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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.
17-JUN-2020, entry version 232.
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 OF PUBMED:1310899.
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; DOI=10.1002/j.1460-2075.1995.tb07214.x;
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 CLU.
PubMed=8555189; DOI=10.1021/bi951880a;
Reddy K.B., Karode M.C., Harmony A.K., Howe P.H.;
"Interaction of transforming growth factor beta receptors with
apolipoprotein J/clusterin.";
Biochemistry 35:309-314(1996).
[13]
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).
[14]
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).
[15]
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).
[16]
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).
[17]
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).
[18]
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).
[19]
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).
[20]
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).
[21]
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).
[22]
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).
[23]
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).
[24]
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).
[25]
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).
[26]
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).
[27]
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).
[28]
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).
[29]
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).
[30]
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).
[31]
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).
[32]
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).
[33]
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).
[34]
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).
[35]
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).
[36]
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).
[37]
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).
[38]
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).
[39]
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).
[40]
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).
[41]
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).
[42]
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).
[43]
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).
[44]
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:
Reaction=[receptor-protein]-L-threonine + ATP = [receptor-protein]-O-
phospho-L-threonine + ADP + H(+); Xref=Rhea:RHEA:44880, Rhea:RHEA-
COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378,
ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
ChEBI:CHEBI:456216; EC=2.7.11.30;
-!- CATALYTIC ACTIVITY:
Reaction=[receptor-protein]-L-serine + ATP = [receptor-protein]-O-
phospho-L-serine + ADP + H(+); Xref=Rhea:RHEA:18673, Rhea:RHEA-
COMP:11022, Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378,
ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
ChEBI:CHEBI:456216; EC=2.7.11.30;
-!- 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. Interacts with CLU
(PubMed:8555189). {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:8555189, ECO:0000269|PubMed:9865696}.
-!- INTERACTION:
P37173; Q9UER7: DAXX; NbExp=2; IntAct=EBI-296151, EBI-77321;
P37173; Q93074: MED12; NbExp=3; IntAct=EBI-296151, EBI-394357;
P37173; Q8IX30: SCUBE3; NbExp=6; IntAct=EBI-296151, EBI-4479975;
P37173; P01137: TGFB1; NbExp=6; IntAct=EBI-296151, EBI-779636;
P37173; P10600: TGFB3; NbExp=8; IntAct=EBI-296151, EBI-1033020;
P37173; A2AGH6: Med12; Xeno; NbExp=3; IntAct=EBI-296151, EBI-5744969;
P37173; P07200: TGFB1; Xeno; NbExp=2; IntAct=EBI-296151, EBI-907660;
P37173-2; P02750: LRG1; NbExp=3; IntAct=EBI-16065370, EBI-9083443;
-!- 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]
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; 5QIN; X-ray; 1.57 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; 5QIN; -.
PDBsum; 5TX4; -.
PDBsum; 5TY4; -.
SMR; P37173; -.
BioGRID; 112906; 152.
ComplexPortal; CPX-2544; TGF-beta-3-TGFR complex.
ComplexPortal; CPX-529; TGF-beta-1-TGFR complex.
ComplexPortal; CPX-834; TGF-beta-2-TGFR complex.
CORUM; P37173; -.
DIP; DIP-5939N; -.
IntAct; P37173; 54.
MINT; P37173; -.
STRING; 9606.ENSP00000351905; -.
BindingDB; P37173; -.
ChEMBL; CHEMBL4267; -.
DrugBank; DB10770; Foreskin fibroblast (neonatal).
DrugBank; DB10772; Foreskin keratinocyte (neonatal).
DrugBank; DB12010; Fostamatinib.
DrugBank; DB09462; Glycerin.
DrugCentral; P37173; -.
GuidetoPHARMACOLOGY; 1795; -.
GlyConnect; 1979; -.
iPTMnet; P37173; -.
PhosphoSitePlus; P37173; -.
BioMuta; TGFBR2; -.
DMDM; 116242818; -.
EPD; P37173; -.
jPOST; P37173; -.
MassIVE; P37173; -.
MaxQB; P37173; -.
PaxDb; P37173; -.
PeptideAtlas; P37173; -.
PRIDE; P37173; -.
ProteomicsDB; 55264; -. [P37173-1]
ProteomicsDB; 55265; -. [P37173-2]
Antibodypedia; 11570; 790 antibodies.
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; -.
EuPathDB; HostDB:ENSG00000163513.17; -.
GeneCards; TGFBR2; -.
GeneReviews; TGFBR2; -.
HGNC; HGNC:11773; TGFBR2.
HPA; ENSG00000163513; Low tissue specificity.
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; 60030; Loeys-Dietz syndrome.
Orphanet; 144; Lynch syndrome.
Orphanet; 284973; Marfan syndrome type 2.
Orphanet; 99977; Squamous cell carcinoma of the esophagus.
PharmGKB; PA36486; -.
eggNOG; KOG3653; Eukaryota.
eggNOG; ENOG410XS2Z; LUCA.
GeneTree; ENSGT00940000157527; -.
HOGENOM; CLU_000288_8_3_1; -.
InParanoid; P37173; -.
KO; K04388; -.
OMA; HQGIQTV; -.
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-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; -.
BioGRID-ORCS; 7048; 17 hits in 827 CRISPR screens.
ChiTaRS; TGFBR2; human.
EvolutionaryTrace; P37173; -.
GeneWiki; TGF_beta_receptor_2; -.
GenomeRNAi; 7048; -.
Pharos; P37173; Tchem.
PRO; PR:P37173; -.
Proteomes; UP000005640; Chromosome 3.
RNAct; P37173; protein.
Bgee; ENSG00000163513; Expressed in metanephric glomerulus and 230 other tissues.
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:0005887; C:integral component of plasma membrane; IEA:Ensembl.
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:0048185; F:activin binding; IBA:GO_Central.
GO; GO:0017002; F:activin-activated receptor activity; IBA:GO_Central.
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:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
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:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central.
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:1990428; P:miRNA transport; 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: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 population 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 population 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:0062009; P:secondary palate development; ISS:BHF-UCL.
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.
DisProt; DP01760; -.
IDEAL; IID00414; -.
InterPro; IPR011009; Kinase-like_dom_sf.
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; Craniosynostosis; 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
/evidence="ECO:0000269|PubMed:15340161"
CHAIN 23..567
/note="TGF-beta receptor type-2"
/id="PRO_0000024426"
TOPO_DOM 23..166
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 167..187
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 188..567
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 244..544
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 250..258
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
REGION 439..567
/note="Sufficient for interaction with CLU"
/evidence="ECO:0000269|PubMed:8555189"
ACT_SITE 379
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10027"
BINDING 277
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
MOD_RES 409
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q62312"
MOD_RES 548
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569"
MOD_RES 553
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q62312"
CARBOHYD 70
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 94
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 154
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 51..84
/evidence="ECO:0000269|PubMed:11850637,
ECO:0000269|PubMed:12121646, ECO:0000269|PubMed:12939140,
ECO:0000269|PubMed:18243111, ECO:0000269|PubMed:20207738"
DISULFID 54..71
/evidence="ECO:0000269|PubMed:11850637,
ECO:0000269|PubMed:12121646, ECO:0000269|PubMed:12939140,
ECO:0000269|PubMed:18243111, ECO:0000269|PubMed:20207738"
DISULFID 61..67
/evidence="ECO:0000269|PubMed:11850637,
ECO:0000269|PubMed:12121646, ECO:0000269|PubMed:12939140,
ECO:0000269|PubMed:18243111, ECO:0000269|PubMed:20207738"
DISULFID 77..101
/evidence="ECO:0000269|PubMed:11850637,
ECO:0000269|PubMed:12121646, ECO:0000269|PubMed:12939140,
ECO:0000269|PubMed:18243111, ECO:0000269|PubMed:20207738"
DISULFID 121..136
/evidence="ECO:0000269|PubMed:11850637,
ECO:0000269|PubMed:12121646, ECO:0000269|PubMed:12939140,
ECO:0000269|PubMed:18243111, ECO:0000269|PubMed:20207738"
DISULFID 138..143
/evidence="ECO:0000269|PubMed:11850637,
ECO:0000269|PubMed:12121646, ECO:0000269|PubMed:12939140,
ECO:0000269|PubMed:18243111, ECO:0000269|PubMed:20207738"
VAR_SEQ 31..32
/note="SV -> SDVEMEAQKDEIICPSCNRTAHPLRHI (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:7959019"
/id="VSP_012157"
VARIANT 36
/note="M -> V (in dbSNP:rs17025864)"
/evidence="ECO:0000269|Ref.7"
/id="VAR_020510"
VARIANT 61
/note="C -> R (in a gastric adenocarcinoma sample; somatic
mutation)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_041414"
VARIANT 73
/note="I -> V (in a colorectal cancer sample; somatic
mutation)"
/evidence="ECO:0000269|PubMed:16959974"
/id="VAR_036070"
VARIANT 190
/note="R -> H (in LDS2; dbSNP:rs780542125)"
/evidence="ECO:0000269|PubMed:19533785"
/id="VAR_076167"
VARIANT 191
/note="V -> I (in dbSNP:rs56105708)"
/evidence="ECO:0000269|PubMed:12202987,
ECO:0000269|PubMed:17344846"
/id="VAR_017606"
VARIANT 247
/note="D -> V (in LDS2; dbSNP:rs761231369)"
/evidence="ECO:0000269|PubMed:19533785"
/id="VAR_076168"
VARIANT 306
/note="Q -> HE (in LDS2)"
/evidence="ECO:0000269|PubMed:22113417"
/id="VAR_066723"
VARIANT 308
/note="L -> P (in LDS2; has a negative effect on TGF-beta
signaling; dbSNP:rs28934568)"
/evidence="ECO:0000269|PubMed:15235604,
ECO:0000269|PubMed:20358619"
/id="VAR_022351"
VARIANT 315
/note="T -> M (in HNPCC6; dbSNP:rs34833812)"
/evidence="ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:9590282"
/id="VAR_008156"
VARIANT 325
/note="T -> P (in LDS2)"
/evidence="ECO:0000269|PubMed:19533785"
/id="VAR_076169"
VARIANT 328
/note="H -> Y (in a lung neuroendocrine carcinoma sample;
somatic mutation)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_041415"
VARIANT 336
/note="Y -> N (in LDS2; dbSNP:rs104893812)"
/evidence="ECO:0000269|PubMed:15731757"
/id="VAR_022352"
VARIANT 355
/note="A -> P (in LDS2; dbSNP:rs104893813)"
/evidence="ECO:0000269|PubMed:15731757"
/id="VAR_022353"
VARIANT 357
/note="G -> R (in LDS2)"
/evidence="ECO:0000269|PubMed:19533785"
/id="VAR_076170"
VARIANT 357
/note="G -> W (in LDS2; dbSNP:rs104893814)"
/evidence="ECO:0000269|PubMed:15731757"
/id="VAR_022354"
VARIANT 373
/note="M -> I (in dbSNP:rs35719192)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_041416"
VARIANT 377
/note="H -> R (in LDS2; dbSNP:rs1553630274)"
/evidence="ECO:0000269|PubMed:22113417"
/id="VAR_066724"
VARIANT 387
/note="V -> M (in a breast tumor; dbSNP:rs35766612)"
/evidence="ECO:0000269|PubMed:11212236,
ECO:0000269|PubMed:17344846"
/id="VAR_022355"
VARIANT 435
/note="N -> S (in a breast tumor; signaling of TGF-beta
significantly inhibited)"
/evidence="ECO:0000269|PubMed:11212236"
/id="VAR_022356"
VARIANT 439
/note="V -> A (in dbSNP:rs1050833)"
/evidence="ECO:0000269|PubMed:1310899,
ECO:0000269|PubMed:8812462, ECO:0000269|PubMed:8840968,
ECO:0000269|PubMed:8973329"
/id="VAR_028063"
VARIANT 446
/note="D -> N (in LDS2; dbSNP:rs886039551)"
/evidence="ECO:0000269|PubMed:16251899"
/id="VAR_066725"
VARIANT 447
/note="V -> A (in a breast tumor; signaling of TGF-beta
significantly inhibited)"
/evidence="ECO:0000269|PubMed:11212236"
/id="VAR_022357"
VARIANT 449
/note="S -> F (in LDS2; has a negative effect on TGF-beta
signaling; dbSNP:rs104893807)"
/evidence="ECO:0000269|PubMed:15235604,
ECO:0000269|PubMed:22113417"
/id="VAR_022358"
VARIANT 452
/note="L -> M (in a breast tumor; signaling of TGF-beta
significantly inhibited)"
/evidence="ECO:0000269|PubMed:11212236"
/id="VAR_022359"
VARIANT 457
/note="M -> K (in LDS2)"
/evidence="ECO:0000269|PubMed:20101701"
/id="VAR_066726"
VARIANT 460
/note="R -> C (in LDS2; dbSNP:rs104893811)"
/evidence="ECO:0000269|PubMed:16027248"
/id="VAR_029760"
VARIANT 460
/note="R -> H (in LDS2; dbSNP:rs104893816)"
/evidence="ECO:0000269|PubMed:16027248"
/id="VAR_029761"
VARIANT 490
/note="N -> S (in a gastric adenocarcinoma sample; somatic
mutation)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_041417"
VARIANT 509
/note="G -> V (in LDS2; dbSNP:rs863223853)"
/evidence="ECO:0000269|PubMed:21949523"
/id="VAR_066727"
VARIANT 510
/note="I -> F (in LDS2)"
/evidence="ECO:0000269|PubMed:21949523"
/id="VAR_066728"
VARIANT 510
/note="I -> S (in LDS2)"
/evidence="ECO:0000269|PubMed:19883511"
/id="VAR_066729"
VARIANT 514
/note="C -> R (in LDS2; dbSNP:rs193922664)"
/evidence="ECO:0000269|PubMed:22113417"
/id="VAR_066730"
VARIANT 521
/note="W -> R (in LDS2)"
/evidence="ECO:0000269|PubMed:20358619"
/id="VAR_066731"
VARIANT 526
/note="E -> Q (in esophageal cancer; dbSNP:rs121918714)"
/evidence="ECO:0000269|PubMed:10789724"
/id="VAR_015816"
VARIANT 528
/note="R -> C (in LDS2; dbSNP:rs104893810)"
/evidence="ECO:0000269|PubMed:15731757"
/id="VAR_022360"
VARIANT 528
/note="R -> H (in LDS2; dbSNP:rs104893815)"
/evidence="ECO:0000269|PubMed:15731757,
ECO:0000269|PubMed:16959974"
/id="VAR_022361"
VARIANT 530
/note="T -> I (in LDS2)"
/evidence="ECO:0000269|PubMed:19533785"
/id="VAR_076171"
VARIANT 537
/note="R -> C (in LDS2; has a negative effect on TGF-beta
signaling; dbSNP:rs104893809)"
/evidence="ECO:0000269|PubMed:15235604"
/id="VAR_022362"
MUTAGEN 277
/note="K->R: Abolishes kinase activity, TGF-beta signaling
and interaction with DAXX."
/evidence="ECO:0000269|PubMed:11483955"
CONFLICT 381
/note="K -> N (in Ref. 6; BAA09332)"
/evidence="ECO:0000305"
STRAND 40..45
/evidence="ECO:0000244|PDB:1PLO"
STRAND 50..52
/evidence="ECO:0000244|PDB:1M9Z"
STRAND 55..58
/evidence="ECO:0000244|PDB:1M9Z"
STRAND 65..68
/evidence="ECO:0000244|PDB:1M9Z"
STRAND 74..76
/evidence="ECO:0000244|PDB:1M9Z"
STRAND 78..81
/evidence="ECO:0000244|PDB:1PLO"
STRAND 83..90
/evidence="ECO:0000244|PDB:1M9Z"
STRAND 95..102
/evidence="ECO:0000244|PDB:1M9Z"
STRAND 104..106
/evidence="ECO:0000244|PDB:5TY4"
STRAND 108..110
/evidence="ECO:0000244|PDB:2PJY"
TURN 114..117
/evidence="ECO:0000244|PDB:1M9Z"
STRAND 119..122
/evidence="ECO:0000244|PDB:1M9Z"
STRAND 124..126
/evidence="ECO:0000244|PDB:1M9Z"
STRAND 131..138
/evidence="ECO:0000244|PDB:1M9Z"
STRAND 140..142
/evidence="ECO:0000244|PDB:1PLO"
HELIX 143..145
/evidence="ECO:0000244|PDB:1M9Z"
STRAND 146..148
/evidence="ECO:0000244|PDB:1M9Z"
STRAND 149..154
/evidence="ECO:0000244|PDB:1PLO"
STRAND 244..252
/evidence="ECO:0000244|PDB:5QIN"
STRAND 257..263
/evidence="ECO:0000244|PDB:5QIN"
STRAND 272..280
/evidence="ECO:0000244|PDB:5QIN"
HELIX 281..283
/evidence="ECO:0000244|PDB:5QIN"
HELIX 284..294
/evidence="ECO:0000244|PDB:5QIN"
TURN 297..299
/evidence="ECO:0000244|PDB:5QIN"
STRAND 307..315
/evidence="ECO:0000244|PDB:5QIN"
STRAND 318..326
/evidence="ECO:0000244|PDB:5QIN"
HELIX 333..339
/evidence="ECO:0000244|PDB:5QIN"
HELIX 344..362
/evidence="ECO:0000244|PDB:5QIN"
HELIX 382..384
/evidence="ECO:0000244|PDB:5QIN"
STRAND 385..387
/evidence="ECO:0000244|PDB:5QIN"
STRAND 393..395
/evidence="ECO:0000244|PDB:5QIN"
HELIX 410..413
/evidence="ECO:0000244|PDB:5QIN"
HELIX 422..424
/evidence="ECO:0000244|PDB:5QIN"
HELIX 427..430
/evidence="ECO:0000244|PDB:5QIN"
HELIX 440..459
/evidence="ECO:0000244|PDB:5QIN"
HELIX 462..464
/evidence="ECO:0000244|PDB:5QIN"
TURN 473..477
/evidence="ECO:0000244|PDB:5QIN"
HELIX 484..491
/evidence="ECO:0000244|PDB:5QIN"
TURN 492..494
/evidence="ECO:0000244|PDB:5QIN"
HELIX 502..506
/evidence="ECO:0000244|PDB:5QIN"
HELIX 508..520
/evidence="ECO:0000244|PDB:5QIN"
HELIX 525..527
/evidence="ECO:0000244|PDB:5QIN"
HELIX 531..539
/evidence="ECO:0000244|PDB:5QIN"
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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WP1161: TGF-beta Receptor Signaling Pathway
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WP566: canonical wnt - zebrafish
WP1045: TGF-beta Receptor Signaling Pathway
WP926: TGF-beta Receptor Signaling Pathway
WP1367: TGF-beta Receptor Signaling Pathway
WP2272: Pathogenic Escherichia coli infection
WP809: TGF-beta Receptor Signaling Pathway
WP1046: Signaling of Hepatocyte Growth Factor Receptor
WP313: Signaling of Hepatocyte Growth Factor Receptor
WP927: Signaling of Hepatocyte Growth Factor Receptor
WP1206: Signaling of Hepatocyte Growth Factor Receptor
WP444: Signaling of Hepatocyte Growth Factor Receptor
WP810: Signaling of Hepatocyte Growth Factor Receptor
WP94: Signaling of Hepatocyte Growth Factor Receptor
WP1235: Signaling of Hepatocyte Growth Factor Receptor
WP193: Signaling of Hepatocyte Growth Factor Receptor
WP1162: Signaling of Hepatocyte Growth Factor Receptor
WP474: Endochondral Ossification
WP871: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1004: Kit Receptor Signaling Pathway
WP1226: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1584: Type II diabetes mellitus
WP219: Cytoplasmic tRNA Synthetases

Related Genes :
[TGFBR2] 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)
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[Tgfbr1] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (Serine/threonine-protein kinase receptor R4) (SKR4) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[Tgfbr1] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (ESK2) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[TGFBR1] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[TGFBR1] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[Tgfbr3] Transforming growth factor beta receptor type 3 (TGF-beta receptor type 3) (TGFR-3) (Betaglycan) (Transforming growth factor beta receptor III) (TGF-beta receptor type III)
[ACVR1 ACVRLK2] Activin receptor type-1 (EC 2.7.11.30) (Activin receptor type I) (ACTR-I) (Activin receptor-like kinase 2) (ALK-2) (Serine/threonine-protein kinase receptor R1) (SKR1) (TGF-B superfamily receptor type I) (TSR-I)
[TGFB2] Transforming growth factor beta-2 proprotein (Cetermin) (Glioblastoma-derived T-cell suppressor factor) (G-TSF) [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-2 (TGF-beta-2)]
[MAP3K7 TAK1] Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) (Transforming growth factor-beta-activated kinase 1) (TGF-beta-activated kinase 1)
[Map3k7 Tak1] Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) (Transforming growth factor-beta-activated kinase 1) (TGF-beta-activated kinase 1)
[TGFB2] Transforming growth factor beta-2 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-2 (TGF-beta-2)]
[TGFB1 TGFB] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[LEFTY2 EBAF LEFTA LEFTYA TGFB4 PSEC0024] Left-right determination factor 2 (Endometrial bleeding-associated factor) (Left-right determination factor A) (Protein lefty-2) (Protein lefty-A) (Transforming growth factor beta-4) (TGF-beta-4)
[TGFB3] Transforming growth factor beta-3 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-3 (TGF-beta-3)]
[Tgfb1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[PDGFRB PDGFR PDGFR1] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor) (CD140 antigen-like family member B) (Platelet-derived growth factor receptor 1) (PDGFR-1) (CD antigen CD140b)
[EIF3I EIF3S2 TRIP1] Eukaryotic translation initiation factor 3 subunit I (eIF3i) (Eukaryotic translation initiation factor 3 subunit 2) (TGF-beta receptor-interacting protein 1) (TRIP-1) (eIF-3-beta) (eIF3 p36)
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[Pdgfrb Pdgfr Pdgfr1] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor) (CD140 antigen-like family member B) (Platelet-derived growth factor receptor 1) (PDGFR-1) (CD antigen CD140b)
[Tgfb1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[BMPR2 PPH1] Bone morphogenetic protein receptor type-2 (BMP type-2 receptor) (BMPR-2) (EC 2.7.11.30) (Bone morphogenetic protein receptor type II) (BMP type II receptor) (BMPR-II)
[Pdgfrb Pdgfr Pdgfr1] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor) (CD140 antigen-like family member B) (Platelet-derived growth factor receptor 1) (PDGFR-1) (CD antigen CD140b)

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