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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.
25-OCT-2017, entry version 205.
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;
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, ENZYME 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]
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).
[31]
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).
[32]
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).
[33]
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).
[34]
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).
[35]
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).
[36]
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).
[37]
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).
[38]
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).
[39]
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).
[40]
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).
[41]
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).
[42]
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).
[43]
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).
[44]
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).
[45]
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).
[46]
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).
[47]
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).
[48]
ERRATUM.
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).
[49]
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: ATP + [receptor-protein] = ADP + [receptor-
protein] phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- ENZYME 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). {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:7774578, ECO:0000269|PubMed:8980228,
ECO:0000269|PubMed:9233797, ECO:0000269|PubMed:9311995,
ECO:0000269|PubMed:9346908, ECO:0000269|PubMed:9865696}.
-!- INTERACTION:
Q99IB8:- (xeno); NbExp=5; IntAct=EBI-1027557, EBI-6858501;
P62942:FKBP1A; NbExp=2; IntAct=EBI-1027557, EBI-1027571;
P02750:LRG1; NbExp=6; IntAct=EBI-16065417, EBI-9083443;
P01137:TGFB1; NbExp=2; IntAct=EBI-1027557, EBI-779636;
P63104:YWHAZ; NbExp=4; IntAct=EBI-1027557, EBI-347088;
-!- 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.48).
{ECO:0000269|PubMed:22113417, ECO:0000269|Ref.48}.
-!- 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]
UniGene; Hs.494622; -.
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; 5USQ; X-ray; 2.55 A; A=200-498.
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; 5USQ; -.
ProteinModelPortal; P36897; -.
SMR; P36897; -.
BioGrid; 112904; 185.
CORUM; P36897; -.
DIP; DIP-5935N; -.
IntAct; P36897; 20.
MINT; MINT-152959; -.
STRING; 9606.ENSP00000364133; -.
BindingDB; P36897; -.
ChEMBL; CHEMBL4439; -.
DrugBank; DB07267; 2-(6-methylpyridin-2-yl)-N-pyridin-4-ylquinazolin-4-amine.
DrugBank; DB03921; 4-(3-Pyridin-2-Yl-1h-Pyrazol-4-Yl)Quinoline.
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.
GuidetoPHARMACOLOGY; 1788; -.
iPTMnet; P36897; -.
PhosphoSitePlus; P36897; -.
BioMuta; TGFBR1; -.
DMDM; 547777; -.
EPD; P36897; -.
PaxDb; P36897; -.
PeptideAtlas; P36897; -.
PRIDE; P36897; -.
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; CAB002441; -.
HPA; CAB031481; -.
HPA; HPA056473; -.
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 keratoacanthoma, Ferguson-Smith type.
PharmGKB; PA36485; -.
eggNOG; KOG2052; Eukaryota.
eggNOG; ENOG410XQT0; LUCA.
GeneTree; ENSGT00760000118876; -.
HOGENOM; HOG000230587; -.
HOVERGEN; HBG054502; -.
InParanoid; P36897; -.
KO; K04674; -.
OMA; GATALQC; -.
OrthoDB; EOG091G0BIU; -.
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-3315487; SMAD2/3 MH2 Domain 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; -.
ChiTaRS; TGFBR1; human.
EvolutionaryTrace; P36897; -.
GeneWiki; TGF_beta_receptor_1; -.
GenomeRNAi; 7046; -.
PRO; PR:P36897; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000106799; -.
CleanEx; HS_TGFBR1; -.
ExpressionAtlas; P36897; baseline and differential.
Genevisible; P36897; HS.
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; IEA:Ensembl.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0016020; C:membrane; ISS:AgBase.
GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0043235; C:receptor complex; IDA:BHF-UCL.
GO; GO:0070022; C:transforming growth factor beta receptor complex; IC:BHF-UCL.
GO; GO:0005524; F:ATP binding; IDA:HGNC.
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.
GO; GO:0005057; F:signal transducer activity, downstream of receptor; ISS:AgBase.
GO; GO:0004702; F:signal transducer, downstream of receptor, with serine/threonine kinase activity; IEA:Ensembl.
GO; GO:0046332; F:SMAD binding; IDA:HGNC.
GO; GO:0050431; F:transforming growth factor beta binding; IDA:BHF-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: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:0048663; P:neuron fate commitment; ISS:BHF-UCL.
GO; GO:0060021; P:palate development; 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 proliferation; IMP:HGNC.
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:1905075; P:positive regulation of occluding junction disassembly; ISS: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 import into nucleus; IDA:BHF-UCL.
GO; GO:0051496; P:positive regulation of stress fiber assembly; 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.
GO; GO:0070723; P:response to cholesterol; IDA:BHF-UCL.
GO; GO:0007165; P:signal transduction; IDA:HGNC.
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.
InterPro; IPR000472; Activin_recp.
InterPro; IPR003605; GS_dom.
InterPro; IPR011009; Kinase-like_dom.
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; Complete proteome;
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 {ECO:0000269|PubMed:9661882}.
CHAIN 34 503 TGF-beta receptor type-1.
/FTId=PRO_0000024423.
TOPO_DOM 34 126 Extracellular. {ECO:0000255}.
TRANSMEM 127 147 Helical. {ECO:0000255}.
TOPO_DOM 148 503 Cytoplasmic. {ECO:0000255}.
DOMAIN 175 204 GS. {ECO:0000255|PROSITE-
ProRule:PRU00585}.
DOMAIN 205 495 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 211 219 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 193 194 FKBP1A-binding.
ACT_SITE 333 333 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 232 232 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 165 165 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 185 185 Phosphothreonine; by TGFBR2.
{ECO:0000269|PubMed:7774578}.
MOD_RES 186 186 Phosphothreonine; by TGFBR2.
{ECO:0000269|PubMed:7774578}.
MOD_RES 187 187 Phosphoserine; by TGFBR2.
{ECO:0000269|PubMed:7774578}.
MOD_RES 189 189 Phosphoserine; by TGFBR2.
{ECO:0000269|PubMed:7774578}.
MOD_RES 191 191 Phosphoserine; by TGFBR2.
{ECO:0000269|PubMed:7774578}.
CARBOHYD 45 45 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 36 54 {ECO:0000269|PubMed:18243111,
ECO:0000269|PubMed:20207738}.
DISULFID 38 41 {ECO:0000269|PubMed:18243111,
ECO:0000269|PubMed:20207738}.
DISULFID 48 71 {ECO:0000269|PubMed:18243111,
ECO:0000269|PubMed:20207738}.
DISULFID 86 100 {ECO:0000269|PubMed:18243111,
ECO:0000269|PubMed:20207738}.
DISULFID 101 106 {ECO:0000269|PubMed:18243111,
ECO:0000269|PubMed:20207738}.
CROSSLNK 391 391 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
VAR_SEQ 114 114 T -> TGPFS (in isoform 2).
{ECO:0000303|PubMed:17845732}.
/FTId=VSP_041326.
VAR_SEQ 115 191 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_041327.
VARIANT 24 26 Missing (in allele TGFBR1*6A; could be a
tumor susceptibility allele).
/FTId=VAR_022342.
VARIANT 26 26 A -> AA (in allele TGFBR1*10A; rare
polymorphism).
{ECO:0000269|PubMed:9661882}.
/FTId=VAR_022343.
VARIANT 41 41 C -> Y (in MSSE; hypomorphic mutation).
{ECO:0000269|PubMed:21358634}.
/FTId=VAR_065826.
VARIANT 45 45 N -> S (in MSSE; hypomorphic mutation;
dbSNP:rs387906696).
{ECO:0000269|PubMed:21358634}.
/FTId=VAR_065827.
VARIANT 52 52 G -> R (in MSSE; hypomorphic mutation;
dbSNP:rs587776865).
{ECO:0000269|PubMed:21358634}.
/FTId=VAR_065828.
VARIANT 83 83 P -> L (in MSSE; hypomorphic mutation;
dbSNP:rs757374917).
{ECO:0000269|PubMed:21358634}.
/FTId=VAR_065829.
VARIANT 139 139 I -> V (in dbSNP:rs148176750).
{ECO:0000269|PubMed:18987736}.
/FTId=VAR_054160.
VARIANT 153 153 V -> I (in dbSNP:rs56014374).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041412.
VARIANT 200 200 T -> I (in LDS1; dbSNP:rs121918712).
{ECO:0000269|PubMed:15731757}.
/FTId=VAR_022344.
VARIANT 232 232 K -> E (in LDS1).
{ECO:0000269|PubMed:16928994}.
/FTId=VAR_029481.
VARIANT 241 241 S -> L (in LDS1; dbSNP:rs111854391).
{ECO:0000269|PubMed:16596670,
ECO:0000269|PubMed:16791849}.
/FTId=VAR_029482.
VARIANT 266 266 D -> Y (in LDS1).
{ECO:0000269|PubMed:22113417}.
/FTId=VAR_066720.
VARIANT 267 267 N -> H (in a patient with Marfan
syndrome). {ECO:0000269|PubMed:16791849}.
/FTId=VAR_029483.
VARIANT 291 291 Y -> C (in dbSNP:rs35974499).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041413.
VARIANT 318 318 M -> R (in LDS1; dbSNP:rs121918710).
{ECO:0000269|PubMed:15731757}.
/FTId=VAR_022345.
VARIANT 351 351 D -> G (in LDS1).
{ECO:0000269|PubMed:19883511}.
/FTId=VAR_066721.
VARIANT 375 375 T -> R (in LDS1).
{ECO:0000269|PubMed:22113417}.
/FTId=VAR_066722.
VARIANT 400 400 D -> G (in LDS1; dbSNP:rs121918711).
{ECO:0000269|PubMed:15731757}.
/FTId=VAR_022346.
VARIANT 487 487 R -> P (in LDS1; dbSNP:rs113605875).
{ECO:0000269|PubMed:15731757,
ECO:0000269|PubMed:16928994}.
/FTId=VAR_022347.
VARIANT 487 487 R -> Q (in LDS1; dbSNP:rs113605875).
{ECO:0000269|PubMed:16791849,
ECO:0000269|PubMed:16928994,
ECO:0000269|PubMed:22113417}.
/FTId=VAR_029484.
VARIANT 487 487 R -> W (in LDS1; dbSNP:rs111426349).
{ECO:0000269|PubMed:16928994}.
/FTId=VAR_029485.
MUTAGEN 185 186 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.
{ECO:0000269|PubMed:7774578}.
MUTAGEN 187 187 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.
{ECO:0000269|PubMed:7774578}.
MUTAGEN 189 189 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.
{ECO:0000269|PubMed:7774578}.
MUTAGEN 191 191 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.
{ECO:0000269|PubMed:7774578}.
MUTAGEN 193 193 L->G: Loss of interaction with FKBP1A.
{ECO:0000269|PubMed:9233797}.
MUTAGEN 194 194 P->K: Loss of interaction with FKBP1A.
{ECO:0000269|PubMed:9233797}.
MUTAGEN 200 200 T->D: Loss of response to TGF-beta.
{ECO:0000269|PubMed:7774578}.
MUTAGEN 200 200 T->V: Loss of phosphorylation. Loss of
response to TGF-beta.
{ECO:0000269|PubMed:7774578}.
MUTAGEN 204 204 T->D: Constitutive activation.
{ECO:0000269|PubMed:7774578}.
MUTAGEN 204 204 T->V: Reduced phosphorylation. Reduced
response to TGF-beta.
{ECO:0000269|PubMed:7774578}.
STRAND 35 37 {ECO:0000244|PDB:3KFD}.
TURN 42 46 {ECO:0000244|PDB:3KFD}.
STRAND 51 57 {ECO:0000244|PDB:3KFD}.
STRAND 61 63 {ECO:0000244|PDB:2PJY}.
STRAND 69 72 {ECO:0000244|PDB:3KFD}.
TURN 74 76 {ECO:0000244|PDB:3KFD}.
STRAND 77 82 {ECO:0000244|PDB:2PJY}.
TURN 84 86 {ECO:0000244|PDB:3KFD}.
HELIX 89 92 {ECO:0000244|PDB:2PJY}.
STRAND 94 101 {ECO:0000244|PDB:2PJY}.
STRAND 102 105 {ECO:0000244|PDB:3KFD}.
HELIX 107 109 {ECO:0000244|PDB:2L5S}.
HELIX 177 183 {ECO:0000244|PDB:1B6C}.
STRAND 187 190 {ECO:0000244|PDB:3KCF}.
STRAND 191 193 {ECO:0000244|PDB:1B6C}.
HELIX 202 204 {ECO:0000244|PDB:5E8S}.
STRAND 205 213 {ECO:0000244|PDB:5E8S}.
STRAND 215 224 {ECO:0000244|PDB:5E8S}.
STRAND 227 234 {ECO:0000244|PDB:5E8S}.
HELIX 236 238 {ECO:0000244|PDB:5E8S}.
HELIX 239 249 {ECO:0000244|PDB:5E8S}.
STRAND 251 253 {ECO:0000244|PDB:3KCF}.
STRAND 262 269 {ECO:0000244|PDB:5E8S}.
STRAND 271 281 {ECO:0000244|PDB:5E8S}.
HELIX 288 294 {ECO:0000244|PDB:5E8S}.
HELIX 299 317 {ECO:0000244|PDB:5E8S}.
STRAND 322 324 {ECO:0000244|PDB:5E8X}.
STRAND 328 330 {ECO:0000244|PDB:5E8Z}.
HELIX 336 338 {ECO:0000244|PDB:5E8S}.
STRAND 339 341 {ECO:0000244|PDB:5E8S}.
STRAND 347 349 {ECO:0000244|PDB:5E8S}.
HELIX 352 354 {ECO:0000244|PDB:5E8S}.
STRAND 356 359 {ECO:0000244|PDB:5E8S}.
TURN 360 363 {ECO:0000244|PDB:5E8S}.
STRAND 364 367 {ECO:0000244|PDB:5E8S}.
STRAND 368 371 {ECO:0000244|PDB:5E8X}.
HELIX 376 378 {ECO:0000244|PDB:5E8S}.
HELIX 381 384 {ECO:0000244|PDB:5E8S}.
HELIX 393 413 {ECO:0000244|PDB:5E8S}.
STRAND 417 419 {ECO:0000244|PDB:3KCF}.
TURN 427 431 {ECO:0000244|PDB:5E8S}.
HELIX 438 445 {ECO:0000244|PDB:5E8S}.
HELIX 456 460 {ECO:0000244|PDB:5E8S}.
HELIX 462 474 {ECO:0000244|PDB:5E8S}.
HELIX 479 481 {ECO:0000244|PDB:5E8S}.
HELIX 485 497 {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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