| Transforming growth factor, beta receptor 1 |

PDB rendering based on 1b6c. |
| Available structures |
| PDB |
Ortholog search: PDBe, RCSB |
| List of PDB id codes |
|
1B6C, 1IAS, 1PY5, 1RW8, 1VJY, 2L5S, 2PJY, 2WOT, 2WOU, 2X7O, 3FAA, 3GXL, 3HMM, 3KCF, 3KFD, 3TZM
|
|
|
| Identifiers |
| Symbols |
TGFBR1; AAT5; ACVRLK4; ALK-5; ALK5; LDS1A; LDS2A; MSSE; SKR4; TGFR-1 |
| External IDs |
OMIM: 190181 MGI: 98728 HomoloGene: 3177 ChEMBL: 4439 GeneCards: TGFBR1 Gene |
| EC number |
2.7.11.30 |
|
|
| Orthologs |
| Species |
Human |
Mouse |
|
| Entrez |
7046 |
21812 |
|
| Ensembl |
ENSG00000106799 |
ENSMUSG00000007613 |
|
| UniProt |
P36897 |
Q64729 |
|
| RefSeq (mRNA) |
NM_001130916 |
NM_009370 |
|
| RefSeq (protein) |
NP_001124388 |
NP_033396 |
|
| Location (UCSC) |
Chr 9:
101.87 – 101.92 Mb |
Chr 4:
47.35 – 47.41 Mb |
|
| PubMed search |
[1] |
[2] |
|
|
|
Transforming growth factor, beta receptor I (activin A receptor type II-like kinase, 53kDa) is a TGF beta receptor. TGFBR1 is its human gene.
The protein encoded by this gene forms a heteromeric complex with type II TGF-beta receptors when bound to TGF-beta, transducing the TGF-beta signal from the cell surface to the cytoplasm. The encoded protein is a serine/threonine protein kinase. Mutations in this gene have been associated with Loeys-Dietz aortic aneurysm syndrome (LDAS).[1]
Interactions [edit]
TGF beta receptor 1 has been shown to interact with Mothers against decapentaplegic homolog 7,[2][3][4][5][6][7] FKBP1A,[8][9] TGF beta 1,[10][11] Caveolin 1,[12] FNTA,[13] PPP2R2A,[14] TGF beta receptor 2,[12][15] Endoglin,[16][17] Heat shock protein 90kDa alpha (cytosolic), member A1[18] and STRAP.[7][19]
See also [edit]
References [edit]
- ^ "Entrez Gene: TGFBR1 transforming growth factor, beta receptor I (activin A receptor type II-like kinase, 53kDa)".
- ^ Mochizuki, Toshiaki; Miyazaki Hideyo, Hara Takane, Furuya Toshio, Imamura Takeshi, Watabe Tetsuro, Miyazono Kohei (July 2004). "Roles for the MH2 domain of Smad7 in the specific inhibition of transforming growth factor-beta superfamily signaling". J. Biol. Chem. (United States) 279 (30): 31568–74. doi:10.1074/jbc.M313977200. ISSN 0021-9258. PMID 15148321.
- ^ Asano, Yoshihide; Ihn Hironobu, Yamane Kenichi, Kubo Masahide, Tamaki Kunihiko (January 2004). "Impaired Smad7-Smurf-mediated negative regulation of TGF-beta signaling in scleroderma fibroblasts". J. Clin. Invest. (United States) 113 (2): 253–64. doi:10.1172/JCI16269. ISSN 0021-9738. PMC 310747. PMID 14722617.
- ^ Koinuma, Daizo; Shinozaki Masahiko, Komuro Akiyoshi, Goto Kouichiro, Saitoh Masao, Hanyu Aki, Ebina Masahito, Nukiwa Toshihiro, Miyazawa Keiji, Imamura Takeshi, Miyazono Kohei (Dec. 2003). "Arkadia amplifies TGF-beta superfamily signalling through degradation of Smad7". EMBO J. (England) 22 (24): 6458–70. doi:10.1093/emboj/cdg632. ISSN 0261-4189. PMC 291827. PMID 14657019.
- ^ Kavsak, P; Rasmussen R K, Causing C G, Bonni S, Zhu H, Thomsen G H, Wrana J L (Dec. 2000). "Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF beta receptor for degradation". Mol. Cell (United States) 6 (6): 1365–75. doi:10.1016/S1097-2765(00)00134-9. ISSN 1097-2765. PMID 11163210.
- ^ Hayashi, H; Abdollah S, Qiu Y, Cai J, Xu Y Y, Grinnell B W, Richardson M A, Topper J N, Gimbrone M A, Wrana J L, Falb D (June 1997). "The MAD-related protein Smad7 associates with the TGFbeta receptor and functions as an antagonist of TGFbeta signaling". Cell (UNITED STATES) 89 (7): 1165–73. doi:10.1016/S0092-8674(00)80303-7. ISSN 0092-8674. PMID 9215638.
- ^ a b Datta, P K; Moses H L (May 2000). "STRAP and Smad7 synergize in the inhibition of transforming growth factor beta signaling". Mol. Cell. Biol. (UNITED STATES) 20 (9): 3157–67. doi:10.1128/MCB.20.9.3157-3167.2000. ISSN 0270-7306. PMC 85610. PMID 10757800.
- ^ Wang, T; Donahoe P K, Zervos A S (July 1994). "Specific interaction of type I receptors of the TGF-beta family with the immunophilin FKBP-12". Science (UNITED STATES) 265 (5172): 674–6. doi:10.1126/science.7518616. ISSN 0036-8075. PMID 7518616.
- ^ Liu, F; Ventura F, Doody J, Massagué J (July 1995). "Human type II receptor for bone morphogenic proteins (BMPs): extension of the two-kinase receptor model to the BMPs". Mol. Cell. Biol. (UNITED STATES) 15 (7): 3479–86. ISSN 0270-7306. PMC 230584. PMID 7791754.
- ^ Ebner, R; Chen R H, Lawler S, Zioncheck T, Derynck R (November 1993). "Determination of type I receptor specificity by the type II receptors for TGF-beta or activin". Science (UNITED STATES) 262 (5135): 900–2. doi:10.1126/science.8235612. ISSN 0036-8075. PMID 8235612.
- ^ Oh, S P; Seki T, Goss K A, Imamura T, Yi Y, Donahoe P K, Li L, Miyazono K, ten Dijke P, Kim S, Li E (March 2000). "Activin receptor-like kinase 1 modulates transforming growth factor-beta 1 signaling in the regulation of angiogenesis". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 97 (6): 2626–31. doi:10.1073/pnas.97.6.2626. ISSN 0027-8424. PMC 15979. PMID 10716993.
- ^ a b Razani, B; Zhang X L, Bitzer M, von Gersdorff G, Böttinger E P, Lisanti M P (March 2001). "Caveolin-1 regulates transforming growth factor (TGF)-beta/SMAD signaling through an interaction with the TGF-beta type I receptor". J. Biol. Chem. (United States) 276 (9): 6727–38. doi:10.1074/jbc.M008340200. ISSN 0021-9258. PMID 11102446.
- ^ Kawabata, M; Imamura T, Miyazono K, Engel M E, Moses H L (Dec. 1995). "Interaction of the transforming growth factor-beta type I receptor with farnesyl-protein transferase-alpha". J. Biol. Chem. (UNITED STATES) 270 (50): 29628–31. doi:10.1074/jbc.270.50.29628. ISSN 0021-9258. PMID 8530343.
- ^ Griswold-Prenner, I; Kamibayashi C, Maruoka E M, Mumby M C, Derynck R (November 1998). "Physical and functional interactions between type I transforming growth factor beta receptors and Balpha, a WD-40 repeat subunit of phosphatase 2A". Mol. Cell. Biol. (UNITED STATES) 18 (11): 6595–604. ISSN 0270-7306. PMC 109244. PMID 9774674.
- ^ Kawabata, M; Chytil A, Moses H L (March 1995). "Cloning of a novel type II serine/threonine kinase receptor through interaction with the type I transforming growth factor-beta receptor". J. Biol. Chem. (UNITED STATES) 270 (10): 5625–30. doi:10.1074/jbc.270.10.5625. ISSN 0021-9258. PMID 7890683.
- ^ Guerrero-Esteo, Mercedes; Sanchez-Elsner Tilman, Letamendia Ainhoa, Bernabeu Carmelo (August 2002). "Extracellular and cytoplasmic domains of endoglin interact with the transforming growth factor-beta receptors I and II". J. Biol. Chem. (United States) 277 (32): 29197–209. doi:10.1074/jbc.M111991200. ISSN 0021-9258. PMID 12015308.
- ^ Barbara, N P; Wrana J L, Letarte M (January 1999). "Endoglin is an accessory protein that interacts with the signaling receptor complex of multiple members of the transforming growth factor-beta superfamily". J. Biol. Chem. (UNITED STATES) 274 (2): 584–94. doi:10.1074/jbc.274.2.584. ISSN 0021-9258. PMID 9872992.
- ^ Wrighton, Katharine H; Lin Xia, Feng Xin-Hua (July 2008). "Critical regulation of TGFbeta signaling by Hsp90". Proc. Natl. Acad. Sci. U.S.A. (United States) 105 (27): 9244–9. doi:10.1073/pnas.0800163105. PMC 2453700. PMID 18591668.
- ^ Datta, P K; Chytil A, Gorska A E, Moses H L (Dec. 1998). "Identification of STRAP, a novel WD domain protein in transforming growth factor-beta signaling". J. Biol. Chem. (UNITED STATES) 273 (52): 34671–4. doi:10.1074/jbc.273.52.34671. ISSN 0021-9258. PMID 9856985.
External links [edit]
Further reading [edit]
|
PDB gallery
|
|
|
|
|
1b6c: CRYSTAL STRUCTURE OF THE CYTOPLASMIC DOMAIN OF THE TYPE I TGF-BETA RECEPTOR IN COMPLEX WITH FKBP12
|
|
|
|
1ias: CYTOPLASMIC DOMAIN OF UNPHOSPHORYLATED TYPE I TGF-BETA RECEPTOR CRYSTALLIZED WITHOUT FKBP12
|
|
|
|
1py5: Crystal Structure of TGF-beta receptor I kinase with inhibitor
|
|
|
|
1rw8: Crystal Structure of TGF-beta receptor I kinase with ATP site inhibitor
|
|
|
|
1vjy: Crystal Structure of a Naphthyridine Inhibitor of Human TGF-beta Type I Receptor
|
|
|
|
|
|
|
Chemokine receptor
(GPCRs) |
|
|
| TNF receptor |
|
|
| JAK-STAT |
|
|
| Ig superfamily |
|
|
| IL-17 family |
|
|
| S/T |
|
|
B trdu: iter (nrpl/grfl/cytl/horl), csrc (lgic, enzr, gprc, igsr, intg, nrpr/grfr/cytr), itra (adap, gbpr, mapk), calc, lipd; path (hedp, wntp, tgfp+mapp, notp, jakp, fsap, hipp, tlrp)
|
|
|
|
|
| Type I cytokine receptor |
|
|
| Receptor protein serine/threonine kinase |
|
|
| Receptor tyrosine kinase |
|
|
| Tumor necrosis factor receptor |
|
|
| Ig superfamily |
|
|
| Other/ungrouped |
|
|
B trdu: iter (nrpl/grfl/cytl/horl), csrc (lgic, enzr, gprc, igsr, intg, nrpr/grfr/cytr), itra (adap, gbpr, mapk), calc, lipd; path (hedp, wntp, tgfp+mapp, notp, jakp, fsap, hipp, tlrp)
|
|