Thyroid hormone receptor beta

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Protein THRB PDB 1bsx.png
Available structures
PDB Ortholog search: PDBe RCSB
Aliases THRB, C-ERBA-2, C-ERBA-BETA, ERBA2, GRTH, NR1A2, PRTH, THR1, THRB1, THRB2, thyroid hormone receptor beta
External IDs MGI: 98743 HomoloGene: 36025 GeneCards: THRB
RNA expression pattern
PBB GE THRB 207044 at fs.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC) Chr 3: 24.12 – 24.5 Mb Chr 14: 17.66 – 18.04 Mb
PubMed search [1] [2]
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Thyroid hormone receptor beta (TR-beta) also known as nuclear receptor subfamily 1, group A, member 2 (NR1A2), is a nuclear receptor protein that in humans is encoded by the THRB gene.[3][4]


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. Defects in this gene are known to be a cause of generalized thyroid hormone resistance (GTHR), a syndrome characterized by goiter and high levels of circulating thyroid hormone (T3-T4), with normal or slightly elevated thyroid stimulating hormone (TSH). Several transcript variants have been observed for this gene, but the full-length nature of only one has been observed so far.[5]


Thyroid hormone receptor beta has been shown to interact with:


  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ "Entrez Gene: THRA thyroid hormone receptor, alpha (erythroblastic leukemia viral (v-erb-a) oncogene homolog, avian)". 
  4. ^ Sakurai A, Nakai A, DeGroot LJ (June 1990). "Structural analysis of human thyroid hormone receptor beta gene". Mol. Cell. Endocrinol. 71 (2): 83–91. PMID 1973914. doi:10.1016/0303-7207(90)90245-4. 
  5. ^ "Entrez Gene: THRB thyroid hormone receptor, beta (erythroblastic leukemia viral (v-erb-a) oncogene homolog 2, avian)". 
  6. ^ a b Monden T, Wondisford FE, Hollenberg AN (November 1997). "Isolation and characterization of a novel ligand-dependent thyroid hormone receptor-coactivating protein". J. Biol. Chem. 272 (47): 29834–41. PMID 9368056. doi:10.1074/jbc.272.47.29834. 
  7. ^ Lin HM, Zhao L, Cheng SY (August 2002). "Cyclin D1 Is a Ligand-independent Co-repressor for Thyroid Hormone Receptors". J. Biol. Chem. 277 (32): 28733–41. PMID 12048199. doi:10.1074/jbc.M203380200. 
  8. ^ a b Liu Y, Takeshita A, Misiti S, Chin WW, Yen PM (October 1998). "Lack of coactivator interaction can be a mechanism for dominant negative activity by mutant thyroid hormone receptors". Endocrinology. 139 (10): 4197–204. PMID 9751500. doi:10.1210/endo.139.10.6218. 
  9. ^ a b Jeyakumar M, Tanen MR, Bagchi MK (June 1997). "Analysis of the functional role of steroid receptor coactivator-1 in ligand-induced transactivation by thyroid hormone receptor". Mol. Endocrinol. 11 (6): 755–67. PMID 9171239. doi:10.1210/mend.11.6.0003. 
  10. ^ Lee SK, Jung SY, Kim YS, Na SY, Lee YC, Lee JW (February 2001). "Two distinct nuclear receptor-interaction domains and CREB-binding protein-dependent transactivation function of activating signal cointegrator-2". Mol. Endocrinol. 15 (2): 241–54. PMID 11158331. doi:10.1210/me.15.2.241. 
  11. ^ 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. PMID 10567404. doi:10.1074/jbc.274.48.34283. 
  12. ^ Ko L, Cardona GR, Chin WW (May 2000). "Thyroid hormone receptor-binding protein, an LXXLL motif-containing protein, functions as a general coactivator". Proc. Natl. Acad. Sci. U.S.A. 97 (11): 6212–7. PMC 18584Freely accessible. PMID 10823961. doi:10.1073/pnas.97.11.6212. 
  13. ^ Ko L, Cardona GR, Iwasaki T, Bramlett KS, Burris TP, Chin WW (January 2002). "Ser-884 adjacent to the LXXLL motif of coactivator TRBP defines selectivity for ERs and TRs". Mol. Endocrinol. 16 (1): 128–40. PMID 11773444. doi:10.1210/mend.16.1.0755. 
  14. ^ Tagami T, Lutz WH, Kumar R, Jameson JL (December 1998). "The interaction of the vitamin D receptor with nuclear receptor corepressors and coactivators". Biochem. Biophys. Res. Commun. 253 (2): 358–63. PMID 9878542. doi:10.1006/bbrc.1998.9799. 
  15. ^ Ando S, Sarlis NJ, Krishnan J, Feng X, Refetoff S, Zhang MQ, Oldfield EH, Yen PM (September 2001). "Aberrant alternative splicing of thyroid hormone receptor in a TSH-secreting pituitary tumor is a mechanism for hormone resistance". Mol. Endocrinol. 15 (9): 1529–38. PMID 11518802. doi:10.1210/me.15.9.1529. 
  16. ^ Zhu XG, Park KS, Kaneshige M, Bhat MK, Zhu Q, Mariash CN, McPhie P, Cheng SY (April 2000). "The orphan nuclear receptor Ear-2 is a negative coregulator for thyroid hormone nuclear receptor function". Mol. Cell. Biol. 20 (7): 2604–18. PMC 85476Freely accessible. PMID 10713182. doi:10.1128/MCB.20.7.2604-2618.2000. 
  17. ^ Wu Y, Delerive P, Chin WW, Burris TP (March 2002). "Requirement of helix 1 and the AF-2 domain of the thyroid hormone receptor for coactivation by PGC-1". J. Biol. Chem. 277 (11): 8898–905. PMID 11751919. doi:10.1074/jbc.M110761200. 

Further reading[edit]

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