5K5X}.
STRAND 671 675 {ECO:0000244|PDB:5K5X}.
HELIX 682 688 {ECO:0000244|PDB:5K5X}.
HELIX 774 776 {ECO:0000244|PDB:5K5X}.
HELIX 778 781 {ECO:0000244|PDB:5K5X}.
HELIX 792 811 {ECO:0000244|PDB:5K5X}.
HELIX 821 823 {ECO:0000244|PDB:5K5X}.
STRAND 824 827 {ECO:0000244|PDB:5K5X}.
TURN 828 830 {ECO:0000244|PDB:5K5X}.
STRAND 831 834 {ECO:0000244|PDB:5K5X}.
HELIX 838 840 {ECO:0000244|PDB:5K5X}.
HELIX 843 845 {ECO:0000244|PDB:5K5X}.
STRAND 850 852 {ECO:0000244|PDB:5K5X}.
STRAND 855 857 {ECO:0000244|PDB:5K5X}.
HELIX 859 861 {ECO:0000244|PDB:5K5X}.
HELIX 864 869 {ECO:0000244|PDB:5K5X}.
HELIX 874 889 {ECO:0000244|PDB:5K5X}.
HELIX 903 910 {ECO:0000244|PDB:5K5X}.
HELIX 923 932 {ECO:0000244|PDB:5K5X}.
HELIX 937 939 {ECO:0000244|PDB:5K5X}.
HELIX 943 951 {ECO:0000244|PDB:5K5X}.
HELIX 956 971 {ECO:0000244|PDB:5K5X}.
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


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