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TGF-beta receptor type-2 (TGFR-2) (EC 2.7.11.30) (TGF-beta type II receptor) (Transforming growth factor-beta receptor type II) (TGF-beta receptor type II) (TbetaR-II)

 TGFR2_HUMAN             Reviewed;         567 AA.
P37173; B4DTV5; Q15580; Q6DKT6; Q99474;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
30-AUG-2017, entry version 208.
RecName: Full=TGF-beta receptor type-2;
Short=TGFR-2;
EC=2.7.11.30;
AltName: Full=TGF-beta type II receptor;
AltName: Full=Transforming growth factor-beta receptor type II;
Short=TGF-beta receptor type II;
Short=TbetaR-II;
Flags: Precursor;
Name=TGFBR2;
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), VARIANT ALA-439, AND
SUBCELLULAR LOCATION.
TISSUE=Liver;
PubMed=1310899; DOI=10.1016/0092-8674(92)90152-3;
Lin H.Y., Wang X.-F., Ng-Eaton E., Weinberg R.A., Lodish H.F.;
"Expression cloning of the TGF-beta type II receptor, a functional
transmembrane serine/threonine kinase.";
Cell 68:775-785(1992).
[2]
ERRATUM.
PubMed=1525823;
Lin H.Y., Wang X.-F., Ng-Eaton E., Weinberg R.A., Lodish H.F.;
Cell 70:1069-1069(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Glial cell;
PubMed=7959019; DOI=10.1016/0378-1119(94)90178-3;
Nikawa J.;
"A cDNA encoding the human transforming growth factor beta receptor
suppresses the growth defect of a yeast mutant.";
Gene 149:367-372(1994).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANT ALA-439.
PubMed=8812462; DOI=10.1006/geno.1996.0471;
Takenoshita S., Hagiwara K., Nagashima M., Gemma A., Bennett W.P.,
Harris C.C.;
"The genomic structure of the gene encoding the human transforming
growth factor beta type II receptor (TGF-beta RII).";
Genomics 36:341-344(1996).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANT ALA-439.
PubMed=8840968;
Lu S.-L., Zhang W.C., Akiyama Y., Nomizu T., Yuasa Y.;
"Genomic structure of the transforming growth factor beta type II
receptor gene and its mutations in hereditary nonpolyposis colorectal
cancers.";
Cancer Res. 56:4595-4598(1996).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-439.
TISSUE=Liver;
PubMed=8973329; DOI=10.1016/S0378-1119(96)00501-X;
Ogasa H., Noma T., Murata H., Kawai S., Nakazawa A.;
"Cloning of a cDNA encoding the human transforming growth factor-beta
type II receptor: heterogeneity of the mRNA.";
Gene 181:185-190(1996).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-36.
NIEHS SNPs program;
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Placenta;
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).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
PROTEIN SEQUENCE OF 23-37.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[11]
FUNCTION IN PHOSPHORYLATION OF TGFBR1.
PubMed=7774578;
Wieser R., Wrana J.L., Massague J.;
"GS domain mutations that constitutively activate T beta R-I, the
downstream signaling component in the TGF-beta receptor complex.";
EMBO J. 14:2199-2208(1995).
[12]
INTERACTION WITH ZFYVE9.
PubMed=9865696; DOI=10.1016/S0092-8674(00)81701-8;
Tsukazaki T., Chiang T.A., Davison A.F., Attisano L., Wrana J.L.;
"SARA, a FYVE domain protein that recruits Smad2 to the TGFbeta
receptor.";
Cell 95:779-791(1998).
[13]
HOMODIMERIZATION.
PubMed=9472030; DOI=10.1083/jcb.140.4.767;
Gilboa L., Wells R.G., Lodish H.F., Henis Y.I.;
"Oligomeric structure of type I and type II transforming growth factor
beta receptors: homodimers form in the ER and persist at the plasma
membrane.";
J. Cell Biol. 140:767-777(1998).
[14]
INTERACTION WITH DAXX, AND MUTAGENESIS OF LYS-277.
PubMed=11483955; DOI=10.1038/35087019;
Perlman R., Schiemann W.P., Brooks M.W., Lodish H.F., Weinberg R.A.;
"TGF-beta-induced apoptosis is mediated by the adapter protein Daxx
that facilitates JNK activation.";
Nat. Cell Biol. 3:708-714(2001).
[15]
INTERACTION WITH VPS39.
PubMed=12941698; DOI=10.1093/emboj/cdg428;
Felici A., Wurthner J.U., Parks W.T., Giam L.R., Reiss M.,
Karpova T.S., McNally J.G., Roberts A.B.;
"TLP, a novel modulator of TGF-beta signaling, has opposite effects on
Smad2- and Smad3-dependent signaling.";
EMBO J. 22:4465-4477(2003).
[16]
INTERACTION WITH TCTEX1D4.
PubMed=16982625; DOI=10.1074/jbc.M608614200;
Meng Q.-J., Lux A., Holloschi A., Li J., Hughes J.M.X., Foerg T.,
McCarthy J.E.G., Heagerty A.M., Kioschis P., Hafner M., Garland J.M.;
"Identification of Tctex2beta, a novel dynein light chain family
member that interacts with different transforming growth factor-beta
receptors.";
J. Biol. Chem. 281:37069-37080(2006).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[19]
INTERACTION WITH SCUBE3.
PubMed=21441952; DOI=10.1038/onc.2011.85;
Wu Y.Y., Peck K., Chang Y.L., Pan S.H., Cheng Y.F., Lin J.C.,
Yang R.B., Hong T.M., Yang P.C.;
"SCUBE3 is an endogenous TGF-beta receptor ligand and regulates the
epithelial-mesenchymal transition in lung cancer.";
Oncogene 30:3682-3693(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[22]
SUBCELLULAR LOCATION.
PubMed=25893292; DOI=10.1038/onc.2015.100;
Hwangbo C., Tae N., Lee S., Kim O., Park O.K., Kim J., Kwon S.H.,
Lee J.H.;
"Syntenin regulates TGF-beta1-induced Smad activation and the
epithelial-to-mesenchymal transition by inhibiting caveolin-mediated
TGF-beta type I receptor internalization.";
Oncogene 35:389-401(2016).
[23]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 38-159 IN COMPLEX WITH
TGF-BETA3, AND DISULFIDE BONDS.
PubMed=11850637; DOI=10.1038/nsb766;
Hart P.J., Deep S., Taylor A.B., Shu Z., Hinck C.S., Hinck A.P.;
"Crystal structure of the human TbetaR2 ectodomain--TGF-beta3
complex.";
Nat. Struct. Biol. 9:203-208(2002).
[24]
X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF 49-159, AND DISULFIDE BONDS.
PubMed=12121646; DOI=10.1016/S0969-2126(02)00780-3;
Boesen C.C., Radaev S., Motyka S.A., Patamawenu A., Sun P.D.;
"The 1.1 A crystal structure of human TGF-beta type II receptor ligand
binding domain.";
Structure 10:913-919(2002).
[25]
STRUCTURE BY NMR OF 38-159, AND DISULFIDE BONDS.
PubMed=12939140; DOI=10.1021/bi034366a;
Deep S., Walker K.P. III, Shu Z., Hinck A.P.;
"Solution structure and backbone dynamics of the TGFbeta type II
receptor extracellular domain.";
Biochemistry 42:10126-10139(2003).
[26]
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 43-149 IN COMPLEX WITH
TGFBR1 AND TGFB3, AND DISULFIDE BONDS.
PubMed=18243111; DOI=10.1016/j.molcel.2007.11.039;
Groppe J., Hinck C.S., Samavarchi-Tehrani P., Zubieta C.,
Schuermann J.P., Taylor A.B., Schwarz P.M., Wrana J.L., Hinck A.P.;
"Cooperative assembly of TGF-beta superfamily signaling complexes is
mediated by two disparate mechanisms and distinct modes of receptor
binding.";
Mol. Cell 29:157-168(2008).
[27]
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 38-153 IN COMPLEX WITH
TGFBR1 AND TGFB1, RECEPTOR AFFINITY FOR LIGANDS, AND DISULFIDE BONDS.
PubMed=20207738; DOI=10.1074/jbc.M109.079921;
Radaev S., Zou Z., Huang T., Lafer E.M., Hinck A.P., Sun P.D.;
"Ternary complex of transforming growth factor-beta1 reveals isoform-
specific ligand recognition and receptor recruitment in the
superfamily.";
J. Biol. Chem. 285:14806-14814(2010).
[28]
VARIANT HNPCC6 MET-315.
PubMed=9590282; DOI=10.1038/ng0598-17;
Lu S.-L., Kawabata M., Imamura T., Akiyama Y., Nomizu T., Miyazono K.,
Yuasa Y.;
"HNPCC associated with germline mutation in the TGF-beta type II
receptor gene.";
Nat. Genet. 19:17-18(1998).
[29]
VARIANT ESOPHAGEAL CANCER GLN-526.
PubMed=10789724; DOI=10.1054/bjoc.1999.1178;
Tanaka S., Mori M., Mafune K., Ohno S., Sugimachi K.;
"A dominant negative mutation of transforming growth factor-beta
receptor type II gene in microsatellite stable oesophageal
carcinoma.";
Br. J. Cancer 82:1557-1560(2000).
[30]
VARIANTS BREAST TUMOR MET-387; SER-435; ALA-447 AND MET-452, AND
CHARACTERIZATION OF VARIANTS BREAST TUMOR SER-435; ALA-447 AND
MET-452.
PubMed=11212236;
Luecke C.D., Philpott A., Metcalfe J.C., Thompson A.M.,
Hughes-Davies L., Kemp P.R., Hesketh R.;
"Inhibiting mutations in the transforming growth factor beta type 2
receptor in recurrent human breast cancer.";
Cancer Res. 61:482-485(2001).
[31]
VARIANT ILE-191.
PubMed=12202987; DOI=10.1007/s100380200069;
Watanabe Y., Kinoshita A., Yamada T., Ohta T., Kishino T.,
Matsumoto N., Ishikawa M., Niikawa N., Yoshiura K.;
"A catalog of 106 single-nucleotide polymorphisms (SNPs) and 11 other
types of variations in genes for transforming growth factor-beta1
(TGF-beta1) and its signaling pathway.";
J. Hum. Genet. 47:478-483(2002).
[32]
VARIANTS LDS2 PRO-308; PHE-449 AND CYS-537, AND CHARACTERIZATION OF
VARIANTS LDS2 PRO-308; PHE-449 AND CYS-537.
PubMed=15235604; DOI=10.1038/ng1392;
Mizuguchi T., Collod-Beroud G., Akiyama T., Abifadel M., Harada N.,
Morisaki T., Allard D., Varret M., Claustres M., Morisaki H.,
Ihara M., Kinoshita A., Yoshiura K., Junien C., Kajii T., Jondeau G.,
Ohta T., Kishino T., Furukawa Y., Nakamura Y., Niikawa N., Boileau C.,
Matsumoto N.;
"Heterozygous TGFBR2 mutations in Marfan syndrome.";
Nat. Genet. 36:855-860(2004).
[33]
VARIANTS LDS2 CYS-460 AND HIS-460.
PubMed=16027248; DOI=10.1161/CIRCULATIONAHA.105.537340;
Pannu H., Fadulu V.T., Chang J., Lafont A., Hasham S.N., Sparks E.,
Giampietro P.F., Zaleski C., Estrera A.L., Safi H.J., Shete S.,
Willing M.C., Raman C.S., Milewicz D.M.;
"Mutations in transforming growth factor-beta receptor type II cause
familial thoracic aortic aneurysms and dissections.";
Circulation 112:513-520(2005).
[34]
VARIANTS LDS2 ASN-336; PRO-355; TRP-357; HIS-528 AND CYS-528.
PubMed=15731757; DOI=10.1038/ng1511;
Loeys B.L., Chen J., Neptune E.R., Judge D.P., Podowski M., Holm T.,
Meyers J., Leitch C.C., Katsanis N., Sharifi N., Xu F.L., Myers L.A.,
Spevak P.J., Cameron D.E., De Backer J.F., Hellemans J., Chen Y.,
Davis E.C., Webb C.L., Kress W., Coucke P.J., Rifkin D.B.,
De Paepe A.M., Dietz H.C.;
"A syndrome of altered cardiovascular, craniofacial, neurocognitive
and skeletal development caused by mutations in TGFBR1 or TGFBR2.";
Nat. Genet. 37:275-281(2005).
[35]
VARIANT LDS2 ASN-446.
PubMed=16251899; DOI=10.1038/sj.ejhg.5201502;
Disabella E., Grasso M., Marziliano N., Ansaldi S., Lucchelli C.,
Porcu E., Tagliani M., Pilotto A., Diegoli M., Lanzarini L.,
Malattia C., Pelliccia A., Ficcadenti A., Gabrielli O., Arbustini E.;
"Two novel and one known mutation of the TGFBR2 gene in Marfan
syndrome not associated with FBN1 gene defects.";
Eur. J. Hum. Genet. 14:34-38(2006).
[36]
VARIANTS [LARGE SCALE ANALYSIS] VAL-73 AND HIS-528.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[37]
VARIANTS [LARGE SCALE ANALYSIS] ARG-61; ILE-191; MET-315; TYR-328;
ILE-373; MET-387 AND SER-490.
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).
[38]
VARIANTS LDS2 HIS-190; VAL-247; PRO-325; ARG-357 AND ILE-530.
PubMed=19533785; DOI=10.1002/ajmg.a.32918;
Chung B.H., Lam S.T., Tong T.M., Li S.Y., Lun K.S., Chan D.H.,
Fok S.F., Or J.S., Smith D.K., Yang W., Lau Y.L.;
"Identification of novel FBN1 and TGFBR2 mutations in 65 probands with
Marfan syndrome or Marfan-like phenotypes.";
Am. J. Med. Genet. A 149A:1452-1459(2009).
[39]
VARIANT LDS2 SER-510.
PubMed=19883511; DOI=10.1186/1750-1172-4-24;
Drera B., Ritelli M., Zoppi N., Wischmeijer A., Gnoli M., Fattori R.,
Calzavara-Pinton P.G., Barlati S., Colombi M.;
"Loeys-Dietz syndrome type I and type II: clinical findings and novel
mutations in two Italian patients.";
Orphanet J. Rare Dis. 4:24-24(2009).
[40]
VARIANT LDS2 LYS-457.
PubMed=20101701; DOI=10.1002/ajmg.a.33263;
Muramatsu Y., Kosho T., Magota M., Yokotsuka T., Ito M., Yasuda A.,
Kito O., Suzuki C., Nagata Y., Kawai S., Ikoma M., Hatano T.,
Nakayama M., Kawamura R., Wakui K., Morisaki H., Morisaki T.,
Fukushima Y.;
"Progressive aortic root and pulmonary artery aneurysms in a neonate
with Loeys-Dietz syndrome type 1B.";
Am. J. Med. Genet. A 152:417-421(2010).
[41]
VARIANTS LDS2 PRO-308 AND ARG-521.
PubMed=20358619; DOI=10.1002/ajmg.a.33356;
Kirmani S., Tebben P.J., Lteif A.N., Gordon D., Clarke B.L.,
Hefferan T.E., Yaszemski M.J., McGrann P.S., Lindor N.M.,
Ellison J.W.;
"Germline TGF-beta receptor mutations and skeletal fragility: a report
on two patients with Loeys-Dietz syndrome.";
Am. J. Med. Genet. A 152:1016-1019(2010).
[42]
VARIANTS LDS2 GLN-306 DELINS HIS-GLU; ARG-377; PHE-449 AND ARG-514.
PubMed=22113417; DOI=10.1038/jhg.2011.130;
Yang J.H., Ki C.S., Han H., Song B.G., Jang S.Y., Chung T.Y., Sung K.,
Lee H.J., Kim D.K.;
"Clinical features and genetic analysis of Korean patients with Loeys-
Dietz syndrome.";
J. Hum. Genet. 57:52-56(2012).
[43]
VARIANTS LDS2 VAL-509 AND PHE-510.
PubMed=21949523; DOI=10.3345/kjp.2011.54.6.272;
Ha J.S., Kim Y.H.;
"A sporadic case of Loeys-Dietz syndrome type I with two novel
mutations of the TGFBR2 gene.";
Korean J. Pediatr. 54:272-275(2011).
-!- FUNCTION: Transmembrane serine/threonine kinase forming with the
TGF-beta type I serine/threonine kinase receptor, TGFBR1, the non-
promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and
TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell
surface to the cytoplasm and is thus regulating a plethora of
physiological and pathological processes including cell cycle
arrest in epithelial and hematopoietic cells, control of
mesenchymal cell proliferation and differentiation, wound healing,
extracellular matrix production, immunosuppression and
carcinogenesis. The formation of the receptor complex composed of
2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the
cytokine dimer results in the phosphorylation and the activation
of TGFRB1 by the constitutively active TGFBR2. Activated TGFBR1
phosphorylates SMAD2 which dissociates from the receptor and
interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently
translocated to the nucleus where it modulates the transcription
of the TGF-beta-regulated genes. This constitutes the canonical
SMAD-dependent TGF-beta signaling cascade. Also involved in non-
canonical, SMAD-independent TGF-beta signaling pathways.
{ECO:0000269|PubMed:7774578}.
-!- CATALYTIC ACTIVITY: ATP + [receptor-protein] = ADP + [receptor-
protein] phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- SUBUNIT: Homodimer. Heterohexamer; TGFB1, TGFB2 and TGFB3
homodimeric ligands assemble a functional receptor composed of two
TGFBR1 and TGFBR2 heterodimers to form a ligand-receptor
heterohexamer. The respective affinity of TGFRB1 and TGFRB2 for
the ligands may modulate the kinetics of assembly of the receptor
and may explain the different biological activities of TGFB1,
TGFB2 and TGFB3. Interacts with DAXX. Interacts with TCTEX1D4.
Interacts with ZFYVE9; ZFYVE9 recruits SMAD2 and SMAD3 to the TGF-
beta receptor. Interacts with and is activated by SCUBE3; this
interaction does not affect TGFB1-binding to TGFBR2. Interacts
with VPS39; this interaction is independent of the receptor kinase
activity and of the presence of TGF-beta.
{ECO:0000269|PubMed:11483955, ECO:0000269|PubMed:11850637,
ECO:0000269|PubMed:12941698, ECO:0000269|PubMed:16982625,
ECO:0000269|PubMed:18243111, ECO:0000269|PubMed:20207738,
ECO:0000269|PubMed:21441952, ECO:0000269|PubMed:9865696}.
-!- INTERACTION:
Q9UER7:DAXX; NbExp=2; IntAct=EBI-296151, EBI-77321;
Q93074:MED12; NbExp=3; IntAct=EBI-296151, EBI-394357;
A2AGH6:Med12 (xeno); NbExp=3; IntAct=EBI-296151, EBI-5744969;
Q8IX30:SCUBE3; NbExp=6; IntAct=EBI-296151, EBI-4479975;
P01137:TGFB1; NbExp=6; IntAct=EBI-296151, EBI-779636;
P07200:TGFB1 (xeno); NbExp=2; IntAct=EBI-296151, EBI-907660;
P10600:TGFB3; NbExp=8; IntAct=EBI-296151, EBI-1033020;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1310899,
ECO:0000269|PubMed:25893292}; Single-pass type I membrane protein
{ECO:0000269|PubMed:1310899}. Membrane raft
{ECO:0000269|PubMed:25893292}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P37173-1; Sequence=Displayed;
Name=2;
IsoId=P37173-2; Sequence=VSP_012157;
-!- PTM: Phosphorylated on a Ser/Thr residue in the cytoplasmic
domain.
-!- DISEASE: Hereditary non-polyposis colorectal cancer 6 (HNPCC6)
[MIM:614331]: An autosomal dominant disease associated with marked
increase in cancer susceptibility. It is characterized by a
familial predisposition to early-onset colorectal carcinoma (CRC)
and extra-colonic tumors of the gastrointestinal, urological and
female reproductive tracts. HNPCC is reported to be the most
common form of inherited colorectal cancer in the Western world.
Clinically, HNPCC is often divided into two subgroups. Type I is
characterized by hereditary predisposition to colorectal cancer, a
young age of onset, and carcinoma observed in the proximal colon.
Type II is characterized by increased risk for cancers in certain
tissues such as the uterus, ovary, breast, stomach, small
intestine, skin, and larynx in addition to the colon. Diagnosis of
classical HNPCC is based on the Amsterdam criteria: 3 or more
relatives affected by colorectal cancer, one a first degree
relative of the other two; 2 or more generation affected; 1 or
more colorectal cancers presenting before 50 years of age;
exclusion of hereditary polyposis syndromes. The term 'suspected
HNPCC' or 'incomplete HNPCC' can be used to describe families who
do not or only partially fulfill the Amsterdam criteria, but in
whom a genetic basis for colon cancer is strongly suspected.
{ECO:0000269|PubMed:9590282}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Esophageal cancer (ESCR) [MIM:133239]: A malignancy of
the esophagus. The most common types are esophageal squamous cell
carcinoma and adenocarcinoma. Cancer of the esophagus remains a
devastating disease because it is usually not detected until it
has progressed to an advanced incurable stage.
{ECO:0000269|PubMed:10789724}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Loeys-Dietz syndrome 2 (LDS2) [MIM:610168]: An aortic
aneurysm syndrome with widespread systemic involvement,
characterized by arterial tortuosity and aneurysms, hypertelorism,
and bifid uvula or cleft palate. Physical findings include
prominent joint laxity, easy bruising, wide and atrophic scars,
velvety and translucent skin with easily visible veins,
spontaneous rupture of the spleen or bowel, and catastrophic
complications of pregnancy, including rupture of the gravid uterus
and the arteries, either during pregnancy or in the immediate
postpartum period. Some patients have craniosynostosis, exotropy,
micrognathia and retrognathia, structural brain abnormalities, and
intellectual deficit. {ECO:0000269|PubMed:15235604,
ECO:0000269|PubMed:15731757, ECO:0000269|PubMed:16027248,
ECO:0000269|PubMed:16251899, ECO:0000269|PubMed:19533785,
ECO:0000269|PubMed:19883511, ECO:0000269|PubMed:20101701,
ECO:0000269|PubMed:20358619, ECO:0000269|PubMed:21949523,
ECO:0000269|PubMed:22113417}. Note=The disease is caused by
mutations affecting the gene represented in this entry. TGFBR2
mutations Cys-460 and His-460 have been reported to be associated
with thoracic aortic aneurysms and dissection (TAAD). This
phenotype, also known as thoracic aortic aneurysms type 3 (AAT3),
is distinguised from LDS2 by having aneurysms restricted to
thoracic aorta. As individuals carrying these mutations also
exhibit descending aortic disease and aneurysms of other arteries
(PubMed:16027248), they have been considered as LDS2 by the OMIM
resource. {ECO:0000269|PubMed:16027248}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/tgfbr2/";
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M85079; AAA61164.1; -; mRNA.
EMBL; D28131; BAA05673.1; -; mRNA.
EMBL; U52246; AAB17553.1; -; Genomic_DNA.
EMBL; U52240; AAB17553.1; JOINED; Genomic_DNA.
EMBL; U52241; AAB17553.1; JOINED; Genomic_DNA.
EMBL; U52242; AAB17553.1; JOINED; Genomic_DNA.
EMBL; U52244; AAB17553.1; JOINED; Genomic_DNA.
EMBL; U52245; AAB17553.1; JOINED; Genomic_DNA.
EMBL; U69152; AAB40916.1; -; Genomic_DNA.
EMBL; U69146; AAB40916.1; JOINED; Genomic_DNA.
EMBL; U69147; AAB40916.1; JOINED; Genomic_DNA.
EMBL; U69148; AAB40916.1; JOINED; Genomic_DNA.
EMBL; U69149; AAB40916.1; JOINED; Genomic_DNA.
EMBL; U69150; AAB40916.1; JOINED; Genomic_DNA.
EMBL; U69151; AAB40916.1; JOINED; Genomic_DNA.
EMBL; D50683; BAA09332.1; -; mRNA.
EMBL; AY675319; AAT70724.1; -; Genomic_DNA.
EMBL; AK300383; BAG62117.1; -; mRNA.
EMBL; CH471055; EAW64412.1; -; Genomic_DNA.
CCDS; CCDS2648.1; -. [P37173-1]
CCDS; CCDS33727.1; -. [P37173-2]
PIR; A42100; A42100.
RefSeq; NP_001020018.1; NM_001024847.2. [P37173-2]
RefSeq; NP_003233.4; NM_003242.5. [P37173-1]
UniGene; Hs.604277; -.
UniGene; Hs.82028; -.
PDB; 1KTZ; X-ray; 2.15 A; B=38-159.
PDB; 1M9Z; X-ray; 1.05 A; A=49-159.
PDB; 1PLO; NMR; -; A=38-159.
PDB; 2PJY; X-ray; 3.00 A; B=42-149.
PDB; 3KFD; X-ray; 3.00 A; E/F/G/H=38-153.
PDB; 4P7U; X-ray; 1.50 A; A=49-159.
PDB; 4XJJ; X-ray; 1.40 A; A=50-159.
PDB; 5E8V; X-ray; 1.69 A; A=237-549.
PDB; 5E8Y; X-ray; 2.05 A; A=237-549.
PDB; 5E91; X-ray; 2.42 A; A=237-549.
PDB; 5E92; X-ray; 2.08 A; A=237-549.
PDB; 5TX4; X-ray; 1.88 A; A=38-153.
PDB; 5TY4; EM; 2.90 A; A=47-149.
PDBsum; 1KTZ; -.
PDBsum; 1M9Z; -.
PDBsum; 1PLO; -.
PDBsum; 2PJY; -.
PDBsum; 3KFD; -.
PDBsum; 4P7U; -.
PDBsum; 4XJJ; -.
PDBsum; 5E8V; -.
PDBsum; 5E8Y; -.
PDBsum; 5E91; -.
PDBsum; 5E92; -.
PDBsum; 5TX4; -.
PDBsum; 5TY4; -.
ProteinModelPortal; P37173; -.
SMR; P37173; -.
BioGrid; 112906; 86.
DIP; DIP-5939N; -.
IntAct; P37173; 26.
MINT; MINT-206666; -.
STRING; 9606.ENSP00000351905; -.
BindingDB; P37173; -.
ChEMBL; CHEMBL4267; -.
DrugBank; DB04077; Glycerol.
GuidetoPHARMACOLOGY; 1795; -.
iPTMnet; P37173; -.
PhosphoSitePlus; P37173; -.
BioMuta; TGFBR2; -.
DMDM; 116242818; -.
MaxQB; P37173; -.
PaxDb; P37173; -.
PeptideAtlas; P37173; -.
PRIDE; P37173; -.
DNASU; 7048; -.
Ensembl; ENST00000295754; ENSP00000295754; ENSG00000163513. [P37173-1]
Ensembl; ENST00000359013; ENSP00000351905; ENSG00000163513. [P37173-2]
GeneID; 7048; -.
KEGG; hsa:7048; -.
UCSC; uc003cen.4; human. [P37173-1]
CTD; 7048; -.
DisGeNET; 7048; -.
GeneCards; TGFBR2; -.
GeneReviews; TGFBR2; -.
H-InvDB; HIX0024332; -.
HGNC; HGNC:11773; TGFBR2.
HPA; CAB073537; -.
MalaCards; TGFBR2; -.
MIM; 133239; phenotype.
MIM; 190182; gene.
MIM; 610168; phenotype.
MIM; 614331; phenotype.
neXtProt; NX_P37173; -.
OpenTargets; ENSG00000163513; -.
Orphanet; 91387; Familial thoracic aortic aneurysm and aortic dissection.
Orphanet; 144; Hereditary nonpolyposis colon cancer.
Orphanet; 60030; Loeys-Dietz syndrome.
Orphanet; 284973; Marfan syndrome type 2.
PharmGKB; PA36486; -.
eggNOG; KOG3653; Eukaryota.
eggNOG; ENOG410XS2Z; LUCA.
GeneTree; ENSGT00760000118876; -.
HOGENOM; HOG000231495; -.
HOVERGEN; HBG104975; -.
InParanoid; P37173; -.
KO; K04388; -.
OMA; NDMMVTD; -.
PhylomeDB; P37173; -.
TreeFam; TF314724; -.
BRENDA; 2.7.10.2; 2681.
Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling.
Reactome; R-HSA-2173789; TGF-beta receptor signaling activates SMADs.
Reactome; R-HSA-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
Reactome; R-HSA-3304356; SMAD2/3 Phosphorylation Motif Mutants in Cancer.
Reactome; R-HSA-3315487; SMAD2/3 MH2 Domain Mutants in Cancer.
Reactome; R-HSA-3642279; TGFBR2 MSI Frameshift Mutants in Cancer.
Reactome; R-HSA-3645790; TGFBR2 Kinase Domain Mutants in Cancer.
Reactome; R-HSA-3656532; TGFBR1 KD Mutants in Cancer.
Reactome; R-HSA-3656535; TGFBR1 LBD Mutants in Cancer.
Reactome; R-HSA-5689603; UCH proteinases.
SignaLink; P37173; -.
SIGNOR; P37173; -.
ChiTaRS; TGFBR2; human.
EvolutionaryTrace; P37173; -.
GeneWiki; TGF_beta_receptor_2; -.
GenomeRNAi; 7048; -.
PRO; PR:P37173; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000163513; -.
CleanEx; HS_TGFBR2; -.
ExpressionAtlas; P37173; baseline and differential.
Genevisible; P37173; HS.
GO; GO:0005901; C:caveola; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
GO; GO:0016021; C:integral component of membrane; IDA:BHF-UCL.
GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0043235; C:receptor complex; IDA:BHF-UCL.
GO; GO:0070022; C:transforming growth factor beta receptor complex; IC:BHF-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005539; F:glycosaminoglycan binding; IDA:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IEA:Ensembl.
GO; GO:0004702; F:signal transducer, downstream of receptor, with serine/threonine kinase activity; IEA:InterPro.
GO; GO:0046332; F:SMAD binding; IDA:BHF-UCL.
GO; GO:0050431; F:transforming growth factor beta binding; IDA:BHF-UCL.
GO; GO:0005026; F:transforming growth factor beta receptor activity, type II; IEA:Ensembl.
GO; GO:0005024; F:transforming growth factor beta-activated receptor activity; IDA:BHF-UCL.
GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IDA:BHF-UCL.
GO; GO:0034713; F:type I transforming growth factor beta receptor binding; IDA:BHF-UCL.
GO; GO:0034714; F:type III transforming growth factor beta receptor binding; IDA:BHF-UCL.
GO; GO:0032147; P:activation of protein kinase activity; ISS:BHF-UCL.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
GO; GO:0003181; P:atrioventricular valve morphogenesis; ISS:BHF-UCL.
GO; GO:0001568; P:blood vessel development; TAS:BHF-UCL.
GO; GO:0007420; P:brain development; ISS:BHF-UCL.
GO; GO:0001569; P:branching involved in blood vessel morphogenesis; ISS:BHF-UCL.
GO; GO:0060434; P:bronchus morphogenesis; IEA:Ensembl.
GO; GO:0003214; P:cardiac left ventricle morphogenesis; ISS:BHF-UCL.
GO; GO:0007182; P:common-partner SMAD protein phosphorylation; IEA:Ensembl.
GO; GO:0048565; P:digestive tract development; IEA:Ensembl.
GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; ISS:BHF-UCL.
GO; GO:0035162; P:embryonic hemopoiesis; ISS:BHF-UCL.
GO; GO:0003274; P:endocardial cushion fusion; ISS:BHF-UCL.
GO; GO:0007369; P:gastrulation; IEA:Ensembl.
GO; GO:0003430; P:growth plate cartilage chondrocyte growth; IEA:Ensembl.
GO; GO:0007507; P:heart development; ISS:BHF-UCL.
GO; GO:0001947; P:heart looping; ISS:BHF-UCL.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:1905317; P:inferior endocardial cushion morphogenesis; ISS:BHF-UCL.
GO; GO:0002088; P:lens development in camera-type eye; IEA:Ensembl.
GO; GO:1990086; P:lens fiber cell apoptotic process; IEA:Ensembl.
GO; GO:0060463; P:lung lobe morphogenesis; IEA:Ensembl.
GO; GO:0060443; P:mammary gland morphogenesis; IEA:Ensembl.
GO; GO:0003149; P:membranous septum morphogenesis; ISS:BHF-UCL.
GO; GO:0043011; P:myeloid dendritic cell differentiation; ISS:BHF-UCL.
GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; IEA:Ensembl.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; TAS:Reactome.
GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
GO; GO:0003151; P:outflow tract morphogenesis; ISS:BHF-UCL.
GO; GO:0003148; P:outflow tract septum morphogenesis; ISS:BHF-UCL.
GO; GO:0060021; P:palate development; ISS:BHF-UCL.
GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:BHF-UCL.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:BHF-UCL.
GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
GO; GO:0002663; P:positive regulation of B cell tolerance induction; ISS:BHF-UCL.
GO; GO:2000563; P:positive regulation of CD4-positive, alpha-beta T cell proliferation; IDA:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
GO; GO:0010634; P:positive regulation of epithelial cell migration; IEA:Ensembl.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IDA:BHF-UCL.
GO; GO:1905007; P:positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation; ISS:BHF-UCL.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; ISS:BHF-UCL.
GO; GO:0051138; P:positive regulation of NK T cell differentiation; ISS:BHF-UCL.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IMP:BHF-UCL.
GO; GO:0043415; P:positive regulation of skeletal muscle tissue regeneration; IEA:Ensembl.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0002666; P:positive regulation of T cell tolerance induction; ISS:BHF-UCL.
GO; GO:0002651; P:positive regulation of tolerance induction to self antigen; ISS:BHF-UCL.
GO; GO:0006468; P:protein phosphorylation; IDA:BHF-UCL.
GO; GO:0006898; P:receptor-mediated endocytosis; IEA:Ensembl.
GO; GO:0042127; P:regulation of cell proliferation; ISS:BHF-UCL.
GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
GO; GO:0070723; P:response to cholesterol; IDA:BHF-UCL.
GO; GO:0042493; P:response to drug; IDA:BHF-UCL.
GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
GO; GO:0009749; P:response to glucose; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0048545; P:response to steroid hormone; IEA:Ensembl.
GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
GO; GO:0060440; P:trachea formation; IEA:Ensembl.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0003186; P:tricuspid valve morphogenesis; ISS:BHF-UCL.
GO; GO:0001570; P:vasculogenesis; ISS:BHF-UCL.
GO; GO:0060412; P:ventricular septum morphogenesis; ISS:BHF-UCL.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR000333; TGFB_receptor.
InterPro; IPR017194; Transform_growth_fac-b_typ-2.
InterPro; IPR015013; Transforming_GF_b_rcpt_2_ecto.
PANTHER; PTHR23255; PTHR23255; 1.
Pfam; PF08917; ecTbetaR2; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
PIRSF; PIRSF037393; TGFRII; 1.
PRINTS; PR00653; ACTIVIN2R.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Aortic aneurysm; Apoptosis;
ATP-binding; Cell membrane; Complete proteome; Differentiation;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; Growth regulation;
Hereditary nonpolyposis colorectal cancer; Kinase; Magnesium;
Manganese; Membrane; Metal-binding; Nucleotide-binding;
Phosphoprotein; Polymorphism; Receptor; Reference proteome;
Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
Transmembrane helix.
SIGNAL 1 22 {ECO:0000269|PubMed:15340161}.
CHAIN 23 567 TGF-beta receptor type-2.
/FTId=PRO_0000024426.
TOPO_DOM 23 166 Extracellular. {ECO:0000255}.
TRANSMEM 167 187 Helical. {ECO:0000255}.
TOPO_DOM 188 567 Cytoplasmic. {ECO:0000255}.
DOMAIN 244 544 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 250 258 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 379 379 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 277 277 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 409 409 Phosphoserine.
{ECO:0000250|UniProtKB:Q62312}.
MOD_RES 548 548 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 553 553 Phosphoserine.
{ECO:0000250|UniProtKB:Q62312}.
CARBOHYD 70 70 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 94 94 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 154 154 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 51 84 {ECO:0000269|PubMed:11850637,
ECO:0000269|PubMed:12121646,
ECO:0000269|PubMed:12939140,
ECO:0000269|PubMed:18243111,
ECO:0000269|PubMed:20207738}.
DISULFID 54 71 {ECO:0000269|PubMed:11850637,
ECO:0000269|PubMed:12121646,
ECO:0000269|PubMed:12939140,
ECO:0000269|PubMed:18243111,
ECO:0000269|PubMed:20207738}.
DISULFID 61 67 {ECO:0000269|PubMed:11850637,
ECO:0000269|PubMed:12121646,
ECO:0000269|PubMed:12939140,
ECO:0000269|PubMed:18243111,
ECO:0000269|PubMed:20207738}.
DISULFID 77 101 {ECO:0000269|PubMed:11850637,
ECO:0000269|PubMed:12121646,
ECO:0000269|PubMed:12939140,
ECO:0000269|PubMed:18243111,
ECO:0000269|PubMed:20207738}.
DISULFID 121 136 {ECO:0000269|PubMed:11850637,
ECO:0000269|PubMed:12121646,
ECO:0000269|PubMed:12939140,
ECO:0000269|PubMed:18243111,
ECO:0000269|PubMed:20207738}.
DISULFID 138 143 {ECO:0000269|PubMed:11850637,
ECO:0000269|PubMed:12121646,
ECO:0000269|PubMed:12939140,
ECO:0000269|PubMed:18243111,
ECO:0000269|PubMed:20207738}.
VAR_SEQ 31 32 SV -> SDVEMEAQKDEIICPSCNRTAHPLRHI (in
isoform 2). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:7959019}.
/FTId=VSP_012157.
VARIANT 36 36 M -> V (in dbSNP:rs17025864).
{ECO:0000269|Ref.7}.
/FTId=VAR_020510.
VARIANT 61 61 C -> R (in a gastric adenocarcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041414.
VARIANT 73 73 I -> V (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036070.
VARIANT 190 190 R -> H (in LDS2; dbSNP:rs780542125).
{ECO:0000269|PubMed:19533785}.
/FTId=VAR_076167.
VARIANT 191 191 V -> I (in dbSNP:rs56105708).
{ECO:0000269|PubMed:12202987,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_017606.
VARIANT 247 247 D -> V (in LDS2; dbSNP:rs761231369).
{ECO:0000269|PubMed:19533785}.
/FTId=VAR_076168.
VARIANT 306 306 Q -> HE (in LDS2).
{ECO:0000269|PubMed:22113417}.
/FTId=VAR_066723.
VARIANT 308 308 L -> P (in LDS2; has a negative effect on
TGF-beta signaling; dbSNP:rs28934568).
{ECO:0000269|PubMed:15235604,
ECO:0000269|PubMed:20358619}.
/FTId=VAR_022351.
VARIANT 315 315 T -> M (in HNPCC6; dbSNP:rs34833812).
{ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:9590282}.
/FTId=VAR_008156.
VARIANT 325 325 T -> P (in LDS2).
{ECO:0000269|PubMed:19533785}.
/FTId=VAR_076169.
VARIANT 328 328 H -> Y (in a lung neuroendocrine
carcinoma sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041415.
VARIANT 336 336 Y -> N (in LDS2; dbSNP:rs104893812).
{ECO:0000269|PubMed:15731757}.
/FTId=VAR_022352.
VARIANT 355 355 A -> P (in LDS2; dbSNP:rs104893813).
{ECO:0000269|PubMed:15731757}.
/FTId=VAR_022353.
VARIANT 357 357 G -> R (in LDS2).
{ECO:0000269|PubMed:19533785}.
/FTId=VAR_076170.
VARIANT 357 357 G -> W (in LDS2; dbSNP:rs104893814).
{ECO:0000269|PubMed:15731757}.
/FTId=VAR_022354.
VARIANT 373 373 M -> I (in dbSNP:rs35719192).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041416.
VARIANT 377 377 H -> R (in LDS2).
{ECO:0000269|PubMed:22113417}.
/FTId=VAR_066724.
VARIANT 387 387 V -> M (in a breast tumor;
dbSNP:rs35766612).
{ECO:0000269|PubMed:11212236,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_022355.
VARIANT 435 435 N -> S (in a breast tumor; signaling of
TGF-beta significantly inhibited).
{ECO:0000269|PubMed:11212236}.
/FTId=VAR_022356.
VARIANT 439 439 V -> A (in dbSNP:rs1050833).
{ECO:0000269|PubMed:1310899,
ECO:0000269|PubMed:8812462,
ECO:0000269|PubMed:8840968,
ECO:0000269|PubMed:8973329}.
/FTId=VAR_028063.
VARIANT 446 446 D -> N (in LDS2).
{ECO:0000269|PubMed:16251899}.
/FTId=VAR_066725.
VARIANT 447 447 V -> A (in a breast tumor; signaling of
TGF-beta significantly inhibited).
{ECO:0000269|PubMed:11212236}.
/FTId=VAR_022357.
VARIANT 449 449 S -> F (in LDS2; has a negative effect on
TGF-beta signaling; dbSNP:rs104893807).
{ECO:0000269|PubMed:15235604,
ECO:0000269|PubMed:22113417}.
/FTId=VAR_022358.
VARIANT 452 452 L -> M (in a breast tumor; signaling of
TGF-beta significantly inhibited).
{ECO:0000269|PubMed:11212236}.
/FTId=VAR_022359.
VARIANT 457 457 M -> K (in LDS2).
{ECO:0000269|PubMed:20101701}.
/FTId=VAR_066726.
VARIANT 460 460 R -> C (in LDS2; dbSNP:rs104893811).
{ECO:0000269|PubMed:16027248}.
/FTId=VAR_029760.
VARIANT 460 460 R -> H (in LDS2; dbSNP:rs104893816).
{ECO:0000269|PubMed:16027248}.
/FTId=VAR_029761.
VARIANT 490 490 N -> S (in a gastric adenocarcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041417.
VARIANT 509 509 G -> V (in LDS2; dbSNP:rs863223853).
{ECO:0000269|PubMed:21949523}.
/FTId=VAR_066727.
VARIANT 510 510 I -> F (in LDS2).
{ECO:0000269|PubMed:21949523}.
/FTId=VAR_066728.
VARIANT 510 510 I -> S (in LDS2).
{ECO:0000269|PubMed:19883511}.
/FTId=VAR_066729.
VARIANT 514 514 C -> R (in LDS2; dbSNP:rs193922664).
{ECO:0000269|PubMed:22113417}.
/FTId=VAR_066730.
VARIANT 521 521 W -> R (in LDS2).
{ECO:0000269|PubMed:20358619}.
/FTId=VAR_066731.
VARIANT 526 526 E -> Q (in esophageal cancer;
dbSNP:rs121918714).
{ECO:0000269|PubMed:10789724}.
/FTId=VAR_015816.
VARIANT 528 528 R -> C (in LDS2; dbSNP:rs104893810).
{ECO:0000269|PubMed:15731757}.
/FTId=VAR_022360.
VARIANT 528 528 R -> H (in LDS2; dbSNP:rs104893815).
{ECO:0000269|PubMed:15731757,
ECO:0000269|PubMed:16959974}.
/FTId=VAR_022361.
VARIANT 530 530 T -> I (in LDS2).
{ECO:0000269|PubMed:19533785}.
/FTId=VAR_076171.
VARIANT 537 537 R -> C (in LDS2; has a negative effect on
TGF-beta signaling; dbSNP:rs28934869).
{ECO:0000269|PubMed:15235604}.
/FTId=VAR_022362.
MUTAGEN 277 277 K->R: Abolishes kinase activity, TGF-beta
signaling and interaction with DAXX.
{ECO:0000269|PubMed:11483955}.
CONFLICT 381 381 K -> N (in Ref. 6; BAA09332).
{ECO:0000305}.
STRAND 40 45 {ECO:0000244|PDB:1PLO}.
STRAND 50 52 {ECO:0000244|PDB:1M9Z}.
STRAND 55 58 {ECO:0000244|PDB:1M9Z}.
STRAND 65 68 {ECO:0000244|PDB:1M9Z}.
STRAND 74 76 {ECO:0000244|PDB:1M9Z}.
STRAND 78 81 {ECO:0000244|PDB:1PLO}.
STRAND 83 90 {ECO:0000244|PDB:1M9Z}.
STRAND 95 102 {ECO:0000244|PDB:1M9Z}.
STRAND 106 110 {ECO:0000244|PDB:3KFD}.
TURN 114 117 {ECO:0000244|PDB:1M9Z}.
STRAND 119 122 {ECO:0000244|PDB:1M9Z}.
STRAND 124 126 {ECO:0000244|PDB:1M9Z}.
STRAND 131 138 {ECO:0000244|PDB:1M9Z}.
STRAND 140 142 {ECO:0000244|PDB:1PLO}.
HELIX 143 145 {ECO:0000244|PDB:1M9Z}.
STRAND 146 148 {ECO:0000244|PDB:1M9Z}.
STRAND 149 154 {ECO:0000244|PDB:1PLO}.
STRAND 244 252 {ECO:0000244|PDB:5E8V}.
STRAND 257 263 {ECO:0000244|PDB:5E8V}.
STRAND 273 280 {ECO:0000244|PDB:5E8V}.
HELIX 281 283 {ECO:0000244|PDB:5E8V}.
HELIX 284 294 {ECO:0000244|PDB:5E8V}.
HELIX 297 299 {ECO:0000244|PDB:5E8V}.
STRAND 307 314 {ECO:0000244|PDB:5E8V}.
STRAND 316 326 {ECO:0000244|PDB:5E8V}.
HELIX 333 339 {ECO:0000244|PDB:5E8V}.
HELIX 344 362 {ECO:0000244|PDB:5E8V}.
HELIX 382 384 {ECO:0000244|PDB:5E8V}.
STRAND 385 387 {ECO:0000244|PDB:5E8V}.
STRAND 393 395 {ECO:0000244|PDB:5E8V}.
TURN 410 414 {ECO:0000244|PDB:5E8V}.
HELIX 422 424 {ECO:0000244|PDB:5E8V}.
HELIX 427 430 {ECO:0000244|PDB:5E8V}.
HELIX 439 459 {ECO:0000244|PDB:5E8V}.
HELIX 462 464 {ECO:0000244|PDB:5E8V}.
TURN 473 477 {ECO:0000244|PDB:5E8V}.
HELIX 484 491 {ECO:0000244|PDB:5E8V}.
TURN 492 494 {ECO:0000244|PDB:5E8V}.
HELIX 502 506 {ECO:0000244|PDB:5E8V}.
HELIX 508 520 {ECO:0000244|PDB:5E8V}.
HELIX 525 527 {ECO:0000244|PDB:5E8V}.
HELIX 531 540 {ECO:0000244|PDB:5E8V}.
SEQUENCE 567 AA; 64568 MW; C541DA751FFBDBEB CRC64;
MGRGLLRGLW PLHIVLWTRI ASTIPPHVQK SVNNDMIVTD NNGAVKFPQL CKFCDVRFST
CDNQKSCMSN CSITSICEKP QEVCVAVWRK NDENITLETV CHDPKLPYHD FILEDAASPK
CIMKEKKKPG ETFFMCSCSS DECNDNIIFS EEYNTSNPDL LLVIFQVTGI SLLPPLGVAI
SVIIIFYCYR VNRQQKLSST WETGKTRKLM EFSEHCAIIL EDDRSDISST CANNINHNTE
LLPIELDTLV GKGRFAEVYK AKLKQNTSEQ FETVAVKIFP YEEYASWKTE KDIFSDINLK
HENILQFLTA EERKTELGKQ YWLITAFHAK GNLQEYLTRH VISWEDLRKL GSSLARGIAH
LHSDHTPCGR PKMPIVHRDL KSSNILVKND LTCCLCDFGL SLRLDPTLSV DDLANSGQVG
TARYMAPEVL ESRMNLENVE SFKQTDVYSM ALVLWEMTSR CNAVGEVKDY EPPFGSKVRE
HPCVESMKDN VLRDRGRPEI PSFWLNHQGI QMVCETLTEC WDHDPEARLT AQCVAERFSE
LEHLDRLSGR SCSEEKIPED GSLNTTK


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