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TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (Activin A receptor type II-like protein kinase of 53kD) (Activin receptor-like kinase 5) (ALK-5) (ALK5) (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)

 TGFR1_HUMAN             Reviewed;         503 AA.
P36897; Q6IR47; Q706C0; Q706C1;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
17-JUN-2020, entry version 226.
RecName: Full=TGF-beta receptor type-1;
Short=TGFR-1;
EC=2.7.11.30;
AltName: Full=Activin A receptor type II-like protein kinase of 53kD;
AltName: Full=Activin receptor-like kinase 5;
Short=ALK-5;
Short=ALK5;
AltName: Full=Serine/threonine-protein kinase receptor R4;
Short=SKR4;
AltName: Full=TGF-beta type I receptor;
AltName: Full=Transforming growth factor-beta receptor type I;
Short=TGF-beta receptor type I;
Short=TbetaR-I;
Flags: Precursor;
Name=TGFBR1; Synonyms=ALK5, SKR4;
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).
PubMed=8242743; DOI=10.1016/0092-8674(93)90489-d;
Franzen P., ten Dijke P., Ichijo H., Yamashita H., Schulz P., Heldin C.-H.,
Miyazono K.;
"Cloning of a TGF beta type I receptor that forms a heteromeric complex
with the TGF beta type II receptor.";
Cell 75:681-692(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9417915; DOI=10.1006/geno.1997.5023;
Vellucci V.F., Reiss M.;
"Cloning and genomic organization of the human transforming growth factor-
beta type I receptor gene.";
Genomics 46:278-283(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Lynch M.A., Song H., DeGroff V.L., Alam K.Y., Adams E.M., Weghorst C.M.;
"The genomic structure of the gene encoding the human transforming growth
factor beta type I receptor.";
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 34-40, SIGNAL SEQUENCE CLEAVAGE SITE, GLYCOSYLATION,
CHARACTERIZATION OF VARIANT TGFBR1*6A ALA-24--26-ALA DEL, AND VARIANT
TGFBR1*10A ALA-26 INS.
PubMed=9661882;
Pasche B., Luo Y., Rao P.H., Nimer S.D., Dmitrovsky E., Caron P.,
Luzzatto L., Offit K., Cordon-Cardo C., Renault B., Satagopan J.M.,
Murty V.V., Massague J.;
"Type I transforming growth factor beta receptor maps to 9q22 and exhibits
a polymorphism and a rare variant within a polyalanine tract.";
Cancer Res. 58:2727-2732(1998).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF
61-155 (ISOFORM 1), AND ALTERNATIVE SPLICING.
TISSUE=Prostate;
PubMed=17845732; DOI=10.1186/1471-2164-8-318;
Konrad L., Scheiber J.A., Volck-Badouin E., Keilani M.M., Laible L.,
Brandt H., Schmidt A., Aumuller G., Hofmann R.;
"Alternative splicing of TGF-betas and their high-affinity receptors T beta
RI, T beta RII and T beta RIII (betaglycan) reveal new variants in human
prostatic cells.";
BMC Genomics 8:318-318(2007).
[9]
SEQUENCE REVISION (ISOFORM 1).
Konrad L.;
Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
[10]
FUNCTION, PHOSPHORYLATION AT THR-185; THR-186; SER-187; SER-189 AND SER-191
BY TGFBR2, SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF
185-THR-THR-186; SER-187; SER-189; SER-191; THR-200 AND THR-204.
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).
[11]
FUNCTION IN PHOSPHORYLATION OF SMAD2.
PubMed=8752209; DOI=10.1016/s0092-8674(00)80128-2;
Eppert K., Scherer S.W., Ozcelik H., Pirone R., Hoodless P., Kim H.,
Tsui L.-C., Bapat B., Gallinger S., Andrulis I.L., Thomsen G.H.,
Wrana J.L., Attisano L.;
"MADR2 maps to 18q21 and encodes a TGFbeta-regulated MAD-related protein
that is functionally mutated in colorectal carcinoma.";
Cell 86:543-552(1996).
[12]
INTERACTION WITH SMAD2, FUNCTION IN PHOSPHORYLATION OF SMAD2, AND FUNCTION
IN TRANSCRIPTION REGULATION.
PubMed=8980228; DOI=10.1016/s0092-8674(00)81817-6;
Macias-Silva M., Abdollah S., Hoodless P.A., Pirone R., Attisano L.,
Wrana J.L.;
"MADR2 is a substrate of the TGFbeta receptor and its phosphorylation is
required for nuclear accumulation and signaling.";
Cell 87:1215-1224(1996).
[13]
INTERACTION WITH FKBP1A, ACTIVITY REGULATION, AND MUTAGENESIS OF LEU-193
AND PRO-194.
PubMed=9233797; DOI=10.1093/emboj/16.13.3866;
Chen Y.G., Liu F., Massague J.;
"Mechanism of TGFbeta receptor inhibition by FKBP12.";
EMBO J. 16:3866-3876(1997).
[14]
INTERACTION WITH SMAD3.
PubMed=9311995; DOI=10.1093/emboj/16.17.5353;
Nakao A., Imamura T., Souchelnytskyi S., Kawabata M., Ishisaki A., Oeda E.,
Tamaki K., Hanai J., Heldin C.H., Miyazono K., ten Dijke P.;
"TGF-beta receptor-mediated signalling through Smad2, Smad3 and Smad4.";
EMBO J. 16:5353-5362(1997).
[15]
INTERACTION WITH SMAD2, FUNCTION IN PHOSPHORYLATION OF SMAD2, AND FUNCTION
IN TRANSCRIPTION REGULATION.
PubMed=9346908; DOI=10.1074/jbc.272.44.27678;
Abdollah S., Macias-Silva M., Tsukazaki T., Hayashi H., Attisano L.,
Wrana J.L.;
"TbetaRI phosphorylation of Smad2 on Ser465 and Ser467 is required for
Smad2-Smad4 complex formation and signaling.";
J. Biol. Chem. 272:27678-27685(1997).
[16]
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).
[17]
HOMODIMERIZATION, AND SUBCELLULAR LOCATION.
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).
[18]
INTERACTION WITH SMAD7 AND SMURF2, AND PROTEASOMAL AND LYSOSOMAL
DEGRADATION.
PubMed=11163210; DOI=10.1016/s1097-2765(00)00134-9;
Kavsak P., Rasmussen R.K., Causing C.G., Bonni S., Zhu H., Thomsen G.H.,
Wrana J.L.;
"Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF-
beta receptor for degradation.";
Mol. Cell 6:1365-1375(2000).
[19]
INTERACTION WITH SMAD7 AND SMURF1, AND PROTEASOMAL DEGRADATION.
PubMed=11278251; DOI=10.1074/jbc.c100008200;
Ebisawa T., Fukuchi M., Murakami G., Chiba T., Tanaka K., Imamura T.,
Miyazono K.;
"Smurf1 interacts with transforming growth factor-beta type I receptor
through Smad7 and induces receptor degradation.";
J. Biol. Chem. 276:12477-12480(2001).
[20]
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).
[21]
INTERACTION WITH NEDD4L, AND UBIQUITINATION.
PubMed=15496141; DOI=10.1042/bj20040738;
Kuratomi G., Komuro A., Goto K., Shinozaki M., Miyazawa K., Miyazono K.,
Imamura T.;
"NEDD4-2 (neural precursor cell expressed, developmentally down-regulated
4-2) negatively regulates TGF-beta (transforming growth factor-beta)
signalling by inducing ubiquitin-mediated degradation of Smad2 and TGF-beta
type I receptor.";
Biochem. J. 386:461-470(2005).
[22]
FUNCTION IN EPITHELIAL TO MESENCHYMAL TRANSITION, SUBCELLULAR LOCATION,
INTERACTION WITH PARD6A, AND FUNCTION IN PHOSPHORYLATION OF PARD6A.
PubMed=15761148; DOI=10.1126/science.1105718;
Ozdamar B., Bose R., Barrios-Rodiles M., Wang H.R., Zhang Y., Wrana J.L.;
"Regulation of the polarity protein Par6 by TGFbeta receptors controls
epithelial cell plasticity.";
Science 307:1603-1609(2005).
[23]
FUNCTION IN CELLULAR GROWTH INHIBITION, AND INTERACTION WITH CD109.
PubMed=16754747; DOI=10.1096/fj.05-5229fje;
Finnson K.W., Tam B.Y.Y., Liu K., Marcoux A., Lepage P., Roy S.,
Bizet A.A., Philip A.;
"Identification of CD109 as part of the TGF-beta receptor system in human
keratinocytes.";
FASEB J. 20:1525-1527(2006).
[24]
INTERACTION WITH RBPMS.
PubMed=17099224; DOI=10.1093/nar/gkl914;
Sun Y., Ding L., Zhang H., Han J., Yang X., Yan J., Zhu Y., Li J., Song H.,
Ye Q.;
"Potentiation of Smad-mediated transcriptional activation by the RNA-
binding protein RBPMS.";
Nucleic Acids Res. 34:6314-6326(2006).
[25]
FUNCTION IN APOPTOSIS, AND INTERACTION WITH TRAF6 AND MAP3K7.
PubMed=18758450; DOI=10.1038/ncb1780;
Sorrentino A., Thakur N., Grimsby S., Marcusson A., von Bulow V.,
Schuster N., Zhang S., Heldin C.H., Landstrom M.;
"The type I TGF-beta receptor engages TRAF6 to activate TAK1 in a receptor
kinase-independent manner.";
Nat. Cell Biol. 10:1199-1207(2008).
[26]
REVIEW ON PROCESSES REGULATED BY THE TGF-BETA CYTOKINES.
PubMed=9759503; DOI=10.1146/annurev.biochem.67.1.753;
Massague J.;
"TGF-beta signal transduction.";
Annu. Rev. Biochem. 67:753-791(1998).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND 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).
[28]
UBIQUITINATION, AND DEUBIQUITINATION BY USP15.
PubMed=22344298; DOI=10.1038/nm.2619;
Eichhorn P.J., Rodon L., Gonzalez-Junca A., Dirac A., Gili M.,
Martinez-Saez E., Aura C., Barba I., Peg V., Prat A., Cuartas I.,
Jimenez J., Garcia-Dorado D., Sahuquillo J., Bernards R., Baselga J.,
Seoane J.;
"USP15 stabilizes TGF-beta receptor I and promotes oncogenesis through the
activation of TGF-beta signaling in glioblastoma.";
Nat. Med. 18:429-435(2012).
[29]
INTERACTION WITH SDCBP AND CAV1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
UBIQUITINATION, AND PROTEASOMAL DEGRADATION.
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).
[30]
INTERACTION WITH APPL1.
PubMed=26583432; DOI=10.18632/oncotarget.6346;
Song J., Mu Y., Li C., Bergh A., Miaczynska M., Heldin C.H., Landstroem M.;
"APPL proteins promote TGFbeta-induced nuclear transport of the TGFbeta
type I receptor intracellular domain.";
Oncotarget 7:279-292(2016).
[31]
3D-STRUCTURE MODELING OF 34-114.
PubMed=8521960; DOI=10.1016/0014-5793(95)01239-7;
Jokiranta T.S., Tissari J., Teleman O., Meri S.;
"Extracellular domain of type I receptor for transforming growth factor-
beta: molecular modelling using protectin (CD59) as a template.";
FEBS Lett. 376:31-36(1995).
[32]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 162-503 IN COMPLEX WITH FKBP1A.
PubMed=10025408; DOI=10.1016/s0092-8674(00)80555-3;
Huse M., Chen Y.-G., Massague J., Kuriyan J.;
"Crystal structure of the cytoplasmic domain of the type I TGF beta
receptor in complex with FKBP12.";
Cell 96:425-436(1999).
[33]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 162-503, PHOSPHORYLATION, AND
INTERACTION WITH SMAD2 AND FKBP1A.
PubMed=11583628; DOI=10.1016/s1097-2765(01)00332-x;
Huse M., Muir T.W., Xu L., Chen Y.-G., Kuriyan J., Massague J.;
"The TGF beta receptor activation process: an inhibitor- to substrate-
binding switch.";
Mol. Cell 8:671-682(2001).
[34]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 175-500 IN COMPLEX WITH SYNTHETIC
INHIBITOR.
PubMed=15177479; DOI=10.1016/j.bmcl.2004.04.007;
Sawyer J.S., Beight D.W., Britt K.S., Anderson B.D., Campbell R.M.,
Goodson T. Jr., Herron D.K., Li H.-Y., McMillen W.T., Mort N., Parsons S.,
Smith E.C.R., Wagner J.R., Yan L., Zhang F., Yingling J.M.;
"Synthesis and activity of new aryl- and heteroaryl-substituted 5,6-
dihydro-4H-pyrrolo[1,2-b]pyrazole inhibitors of the transforming growth
factor-beta type I receptor kinase domain.";
Bioorg. Med. Chem. Lett. 14:3581-3584(2004).
[35]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 201-503 IN COMPLEX WITH SYNTHETIC
INHIBITOR.
PubMed=15317461; DOI=10.1021/jm0400247;
Gellibert F., Woolven J., Fouchet M.-H., Mathews N., Goodland H.,
Lovegrove V., Laroze A., Nguyen V.-L., Sautet S., Wang R., Janson C.,
Smith W., Krysa G., Boullay V., De Gouville A.-C., Huet S., Hartley D.;
"Identification of 1,5-naphthyridine derivatives as a novel series of
potent and selective TGF-beta type I receptor inhibitors.";
J. Med. Chem. 47:4494-4506(2004).
[36]
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 33-111 IN COMPLEX WITH TGFBR2 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).
[37]
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 31-115 IN COMPLEX WITH TGFBR2 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).
[38]
ANALYSIS OF VARIANT TGFBR1*6A ALA-24--26-ALA DEL IN CANCER RISK.
PubMed=12947057; DOI=10.1200/jco.2003.11.524;
Kaklamani V.G., Hou N., Bian Y., Reich J., Offit K., Michel L.S.,
Rubinstein W.S., Rademaker A., Pasche B.;
"TGFBR1*6A and cancer risk: a meta-analysis of seven case-control
studies.";
J. Clin. Oncol. 21:3236-3243(2003).
[39]
ANALYSIS OF VARIANT TGFBR1*6A ALA-24--26-ALA DEL IN PROSTATE CANCER.
PubMed=15385056; DOI=10.1186/1471-2156-5-28;
Kaklamani V.G., Baddi L., Rosman D., Liu J., Ellis N., Oddoux C.,
Ostrer H., Chen Y., Ahsan H., Offit K., Pasche B.;
"No major association between TGFBR1*6A and prostate cancer.";
BMC Genet. 5:28-28(2004).
[40]
VARIANTS LDS1 ILE-200; ARG-318; GLY-400 AND PRO-487.
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).
[41]
ANALYSIS OF VARIANT TGFBR1*6A ALA-24--26-ALA DEL IN PROSTATE CANCER.
PubMed=15505640; DOI=10.1038/sj.pcan.4500765;
Suarez B.K., Pal P., Jin C.H., Kaushal R., Sun G., Jin L., Pasche B.,
Deka R., Catalona W.J.;
"TGFBR1(*)6A is not associated with prostate cancer in men of European
ancestry.";
Prostate Cancer Prostatic Dis. 8:50-53(2005).
[42]
VARIANT LDS1 LEU-241.
PubMed=16596670; DOI=10.1002/ajmg.a.31202;
Ades L.C., Sullivan K., Biggin A., Haan E.A., Brett M., Holman K.J.,
Dixon J., Robertson S., Holmes A.D., Rogers J., Bennetts B.;
"FBN1, TGFBR1, and the Marfan-craniosynostosis/mental retardation disorders
revisited.";
Am. J. Med. Genet. A 140:1047-1058(2006).
[43]
VARIANTS LDS1 LEU-241 AND GLN-487, AND VARIANT HIS-267.
PubMed=16791849; DOI=10.1002/humu.20353;
Matyas G., Arnold E., Carrel T., Baumgartner D., Boileau C., Berger W.,
Steinmann B.;
"Identification and in silico analyses of novel TGFBR1 and TGFBR2 mutations
in Marfan syndrome-related disorders.";
Hum. Mutat. 27:760-769(2006).
[44]
VARIANTS LDS1 GLU-232; TRP-487; PRO-487 AND GLN-487.
PubMed=16928994; DOI=10.1056/nejmoa055695;
Loeys B.L., Schwarze U., Holm T., Callewaert B.L., Thomas G.H., Pannu H.,
De Backer J.F., Oswald G.L., Symoens S., Manouvrier S., Roberts A.E.,
Faravelli F., Greco M.A., Pyeritz R.E., Milewicz D.M., Coucke P.J.,
Cameron D.E., Braverman A.C., Byers P.H., De Paepe A.M., Dietz H.C.;
"Aneurysm syndromes caused by mutations in the TGF-beta receptor.";
N. Engl. J. Med. 355:788-798(2006).
[45]
VARIANTS [LARGE SCALE ANALYSIS] ILE-153 AND CYS-291.
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).
[46]
VARIANT [LARGE SCALE ANALYSIS] VAL-139.
PubMed=18987736; DOI=10.1038/nature07485;
Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K.,
Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L.,
Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A.,
Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V.,
Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R.,
Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E.,
Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S.,
Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A.,
DiPersio J.F., Wilson R.K.;
"DNA sequencing of a cytogenetically normal acute myeloid leukaemia
genome.";
Nature 456:66-72(2008).
[47]
VARIANT LDS1 GLY-351.
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).
[48]
VARIANTS LDS1 TYR-266; ARG-375 AND GLN-487.
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).
[49]
ERRATUM OF PUBMED:22113417.
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.;
J. Hum. Genet. 57:398-398(2012).
[50]
VARIANTS MSSE TYR-41; SER-45; ARG-52 AND LEU-83.
PubMed=21358634; DOI=10.1038/ng.780;
Goudie D.R., D'Alessandro M., Merriman B., Lee H., Szeverenyi I., Avery S.,
O'Connor B.D., Nelson S.F., Coats S.E., Stewart A., Christie L.,
Pichert G., Friedel J., Hayes I., Burrows N., Whittaker S., Gerdes A.M.,
Broesby-Olsen S., Ferguson-Smith M.A., Verma C., Lunny D.P., Reversade B.,
Lane E.B.;
"Multiple self-healing squamous epithelioma is caused by a disease-specific
spectrum of mutations in TGFBR1.";
Nat. Genet. 43:365-369(2011).
-!- FUNCTION: Transmembrane serine/threonine kinase forming with the TGF-
beta type II serine/threonine kinase receptor, TGFBR2, 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 TGFBR1 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. For instance, TGFBR1 induces TRAF6
autoubiquitination which in turn results in MAP3K7 ubiquitination and
activation to trigger apoptosis. Also regulates epithelial to
mesenchymal transition through a SMAD-independent signaling pathway
through PARD6A phosphorylation and activation.
{ECO:0000269|PubMed:15761148, ECO:0000269|PubMed:16754747,
ECO:0000269|PubMed:18758450, ECO:0000269|PubMed:7774578,
ECO:0000269|PubMed:8752209, ECO:0000269|PubMed:8980228,
ECO:0000269|PubMed:9346908}.
-!- 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};
-!- ACTIVITY REGULATION: Kept in an inactive conformation by FKBP1A
preventing receptor activation in absence of ligand. CD109 is another
inhibitor of the receptor. {ECO:0000269|PubMed:9233797}.
-!- SUBUNIT: Homodimer; in the endoplasmic reticulum but also at the cell
membrane. 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 TGBRB1 and TGFBR2 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 CD109; inhibits
TGF-beta receptor activation in keratinocytes. Interacts with RBPMS.
Interacts (unphosphorylated) with FKBP1A; prevents TGFBR1
phosphorylation by TGFBR2 and stabilizes it in the inactive
conformation. Interacts with SMAD2, SMAD3 and ZFYVE9; ZFYVE9 recruits
SMAD2 and SMAD3 to the TGF-beta receptor. Interacts with TRAF6 and
MAP3K7; induces MAP3K7 activation by TRAF6. Interacts with PARD6A;
involved in TGF-beta induced epithelial to mesenchymal transition.
Interacts with SMAD7, NEDD4L, SMURF1 and SMURF2; SMAD7 recruits NEDD4L,
SMURF1 and SMURF2 to the TGF-beta receptor. Interacts with USP15 and
VPS39. Interacts with SDCBP (via C-terminus) (PubMed:25893292)
Interacts with CAV1 and this interaction is impaired in the presence of
SDCBP (PubMed:25893292). Interacts with APPL1; interaction is TGF beta
dependent; mediates trafficking of the TGFBR1 from the endosomes to the
nucleus via microtubules in a TRAF6-dependent manner (PubMed:26583432).
{ECO:0000269|PubMed:10025408, ECO:0000269|PubMed:11163210,
ECO:0000269|PubMed:11278251, ECO:0000269|PubMed:11583628,
ECO:0000269|PubMed:12941698, ECO:0000269|PubMed:15177479,
ECO:0000269|PubMed:15317461, ECO:0000269|PubMed:15496141,
ECO:0000269|PubMed:15761148, ECO:0000269|PubMed:16754747,
ECO:0000269|PubMed:17099224, ECO:0000269|PubMed:18243111,
ECO:0000269|PubMed:18758450, ECO:0000269|PubMed:20207738,
ECO:0000269|PubMed:25893292, ECO:0000269|PubMed:26583432,
ECO:0000269|PubMed:7774578, ECO:0000269|PubMed:8980228,
ECO:0000269|PubMed:9233797, ECO:0000269|PubMed:9311995,
ECO:0000269|PubMed:9346908, ECO:0000269|PubMed:9865696}.
-!- INTERACTION:
P36897; P62942: FKBP1A; NbExp=2; IntAct=EBI-1027557, EBI-1027571;
P36897; P01137: TGFB1; NbExp=2; IntAct=EBI-1027557, EBI-779636;
P36897; P63104: YWHAZ; NbExp=4; IntAct=EBI-1027557, EBI-347088;
P36897; PRO_0000045599 [Q99IB8]; Xeno; NbExp=5; IntAct=EBI-1027557, EBI-6858501;
P36897-1; P02750: LRG1; NbExp=6; IntAct=EBI-16065417, EBI-9083443;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25893292,
ECO:0000269|PubMed:9472030}; Single-pass type I membrane protein
{ECO:0000269|PubMed:9472030}. Cell junction, tight junction
{ECO:0000269|PubMed:15761148}. Cell surface
{ECO:0000269|PubMed:25893292}. Membrane raft
{ECO:0000269|PubMed:25893292}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P36897-1; Sequence=Displayed;
Name=2; Synonyms=B;
IsoId=P36897-2; Sequence=VSP_041326;
Name=3;
IsoId=P36897-3; Sequence=VSP_041327;
-!- TISSUE SPECIFICITY: Found in all tissues examined, most abundant in
placenta and least abundant in brain and heart. Expressed in a variety
of cancer cell lines (PubMed:25893292). {ECO:0000269|PubMed:25893292}.
-!- PTM: Phosphorylated at basal levels in the absence of ligand. Activated
upon phosphorylation by TGFBR2, mainly in the GS domain.
Phosphorylation in the GS domain abrogates FKBP1A-binding.
{ECO:0000269|PubMed:11583628, ECO:0000269|PubMed:7774578}.
-!- PTM: N-Glycosylated. {ECO:0000269|PubMed:9661882}.
-!- PTM: Ubiquitinated; undergoes ubiquitination catalyzed by several E3
ubiquitin ligases including SMURF1, SMURF2 and NEDD4L2. Results in the
proteasomal and/or lysosomal degradation of the receptor thereby
negatively regulating its activity. Deubiquitinated by USP15, leading
to stabilization of the protein and enhanced TGF-beta signal. Its
ubiquitination and proteasome-mediated degradation is negatively
regulated by SDCBP (PubMed:25893292). {ECO:0000269|PubMed:15496141,
ECO:0000269|PubMed:22344298, ECO:0000269|PubMed:25893292}.
-!- DISEASE: Loeys-Dietz syndrome 1 (LDS1) [MIM:609192]: 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:15731757,
ECO:0000269|PubMed:16596670, ECO:0000269|PubMed:16791849,
ECO:0000269|PubMed:16928994, ECO:0000269|PubMed:19883511,
ECO:0000269|PubMed:22113417}. Note=The disease is caused by mutations
affecting the gene represented in this entry. TGFBR1 mutation Gln-487
has been reported to be associated with thoracic aortic aneurysms and
dissection (TAAD) (PubMed:16791849). This phenotype, also known as
thoracic aortic aneurysms type 5 (AAT5), is distinguised from LDS1 by
having aneurysms restricted to thoracic aorta. It is unclear, however,
if this condition is fulfilled in individuals bearing Gln-487 mutation,
that is why they are considered as LDS1 by the OMIM resource.
{ECO:0000269|PubMed:16791849}.
-!- DISEASE: Multiple self-healing squamous epithelioma (MSSE)
[MIM:132800]: A disorder characterized by multiple skin tumors that
undergo spontaneous regression. Tumors appear most often on sun-exposed
regions, are locally invasive, and undergo spontaneous resolution over
a period of months leaving pitted scars. {ECO:0000269|PubMed:21358634}.
Note=The disease is caused by mutations affecting the gene represented
in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
-!- CAUTION: One report originally reported variant Ile-375
(PubMed:22113417). This variant has been subsequently corrected to Arg-
375 by the same authors (Ref.49). {ECO:0000269|PubMed:22113417,
ECO:0000269|Ref.49}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/tgfbr1/";
---------------------------------------------------------------------------
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EMBL; L11695; AAA16073.1; -; mRNA.
EMBL; AF054598; AAC08998.1; -; Genomic_DNA.
EMBL; AF054590; AAC08998.1; JOINED; Genomic_DNA.
EMBL; AF054591; AAC08998.1; JOINED; Genomic_DNA.
EMBL; AF054592; AAC08998.1; JOINED; Genomic_DNA.
EMBL; AF054593; AAC08998.1; JOINED; Genomic_DNA.
EMBL; AF054594; AAC08998.1; JOINED; Genomic_DNA.
EMBL; AF054595; AAC08998.1; JOINED; Genomic_DNA.
EMBL; AF054596; AAC08998.1; JOINED; Genomic_DNA.
EMBL; AF054597; AAC08998.1; JOINED; Genomic_DNA.
EMBL; AF035670; AAD02042.1; -; Genomic_DNA.
EMBL; AF035662; AAD02042.1; JOINED; Genomic_DNA.
EMBL; AF035663; AAD02042.1; JOINED; Genomic_DNA.
EMBL; AF035664; AAD02042.1; JOINED; Genomic_DNA.
EMBL; AF035665; AAD02042.1; JOINED; Genomic_DNA.
EMBL; AF035666; AAD02042.1; JOINED; Genomic_DNA.
EMBL; AF035667; AAD02042.1; JOINED; Genomic_DNA.
EMBL; AF035668; AAD02042.1; JOINED; Genomic_DNA.
EMBL; AF035669; AAD02042.1; JOINED; Genomic_DNA.
EMBL; AY497473; AAR32097.1; -; Genomic_DNA.
EMBL; AL162427; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC071181; AAH71181.1; -; mRNA.
EMBL; AJ619019; CAF02096.2; -; mRNA.
EMBL; AJ619020; CAF02097.1; -; mRNA.
CCDS; CCDS47998.1; -. [P36897-3]
CCDS; CCDS6738.1; -. [P36897-1]
CCDS; CCDS78413.1; -. [P36897-2]
PIR; A49432; A49432.
RefSeq; NP_001124388.1; NM_001130916.2. [P36897-3]
RefSeq; NP_001293139.1; NM_001306210.1. [P36897-2]
RefSeq; NP_004603.1; NM_004612.3. [P36897-1]
PDB; 1B6C; X-ray; 2.60 A; B/D/F/H=162-503.
PDB; 1IAS; X-ray; 2.90 A; A/B/C/D/E=162-503.
PDB; 1PY5; X-ray; 2.30 A; A=175-500.
PDB; 1RW8; X-ray; 2.40 A; A=200-500.
PDB; 1TBI; Model; -; A=34-114.
PDB; 1VJY; X-ray; 2.00 A; A=201-503.
PDB; 2L5S; NMR; -; A=31-115.
PDB; 2PJY; X-ray; 3.00 A; C=33-111.
PDB; 2WOT; X-ray; 1.85 A; A=200-503.
PDB; 2WOU; X-ray; 2.30 A; A=200-503.
PDB; 2X7O; X-ray; 3.70 A; A/B/C/D/E=162-503.
PDB; 3FAA; X-ray; 3.35 A; A/B/C/D/E=162-503.
PDB; 3GXL; X-ray; 1.80 A; A=201-503.
PDB; 3HMM; X-ray; 1.70 A; A=201-503.
PDB; 3KCF; X-ray; 2.80 A; A/B/C/D/E=162-503.
PDB; 3KFD; X-ray; 3.00 A; I/J/K/L=31-115.
PDB; 3TZM; X-ray; 1.70 A; A=200-503.
PDB; 4X0M; X-ray; 1.68 A; A=200-503.
PDB; 4X2F; X-ray; 1.49 A; A=200-503.
PDB; 4X2G; X-ray; 1.51 A; A=200-503.
PDB; 4X2J; X-ray; 1.69 A; A=200-503.
PDB; 4X2K; X-ray; 1.69 A; A=200-503.
PDB; 4X2N; X-ray; 1.80 A; A=200-503.
PDB; 5E8S; X-ray; 1.45 A; A=200-503.
PDB; 5E8T; X-ray; 1.70 A; A=200-503.
PDB; 5E8U; X-ray; 2.03 A; A=200-503.
PDB; 5E8W; X-ray; 1.86 A; A=200-503.
PDB; 5E8X; X-ray; 1.45 A; A=200-503.
PDB; 5E8Z; X-ray; 1.51 A; A=200-503.
PDB; 5E90; X-ray; 2.05 A; A=200-503.
PDB; 5FRI; X-ray; 2.00 A; A=200-498.
PDB; 5QIK; X-ray; 1.58 A; A=200-503.
PDB; 5QIL; X-ray; 1.98 A; A=200-503.
PDB; 5QIM; X-ray; 1.75 A; A=200-503.
PDB; 5QTZ; X-ray; 1.83 A; A=200-503.
PDB; 5QU0; X-ray; 1.67 A; A=200-503.
PDB; 5USQ; X-ray; 2.55 A; A=200-498.
PDB; 6B8Y; X-ray; 1.65 A; A=200-503.
PDB; 6MAC; X-ray; 2.34 A; K=33-112.
PDBsum; 1B6C; -.
PDBsum; 1IAS; -.
PDBsum; 1PY5; -.
PDBsum; 1RW8; -.
PDBsum; 1TBI; -.
PDBsum; 1VJY; -.
PDBsum; 2L5S; -.
PDBsum; 2PJY; -.
PDBsum; 2WOT; -.
PDBsum; 2WOU; -.
PDBsum; 2X7O; -.
PDBsum; 3FAA; -.
PDBsum; 3GXL; -.
PDBsum; 3HMM; -.
PDBsum; 3KCF; -.
PDBsum; 3KFD; -.
PDBsum; 3TZM; -.
PDBsum; 4X0M; -.
PDBsum; 4X2F; -.
PDBsum; 4X2G; -.
PDBsum; 4X2J; -.
PDBsum; 4X2K; -.
PDBsum; 4X2N; -.
PDBsum; 5E8S; -.
PDBsum; 5E8T; -.
PDBsum; 5E8U; -.
PDBsum; 5E8W; -.
PDBsum; 5E8X; -.
PDBsum; 5E8Z; -.
PDBsum; 5E90; -.
PDBsum; 5FRI; -.
PDBsum; 5QIK; -.
PDBsum; 5QIL; -.
PDBsum; 5QIM; -.
PDBsum; 5QTZ; -.
PDBsum; 5QU0; -.
PDBsum; 5USQ; -.
PDBsum; 6B8Y; -.
PDBsum; 6MAC; -.
SMR; P36897; -.
BioGRID; 112904; 195.
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; P36897; -.
DIP; DIP-5935N; -.
IntAct; P36897; 22.
MINT; P36897; -.
STRING; 9606.ENSP00000364133; -.
ChEMBL; CHEMBL4439; -.
DrugBank; DB07267; 2-(6-methylpyridin-2-yl)-N-pyridin-4-ylquinazolin-4-amine.
DrugBank; DB04480; 3-(4-Fluorophenyl)-2-(6-Methylpyridin-2-Yl)-5,6-Dihydro-4h-Pyrrolo[1,2-B]Pyrazole.
DrugBank; DB03921; 4-(3-Pyridin-2-Yl-1h-Pyrazol-4-Yl)Quinoline.
DrugBank; DB12010; Fostamatinib.
DrugBank; DB08450; N-1H-indazol-5-yl-2-(6-methylpyridin-2-yl)quinazolin-4-amine.
DrugBank; DB07152; N-[4-(5-fluoro-6-methylpyridin-2-yl)-5-quinoxalin-6-yl-1H-imidazol-2-yl]acetamide.
DrugBank; DB04434; Naphthyridine Inhibitor.
DrugCentral; P36897; -.
GuidetoPHARMACOLOGY; 1788; -.
iPTMnet; P36897; -.
PhosphoSitePlus; P36897; -.
BioMuta; TGFBR1; -.
DMDM; 547777; -.
EPD; P36897; -.
jPOST; P36897; -.
MassIVE; P36897; -.
PaxDb; P36897; -.
PeptideAtlas; P36897; -.
PRIDE; P36897; -.
ProteomicsDB; 55234; -. [P36897-1]
ProteomicsDB; 55235; -. [P36897-2]
ProteomicsDB; 55236; -. [P36897-3]
Antibodypedia; 29038; 582 antibodies.
DNASU; 7046; -.
Ensembl; ENST00000374990; ENSP00000364129; ENSG00000106799. [P36897-3]
Ensembl; ENST00000374994; ENSP00000364133; ENSG00000106799. [P36897-1]
Ensembl; ENST00000552516; ENSP00000447297; ENSG00000106799. [P36897-2]
GeneID; 7046; -.
KEGG; hsa:7046; -.
UCSC; uc004azd.4; human. [P36897-1]
CTD; 7046; -.
DisGeNET; 7046; -.
EuPathDB; HostDB:ENSG00000106799.12; -.
GeneCards; TGFBR1; -.
GeneReviews; TGFBR1; -.
HGNC; HGNC:11772; TGFBR1.
HPA; ENSG00000106799; Low tissue specificity.
MalaCards; TGFBR1; -.
MIM; 132800; phenotype.
MIM; 190181; gene.
MIM; 609192; phenotype.
neXtProt; NX_P36897; -.
OpenTargets; ENSG00000106799; -.
Orphanet; 91387; Familial thoracic aortic aneurysm and aortic dissection.
Orphanet; 60030; Loeys-Dietz syndrome.
Orphanet; 65748; Multiple self-healing squamous epithelioma.
PharmGKB; PA36485; -.
eggNOG; KOG2052; Eukaryota.
eggNOG; ENOG410XQT0; LUCA.
GeneTree; ENSGT00940000156394; -.
HOGENOM; CLU_000288_8_1_1; -.
InParanoid; P36897; -.
KO; K04674; -.
OMA; LMIYICH; -.
PhylomeDB; P36897; -.
TreeFam; TF314724; -.
BRENDA; 2.7.10.2; 2681.
BRENDA; 2.7.11.30; 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-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.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
SignaLink; P36897; -.
SIGNOR; P36897; -.
BioGRID-ORCS; 7046; 33 hits in 797 CRISPR screens.
ChiTaRS; TGFBR1; human.
EvolutionaryTrace; P36897; -.
GeneWiki; TGF_beta_receptor_1; -.
GenomeRNAi; 7046; -.
Pharos; P36897; Tchem.
PRO; PR:P36897; -.
Proteomes; UP000005640; Chromosome 9.
RNAct; P36897; protein.
Bgee; ENSG00000106799; Expressed in decidua and 204 other tissues.
ExpressionAtlas; P36897; baseline and differential.
Genevisible; P36897; HS.
GO; GO:0048179; C:activin receptor complex; IBA:GO_Central.
GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
GO; GO:0005623; C:cell; ISS:AgBase.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; ISS:AgBase.
GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; 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:0016361; F:activin receptor activity, type I; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IDA:HGNC-UCL.
GO; GO:0070411; F:I-SMAD binding; IPI:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; IDA:BHF-UCL.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:HGNC-UCL.
GO; GO:0046332; F:SMAD binding; IDA:HGNC-UCL.
GO; GO:0050431; F:transforming growth factor beta binding; IDA:HGNC-UCL.
GO; GO:0005025; F:transforming growth factor beta receptor activity, type I; IDA:BHF-UCL.
GO; GO:0005024; F:transforming growth factor beta-activated receptor activity; IDA:BHF-UCL.
GO; GO:0005114; F:type II transforming growth factor beta receptor binding; IDA:BHF-UCL.
GO; GO:0000186; P:activation of MAPKK activity; IDA:BHF-UCL.
GO; GO:0032924; P:activin receptor signaling pathway; ISS:AgBase.
GO; GO:0060978; P:angiogenesis involved in coronary vascular morphogenesis; ISS:BHF-UCL.
GO; GO:0009952; P:anterior/posterior pattern specification; ISS:BHF-UCL.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0048844; P:artery morphogenesis; ISS:BHF-UCL.
GO; GO:0001824; P:blastocyst development; IEA:Ensembl.
GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; ISS:AgBase.
GO; GO:0007050; P:cell cycle arrest; TAS:UniProtKB.
GO; GO:0048870; P:cell motility; IMP:BHF-UCL.
GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:BHF-UCL.
GO; GO:0030199; P:collagen fibril organization; ISS:BHF-UCL.
GO; GO:0060982; P:coronary artery morphogenesis; ISS:BHF-UCL.
GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; ISS:BHF-UCL.
GO; GO:0042118; P:endothelial cell activation; ISS:AgBase.
GO; GO:0043542; P:endothelial cell migration; IEA:Ensembl.
GO; GO:1905223; P:epicardium morphogenesis; ISS:BHF-UCL.
GO; GO:0001837; P:epithelial to mesenchymal transition; IDA:UniProtKB.
GO; GO:0043062; P:extracellular structure organization; TAS:UniProtKB.
GO; GO:0008354; P:germ cell migration; ISS:BHF-UCL.
GO; GO:0007507; P:heart development; ISS:AgBase.
GO; GO:0001701; P:in utero embryonic development; ISS:BHF-UCL.
GO; GO:0035556; P:intracellular signal transduction; ISS:AgBase.
GO; GO:0001822; P:kidney development; ISS:BHF-UCL.
GO; GO:0002088; P:lens development in camera-type eye; IEA:Ensembl.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:0048762; P:mesenchymal cell differentiation; ISS:AgBase.
GO; GO:0032331; P:negative regulation of chondrocyte differentiation; ISS:BHF-UCL.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IEA:Ensembl.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:BHF-UCL.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; TAS:Reactome.
GO; GO:0007399; P:nervous system development; IBA:GO_Central.
GO; GO:0048663; P:neuron fate commitment; ISS:BHF-UCL.
GO; GO:0060017; P:parathyroid gland development; ISS:BHF-UCL.
GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:BHF-UCL.
GO; GO:0060037; P:pharyngeal system development; ISS:BHF-UCL.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:0030307; P:positive regulation of cell growth; IDA:BHF-UCL.
GO; GO:0030335; P:positive regulation of cell migration; IDA:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:HGNC-UCL.
GO; GO:0051272; P:positive regulation of cellular component movement; IMP:BHF-UCL.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISS:AgBase.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISS:BHF-UCL.
GO; GO:1905007; P:positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation; ISS:BHF-UCL.
GO; GO:0051491; P:positive regulation of filopodium assembly; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:BHF-UCL.
GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IDA:BHF-UCL.
GO; GO:0051496; P:positive regulation of stress fiber assembly; ISS:BHF-UCL.
GO; GO:1905075; P:positive regulation of tight junction disassembly; ISS:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0006468; P:protein phosphorylation; IDA:BHF-UCL.
GO; GO:0060043; P:regulation of cardiac muscle cell proliferation; ISS:BHF-UCL.
GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; ISS:AgBase.
GO; GO:0010468; P:regulation of gene expression; ISS:AgBase.
GO; GO:0043393; P:regulation of protein binding; IEA:Ensembl.
GO; GO:0031396; P:regulation of protein ubiquitination; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:HGNC-UCL.
GO; GO:0070723; P:response to cholesterol; IDA:BHF-UCL.
GO; GO:0060021; P:roof of mouth development; ISS:BHF-UCL.
GO; GO:0007165; P:signal transduction; IDA:HGNC-UCL.
GO; GO:0001501; P:skeletal system development; ISS:BHF-UCL.
GO; GO:0048705; P:skeletal system morphogenesis; ISS:BHF-UCL.
GO; GO:0048538; P:thymus development; ISS:BHF-UCL.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0003223; P:ventricular compact myocardium morphogenesis; ISS:BHF-UCL.
GO; GO:0060412; P:ventricular septum morphogenesis; ISS:BHF-UCL.
GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; ISS:BHF-UCL.
GO; GO:0042060; P:wound healing; TAS:UniProtKB.
IDEAL; IID00413; -.
InterPro; IPR000472; Activin_recp.
InterPro; IPR003605; GS_dom.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR000333; TGFB_receptor.
PANTHER; PTHR23255; PTHR23255; 1.
Pfam; PF01064; Activin_recp; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF08515; TGF_beta_GS; 1.
SMART; SM00467; GS; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51256; GS; 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 junction; Cell membrane; Craniosynostosis;
Differentiation; Direct protein sequencing; Disease mutation;
Disulfide bond; Glycoprotein; Growth regulation; Isopeptide bond; Kinase;
Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding;
Phosphoprotein; Polymorphism; Receptor; Reference proteome;
Serine/threonine-protein kinase; Signal; Tight junction; Transferase;
Transmembrane; Transmembrane helix; Ubl conjugation.
SIGNAL 1..33
/evidence="ECO:0000269|PubMed:9661882"
CHAIN 34..503
/note="TGF-beta receptor type-1"
/id="PRO_0000024423"
TOPO_DOM 34..126
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 127..147
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 148..503
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 175..204
/note="GS"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00585"
DOMAIN 205..495
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 211..219
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
MOTIF 193..194
/note="FKBP1A-binding"
ACT_SITE 333
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10027"
BINDING 232
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
MOD_RES 165
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19369195"
MOD_RES 185
/note="Phosphothreonine; by TGFBR2"
/evidence="ECO:0000269|PubMed:7774578"
MOD_RES 186
/note="Phosphothreonine; by TGFBR2"
/evidence="ECO:0000269|PubMed:7774578"
MOD_RES 187
/note="Phosphoserine; by TGFBR2"
/evidence="ECO:0000269|PubMed:7774578"
MOD_RES 189
/note="Phosphoserine; by TGFBR2"
/evidence="ECO:0000269|PubMed:7774578"
MOD_RES 191
/note="Phosphoserine; by TGFBR2"
/evidence="ECO:0000269|PubMed:7774578"
CARBOHYD 45
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 36..54
/evidence="ECO:0000269|PubMed:18243111,
ECO:0000269|PubMed:20207738"
DISULFID 38..41
/evidence="ECO:0000269|PubMed:18243111,
ECO:0000269|PubMed:20207738"
DISULFID 48..71
/evidence="ECO:0000269|PubMed:18243111,
ECO:0000269|PubMed:20207738"
DISULFID 86..100
/evidence="ECO:0000269|PubMed:18243111,
ECO:0000269|PubMed:20207738"
DISULFID 101..106
/evidence="ECO:0000269|PubMed:18243111,
ECO:0000269|PubMed:20207738"
CROSSLNK 391
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO)"
/evidence="ECO:0000250"
VAR_SEQ 114
/note="T -> TGPFS (in isoform 2)"
/evidence="ECO:0000303|PubMed:17845732"
/id="VSP_041326"
VAR_SEQ 115..191
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_041327"
VARIANT 24..26
/note="Missing (in allele TGFBR1*6A; could be a tumor
susceptibility allele)"
/id="VAR_022342"
VARIANT 26
/note="A -> AA (in allele TGFBR1*10A; rare polymorphism)"
/evidence="ECO:0000269|PubMed:9661882"
/id="VAR_022343"
VARIANT 41
/note="C -> Y (in MSSE; hypomorphic mutation)"
/evidence="ECO:0000269|PubMed:21358634"
/id="VAR_065826"
VARIANT 45
/note="N -> S (in MSSE; hypomorphic mutation;
dbSNP:rs387906696)"
/evidence="ECO:0000269|PubMed:21358634"
/id="VAR_065827"
VARIANT 52
/note="G -> R (in MSSE; hypomorphic mutation;
dbSNP:rs587776865)"
/evidence="ECO:0000269|PubMed:21358634"
/id="VAR_065828"
VARIANT 83
/note="P -> L (in MSSE; hypomorphic mutation;
dbSNP:rs757374917)"
/evidence="ECO:0000269|PubMed:21358634"
/id="VAR_065829"
VARIANT 139
/note="I -> V (in dbSNP:rs148176750)"
/evidence="ECO:0000269|PubMed:18987736"
/id="VAR_054160"
VARIANT 153
/note="V -> I (in dbSNP:rs56014374)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_041412"
VARIANT 200
/note="T -> I (in LDS1; dbSNP:rs121918712)"
/evidence="ECO:0000269|PubMed:15731757"
/id="VAR_022344"
VARIANT 232
/note="K -> E (in LDS1)"
/evidence="ECO:0000269|PubMed:16928994"
/id="VAR_029481"
VARIANT 241
/note="S -> L (in LDS1; dbSNP:rs111854391)"
/evidence="ECO:0000269|PubMed:16596670,
ECO:0000269|PubMed:16791849"
/id="VAR_029482"
VARIANT 266
/note="D -> Y (in LDS1)"
/evidence="ECO:0000269|PubMed:22113417"
/id="VAR_066720"
VARIANT 267
/note="N -> H (in a patient with Marfan syndrome)"
/evidence="ECO:0000269|PubMed:16791849"
/id="VAR_029483"
VARIANT 291
/note="Y -> C (in dbSNP:rs35974499)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_041413"
VARIANT 318
/note="M -> R (in LDS1; dbSNP:rs121918710)"
/evidence="ECO:0000269|PubMed:15731757"
/id="VAR_022345"
VARIANT 351
/note="D -> G (in LDS1)"
/evidence="ECO:0000269|PubMed:19883511"
/id="VAR_066721"
VARIANT 375
/note="T -> R (in LDS1)"
/evidence="ECO:0000269|PubMed:22113417"
/id="VAR_066722"
VARIANT 400
/note="D -> G (in LDS1; dbSNP:rs121918711)"
/evidence="ECO:0000269|PubMed:15731757"
/id="VAR_022346"
VARIANT 487
/note="R -> P (in LDS1; dbSNP:rs113605875)"
/evidence="ECO:0000269|PubMed:15731757,
ECO:0000269|PubMed:16928994"
/id="VAR_022347"
VARIANT 487
/note="R -> Q (in LDS1; dbSNP:rs113605875)"
/evidence="ECO:0000269|PubMed:16791849,
ECO:0000269|PubMed:16928994, ECO:0000269|PubMed:22113417"
/id="VAR_029484"
VARIANT 487
/note="R -> W (in LDS1; dbSNP:rs111426349)"
/evidence="ECO:0000269|PubMed:16928994"
/id="VAR_029485"
MUTAGEN 185..186
/note="TT->VV: Loss of phosphorylation on threonine
residues. Loss of threonine phosphorylation, reduced
phosphorylation on serine residues and loss of response to
TGF-beta; when associated with A-187; A-189 and A-191."
/evidence="ECO:0000269|PubMed:7774578"
MUTAGEN 187
/note="S->A: Loss of threonine phosphorylation, reduced
phosphorylation on serine residues and loss of response to
TGF-beta; when associated with 185-VV-186; A-189 and A-
191."
/evidence="ECO:0000269|PubMed:7774578"
MUTAGEN 189
/note="S->A: Loss of threonine phosphorylation, reduced
phosphorylation on serine residues and loss of response to
TGF-beta; when associated with 185-VV-186; A-187 and A-
191."
/evidence="ECO:0000269|PubMed:7774578"
MUTAGEN 191
/note="S->A: Loss of threonine phosphorylation, reduced
phosphorylation on serine residues and loss of response to
TGF-beta; when associated with 185-VV-186; A-187 and A-
189."
/evidence="ECO:0000269|PubMed:7774578"
MUTAGEN 193
/note="L->G: Loss of interaction with FKBP1A."
/evidence="ECO:0000269|PubMed:9233797"
MUTAGEN 194
/note="P->K: Loss of interaction with FKBP1A."
/evidence="ECO:0000269|PubMed:9233797"
MUTAGEN 200
/note="T->D: Loss of response to TGF-beta."
/evidence="ECO:0000269|PubMed:7774578"
MUTAGEN 200
/note="T->V: Loss of phosphorylation. Loss of response to
TGF-beta."
/evidence="ECO:0000269|PubMed:7774578"
MUTAGEN 204
/note="T->D: Constitutive activation."
/evidence="ECO:0000269|PubMed:7774578"
MUTAGEN 204
/note="T->V: Reduced phosphorylation. Reduced response to
TGF-beta."
/evidence="ECO:0000269|PubMed:7774578"
STRAND 35..37
/evidence="ECO:0000244|PDB:6MAC"
TURN 42..46
/evidence="ECO:0000244|PDB:6MAC"
STRAND 47..49
/evidence="ECO:0000244|PDB:6MAC"
STRAND 51..63
/evidence="ECO:0000244|PDB:6MAC"
STRAND 65..72
/evidence="ECO:0000244|PDB:6MAC"
HELIX 74..76
/evidence="ECO:0000244|PDB:6MAC"
STRAND 77..79
/evidence="ECO:0000244|PDB:6MAC"
TURN 84..86
/evidence="ECO:0000244|PDB:3KFD"
STRAND 89..91
/evidence="ECO:0000244|PDB:6MAC"
STRAND 94..101
/evidence="ECO:0000244|PDB:6MAC"
STRAND 102..105
/evidence="ECO:0000244|PDB:3KFD"
HELIX 107..109
/evidence="ECO:0000244|PDB:2L5S"
HELIX 177..183
/evidence="ECO:0000244|PDB:1B6C"
STRAND 187..190
/evidence="ECO:0000244|PDB:3KCF"
STRAND 191..193
/evidence="ECO:0000244|PDB:1B6C"
HELIX 202..204
/evidence="ECO:0000244|PDB:5E8S"
STRAND 205..213
/evidence="ECO:0000244|PDB:5E8S"
STRAND 215..224
/evidence="ECO:0000244|PDB:5E8S"
STRAND 227..234
/evidence="ECO:0000244|PDB:5E8S"
HELIX 236..238
/evidence="ECO:0000244|PDB:5E8S"
HELIX 239..249
/evidence="ECO:0000244|PDB:5E8S"
STRAND 251..253
/evidence="ECO:0000244|PDB:3KCF"
STRAND 262..269
/evidence="ECO:0000244|PDB:5E8S"
STRAND 271..281
/evidence="ECO:0000244|PDB:5E8S"
HELIX 288..294
/evidence="ECO:0000244|PDB:5E8S"
HELIX 299..317
/evidence="ECO:0000244|PDB:5E8S"
STRAND 322..324
/evidence="ECO:0000244|PDB:5E8X"
STRAND 328..330
/evidence="ECO:0000244|PDB:5E8Z"
HELIX 336..338
/evidence="ECO:0000244|PDB:5E8S"
STRAND 339..341
/evidence="ECO:0000244|PDB:5E8S"
STRAND 347..349
/evidence="ECO:0000244|PDB:5E8S"
HELIX 352..354
/evidence="ECO:0000244|PDB:5E8S"
STRAND 356..359
/evidence="ECO:0000244|PDB:5E8S"
TURN 360..363
/evidence="ECO:0000244|PDB:5E8S"
STRAND 364..367
/evidence="ECO:0000244|PDB:5E8S"
STRAND 368..371
/evidence="ECO:0000244|PDB:5E8X"
HELIX 376..378
/evidence="ECO:0000244|PDB:5E8S"
HELIX 381..384
/evidence="ECO:0000244|PDB:5E8S"
HELIX 393..413
/evidence="ECO:0000244|PDB:5E8S"
STRAND 417..419
/evidence="ECO:0000244|PDB:3KCF"
TURN 427..431
/evidence="ECO:0000244|PDB:5E8S"
HELIX 438..445
/evidence="ECO:0000244|PDB:5E8S"
HELIX 456..460
/evidence="ECO:0000244|PDB:5E8S"
HELIX 462..474
/evidence="ECO:0000244|PDB:5E8S"
HELIX 479..481
/evidence="ECO:0000244|PDB:5E8S"
HELIX 485..497
/evidence="ECO:0000244|PDB:5E8S"
SEQUENCE 503 AA; 55960 MW; 179F11404725DDCB CRC64;
MEAAVAAPRP RLLLLVLAAA AAAAAALLPG ATALQCFCHL CTKDNFTCVT DGLCFVSVTE
TTDKVIHNSM CIAEIDLIPR DRPFVCAPSS KTGSVTTTYC CNQDHCNKIE LPTTVKSSPG
LGPVELAAVI AGPVCFVCIS LMLMVYICHN RTVIHHRVPN EEDPSLDRPF ISEGTTLKDL
IYDMTTSGSG SGLPLLVQRT IARTIVLQES IGKGRFGEVW RGKWRGEEVA VKIFSSREER
SWFREAEIYQ TVMLRHENIL GFIAADNKDN GTWTQLWLVS DYHEHGSLFD YLNRYTVTVE
GMIKLALSTA SGLAHLHMEI VGTQGKPAIA HRDLKSKNIL VKKNGTCCIA DLGLAVRHDS
ATDTIDIAPN HRVGTKRYMA PEVLDDSINM KHFESFKRAD IYAMGLVFWE IARRCSIGGI
HEDYQLPYYD LVPSDPSVEE MRKVVCEQKL RPNIPNRWQS CEALRVMAKI MRECWYANGA
ARLTALRIKK TLSQLSQQEG IKM


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EIAAB42139 Betaglycan,Homo sapiens,Human,TGF-beta receptor type 3,TGF-beta receptor type III,TGFBR3,TGFR-3,Transforming growth factor beta receptor III,Transforming growth factor beta receptor type 3
18-272-195253 TGFBR2 - Goat polyclonal to TGFBR2; EC 2.7.11.30; TGF-beta receptor type II; TGFR-2; TGF-beta type II receptor; Transforming growth factor-beta receptor type II; TbetaR-II Polyclonal 0.05 mg
18-272-195150 Activin Receptor Type IA - Goat polyclonal to Activin Receptor Type IA; EC 2.7.11.30; Activin receptor type I; ACTR-I; Serine_threonine-protein kinase receptor R1; SKR1; Activin receptor-like kinase 2 0.025 mg
EIAAB42137 Betaglycan,Mouse,Mus musculus,TGF-beta receptor type 3,TGF-beta receptor type III,Tgfbr3,TGFR-3,Transforming growth factor beta receptor III,Transforming growth factor beta receptor type 3
EIAAB42140 Betaglycan,Rat,Rattus norvegicus,TGF-beta receptor type 3,TGF-beta receptor type III,Tgfbr3,TGFR-3,Transforming growth factor beta receptor III,Transforming growth factor beta receptor type 3
EIAAB42138 Betaglycan,Pig,Sus scrofa,TGF-beta receptor type 3,TGF-beta receptor type III,TGFBR3,TGFR-3,Transforming growth factor beta receptor III,Transforming growth factor beta receptor type 3
E0015h ELISA kit Activin receptor-like kinase 3,ACVRLK3,ALK3,ALK-3,BMP type-1A receptor,BMPR1A,BMPR-1A,Bone morphogenetic protein receptor type-1A,Homo sapiens,Human,Serine_threonine-protein kinase receptor 96T
U0015h CLIA Activin receptor-like kinase 3,ACVRLK3,ALK3,ALK-3,BMP type-1A receptor,BMPR1A,BMPR-1A,Bone morphogenetic protein receptor type-1A,Homo sapiens,Human,Serine_threonine-protein kinase receptor R5,SK 96T
E0015h ELISA Activin receptor-like kinase 3,ACVRLK3,ALK3,ALK-3,BMP type-1A receptor,BMPR1A,BMPR-1A,Bone morphogenetic protein receptor type-1A,Homo sapiens,Human,Serine_threonine-protein kinase receptor R5,S 96T
18-272-195151 Activin A Receptor Type IB - Goat polyclonal to Activin A Receptor Type IB; EC 2.7.11.30; ACTR-IB; Serine_threonine-protein kinase receptor R2; SKR2; Activin receptor-like kinase 4; ALK-4 Polyclonal 0.025 mg
E0015m ELISA kit Activin receptor-like kinase 3,Acvrlk3,ALK-3,BMP type-1A receptor,BMP-2_BMP-4 receptor,Bmpr,Bmpr1a,BMPR-1A,Bone morphogenetic protein receptor type-1A,Mouse,Mus musculus,Serine_threonine-pr 96T
E0015m ELISA Activin receptor-like kinase 3,Acvrlk3,ALK-3,BMP type-1A receptor,BMP-2_BMP-4 receptor,Bmpr,Bmpr1a,BMPR-1A,Bone morphogenetic protein receptor type-1A,Mouse,Mus musculus,Serine_threonine-protein 96T
U0015m CLIA Activin receptor-like kinase 3,Acvrlk3,ALK-3,BMP type-1A receptor,BMP-2_BMP-4 receptor,Bmpr,Bmpr1a,BMPR-1A,Bone morphogenetic protein receptor type-1A,Mouse,Mus musculus,Serine_threonine-protein 96T