TGF-beta receptor type-1

Details

Name
TGF-beta receptor type-1
Synonyms
  • 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
  • TbetaR-I
  • TGF-beta receptor type I
  • TGF-beta type I receptor
  • TGFR-1
  • Transforming growth factor-beta receptor type I
Gene Name
TGFBR1
Organism
Humans
Amino acid sequence
>lcl|BSEQ0007255|TGF-beta receptor type-1
MEAAVAAPRPRLLLLVLAAAAAAAAALLPGATALQCFCHLCTKDNFTCVTDGLCFVSVTE
TTDKVIHNSMCIAEIDLIPRDRPFVCAPSSKTGSVTTTYCCNQDHCNKIELPTTVKSSPG
LGPVELAAVIAGPVCFVCISLMLMVYICHNRTVIHHRVPNEEDPSLDRPFISEGTTLKDL
IYDMTTSGSGSGLPLLVQRTIARTIVLQESIGKGRFGEVWRGKWRGEEVAVKIFSSREER
SWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSLFDYLNRYTVTVE
GMIKLALSTASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDS
ATDTIDIAPNHRVGTKRYMAPEVLDDSINMKHFESFKRADIYAMGLVFWEIARRCSIGGI
HEDYQLPYYDLVPSDPSVEEMRKVVCEQKLRPNIPNRWQSCEALRVMAKIMRECWYANGA
ARLTALRIKKTLSQLSQQEGIKM
Number of residues
503
Molecular Weight
55959.18
Theoretical pI
7.59
GO Classification
Functions
ATP binding / I-SMAD binding / metal ion binding / protein kinase activity / protein serine/threonine kinase activity / receptor signaling protein activity / receptor signaling protein serine/threonine kinase activity / SMAD binding / transforming growth factor beta binding / transforming growth factor beta receptor activity, type I / transforming growth factor beta-activated receptor activity / type II transforming growth factor beta receptor binding
Processes
activation of MAPKK activity / activin receptor signaling pathway / angiogenesis / anterior/posterior pattern specification / apoptotic process / artery morphogenesis / blastocyst development / cardiac epithelial to mesenchymal transition / cell cycle arrest / cell motility / cellular response to transforming growth factor beta stimulus / collagen fibril organization / embryonic cranial skeleton morphogenesis / endothelial cell activation / endothelial cell migration / epithelial to mesenchymal transition / extracellular structure organization / germ cell migration / heart development / in utero embryonic development / intracellular signal transduction / kidney development / lens development in camera-type eye / male gonad development / mesenchymal cell differentiation / negative regulation of chondrocyte differentiation / negative regulation of endothelial cell proliferation / negative regulation of extrinsic apoptotic signaling pathway / negative regulation of transforming growth factor beta receptor signaling pathway / neuron fate commitment / palate development / parathyroid gland development / pathway-restricted SMAD protein phosphorylation / peptidyl-serine phosphorylation / peptidyl-threonine phosphorylation / pharyngeal system development / positive regulation of apoptotic signaling pathway / positive regulation of cell growth / positive regulation of cell proliferation / positive regulation of cellular component movement / positive regulation of endothelial cell proliferation / positive regulation of filopodium assembly / positive regulation of gene expression / positive regulation of pathway-restricted SMAD protein phosphorylation / positive regulation of protein kinase B signaling / positive regulation of SMAD protein import into nucleus / positive regulation of transcription, DNA-templated / post-embryonic development / protein phosphorylation / regulation of epithelial to mesenchymal transition / regulation of gene expression / regulation of protein binding / regulation of protein ubiquitination / regulation of transcription, DNA-templated / response to cholesterol / signal transduction / skeletal system development / skeletal system morphogenesis / thymus development / transforming growth factor beta receptor signaling pathway / wound healing
Components
bicellular tight junction / cell / endosome / intracellular / membrane / plasma membrane / receptor complex / transforming growth factor beta receptor homodimeric complex
General Function
Type ii transforming growth factor beta receptor binding
Specific 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.
Pfam Domain Function
Transmembrane Regions
127-147
Cellular Location
Cell membrane
Gene sequence
>lcl|BSEQ0017222|TGF-beta receptor type-1 (TGFBR1)
ATGGAGGCGGCGGTCGCTGCTCCGCGTCCCCGGCTGCTCCTCCTCGTGCTGGCGGCGGCG
GCGGCGGCGGCGGCGGCGCTGCTCCCGGGGGCGACGGCGTTACAGTGTTTCTGCCACCTC
TGTACAAAAGACAATTTTACTTGTGTGACAGATGGGCTCTGCTTTGTCTCTGTCACAGAG
ACCACAGACAAAGTTATACACAACAGCATGTGTATAGCTGAAATTGACTTAATTCCTCGA
GATAGGCCGTTTGTATGTGCACCCTCTTCAAAAACTGGGTCTGTGACTACAACATATTGC
TGCAATCAGGACCATTGCAATAAAATAGAACTTCCAACTACTGGTTTACCATTGCTTGTT
CAGAGAACAATTGCGAGAACTATTGTGTTACAAGAAAGCATTGGCAAAGGTCGATTTGGA
GAAGTTTGGAGAGGAAAGTGGCGGGGAGAAGAAGTTGCTGTTAAGATATTCTCCTCTAGA
GAAGAACGTTCGTGGTTCCGTGAGGCAGAGATTTATCAAACTGTAATGTTACGTCATGAA
AACATCCTGGGATTTATAGCAGCAGACAATAAAGACAATGGTACTTGGACTCAGCTCTGG
TTGGTGTCAGATTATCATGAGCATGGATCCCTTTTTGATTACTTAAACAGATACACAGTT
ACTGTGGAAGGAATGATAAAACTTGCTCTGTCCACGGCGAGCGGTCTTGCCCATCTTCAC
ATGGAGATTGTTGGTACCCAAGGAAAGCCAGCCATTGCTCATAGAGATTTGAAATCAAAG
AATATCTTGGTAAAGAAGAATGGAACTTGCTGTATTGCAGACTTAGGACTGGCAGTAAGA
CATGATTCAGCCACAGATACCATTGATATTGCTCCAAACCACAGAGTGGGAACAAAAAGG
TACATGGCCCCTGAAGTTCTCGATGATTCCATAAATATGAAACATTTTGAATCCTTCAAA
CGTGCTGACATCTATGCAATGGGCTTAGTATTCTGGGAAATTGCTCGACGATGTTCCATT
GGTGGAATTCATGAAGATTACCAACTGCCTTATTATGATCTTGTACCTTCTGACCCATCA
GTTGAAGAAATGAGAAAAGTTGTTTGTGAACAGAAGTTAAGGCCAAATATCCCAAACAGA
TGGCAGAGCTGTGAAGCCTTGAGAGTAATGGCTAAAATTATGAGAGAATGTTGGTATGCC
AATGGAGCAGCTAGGCTTACAGCATTGCGGATTAAGAAAACATTATCGCAACTCAGTCAA
CAGGAAGGCATCAAAATGTAA
Chromosome Location
9
Locus
9q22
External Identifiers
ResourceLink
UniProtKB IDP36897
UniProtKB Entry NameTGFR1_HUMAN
GenBank Protein ID431035
GenBank Gene IDL11695
HGNC IDHGNC:11772
General References
  1. Franzen P, ten Dijke P, Ichijo H, Yamashita H, Schulz P, Heldin CH, Miyazono K: Cloning of a TGF beta type I receptor that forms a heteromeric complex with the TGF beta type II receptor. Cell. 1993 Nov 19;75(4):681-92. [Article]
  2. Vellucci VF, Reiss M: Cloning and genomic organization of the human transforming growth factor-beta type I receptor gene. Genomics. 1997 Dec 1;46(2):278-83. [Article]
  3. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [Article]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  5. Pasche B, Luo Y, Rao PH, Nimer SD, Dmitrovsky E, Caron P, Luzzatto L, Offit K, Cordon-Cardo C, Renault B, Satagopan JM, Murty VV, 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. 1998 Jul 1;58(13):2727-32. [Article]
  6. Konrad L, Scheiber JA, Volck-Badouin E, Keilani MM, 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. 2007 Sep 11;8:318. [Article]
  7. Wieser R, Wrana JL, Massague J: GS domain mutations that constitutively activate T beta R-I, the downstream signaling component in the TGF-beta receptor complex. EMBO J. 1995 May 15;14(10):2199-208. [Article]
  8. Eppert K, Scherer SW, Ozcelik H, Pirone R, Hoodless P, Kim H, Tsui LC, Bapat B, Gallinger S, Andrulis IL, Thomsen GH, Wrana JL, Attisano L: MADR2 maps to 18q21 and encodes a TGFbeta-regulated MAD-related protein that is functionally mutated in colorectal carcinoma. Cell. 1996 Aug 23;86(4):543-52. [Article]
  9. Macias-Silva M, Abdollah S, Hoodless PA, Pirone R, Attisano L, Wrana JL: MADR2 is a substrate of the TGFbeta receptor and its phosphorylation is required for nuclear accumulation and signaling. Cell. 1996 Dec 27;87(7):1215-24. [Article]
  10. Chen YG, Liu F, Massague J: Mechanism of TGFbeta receptor inhibition by FKBP12. EMBO J. 1997 Jul 1;16(13):3866-76. [Article]
  11. Nakao A, Imamura T, Souchelnytskyi S, Kawabata M, Ishisaki A, Oeda E, Tamaki K, Hanai J, Heldin CH, Miyazono K, ten Dijke P: TGF-beta receptor-mediated signalling through Smad2, Smad3 and Smad4. EMBO J. 1997 Sep 1;16(17):5353-62. [Article]
  12. Abdollah S, Macias-Silva M, Tsukazaki T, Hayashi H, Attisano L, Wrana JL: TbetaRI phosphorylation of Smad2 on Ser465 and Ser467 is required for Smad2-Smad4 complex formation and signaling. J Biol Chem. 1997 Oct 31;272(44):27678-85. [Article]
  13. Tsukazaki T, Chiang TA, Davison AF, Attisano L, Wrana JL: SARA, a FYVE domain protein that recruits Smad2 to the TGFbeta receptor. Cell. 1998 Dec 11;95(6):779-91. [Article]
  14. Gilboa L, Wells RG, Lodish HF, Henis YI: 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. 1998 Feb 23;140(4):767-77. [Article]
  15. Kavsak P, Rasmussen RK, Causing CG, Bonni S, Zhu H, Thomsen GH, Wrana JL: Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF beta receptor for degradation. Mol Cell. 2000 Dec;6(6):1365-75. [Article]
  16. 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. 2001 Apr 20;276(16):12477-80. Epub 2001 Feb 13. [Article]
  17. Felici A, Wurthner JU, Parks WT, Giam LR, Reiss M, Karpova TS, McNally JG, Roberts AB: TLP, a novel modulator of TGF-beta signaling, has opposite effects on Smad2- and Smad3-dependent signaling. EMBO J. 2003 Sep 1;22(17):4465-77. [Article]
  18. 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. 2005 Mar 15;386(Pt 3):461-70. [Article]
  19. Ozdamar B, Bose R, Barrios-Rodiles M, Wang HR, Zhang Y, Wrana JL: Regulation of the polarity protein Par6 by TGFbeta receptors controls epithelial cell plasticity. Science. 2005 Mar 11;307(5715):1603-9. [Article]
  20. Finnson KW, Tam BY, Liu K, Marcoux A, Lepage P, Roy S, Bizet AA, Philip A: Identification of CD109 as part of the TGF-beta receptor system in human keratinocytes. FASEB J. 2006 Jul;20(9):1525-7. Epub 2006 Jun 5. [Article]
  21. 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. 2006;34(21):6314-26. Epub 2006 Nov 11. [Article]
  22. Sorrentino A, Thakur N, Grimsby S, Marcusson A, von Bulow V, Schuster N, Zhang S, Heldin CH, Landstrom M: The type I TGF-beta receptor engages TRAF6 to activate TAK1 in a receptor kinase-independent manner. Nat Cell Biol. 2008 Oct;10(10):1199-207. doi: 10.1038/ncb1780. Epub 2008 Aug 31. [Article]
  23. Massague J: TGF-beta signal transduction. Annu Rev Biochem. 1998;67:753-91. [Article]
  24. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. doi: 10.1074/mcp.M800588-MCP200. Epub 2009 Apr 15. [Article]
  25. Eichhorn PJ, 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. 2012 Feb 19;18(3):429-35. doi: 10.1038/nm.2619. [Article]
  26. Jokiranta TS, 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. 1995 Nov 27;376(1-2):31-6. [Article]
  27. Huse M, Chen YG, Massague J, Kuriyan J: Crystal structure of the cytoplasmic domain of the type I TGF beta receptor in complex with FKBP12. Cell. 1999 Feb 5;96(3):425-36. [Article]
  28. Huse M, Muir TW, Xu L, Chen YG, Kuriyan J, Massague J: The TGF beta receptor activation process: an inhibitor- to substrate-binding switch. Mol Cell. 2001 Sep;8(3):671-82. [Article]
  29. Sawyer JS, Beight DW, Britt KS, Anderson BD, Campbell RM, Goodson T Jr, Herron DK, Li HY, McMillen WT, Mort N, Parsons S, Smith EC, Wagner JR, Yan L, Zhang F, Yingling JM: 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. 2004 Jul 5;14(13):3581-4. [Article]
  30. Gellibert F, Woolven J, Fouchet MH, Mathews N, Goodland H, Lovegrove V, Laroze A, Nguyen VL, Sautet S, Wang R, Janson C, Smith W, Krysa G, Boullay V, De Gouville AC, 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. 2004 Aug 26;47(18):4494-506. [Article]
  31. Groppe J, Hinck CS, Samavarchi-Tehrani P, Zubieta C, Schuermann JP, Taylor AB, Schwarz PM, Wrana JL, Hinck AP: Cooperative assembly of TGF-beta superfamily signaling complexes is mediated by two disparate mechanisms and distinct modes of receptor binding. Mol Cell. 2008 Feb 1;29(2):157-68. doi: 10.1016/j.molcel.2007.11.039. [Article]
  32. Radaev S, Zou Z, Huang T, Lafer EM, Hinck AP, Sun PD: Ternary complex of transforming growth factor-beta1 reveals isoform-specific ligand recognition and receptor recruitment in the superfamily. J Biol Chem. 2010 May 7;285(19):14806-14. doi: 10.1074/jbc.M109.079921. Epub 2010 Mar 5. [Article]
  33. Kaklamani VG, Hou N, Bian Y, Reich J, Offit K, Michel LS, Rubinstein WS, Rademaker A, Pasche B: TGFBR1*6A and cancer risk: a meta-analysis of seven case-control studies. J Clin Oncol. 2003 Sep 1;21(17):3236-43. [Article]
  34. Kaklamani V, 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. 2004 Sep 22;5:28. [Article]
  35. Loeys BL, Chen J, Neptune ER, Judge DP, Podowski M, Holm T, Meyers J, Leitch CC, Katsanis N, Sharifi N, Xu FL, Myers LA, Spevak PJ, Cameron DE, De Backer J, Hellemans J, Chen Y, Davis EC, Webb CL, Kress W, Coucke P, Rifkin DB, De Paepe AM, Dietz HC: A syndrome of altered cardiovascular, craniofacial, neurocognitive and skeletal development caused by mutations in TGFBR1 or TGFBR2. Nat Genet. 2005 Mar;37(3):275-81. Epub 2005 Jan 30. [Article]
  36. Suarez BK, Pal P, Jin CH, Kaushal R, Sun G, Jin L, Pasche B, Deka R, Catalona WJ: TGFBR1*6A is not associated with prostate cancer in men of European ancestry. Prostate Cancer Prostatic Dis. 2005;8(1):50-3. [Article]
  37. Ades LC, Sullivan K, Biggin A, Haan EA, Brett M, Holman KJ, Dixon J, Robertson S, Holmes AD, Rogers J, Bennetts B: FBN1, TGFBR1, and the Marfan-craniosynostosis/mental retardation disorders revisited. Am J Med Genet A. 2006 May 15;140(10):1047-58. [Article]
  38. 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. 2006 Aug;27(8):760-9. [Article]
  39. Loeys BL, Schwarze U, Holm T, Callewaert BL, Thomas GH, Pannu H, De Backer JF, Oswald GL, Symoens S, Manouvrier S, Roberts AE, Faravelli F, Greco MA, Pyeritz RE, Milewicz DM, Coucke PJ, Cameron DE, Braverman AC, Byers PH, De Paepe AM, Dietz HC: Aneurysm syndromes caused by mutations in the TGF-beta receptor. N Engl J Med. 2006 Aug 24;355(8):788-98. [Article]
  40. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, 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 DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [Article]
  41. Ley TJ, Mardis ER, Ding L, Fulton B, McLellan MD, Chen K, Dooling D, Dunford-Shore BH, McGrath S, Hickenbotham M, Cook L, Abbott R, Larson DE, Koboldt DC, Pohl C, Smith S, Hawkins A, Abbott S, Locke D, Hillier LW, Miner T, Fulton L, Magrini V, Wylie T, Glasscock J, Conyers J, Sander N, Shi X, Osborne JR, Minx P, Gordon D, Chinwalla A, Zhao Y, Ries RE, Payton JE, Westervelt P, Tomasson MH, Watson M, Baty J, Ivanovich J, Heath S, Shannon WD, Nagarajan R, Walter MJ, Link DC, Graubert TA, DiPersio JF, Wilson RK: DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome. Nature. 2008 Nov 6;456(7218):66-72. doi: 10.1038/nature07485. [Article]
  42. Drera B, Ritelli M, Zoppi N, Wischmeijer A, Gnoli M, Fattori R, Calzavara-Pinton PG, 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. 2009 Nov 2;4:24. doi: 10.1186/1750-1172-4-24. [Article]
  43. Yang JH, Ki CS, Han H, Song BG, Jang SY, Chung TY, Sung K, Lee HJ, Kim DK: Clinical features and genetic analysis of Korean patients with Loeys-Dietz syndrome. J Hum Genet. 2012 Jan;57(1):52-6. doi: 10.1038/jhg.2011.130. Epub 2011 Nov 24. [Article]
  44. Goudie DR, D'Alessandro M, Merriman B, Lee H, Szeverenyi I, Avery S, O'Connor BD, Nelson SF, Coats SE, Stewart A, Christie L, Pichert G, Friedel J, Hayes I, Burrows N, Whittaker S, Gerdes AM, Broesby-Olsen S, Ferguson-Smith MA, Verma C, Lunny DP, Reversade B, Lane EB: Multiple self-healing squamous epithelioma is caused by a disease-specific spectrum of mutations in TGFBR1. Nat Genet. 2011 Feb 27;43(4):365-9. doi: 10.1038/ng.780. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB04434Naphthyridine InhibitorexperimentalunknownDetails
DB07152N-[4-(5-fluoro-6-methylpyridin-2-yl)-5-quinoxalin-6-yl-1H-imidazol-2-yl]acetamideexperimentalunknownDetails
DB044803-(4-Fluorophenyl)-2-(6-Methylpyridin-2-Yl)-5,6-Dihydro-4h-Pyrrolo[1,2-B]PyrazoleexperimentalunknownDetails
DB072672-(6-methylpyridin-2-yl)-N-pyridin-4-ylquinazolin-4-amineexperimentalunknownDetails
DB039214-(3-Pyridin-2-Yl-1h-Pyrazol-4-Yl)QuinolineexperimentalunknownDetails
DB08450N-1H-indazol-5-yl-2-(6-methylpyridin-2-yl)quinazolin-4-amineexperimentalunknownDetails
DB12010Fostamatinibapproved, investigationalunknowninhibitorDetails