Thyroid hormone receptor alpha

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Thyroid hormone receptor, alpha
Protein THRA PDB 1nav.png
PDB rendering based on 1nav.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols THRA ; AR7; CHNG6; EAR7; ERB-T-1; ERBA; ERBA1; NR1A1; THRA1; THRA2; c-ERBA-1
External IDs OMIM190120 MGI98742 HomoloGene37747 IUPHAR: NR1A1 ChEMBL: 1860 GeneCards: THRA Gene
RNA expression pattern
PBB GE THRA 35846 at tn.png
PBB GE THRA 204100 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 7067 21833
Ensembl ENSG00000126351 ENSMUSG00000058756
UniProt P10827 P63058
RefSeq (mRNA) NM_001190918 NM_178060
RefSeq (protein) NP_001177847 NP_835161
Location (UCSC) Chr 17:
40.06 – 40.09 Mb
Chr 11:
98.74 – 98.77 Mb
PubMed search [1] [2]

Thyroid hormone receptor alpha (TR-alpha) also known as nuclear receptor subfamily 1, group A, member 1 (NR1A1), is a nuclear receptor protein that in humans is encoded by the THRA gene.[1][2][3]

Function[edit]

The protein encoded by this gene is a nuclear hormone receptor for triiodothyronine. It is one of the several receptors for thyroid hormone, and has been shown to mediate the biological activities of thyroid hormone. Knockout studies in mice suggest that the different receptors, while having certain extent of redundancy, may mediate different functions of thyroid hormone. Alternatively spliced transcript variants encoding distinct isoforms have been reported.[1]

Interactions[edit]

THR1 has been shown to interact with:

References[edit]

  1. ^ a b "Entrez Gene: THRA thyroid hormone receptor, alpha (erythroblastic leukemia viral (v-erb-a) oncogene homolog, avian)". 
  2. ^ Spurr NK, Solomon E, Jansson M, Sheer D, Goodfellow PN, Bodmer WF, Vennstrom B (January 1984). "Chromosomal localisation of the human homologues to the oncogenes erbA and B". EMBO J. 3 (1): 159–63. PMC 557313. PMID 6323162. 
  3. ^ Dayton AI, Selden JR, Laws G, Dorney DJ, Finan J, Tripputi P, Emanuel BS, Rovera G, Nowell PC, Croce CM (July 1984). "A human c-erbA oncogene homologue is closely proximal to the chromosome 17 breakpoint in acute promyelocytic leukemia". Proc. Natl. Acad. Sci. U.S.A. 81 (14): 4495–9. doi:10.1073/pnas.81.14.4495. PMC 345617. PMID 6589608. 
  4. ^ Dressel U, Thormeyer D, Altincicek B, Paululat A, Eggert M, Schneider S, Tenbaum SP, Renkawitz R, Baniahmad A (May 1999). "Alien, a highly conserved protein with characteristics of a corepressor for members of the nuclear hormone receptor superfamily". Mol. Cell. Biol. 19 (5): 3383–94. PMC 84131. PMID 10207062. 
  5. ^ a b De Luca A, Severino A, De Paolis P, Cottone G, De Luca L, De Falco M, Porcellini A, Volpe M, Condorelli G (February 2003). "p300/cAMP-response-element-binding-protein ('CREB')-binding protein (CBP) modulates co-operation between myocyte enhancer factor 2A (MEF2A) and thyroid hormone receptor-retinoid X receptor". Biochem. J. 369 (Pt 3): 477–84. doi:10.1042/BJ20020057. PMC 1223100. PMID 12371907. 
  6. ^ Li D, Wang F, Samuels HH (December 2001). "Domain structure of the NRIF3 family of coregulators suggests potential dual roles in transcriptional regulation". Mol. Cell. Biol. 21 (24): 8371–84. doi:10.1128/MCB.21.24.8371-8384.2001. PMC 100002. PMID 11713274. 
  7. ^ Li D, Desai-Yajnik V, Lo E, Schapira M, Abagyan R, Samuels HH (October 1999). "NRIF3 is a novel coactivator mediating functional specificity of nuclear hormone receptors". Mol. Cell. Biol. 19 (10): 7191–202. PMC 84712. PMID 10490654. 
  8. ^ Yuan CX, Ito M, Fondell JD, Fu ZY, Roeder RG (July 1998). "The TRAP220 component of a thyroid hormone receptor- associated protein (TRAP) coactivator complex interacts directly with nuclear receptors in a ligand-dependent fashion". Proc. Natl. Acad. Sci. U.S.A. 95 (14): 7939–44. doi:10.1073/pnas.95.14.7939. PMC 20908. PMID 9653119. 
  9. ^ a b c Ito M, Yuan CX, Malik S, Gu W, Fondell JD, Yamamura S, Fu ZY, Zhang X, Qin J, Roeder RG (March 1999). "Identity between TRAP and SMCC complexes indicates novel pathways for the function of nuclear receptors and diverse mammalian activators". Mol. Cell 3 (3): 361–70. doi:10.1016/S1097-2765(00)80463-3. PMID 10198638. 
  10. ^ Lee SK, Anzick SL, Choi JE, Bubendorf L, Guan XY, Jung YK, Kallioniemi OP, Kononen J, Trent JM, Azorsa D, Jhun BH, Cheong JH, Lee YC, Meltzer PS, Lee JW (November 1999). "A nuclear factor, ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo". J. Biol. Chem. 274 (48): 34283–93. doi:10.1074/jbc.274.48.34283. PMID 10567404. 
  11. ^ Lee SK, Na SY, Jung SY, Choi JE, Jhun BH, Cheong J, Meltzer PS, Lee YC, Lee JW (June 2000). "Activating protein-1, nuclear factor-kappaB, and serum response factor as novel target molecules of the cancer-amplified transcription coactivator ASC-2". Mol. Endocrinol. 14 (6): 915–25. doi:10.1210/mend.14.6.0471. PMID 10847592. 
  12. ^ Chang KH, Chen Y, Chen TT, Chou WH, Chen PL, Ma YY, Yang-Feng TL, Leng X, Tsai MJ, O'Malley BW, Lee WH (August 1997). "A thyroid hormone receptor coactivator negatively regulated by the retinoblastoma protein". Proc. Natl. Acad. Sci. U.S.A. 94 (17): 9040–5. doi:10.1073/pnas.94.17.9040. PMC 23019. PMID 9256431. 
  13. ^ Tan F, Lu L, Cai Y, Wang J, Xie Y, Wang L, Gong Y, Xu BE, Wu J, Luo Y, Qiang B, Yuan J, Sun X, Peng X (July 2008). "Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell line Chang liver cells". Proteomics 8 (14): 2885–96. doi:10.1002/pmic.200700887. PMID 18655026. 

Further reading[edit]

This article incorporates text from the United States National Library of Medicine, which is in the public domain.