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TGFR2_HUMAN
ID   TGFR2_HUMAN             Reviewed;         567 AA.
AC   P37173; B4DTV5; Q15580; Q6DKT6; Q99474;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 242.
DE   RecName: Full=TGF-beta receptor type-2;
DE            Short=TGFR-2;
DE            EC=2.7.11.30;
DE   AltName: Full=TGF-beta type II receptor;
DE   AltName: Full=Transforming growth factor-beta receptor type II;
DE            Short=TGF-beta receptor type II;
DE            Short=TbetaR-II;
DE   Flags: Precursor;
GN   Name=TGFBR2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-439, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Liver;
RX   PubMed=1310899; DOI=10.1016/0092-8674(92)90152-3;
RA   Lin H.Y., Wang X.-F., Ng-Eaton E., Weinberg R.A., Lodish H.F.;
RT   "Expression cloning of the TGF-beta type II receptor, a functional
RT   transmembrane serine/threonine kinase.";
RL   Cell 68:775-785(1992).
RN   [2]
RP   ERRATUM OF PUBMED:1310899.
RX   PubMed=1525823;
RA   Lin H.Y., Wang X.-F., Ng-Eaton E., Weinberg R.A., Lodish H.F.;
RL   Cell 70:1069-1069(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Glial cell;
RX   PubMed=7959019; DOI=10.1016/0378-1119(94)90178-3;
RA   Nikawa J.;
RT   "A cDNA encoding the human transforming growth factor beta receptor
RT   suppresses the growth defect of a yeast mutant.";
RL   Gene 149:367-372(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANT ALA-439.
RX   PubMed=8812462; DOI=10.1006/geno.1996.0471;
RA   Takenoshita S., Hagiwara K., Nagashima M., Gemma A., Bennett W.P.,
RA   Harris C.C.;
RT   "The genomic structure of the gene encoding the human transforming growth
RT   factor beta type II receptor (TGF-beta RII).";
RL   Genomics 36:341-344(1996).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANT ALA-439.
RX   PubMed=8840968;
RA   Lu S.-L., Zhang W.C., Akiyama Y., Nomizu T., Yuasa Y.;
RT   "Genomic structure of the transforming growth factor beta type II receptor
RT   gene and its mutations in hereditary nonpolyposis colorectal cancers.";
RL   Cancer Res. 56:4595-4598(1996).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-439.
RC   TISSUE=Liver;
RX   PubMed=8973329; DOI=10.1016/s0378-1119(96)00501-x;
RA   Ogasa H., Noma T., Murata H., Kawai S., Nakazawa A.;
RT   "Cloning of a cDNA encoding the human transforming growth factor-beta type
RT   II receptor: heterogeneity of the mRNA.";
RL   Gene 181:185-190(1996).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION (ISOFORM 3), SUBUNIT
RP   (ISOFORM 3), AND SUBCELLULAR LOCATION (ISOFORM 3).
RC   TISSUE=Peripheral blood T-cell {ECO:0000303|PubMed:34568316};
RX   PubMed=34568316; DOI=10.3389/fcell.2021.690397;
RA   Bertolio M.S., La Colla A., Carrea A., Romo A., Canziani G., Echarte S.M.,
RA   Campisano S., Barletta G.P., Monzon A.M., Rodriguez T.M., Chisari A.N.,
RA   Dewey R.A.;
RT   "A Novel Splice Variant of Human TGF-beta Type II Receptor Encodes a
RT   Soluble Protein and Its Fc-Tagged Version Prevents Liver Fibrosis in
RT   vivo.";
RL   Front. Cell Dev. Biol. 9:690397-690397(2021).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-36.
RG   NIEHS SNPs program;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Placenta;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   PROTEIN SEQUENCE OF 23-37.
RX   PubMed=15340161; DOI=10.1110/ps.04682504;
RA   Zhang Z., Henzel W.J.;
RT   "Signal peptide prediction based on analysis of experimentally verified
RT   cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
RN   [12]
RP   FUNCTION IN PHOSPHORYLATION OF TGFBR1.
RX   PubMed=7774578; DOI=10.1002/j.1460-2075.1995.tb07214.x;
RA   Wieser R., Wrana J.L., Massague J.;
RT   "GS domain mutations that constitutively activate T beta R-I, the
RT   downstream signaling component in the TGF-beta receptor complex.";
RL   EMBO J. 14:2199-2208(1995).
RN   [13]
RP   INTERACTION WITH CLU.
RX   PubMed=8555189; DOI=10.1021/bi951880a;
RA   Reddy K.B., Karode M.C., Harmony A.K., Howe P.H.;
RT   "Interaction of transforming growth factor beta receptors with
RT   apolipoprotein J/clusterin.";
RL   Biochemistry 35:309-314(1996).
RN   [14]
RP   ALTERNATIVE SPLICING (ISOFORM 2), AND FUNCTION (ISOFORMS 1 AND 2).
RX   PubMed=8635485; DOI=10.1006/excr.1996.0066;
RA   Hirai R., Fijita T.;
RT   "A human transforming growth factor-beta type II receptor that contains an
RT   insertion in the extracellular domain.";
RL   Exp. Cell Res. 223:135-141(1996).
RN   [15]
RP   INTERACTION WITH ZFYVE9.
RX   PubMed=9865696; DOI=10.1016/s0092-8674(00)81701-8;
RA   Tsukazaki T., Chiang T.A., Davison A.F., Attisano L., Wrana J.L.;
RT   "SARA, a FYVE domain protein that recruits Smad2 to the TGFbeta receptor.";
RL   Cell 95:779-791(1998).
RN   [16]
RP   HOMODIMERIZATION.
RX   PubMed=9472030; DOI=10.1083/jcb.140.4.767;
RA   Gilboa L., Wells R.G., Lodish H.F., Henis Y.I.;
RT   "Oligomeric structure of type I and type II transforming growth factor beta
RT   receptors: homodimers form in the ER and persist at the plasma membrane.";
RL   J. Cell Biol. 140:767-777(1998).
RN   [17]
RP   INTERACTION WITH DAXX, AND MUTAGENESIS OF LYS-277.
RX   PubMed=11483955; DOI=10.1038/35087019;
RA   Perlman R., Schiemann W.P., Brooks M.W., Lodish H.F., Weinberg R.A.;
RT   "TGF-beta-induced apoptosis is mediated by the adapter protein Daxx that
RT   facilitates JNK activation.";
RL   Nat. Cell Biol. 3:708-714(2001).
RN   [18]
RP   INTERACTION WITH VPS39.
RX   PubMed=12941698; DOI=10.1093/emboj/cdg428;
RA   Felici A., Wurthner J.U., Parks W.T., Giam L.R., Reiss M., Karpova T.S.,
RA   McNally J.G., Roberts A.B.;
RT   "TLP, a novel modulator of TGF-beta signaling, has opposite effects on
RT   Smad2- and Smad3-dependent signaling.";
RL   EMBO J. 22:4465-4477(2003).
RN   [19]
RP   INTERACTION WITH DYNLT4.
RX   PubMed=16982625; DOI=10.1074/jbc.m608614200;
RA   Meng Q.-J., Lux A., Holloschi A., Li J., Hughes J.M.X., Foerg T.,
RA   McCarthy J.E.G., Heagerty A.M., Kioschis P., Hafner M., Garland J.M.;
RT   "Identification of Tctex2beta, a novel dynein light chain family member
RT   that interacts with different transforming growth factor-beta receptors.";
RL   J. Biol. Chem. 281:37069-37080(2006).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [21]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [22]
RP   INTERACTION WITH SCUBE3.
RX   PubMed=21441952; DOI=10.1038/onc.2011.85;
RA   Wu Y.Y., Peck K., Chang Y.L., Pan S.H., Cheng Y.F., Lin J.C., Yang R.B.,
RA   Hong T.M., Yang P.C.;
RT   "SCUBE3 is an endogenous TGF-beta receptor ligand and regulates the
RT   epithelial-mesenchymal transition in lung cancer.";
RL   Oncogene 30:3682-3693(2011).
RN   [23]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [24]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [25]
RP   SUBCELLULAR LOCATION.
RX   PubMed=25893292; DOI=10.1038/onc.2015.100;
RA   Hwangbo C., Tae N., Lee S., Kim O., Park O.K., Kim J., Kwon S.H., Lee J.H.;
RT   "Syntenin regulates TGF-beta1-induced Smad activation and the epithelial-
RT   to-mesenchymal transition by inhibiting caveolin-mediated TGF-beta type I
RT   receptor internalization.";
RL   Oncogene 35:389-401(2016).
RN   [26]
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 38-159 IN COMPLEX WITH TGF-BETA3,
RP   AND DISULFIDE BONDS.
RX   PubMed=11850637; DOI=10.1038/nsb766;
RA   Hart P.J., Deep S., Taylor A.B., Shu Z., Hinck C.S., Hinck A.P.;
RT   "Crystal structure of the human TbetaR2 ectodomain--TGF-beta3 complex.";
RL   Nat. Struct. Biol. 9:203-208(2002).
RN   [27]
RP   X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF 49-159, AND DISULFIDE BONDS.
RX   PubMed=12121646; DOI=10.1016/s0969-2126(02)00780-3;
RA   Boesen C.C., Radaev S., Motyka S.A., Patamawenu A., Sun P.D.;
RT   "The 1.1 A crystal structure of human TGF-beta type II receptor ligand
RT   binding domain.";
RL   Structure 10:913-919(2002).
RN   [28]
RP   STRUCTURE BY NMR OF 38-159, AND DISULFIDE BONDS.
RX   PubMed=12939140; DOI=10.1021/bi034366a;
RA   Deep S., Walker K.P. III, Shu Z., Hinck A.P.;
RT   "Solution structure and backbone dynamics of the TGFbeta type II receptor
RT   extracellular domain.";
RL   Biochemistry 42:10126-10139(2003).
RN   [29]
RP   X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 43-149 IN COMPLEX WITH TGFBR1 AND
RP   TGFB3, AND DISULFIDE BONDS.
RX   PubMed=18243111; DOI=10.1016/j.molcel.2007.11.039;
RA   Groppe J., Hinck C.S., Samavarchi-Tehrani P., Zubieta C., Schuermann J.P.,
RA   Taylor A.B., Schwarz P.M., Wrana J.L., Hinck A.P.;
RT   "Cooperative assembly of TGF-beta superfamily signaling complexes is
RT   mediated by two disparate mechanisms and distinct modes of receptor
RT   binding.";
RL   Mol. Cell 29:157-168(2008).
RN   [30]
RP   X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 38-153 IN COMPLEX WITH TGFBR1 AND
RP   TGFB1, RECEPTOR AFFINITY FOR LIGANDS, AND DISULFIDE BONDS.
RX   PubMed=20207738; DOI=10.1074/jbc.m109.079921;
RA   Radaev S., Zou Z., Huang T., Lafer E.M., Hinck A.P., Sun P.D.;
RT   "Ternary complex of transforming growth factor-beta1 reveals isoform-
RT   specific ligand recognition and receptor recruitment in the superfamily.";
RL   J. Biol. Chem. 285:14806-14814(2010).
RN   [31]
RP   VARIANT HNPCC6 MET-315.
RX   PubMed=9590282; DOI=10.1038/ng0598-17;
RA   Lu S.-L., Kawabata M., Imamura T., Akiyama Y., Nomizu T., Miyazono K.,
RA   Yuasa Y.;
RT   "HNPCC associated with germline mutation in the TGF-beta type II receptor
RT   gene.";
RL   Nat. Genet. 19:17-18(1998).
RN   [32]
RP   VARIANT ESOPHAGEAL CANCER GLN-526.
RX   PubMed=10789724; DOI=10.1054/bjoc.1999.1178;
RA   Tanaka S., Mori M., Mafune K., Ohno S., Sugimachi K.;
RT   "A dominant negative mutation of transforming growth factor-beta receptor
RT   type II gene in microsatellite stable oesophageal carcinoma.";
RL   Br. J. Cancer 82:1557-1560(2000).
RN   [33]
RP   VARIANTS BREAST TUMOR MET-387; SER-435; ALA-447 AND MET-452, AND
RP   CHARACTERIZATION OF VARIANTS BREAST TUMOR SER-435; ALA-447 AND MET-452.
RX   PubMed=11212236;
RA   Luecke C.D., Philpott A., Metcalfe J.C., Thompson A.M., Hughes-Davies L.,
RA   Kemp P.R., Hesketh R.;
RT   "Inhibiting mutations in the transforming growth factor beta type 2
RT   receptor in recurrent human breast cancer.";
RL   Cancer Res. 61:482-485(2001).
RN   [34]
RP   VARIANT ILE-191.
RX   PubMed=12202987; DOI=10.1007/s100380200069;
RA   Watanabe Y., Kinoshita A., Yamada T., Ohta T., Kishino T., Matsumoto N.,
RA   Ishikawa M., Niikawa N., Yoshiura K.;
RT   "A catalog of 106 single-nucleotide polymorphisms (SNPs) and 11 other types
RT   of variations in genes for transforming growth factor-beta1 (TGF-beta1) and
RT   its signaling pathway.";
RL   J. Hum. Genet. 47:478-483(2002).
RN   [35]
RP   VARIANTS LDS2 PRO-308; PHE-449 AND CYS-537, AND CHARACTERIZATION OF
RP   VARIANTS LDS2 PRO-308; PHE-449 AND CYS-537.
RX   PubMed=15235604; DOI=10.1038/ng1392;
RA   Mizuguchi T., Collod-Beroud G., Akiyama T., Abifadel M., Harada N.,
RA   Morisaki T., Allard D., Varret M., Claustres M., Morisaki H., Ihara M.,
RA   Kinoshita A., Yoshiura K., Junien C., Kajii T., Jondeau G., Ohta T.,
RA   Kishino T., Furukawa Y., Nakamura Y., Niikawa N., Boileau C., Matsumoto N.;
RT   "Heterozygous TGFBR2 mutations in Marfan syndrome.";
RL   Nat. Genet. 36:855-860(2004).
RN   [36]
RP   VARIANTS LDS2 CYS-460 AND HIS-460.
RX   PubMed=16027248; DOI=10.1161/circulationaha.105.537340;
RA   Pannu H., Fadulu V.T., Chang J., Lafont A., Hasham S.N., Sparks E.,
RA   Giampietro P.F., Zaleski C., Estrera A.L., Safi H.J., Shete S.,
RA   Willing M.C., Raman C.S., Milewicz D.M.;
RT   "Mutations in transforming growth factor-beta receptor type II cause
RT   familial thoracic aortic aneurysms and dissections.";
RL   Circulation 112:513-520(2005).
RN   [37]
RP   VARIANTS LDS2 ASN-336; PRO-355; TRP-357; HIS-528 AND CYS-528.
RX   PubMed=15731757; DOI=10.1038/ng1511;
RA   Loeys B.L., Chen J., Neptune E.R., Judge D.P., Podowski M., Holm T.,
RA   Meyers J., Leitch C.C., Katsanis N., Sharifi N., Xu F.L., Myers L.A.,
RA   Spevak P.J., Cameron D.E., De Backer J.F., Hellemans J., Chen Y.,
RA   Davis E.C., Webb C.L., Kress W., Coucke P.J., Rifkin D.B., De Paepe A.M.,
RA   Dietz H.C.;
RT   "A syndrome of altered cardiovascular, craniofacial, neurocognitive and
RT   skeletal development caused by mutations in TGFBR1 or TGFBR2.";
RL   Nat. Genet. 37:275-281(2005).
RN   [38]
RP   VARIANT LDS2 ASN-446.
RX   PubMed=16251899; DOI=10.1038/sj.ejhg.5201502;
RA   Disabella E., Grasso M., Marziliano N., Ansaldi S., Lucchelli C., Porcu E.,
RA   Tagliani M., Pilotto A., Diegoli M., Lanzarini L., Malattia C.,
RA   Pelliccia A., Ficcadenti A., Gabrielli O., Arbustini E.;
RT   "Two novel and one known mutation of the TGFBR2 gene in Marfan syndrome not
RT   associated with FBN1 gene defects.";
RL   Eur. J. Hum. Genet. 14:34-38(2006).
RN   [39]
RP   VARIANTS [LARGE SCALE ANALYSIS] VAL-73 AND HIS-528.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
RN   [40]
RP   VARIANTS [LARGE SCALE ANALYSIS] ARG-61; ILE-191; MET-315; TYR-328; ILE-373;
RP   MET-387 AND SER-490.
RX   PubMed=17344846; DOI=10.1038/nature05610;
RA   Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA   Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA   Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA   Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA   Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA   Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA   Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA   Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA   Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA   Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA   Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA   Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
RN   [41]
RP   VARIANTS LDS2 HIS-190; VAL-247; PRO-325; ARG-357 AND ILE-530.
RX   PubMed=19533785; DOI=10.1002/ajmg.a.32918;
RA   Chung B.H., Lam S.T., Tong T.M., Li S.Y., Lun K.S., Chan D.H., Fok S.F.,
RA   Or J.S., Smith D.K., Yang W., Lau Y.L.;
RT   "Identification of novel FBN1 and TGFBR2 mutations in 65 probands with
RT   Marfan syndrome or Marfan-like phenotypes.";
RL   Am. J. Med. Genet. A 149A:1452-1459(2009).
RN   [42]
RP   VARIANT LDS2 SER-510.
RX   PubMed=19883511; DOI=10.1186/1750-1172-4-24;
RA   Drera B., Ritelli M., Zoppi N., Wischmeijer A., Gnoli M., Fattori R.,
RA   Calzavara-Pinton P.G., Barlati S., Colombi M.;
RT   "Loeys-Dietz syndrome type I and type II: clinical findings and novel
RT   mutations in two Italian patients.";
RL   Orphanet J. Rare Dis. 4:24-24(2009).
RN   [43]
RP   VARIANT LDS2 LYS-457.
RX   PubMed=20101701; DOI=10.1002/ajmg.a.33263;
RA   Muramatsu Y., Kosho T., Magota M., Yokotsuka T., Ito M., Yasuda A.,
RA   Kito O., Suzuki C., Nagata Y., Kawai S., Ikoma M., Hatano T., Nakayama M.,
RA   Kawamura R., Wakui K., Morisaki H., Morisaki T., Fukushima Y.;
RT   "Progressive aortic root and pulmonary artery aneurysms in a neonate with
RT   Loeys-Dietz syndrome type 1B.";
RL   Am. J. Med. Genet. A 152:417-421(2010).
RN   [44]
RP   VARIANTS LDS2 PRO-308 AND ARG-521.
RX   PubMed=20358619; DOI=10.1002/ajmg.a.33356;
RA   Kirmani S., Tebben P.J., Lteif A.N., Gordon D., Clarke B.L., Hefferan T.E.,
RA   Yaszemski M.J., McGrann P.S., Lindor N.M., Ellison J.W.;
RT   "Germline TGF-beta receptor mutations and skeletal fragility: a report on
RT   two patients with Loeys-Dietz syndrome.";
RL   Am. J. Med. Genet. A 152:1016-1019(2010).
RN   [45]
RP   VARIANTS LDS2 GLN-306 DELINS HIS-GLU; ARG-377; PHE-449 AND ARG-514.
RX   PubMed=22113417; DOI=10.1038/jhg.2011.130;
RA   Yang J.H., Ki C.S., Han H., Song B.G., Jang S.Y., Chung T.Y., Sung K.,
RA   Lee H.J., Kim D.K.;
RT   "Clinical features and genetic analysis of Korean patients with Loeys-Dietz
RT   syndrome.";
RL   J. Hum. Genet. 57:52-56(2012).
RN   [46]
RP   VARIANTS LDS2 VAL-509 AND PHE-510.
RX   PubMed=21949523; DOI=10.3345/kjp.2011.54.6.272;
RA   Ha J.S., Kim Y.H.;
RT   "A sporadic case of Loeys-Dietz syndrome type I with two novel mutations of
RT   the TGFBR2 gene.";
RL   Korean J. Pediatr. 54:272-275(2011).
CC   -!- FUNCTION: Transmembrane serine/threonine kinase forming with the TGF-
CC       beta type I serine/threonine kinase receptor, TGFBR1, the non-
CC       promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3.
CC       Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to
CC       the cytoplasm and thus regulates a plethora of physiological and
CC       pathological processes including cell cycle arrest in epithelial and
CC       hematopoietic cells, control of mesenchymal cell proliferation and
CC       differentiation, wound healing, extracellular matrix production,
CC       immunosuppression and carcinogenesis. The formation of the receptor
CC       complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound
CC       to the cytokine dimer results in the phosphorylation and activation of
CC       TGFBR1 by the constitutively active TGFBR2. Activated TGFBR1
CC       phosphorylates SMAD2 which dissociates from the receptor and interacts
CC       with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the
CC       nucleus where it modulates the transcription of the TGF-beta-regulated
CC       genes. This constitutes the canonical SMAD-dependent TGF-beta signaling
CC       cascade. Also involved in non-canonical, SMAD-independent TGF-beta
CC       signaling pathways. {ECO:0000269|PubMed:7774578}.
CC   -!- FUNCTION: [Isoform 1]: Has transforming growth factor beta-activated
CC       receptor activity. {ECO:0000269|PubMed:8635485}.
CC   -!- FUNCTION: [Isoform 2]: Has transforming growth factor beta-activated
CC       receptor activity. {ECO:0000269|PubMed:8635485}.
CC   -!- FUNCTION: [Isoform 3]: Binds TGFB1, TGFB2 and TGFB3 in the picomolar
CC       affinity range without the participation of additional receptors.
CC       Blocks activation of SMAD2 and SMAD3 by TGFB1.
CC       {ECO:0000269|PubMed:34568316}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-
CC         L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA-
CC         COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
CC         ChEBI:CHEBI:456216; EC=2.7.11.30;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[receptor-protein] = ADP + H(+) + O-phospho-L-
CC         seryl-[receptor-protein]; Xref=Rhea:RHEA:18673, Rhea:RHEA-COMP:11022,
CC         Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC         EC=2.7.11.30;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. Heterohexamer; TGFB1, TGFB2 and TGFB3 homodimeric
CC       ligands assemble a functional receptor composed of two TGFBR1 and
CC       TGFBR2 heterodimers to form a ligand-receptor heterohexamer. The
CC       respective affinity of TGFRB1 and TGFRB2 for the ligands may modulate
CC       the kinetics of assembly of the receptor and may explain the different
CC       biological activities of TGFB1, TGFB2 and TGFB3. Interacts with DAXX.
CC       Interacts with DYNLT4. Interacts with ZFYVE9; ZFYVE9 recruits SMAD2 and
CC       SMAD3 to the TGF-beta receptor. Interacts with and is activated by
CC       SCUBE3; this interaction does not affect TGFB1-binding to TGFBR2.
CC       Interacts with VPS39; this interaction is independent of the receptor
CC       kinase activity and of the presence of TGF-beta. Interacts with CLU
CC       (PubMed:8555189). {ECO:0000269|PubMed:11483955,
CC       ECO:0000269|PubMed:11850637, ECO:0000269|PubMed:12941698,
CC       ECO:0000269|PubMed:16982625, ECO:0000269|PubMed:18243111,
CC       ECO:0000269|PubMed:20207738, ECO:0000269|PubMed:21441952,
CC       ECO:0000269|PubMed:8555189, ECO:0000269|PubMed:9865696}.
CC   -!- SUBUNIT: [Isoform 3]: Homodimer; disulfide-linked.
CC       {ECO:0000269|PubMed:34568316}.
CC   -!- INTERACTION:
CC       P37173; P54819: AK2; NbExp=3; IntAct=EBI-296151, EBI-1056291;
CC       P37173; P61966-2: AP1S1; NbExp=3; IntAct=EBI-296151, EBI-12067760;
CC       P37173; Q9NP61: ARFGAP3; NbExp=3; IntAct=EBI-296151, EBI-2875816;
CC       P37173; O75143-2: ATG13; NbExp=3; IntAct=EBI-296151, EBI-20151086;
CC       P37173; Q93084-2: ATP2A3; NbExp=3; IntAct=EBI-296151, EBI-21505448;
CC       P37173; P54253: ATXN1; NbExp=3; IntAct=EBI-296151, EBI-930964;
CC       P37173; P54252: ATXN3; NbExp=3; IntAct=EBI-296151, EBI-946046;
CC       P37173; Q4VBR4: ATXN3; NbExp=3; IntAct=EBI-296151, EBI-12928880;
CC       P37173; Q8TBE0: BAHD1; NbExp=3; IntAct=EBI-296151, EBI-742750;
CC       P37173; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-296151, EBI-747505;
CC       P37173; P40227: CCT6A; NbExp=3; IntAct=EBI-296151, EBI-356687;
CC       P37173; P12830: CDH1; NbExp=3; IntAct=EBI-296151, EBI-727477;
CC       P37173; Q8NE08: COL25A1; NbExp=3; IntAct=EBI-296151, EBI-25836642;
CC       P37173; P48730-2: CSNK1D; NbExp=3; IntAct=EBI-296151, EBI-9087876;
CC       P37173; Q9UER7: DAXX; NbExp=2; IntAct=EBI-296151, EBI-77321;
CC       P37173; Q9UMR2: DDX19B; NbExp=3; IntAct=EBI-296151, EBI-719232;
CC       P37173; P49184: DNASE1L1; NbExp=3; IntAct=EBI-296151, EBI-20894690;
CC       P37173; O14531: DPYSL4; NbExp=3; IntAct=EBI-296151, EBI-719542;
CC       P37173; P26378-2: ELAVL4; NbExp=3; IntAct=EBI-296151, EBI-21603100;
CC       P37173; P15036: ETS2; NbExp=3; IntAct=EBI-296151, EBI-1646991;
CC       P37173; Q969W3: FAM104A; NbExp=3; IntAct=EBI-296151, EBI-10281506;
CC       P37173; P09471: GNAO1; NbExp=3; IntAct=EBI-296151, EBI-715087;
CC       P37173; P51674: GPM6A; NbExp=3; IntAct=EBI-296151, EBI-7187133;
CC       P37173; P42858: HTT; NbExp=3; IntAct=EBI-296151, EBI-466029;
CC       P37173; O75874: IDH1; NbExp=3; IntAct=EBI-296151, EBI-715695;
CC       P37173; Q6PI98: INO80C; NbExp=3; IntAct=EBI-296151, EBI-722540;
CC       P37173; Q9ULR0: ISY1; NbExp=3; IntAct=EBI-296151, EBI-2557660;
CC       P37173; P06756: ITGAV; NbExp=3; IntAct=EBI-296151, EBI-298282;
CC       P37173; P23276: KEL; NbExp=3; IntAct=EBI-296151, EBI-746662;
CC       P37173; O60259: KLK8; NbExp=3; IntAct=EBI-296151, EBI-3915857;
CC       P37173; Q96E93: KLRG1; NbExp=3; IntAct=EBI-296151, EBI-750770;
CC       P37173; Q8N448: LNX2; NbExp=3; IntAct=EBI-296151, EBI-2340947;
CC       P37173; Q7Z434: MAVS; NbExp=3; IntAct=EBI-296151, EBI-995373;
CC       P37173; Q93074: MED12; NbExp=3; IntAct=EBI-296151, EBI-394357;
CC       P37173; Q14728: MFSD10; NbExp=3; IntAct=EBI-296151, EBI-11337904;
CC       P37173; P01106: MYC; NbExp=3; IntAct=EBI-296151, EBI-447544;
CC       P37173; Q9NPC7: MYNN; NbExp=3; IntAct=EBI-296151, EBI-3446748;
CC       P37173; Q99435-2: NELL2; NbExp=3; IntAct=EBI-296151, EBI-17754404;
CC       P37173; Q8TAT6: NPLOC4; NbExp=3; IntAct=EBI-296151, EBI-1994109;
CC       P37173; Q9BZ95-3: NSD3; NbExp=3; IntAct=EBI-296151, EBI-22002759;
CC       P37173; Q96IY1: NSL1; NbExp=3; IntAct=EBI-296151, EBI-2554690;
CC       P37173; Q16549: PCSK7; NbExp=3; IntAct=EBI-296151, EBI-8059854;
CC       P37173; Q9NUD9: PIGV; NbExp=3; IntAct=EBI-296151, EBI-25836582;
CC       P37173; Q8TBJ4: PLPPR1; NbExp=3; IntAct=EBI-296151, EBI-18063495;
CC       P37173; Q07869: PPARA; NbExp=3; IntAct=EBI-296151, EBI-78615;
CC       P37173; Q13200: PSMD2; NbExp=3; IntAct=EBI-296151, EBI-357648;
CC       P37173; P21246: PTN; NbExp=3; IntAct=EBI-296151, EBI-473725;
CC       P37173; Q13702-2: RAPSN; NbExp=3; IntAct=EBI-296151, EBI-22012855;
CC       P37173; P52756: RBM5; NbExp=3; IntAct=EBI-296151, EBI-714003;
CC       P37173; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-296151, EBI-17589229;
CC       P37173; Q96NA2: RILP; NbExp=3; IntAct=EBI-296151, EBI-2856119;
CC       P37173; P61513: RPL37A; NbExp=3; IntAct=EBI-296151, EBI-356793;
CC       P37173; Q8IX30: SCUBE3; NbExp=6; IntAct=EBI-296151, EBI-4479975;
CC       P37173; Q8NC51: SERBP1; NbExp=3; IntAct=EBI-296151, EBI-523558;
CC       P37173; Q16586: SGCA; NbExp=3; IntAct=EBI-296151, EBI-5663553;
CC       P37173; Q99720-4: SIGMAR1; NbExp=3; IntAct=EBI-296151, EBI-25831036;
CC       P37173; Q8NCS7: SLC44A5; NbExp=3; IntAct=EBI-296151, EBI-21504521;
CC       P37173; Q16560-2: SNRNP35; NbExp=3; IntAct=EBI-296151, EBI-12938570;
CC       P37173; Q7Z614-3: SNX20; NbExp=3; IntAct=EBI-296151, EBI-12336127;
CC       P37173; Q3SY56: SP6; NbExp=3; IntAct=EBI-296151, EBI-11175533;
CC       P37173; P46977: STT3A; NbExp=3; IntAct=EBI-296151, EBI-719212;
CC       P37173; O43463: SUV39H1; NbExp=3; IntAct=EBI-296151, EBI-349968;
CC       P37173; Q13428-5: TCOF1; NbExp=3; IntAct=EBI-296151, EBI-25832010;
CC       P37173; P01137: TGFB1; NbExp=6; IntAct=EBI-296151, EBI-779636;
CC       P37173; P10600: TGFB3; NbExp=8; IntAct=EBI-296151, EBI-1033020;
CC       P37173; Q9Y228: TRAF3IP3; NbExp=3; IntAct=EBI-296151, EBI-765817;
CC       P37173; Q96BQ3: TRIM43; NbExp=3; IntAct=EBI-296151, EBI-2129899;
CC       P37173; Q9UHP3: USP25; NbExp=3; IntAct=EBI-296151, EBI-2513462;
CC       P37173; P19544-6: WT1; NbExp=3; IntAct=EBI-296151, EBI-11745701;
CC       P37173; P25490: YY1; NbExp=3; IntAct=EBI-296151, EBI-765538;
CC       P37173; A2AGH6: Med12; Xeno; NbExp=3; IntAct=EBI-296151, EBI-5744969;
CC       P37173; P07200: TGFB1; Xeno; NbExp=2; IntAct=EBI-296151, EBI-907660;
CC       P37173-2; P02750: LRG1; NbExp=3; IntAct=EBI-16065370, EBI-9083443;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1310899,
CC       ECO:0000269|PubMed:25893292}; Single-pass type I membrane protein
CC       {ECO:0000269|PubMed:1310899}. Membrane raft
CC       {ECO:0000269|PubMed:25893292}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted
CC       {ECO:0000269|PubMed:34568316}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=betaR-II {ECO:0000303|PubMed:8635485};
CC         IsoId=P37173-1; Sequence=Displayed;
CC       Name=2; Synonyms=betaR-IIB {ECO:0000303|PubMed:8635485};
CC         IsoId=P37173-2; Sequence=VSP_012157;
CC       Name=3; Synonyms=TbetaRII-SE {ECO:0000303|PubMed:34568316};
CC         IsoId=P37173-3; Sequence=VSP_061513, VSP_061514;
CC   -!- PTM: Phosphorylated on a Ser/Thr residue in the cytoplasmic domain.
CC   -!- DISEASE: Hereditary non-polyposis colorectal cancer 6 (HNPCC6)
CC       [MIM:614331]: An autosomal dominant disease associated with marked
CC       increase in cancer susceptibility. It is characterized by a familial
CC       predisposition to early-onset colorectal carcinoma (CRC) and extra-
CC       colonic tumors of the gastrointestinal, urological and female
CC       reproductive tracts. HNPCC is reported to be the most common form of
CC       inherited colorectal cancer in the Western world. Clinically, HNPCC is
CC       often divided into two subgroups. Type I is characterized by hereditary
CC       predisposition to colorectal cancer, a young age of onset, and
CC       carcinoma observed in the proximal colon. Type II is characterized by
CC       increased risk for cancers in certain tissues such as the uterus,
CC       ovary, breast, stomach, small intestine, skin, and larynx in addition
CC       to the colon. Diagnosis of classical HNPCC is based on the Amsterdam
CC       criteria: 3 or more relatives affected by colorectal cancer, one a
CC       first degree relative of the other two; 2 or more generation affected;
CC       1 or more colorectal cancers presenting before 50 years of age;
CC       exclusion of hereditary polyposis syndromes. The term 'suspected HNPCC'
CC       or 'incomplete HNPCC' can be used to describe families who do not or
CC       only partially fulfill the Amsterdam criteria, but in whom a genetic
CC       basis for colon cancer is strongly suspected.
CC       {ECO:0000269|PubMed:9590282}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Esophageal cancer (ESCR) [MIM:133239]: A malignancy of the
CC       esophagus. The most common types are esophageal squamous cell carcinoma
CC       and adenocarcinoma. Cancer of the esophagus remains a devastating
CC       disease because it is usually not detected until it has progressed to
CC       an advanced incurable stage. {ECO:0000269|PubMed:10789724}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- DISEASE: Loeys-Dietz syndrome 2 (LDS2) [MIM:610168]: An aortic aneurysm
CC       syndrome with widespread systemic involvement, characterized by
CC       arterial tortuosity and aneurysms, hypertelorism, and bifid uvula or
CC       cleft palate. Physical findings include prominent joint laxity, easy
CC       bruising, wide and atrophic scars, velvety and translucent skin with
CC       easily visible veins, spontaneous rupture of the spleen or bowel, and
CC       catastrophic complications of pregnancy, including rupture of the
CC       gravid uterus and the arteries, either during pregnancy or in the
CC       immediate postpartum period. Some patients have craniosynostosis,
CC       exotropy, micrognathia and retrognathia, structural brain
CC       abnormalities, and intellectual deficit. {ECO:0000269|PubMed:15235604,
CC       ECO:0000269|PubMed:15731757, ECO:0000269|PubMed:16027248,
CC       ECO:0000269|PubMed:16251899, ECO:0000269|PubMed:19533785,
CC       ECO:0000269|PubMed:19883511, ECO:0000269|PubMed:20101701,
CC       ECO:0000269|PubMed:20358619, ECO:0000269|PubMed:21949523,
CC       ECO:0000269|PubMed:22113417}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry. TGFBR2 mutations Cys-460
CC       and His-460 have been reported to be associated with thoracic aortic
CC       aneurysms and dissection (TAAD). This phenotype, also known as thoracic
CC       aortic aneurysms type 3 (AAT3), is distinguised from LDS2 by having
CC       aneurysms restricted to thoracic aorta. As individuals carrying these
CC       mutations also exhibit descending aortic disease and aneurysms of other
CC       arteries (PubMed:16027248), they have been considered as LDS2 by the
CC       OMIM resource. {ECO:0000269|PubMed:16027248}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/tgfbr2/";
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DR   EMBL; M85079; AAA61164.1; -; mRNA.
DR   EMBL; D28131; BAA05673.1; -; mRNA.
DR   EMBL; U52246; AAB17553.1; -; Genomic_DNA.
DR   EMBL; U52240; AAB17553.1; JOINED; Genomic_DNA.
DR   EMBL; U52241; AAB17553.1; JOINED; Genomic_DNA.
DR   EMBL; U52242; AAB17553.1; JOINED; Genomic_DNA.
DR   EMBL; U52244; AAB17553.1; JOINED; Genomic_DNA.
DR   EMBL; U52245; AAB17553.1; JOINED; Genomic_DNA.
DR   EMBL; U69152; AAB40916.1; -; Genomic_DNA.
DR   EMBL; U69146; AAB40916.1; JOINED; Genomic_DNA.
DR   EMBL; U69147; AAB40916.1; JOINED; Genomic_DNA.
DR   EMBL; U69148; AAB40916.1; JOINED; Genomic_DNA.
DR   EMBL; U69149; AAB40916.1; JOINED; Genomic_DNA.
DR   EMBL; U69150; AAB40916.1; JOINED; Genomic_DNA.
DR   EMBL; U69151; AAB40916.1; JOINED; Genomic_DNA.
DR   EMBL; D50683; BAA09332.1; -; mRNA.
DR   EMBL; MW881156; UDE22710.1; -; mRNA.
DR   EMBL; AY675319; AAT70724.1; -; Genomic_DNA.
DR   EMBL; AK300383; BAG62117.1; -; mRNA.
DR   EMBL; CH471055; EAW64412.1; -; Genomic_DNA.
DR   CCDS; CCDS2648.1; -. [P37173-1]
DR   CCDS; CCDS33727.1; -. [P37173-2]
DR   PIR; A42100; A42100.
DR   RefSeq; NP_001020018.1; NM_001024847.2. [P37173-2]
DR   RefSeq; NP_003233.4; NM_003242.5. [P37173-1]
DR   PDB; 1KTZ; X-ray; 2.15 A; B=38-159.
DR   PDB; 1M9Z; X-ray; 1.05 A; A=49-159.
DR   PDB; 1PLO; NMR; -; A=38-159.
DR   PDB; 2PJY; X-ray; 3.00 A; B=42-149.
DR   PDB; 3KFD; X-ray; 3.00 A; E/F/G/H=38-153.
DR   PDB; 4P7U; X-ray; 1.50 A; A=49-159.
DR   PDB; 4XJJ; X-ray; 1.40 A; A=50-159.
DR   PDB; 5E8V; X-ray; 1.69 A; A=237-549.
DR   PDB; 5E8Y; X-ray; 2.05 A; A=237-549.
DR   PDB; 5E91; X-ray; 2.42 A; A=237-549.
DR   PDB; 5E92; X-ray; 2.08 A; A=237-549.
DR   PDB; 5QIN; X-ray; 1.57 A; A=237-549.
DR   PDB; 5TX4; X-ray; 1.88 A; A=38-153.
DR   PDB; 5TY4; EM; 2.90 A; A=47-149.
DR   PDB; 7DV6; X-ray; 2.39 A; A=237-549.
DR   PDBsum; 1KTZ; -.
DR   PDBsum; 1M9Z; -.
DR   PDBsum; 1PLO; -.
DR   PDBsum; 2PJY; -.
DR   PDBsum; 3KFD; -.
DR   PDBsum; 4P7U; -.
DR   PDBsum; 4XJJ; -.
DR   PDBsum; 5E8V; -.
DR   PDBsum; 5E8Y; -.
DR   PDBsum; 5E91; -.
DR   PDBsum; 5E92; -.
DR   PDBsum; 5QIN; -.
DR   PDBsum; 5TX4; -.
DR   PDBsum; 5TY4; -.
DR   PDBsum; 7DV6; -.
DR   AlphaFoldDB; P37173; -.
DR   BMRB; P37173; -.
DR   SMR; P37173; -.
DR   BioGRID; 112906; 185.
DR   ComplexPortal; CPX-2544; TGF-beta-3-TGFR complex.
DR   ComplexPortal; CPX-529; TGF-beta-1-TGFR complex.
DR   ComplexPortal; CPX-834; TGF-beta-2-TGFR complex.
DR   CORUM; P37173; -.
DR   DIP; DIP-5939N; -.
DR   IntAct; P37173; 123.
DR   MINT; P37173; -.
DR   STRING; 9606.ENSP00000351905; -.
DR   BindingDB; P37173; -.
DR   ChEMBL; CHEMBL4267; -.
DR   DrugBank; DB10770; Foreskin fibroblast (neonatal).
DR   DrugBank; DB10772; Foreskin keratinocyte (neonatal).
DR   DrugBank; DB12010; Fostamatinib.
DR   DrugCentral; P37173; -.
DR   GuidetoPHARMACOLOGY; 1795; -.
DR   GlyConnect; 1979; 9 N-Linked glycans (3 sites).
DR   GlyGen; P37173; 5 sites, 9 N-linked glycans (3 sites).
DR   iPTMnet; P37173; -.
DR   PhosphoSitePlus; P37173; -.
DR   BioMuta; TGFBR2; -.
DR   DMDM; 116242818; -.
DR   EPD; P37173; -.
DR   jPOST; P37173; -.
DR   MassIVE; P37173; -.
DR   MaxQB; P37173; -.
DR   PaxDb; P37173; -.
DR   PeptideAtlas; P37173; -.
DR   PRIDE; P37173; -.
DR   ProteomicsDB; 55264; -. [P37173-1]
DR   ProteomicsDB; 55265; -. [P37173-2]
DR   Antibodypedia; 11570; 801 antibodies from 39 providers.
DR   DNASU; 7048; -.
DR   Ensembl; ENST00000295754.10; ENSP00000295754.5; ENSG00000163513.19. [P37173-1]
DR   Ensembl; ENST00000359013.4; ENSP00000351905.4; ENSG00000163513.19. [P37173-2]
DR   GeneID; 7048; -.
DR   KEGG; hsa:7048; -.
DR   MANE-Select; ENST00000295754.10; ENSP00000295754.5; NM_003242.6; NP_003233.4.
DR   UCSC; uc003cen.4; human. [P37173-1]
DR   CTD; 7048; -.
DR   DisGeNET; 7048; -.
DR   GeneCards; TGFBR2; -.
DR   GeneReviews; TGFBR2; -.
DR   HGNC; HGNC:11773; TGFBR2.
DR   HPA; ENSG00000163513; Low tissue specificity.
DR   MalaCards; TGFBR2; -.
DR   MIM; 133239; phenotype.
DR   MIM; 190182; gene.
DR   MIM; 610168; phenotype.
DR   MIM; 614331; phenotype.
DR   neXtProt; NX_P37173; -.
DR   OpenTargets; ENSG00000163513; -.
DR   Orphanet; 91387; Familial thoracic aortic aneurysm and aortic dissection.
DR   Orphanet; 60030; Loeys-Dietz syndrome.
DR   Orphanet; 144; Lynch syndrome.
DR   Orphanet; 284973; Marfan syndrome type 2.
DR   Orphanet; 99977; Squamous cell carcinoma of the esophagus.
DR   PharmGKB; PA36486; -.
DR   VEuPathDB; HostDB:ENSG00000163513; -.
DR   eggNOG; KOG3653; Eukaryota.
DR   GeneTree; ENSGT00940000157527; -.
DR   HOGENOM; CLU_000288_8_3_1; -.
DR   InParanoid; P37173; -.
DR   OMA; MCSCSAE; -.
DR   PhylomeDB; P37173; -.
DR   TreeFam; TF314724; -.
DR   BRENDA; 2.7.10.2; 2681.
DR   PathwayCommons; P37173; -.
DR   Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling.
DR   Reactome; R-HSA-2173789; TGF-beta receptor signaling activates SMADs.
DR   Reactome; R-HSA-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR   Reactome; R-HSA-3304356; SMAD2/3 Phosphorylation Motif Mutants in Cancer.
DR   Reactome; R-HSA-3642279; TGFBR2 MSI Frameshift Mutants in Cancer.
DR   Reactome; R-HSA-3645790; TGFBR2 Kinase Domain Mutants in Cancer.
DR   Reactome; R-HSA-3656532; TGFBR1 KD Mutants in Cancer.
DR   Reactome; R-HSA-3656535; TGFBR1 LBD Mutants in Cancer.
DR   Reactome; R-HSA-5689603; UCH proteinases.
DR   SignaLink; P37173; -.
DR   SIGNOR; P37173; -.
DR   BioGRID-ORCS; 7048; 41 hits in 1123 CRISPR screens.
DR   ChiTaRS; TGFBR2; human.
DR   EvolutionaryTrace; P37173; -.
DR   GeneWiki; TGF_beta_receptor_2; -.
DR   GenomeRNAi; 7048; -.
DR   Pharos; P37173; Tchem.
DR   PRO; PR:P37173; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; P37173; protein.
DR   Bgee; ENSG00000163513; Expressed in pericardium and 209 other tissues.
DR   ExpressionAtlas; P37173; baseline and differential.
DR   Genevisible; P37173; HS.
DR   GO; GO:0005901; C:caveola; IDA:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IDA:BHF-UCL.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
DR   GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0043235; C:receptor complex; IDA:BHF-UCL.
DR   GO; GO:0070021; C:transforming growth factor beta ligand-receptor complex; IPI:ComplexPortal.
DR   GO; GO:0048185; F:activin binding; IBA:GO_Central.
DR   GO; GO:0017002; F:activin receptor activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005539; F:glycosaminoglycan binding; IDA:BHF-UCL.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IEA:Ensembl.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0046332; F:SMAD binding; IDA:BHF-UCL.
DR   GO; GO:0050431; F:transforming growth factor beta binding; IDA:BHF-UCL.
DR   GO; GO:0005024; F:transforming growth factor beta receptor activity; IDA:BHF-UCL.
DR   GO; GO:0005026; F:transforming growth factor beta receptor activity, type II; IEA:Ensembl.
DR   GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IDA:BHF-UCL.
DR   GO; GO:0034713; F:type I transforming growth factor beta receptor binding; IDA:BHF-UCL.
DR   GO; GO:0034714; F:type III transforming growth factor beta receptor binding; IDA:BHF-UCL.
DR   GO; GO:0032147; P:activation of protein kinase activity; ISS:BHF-UCL.
DR   GO; GO:0007568; P:aging; IEA:Ensembl.
DR   GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR   GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
DR   GO; GO:0003181; P:atrioventricular valve morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0001568; P:blood vessel development; TAS:BHF-UCL.
DR   GO; GO:0007420; P:brain development; ISS:BHF-UCL.
DR   GO; GO:0001569; P:branching involved in blood vessel morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0060434; P:bronchus morphogenesis; IEA:Ensembl.
DR   GO; GO:0003214; P:cardiac left ventricle morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central.
DR   GO; GO:0007182; P:common-partner SMAD protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0048565; P:digestive tract development; IEA:Ensembl.
DR   GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR   GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0035162; P:embryonic hemopoiesis; ISS:BHF-UCL.
DR   GO; GO:0003274; P:endocardial cushion fusion; ISS:BHF-UCL.
DR   GO; GO:0007369; P:gastrulation; IEA:Ensembl.
DR   GO; GO:0003430; P:growth plate cartilage chondrocyte growth; IEA:Ensembl.
DR   GO; GO:0007507; P:heart development; ISS:BHF-UCL.
DR   GO; GO:0001947; P:heart looping; ISS:BHF-UCL.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:1905317; P:inferior endocardial cushion morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0061520; P:Langerhans cell differentiation; IEA:Ensembl.
DR   GO; GO:0002088; P:lens development in camera-type eye; IEA:Ensembl.
DR   GO; GO:1990086; P:lens fiber cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0060463; P:lung lobe morphogenesis; IEA:Ensembl.
DR   GO; GO:0060443; P:mammary gland morphogenesis; IEA:Ensembl.
DR   GO; GO:0003149; P:membranous septum morphogenesis; ISS:BHF-UCL.
DR   GO; GO:1990428; P:miRNA transport; ISS:BHF-UCL.
DR   GO; GO:0043011; P:myeloid dendritic cell differentiation; ISS:BHF-UCL.
DR   GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; IEA:Ensembl.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR   GO; GO:0003151; P:outflow tract morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0003148; P:outflow tract septum morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:BHF-UCL.
DR   GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:BHF-UCL.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR   GO; GO:0002663; P:positive regulation of B cell tolerance induction; ISS:BHF-UCL.
DR   GO; GO:2000563; P:positive regulation of CD4-positive, alpha-beta T cell proliferation; IDA:BHF-UCL.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc.
DR   GO; GO:0010634; P:positive regulation of epithelial cell migration; IEA:Ensembl.
DR   GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IDA:BHF-UCL.
DR   GO; GO:1905007; P:positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation; ISS:BHF-UCL.
DR   GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; ISS:BHF-UCL.
DR   GO; GO:0051138; P:positive regulation of NK T cell differentiation; ISS:BHF-UCL.
DR   GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IDA:ComplexPortal.
DR   GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IMP:BHF-UCL.
DR   GO; GO:0043415; P:positive regulation of skeletal muscle tissue regeneration; IEA:Ensembl.
DR   GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR   GO; GO:0002666; P:positive regulation of T cell tolerance induction; ISS:BHF-UCL.
DR   GO; GO:0002651; P:positive regulation of tolerance induction to self antigen; ISS:BHF-UCL.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:BHF-UCL.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; IEA:Ensembl.
DR   GO; GO:0042127; P:regulation of cell population proliferation; ISS:BHF-UCL.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0072091; P:regulation of stem cell proliferation; IEA:Ensembl.
DR   GO; GO:0070723; P:response to cholesterol; IDA:BHF-UCL.
DR   GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR   GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR   GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR   GO; GO:0048545; P:response to steroid hormone; IEA:Ensembl.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IDA:BHF-UCL.
DR   GO; GO:0062009; P:secondary palate development; ISS:BHF-UCL.
DR   GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
DR   GO; GO:0060440; P:trachea formation; IEA:Ensembl.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0003186; P:tricuspid valve morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0001570; P:vasculogenesis; ISS:BHF-UCL.
DR   GO; GO:0060412; P:ventricular septum morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR   DisProt; DP01760; -.
DR   Gene3D; 2.10.60.10; -; 1.
DR   IDEAL; IID00414; -.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   InterPro; IPR000333; TGFB_receptor.
DR   InterPro; IPR017194; Transform_growth_fac-b_typ-2.
DR   InterPro; IPR015013; Transforming_GF_b_rcpt_2_ecto.
DR   PANTHER; PTHR23255; PTHR23255; 1.
DR   Pfam; PF08917; ecTbetaR2; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PIRSF; PIRSF037393; TGFRII; 1.
DR   PRINTS; PR00653; ACTIVIN2R.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   SUPFAM; SSF57302; SSF57302; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Aortic aneurysm; Apoptosis;
KW   ATP-binding; Cell membrane; Craniosynostosis; Differentiation;
KW   Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein;
KW   Growth regulation; Hereditary nonpolyposis colorectal cancer; Kinase;
KW   Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Receptor; Reference proteome; Secreted;
KW   Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:15340161"
FT   CHAIN           23..567
FT                   /note="TGF-beta receptor type-2"
FT                   /id="PRO_0000024426"
FT   TOPO_DOM        23..166
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        188..567
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          244..544
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          439..567
FT                   /note="Sufficient for interaction with CLU"
FT                   /evidence="ECO:0000269|PubMed:8555189"
FT   ACT_SITE        379
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         250..258
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         277
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         409
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62312"
FT   MOD_RES         548
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18691976,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         553
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62312"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        94
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        154
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        51..84
FT                   /evidence="ECO:0000269|PubMed:11850637,
FT                   ECO:0000269|PubMed:12121646, ECO:0000269|PubMed:12939140,
FT                   ECO:0000269|PubMed:18243111, ECO:0000269|PubMed:20207738"
FT   DISULFID        54..71
FT                   /evidence="ECO:0000269|PubMed:11850637,
FT                   ECO:0000269|PubMed:12121646, ECO:0000269|PubMed:12939140,
FT                   ECO:0000269|PubMed:18243111, ECO:0000269|PubMed:20207738"
FT   DISULFID        61..67
FT                   /evidence="ECO:0000269|PubMed:11850637,
FT                   ECO:0000269|PubMed:12121646, ECO:0000269|PubMed:12939140,
FT                   ECO:0000269|PubMed:18243111, ECO:0000269|PubMed:20207738"
FT   DISULFID        77..101
FT                   /evidence="ECO:0000269|PubMed:11850637,
FT                   ECO:0000269|PubMed:12121646, ECO:0000269|PubMed:12939140,
FT                   ECO:0000269|PubMed:18243111, ECO:0000269|PubMed:20207738"
FT   DISULFID        121..136
FT                   /evidence="ECO:0000269|PubMed:11850637,
FT                   ECO:0000269|PubMed:12121646, ECO:0000269|PubMed:12939140,
FT                   ECO:0000269|PubMed:18243111, ECO:0000269|PubMed:20207738"
FT   DISULFID        138..143
FT                   /evidence="ECO:0000269|PubMed:11850637,
FT                   ECO:0000269|PubMed:12121646, ECO:0000269|PubMed:12939140,
FT                   ECO:0000269|PubMed:18243111, ECO:0000269|PubMed:20207738"
FT   VAR_SEQ         31..32
FT                   /note="SV -> SDVEMEAQKDEIICPSCNRTAHPLRHI (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:7959019"
FT                   /id="VSP_012157"
FT   VAR_SEQ         68..80
FT                   /note="MSNCSITSICEKP -> FSKVHYEGKKKAW (in isoform 3)"
FT                   /id="VSP_061513"
FT   VAR_SEQ         81..567
FT                   /note="Missing (in isoform 3)"
FT                   /id="VSP_061514"
FT   VARIANT         36
FT                   /note="M -> V (in dbSNP:rs17025864)"
FT                   /evidence="ECO:0000269|Ref.8"
FT                   /id="VAR_020510"
FT   VARIANT         61
FT                   /note="C -> R (in a gastric adenocarcinoma sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041414"
FT   VARIANT         73
FT                   /note="I -> V (in a colorectal cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036070"
FT   VARIANT         190
FT                   /note="R -> H (in LDS2; dbSNP:rs780542125)"
FT                   /evidence="ECO:0000269|PubMed:19533785"
FT                   /id="VAR_076167"
FT   VARIANT         191
FT                   /note="V -> I (in dbSNP:rs56105708)"
FT                   /evidence="ECO:0000269|PubMed:12202987,
FT                   ECO:0000269|PubMed:17344846"
FT                   /id="VAR_017606"
FT   VARIANT         247
FT                   /note="D -> V (in LDS2; dbSNP:rs761231369)"
FT                   /evidence="ECO:0000269|PubMed:19533785"
FT                   /id="VAR_076168"
FT   VARIANT         306
FT                   /note="Q -> HE (in LDS2)"
FT                   /evidence="ECO:0000269|PubMed:22113417"
FT                   /id="VAR_066723"
FT   VARIANT         308
FT                   /note="L -> P (in LDS2; has a negative effect on TGF-beta
FT                   signaling; dbSNP:rs28934568)"
FT                   /evidence="ECO:0000269|PubMed:15235604,
FT                   ECO:0000269|PubMed:20358619"
FT                   /id="VAR_022351"
FT   VARIANT         315
FT                   /note="T -> M (in HNPCC6; dbSNP:rs34833812)"
FT                   /evidence="ECO:0000269|PubMed:17344846,
FT                   ECO:0000269|PubMed:9590282"
FT                   /id="VAR_008156"
FT   VARIANT         325
FT                   /note="T -> P (in LDS2)"
FT                   /evidence="ECO:0000269|PubMed:19533785"
FT                   /id="VAR_076169"
FT   VARIANT         328
FT                   /note="H -> Y (in a lung neuroendocrine carcinoma sample;
FT                   somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041415"
FT   VARIANT         336
FT                   /note="Y -> N (in LDS2; dbSNP:rs104893812)"
FT                   /evidence="ECO:0000269|PubMed:15731757"
FT                   /id="VAR_022352"
FT   VARIANT         355
FT                   /note="A -> P (in LDS2; dbSNP:rs104893813)"
FT                   /evidence="ECO:0000269|PubMed:15731757"
FT                   /id="VAR_022353"
FT   VARIANT         357
FT                   /note="G -> R (in LDS2)"
FT                   /evidence="ECO:0000269|PubMed:19533785"
FT                   /id="VAR_076170"
FT   VARIANT         357
FT                   /note="G -> W (in LDS2; dbSNP:rs104893814)"
FT                   /evidence="ECO:0000269|PubMed:15731757"
FT                   /id="VAR_022354"
FT   VARIANT         373
FT                   /note="M -> I (in dbSNP:rs35719192)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041416"
FT   VARIANT         377
FT                   /note="H -> R (in LDS2; dbSNP:rs1553630274)"
FT                   /evidence="ECO:0000269|PubMed:22113417"
FT                   /id="VAR_066724"
FT   VARIANT         387
FT                   /note="V -> M (in a breast tumor; dbSNP:rs35766612)"
FT                   /evidence="ECO:0000269|PubMed:11212236,
FT                   ECO:0000269|PubMed:17344846"
FT                   /id="VAR_022355"
FT   VARIANT         435
FT                   /note="N -> S (in a breast tumor; signaling of TGF-beta
FT                   significantly inhibited)"
FT                   /evidence="ECO:0000269|PubMed:11212236"
FT                   /id="VAR_022356"
FT   VARIANT         439
FT                   /note="V -> A (in dbSNP:rs1050833)"
FT                   /evidence="ECO:0000269|PubMed:1310899,
FT                   ECO:0000269|PubMed:8812462, ECO:0000269|PubMed:8840968,
FT                   ECO:0000269|PubMed:8973329"
FT                   /id="VAR_028063"
FT   VARIANT         446
FT                   /note="D -> N (in LDS2; dbSNP:rs886039551)"
FT                   /evidence="ECO:0000269|PubMed:16251899"
FT                   /id="VAR_066725"
FT   VARIANT         447
FT                   /note="V -> A (in a breast tumor; signaling of TGF-beta
FT                   significantly inhibited)"
FT                   /evidence="ECO:0000269|PubMed:11212236"
FT                   /id="VAR_022357"
FT   VARIANT         449
FT                   /note="S -> F (in LDS2; has a negative effect on TGF-beta
FT                   signaling; dbSNP:rs104893807)"
FT                   /evidence="ECO:0000269|PubMed:15235604,
FT                   ECO:0000269|PubMed:22113417"
FT                   /id="VAR_022358"
FT   VARIANT         452
FT                   /note="L -> M (in a breast tumor; signaling of TGF-beta
FT                   significantly inhibited)"
FT                   /evidence="ECO:0000269|PubMed:11212236"
FT                   /id="VAR_022359"
FT   VARIANT         457
FT                   /note="M -> K (in LDS2)"
FT                   /evidence="ECO:0000269|PubMed:20101701"
FT                   /id="VAR_066726"
FT   VARIANT         460
FT                   /note="R -> C (in LDS2; dbSNP:rs104893811)"
FT                   /evidence="ECO:0000269|PubMed:16027248"
FT                   /id="VAR_029760"
FT   VARIANT         460
FT                   /note="R -> H (in LDS2; dbSNP:rs104893816)"
FT                   /evidence="ECO:0000269|PubMed:16027248"
FT                   /id="VAR_029761"
FT   VARIANT         490
FT                   /note="N -> S (in a gastric adenocarcinoma sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041417"
FT   VARIANT         509
FT                   /note="G -> V (in LDS2; dbSNP:rs863223853)"
FT                   /evidence="ECO:0000269|PubMed:21949523"
FT                   /id="VAR_066727"
FT   VARIANT         510
FT                   /note="I -> F (in LDS2)"
FT                   /evidence="ECO:0000269|PubMed:21949523"
FT                   /id="VAR_066728"
FT   VARIANT         510
FT                   /note="I -> S (in LDS2)"
FT                   /evidence="ECO:0000269|PubMed:19883511"
FT                   /id="VAR_066729"
FT   VARIANT         514
FT                   /note="C -> R (in LDS2; dbSNP:rs193922664)"
FT                   /evidence="ECO:0000269|PubMed:22113417"
FT                   /id="VAR_066730"
FT   VARIANT         521
FT                   /note="W -> R (in LDS2; dbSNP:rs1575166666)"
FT                   /evidence="ECO:0000269|PubMed:20358619"
FT                   /id="VAR_066731"
FT   VARIANT         526
FT                   /note="E -> Q (in esophageal cancer; dbSNP:rs121918714)"
FT                   /evidence="ECO:0000269|PubMed:10789724"
FT                   /id="VAR_015816"
FT   VARIANT         528
FT                   /note="R -> C (in LDS2; dbSNP:rs104893810)"
FT                   /evidence="ECO:0000269|PubMed:15731757"
FT                   /id="VAR_022360"
FT   VARIANT         528
FT                   /note="R -> H (in LDS2; dbSNP:rs104893815)"
FT                   /evidence="ECO:0000269|PubMed:15731757,
FT                   ECO:0000269|PubMed:16959974"
FT                   /id="VAR_022361"
FT   VARIANT         530
FT                   /note="T -> I (in LDS2)"
FT                   /evidence="ECO:0000269|PubMed:19533785"
FT                   /id="VAR_076171"
FT   VARIANT         537
FT                   /note="R -> C (in LDS2; has a negative effect on TGF-beta
FT                   signaling; dbSNP:rs104893809)"
FT                   /evidence="ECO:0000269|PubMed:15235604"
FT                   /id="VAR_022362"
FT   MUTAGEN         277
FT                   /note="K->R: Abolishes kinase activity, TGF-beta signaling
FT                   and interaction with DAXX."
FT                   /evidence="ECO:0000269|PubMed:11483955"
FT   CONFLICT        381
FT                   /note="K -> N (in Ref. 6; BAA09332)"
FT                   /evidence="ECO:0000305"
FT   STRAND          40..45
FT                   /evidence="ECO:0007829|PDB:1PLO"
FT   STRAND          50..52
FT                   /evidence="ECO:0007829|PDB:1M9Z"
FT   STRAND          55..58
FT                   /evidence="ECO:0007829|PDB:1M9Z"
FT   STRAND          65..68
FT                   /evidence="ECO:0007829|PDB:1M9Z"
FT   STRAND          74..76
FT                   /evidence="ECO:0007829|PDB:1M9Z"
FT   STRAND          78..81
FT                   /evidence="ECO:0007829|PDB:1PLO"
FT   STRAND          83..90
FT                   /evidence="ECO:0007829|PDB:1M9Z"
FT   STRAND          95..102
FT                   /evidence="ECO:0007829|PDB:1M9Z"
FT   STRAND          104..106
FT                   /evidence="ECO:0007829|PDB:5TY4"
FT   STRAND          108..110
FT                   /evidence="ECO:0007829|PDB:2PJY"
FT   TURN            114..117
FT                   /evidence="ECO:0007829|PDB:1M9Z"
FT   STRAND          119..122
FT                   /evidence="ECO:0007829|PDB:1M9Z"
FT   STRAND          124..126
FT                   /evidence="ECO:0007829|PDB:1M9Z"
FT   STRAND          131..138
FT                   /evidence="ECO:0007829|PDB:1M9Z"
FT   STRAND          140..142
FT                   /evidence="ECO:0007829|PDB:1PLO"
FT   HELIX           143..145
FT                   /evidence="ECO:0007829|PDB:1M9Z"
FT   STRAND          146..148
FT                   /evidence="ECO:0007829|PDB:1M9Z"
FT   STRAND          149..154
FT                   /evidence="ECO:0007829|PDB:1PLO"
FT   STRAND          244..252
FT                   /evidence="ECO:0007829|PDB:5QIN"
FT   STRAND          257..263
FT                   /evidence="ECO:0007829|PDB:5QIN"
FT   STRAND          267..269
FT                   /evidence="ECO:0007829|PDB:7DV6"
FT   STRAND          272..280
FT                   /evidence="ECO:0007829|PDB:5QIN"
FT   HELIX           281..283
FT                   /evidence="ECO:0007829|PDB:5QIN"
FT   HELIX           284..294
FT                   /evidence="ECO:0007829|PDB:5QIN"
FT   TURN            297..299
FT                   /evidence="ECO:0007829|PDB:5QIN"
FT   STRAND          307..315
FT                   /evidence="ECO:0007829|PDB:5QIN"
FT   STRAND          318..326
FT                   /evidence="ECO:0007829|PDB:5QIN"
FT   HELIX           333..339
FT                   /evidence="ECO:0007829|PDB:5QIN"
FT   HELIX           344..362
FT                   /evidence="ECO:0007829|PDB:5QIN"
FT   HELIX           382..384
FT                   /evidence="ECO:0007829|PDB:5QIN"
FT   STRAND          385..387
FT                   /evidence="ECO:0007829|PDB:5QIN"
FT   STRAND          393..395
FT                   /evidence="ECO:0007829|PDB:5QIN"
FT   HELIX           410..413
FT                   /evidence="ECO:0007829|PDB:5QIN"
FT   HELIX           422..424
FT                   /evidence="ECO:0007829|PDB:5QIN"
FT   HELIX           427..430
FT                   /evidence="ECO:0007829|PDB:5QIN"
FT   HELIX           440..459
FT                   /evidence="ECO:0007829|PDB:5QIN"
FT   HELIX           462..464
FT                   /evidence="ECO:0007829|PDB:5QIN"
FT   TURN            473..477
FT                   /evidence="ECO:0007829|PDB:5QIN"
FT   HELIX           484..491
FT                   /evidence="ECO:0007829|PDB:5QIN"
FT   TURN            492..494
FT                   /evidence="ECO:0007829|PDB:5QIN"
FT   HELIX           502..506
FT                   /evidence="ECO:0007829|PDB:5QIN"
FT   HELIX           508..520
FT                   /evidence="ECO:0007829|PDB:5QIN"
FT   HELIX           525..527
FT                   /evidence="ECO:0007829|PDB:5QIN"
FT   HELIX           531..539
FT                   /evidence="ECO:0007829|PDB:5QIN"
SQ   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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