Biology:Thyroid hormone receptor alpha

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Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

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

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]

Role in pathology

Mutations of the THRA gene may cause nongoitrous congenital hypothyroidism-6, a subtype of congenital hypothyroidism.

Interactions

THR1 has been shown to interact with:


References

  1. 1.0 1.1 "Entrez Gene: THRA thyroid hormone receptor, alpha (erythroblastic leukemia viral (v-erb-a) oncogene homolog, avian)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7067. 
  2. "Chromosomal localisation of the human homologues to the oncogenes erbA and B". The EMBO Journal 3 (1): 159–63. Jan 1984. doi:10.1002/j.1460-2075.1984.tb01777.x. PMID 6323162. 
  3. "A human c-erbA oncogene homologue is closely proximal to the chromosome 17 breakpoint in acute promyelocytic leukemia". Proceedings of the National Academy of Sciences of the United States of America 81 (14): 4495–9. Jul 1984. doi:10.1073/pnas.81.14.4495. PMID 6589608. Bibcode1984PNAS...81.4495D. 
  4. "Alien, a highly conserved protein with characteristics of a corepressor for members of the nuclear hormone receptor superfamily". Molecular and Cellular Biology 19 (5): 3383–94. May 1999. doi:10.1128/mcb.19.5.3383. PMID 10207062. 
  5. 5.0 5.1 "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". The Biochemical Journal 369 (Pt 3): 477–84. Feb 2003. doi:10.1042/BJ20020057. PMID 12371907. 
  6. "Domain structure of the NRIF3 family of coregulators suggests potential dual roles in transcriptional regulation". Molecular and Cellular Biology 21 (24): 8371–84. Dec 2001. doi:10.1128/MCB.21.24.8371-8384.2001. PMID 11713274. 
  7. "NRIF3 is a novel coactivator mediating functional specificity of nuclear hormone receptors". Molecular and Cellular Biology 19 (10): 7191–202. Oct 1999. doi:10.1128/mcb.19.10.7191. PMID 10490654. 
  8. "The TRAP220 component of a thyroid hormone receptor- associated protein (TRAP) coactivator complex interacts directly with nuclear receptors in a ligand-dependent fashion". Proceedings of the National Academy of Sciences of the United States of America 95 (14): 7939–44. Jul 1998. doi:10.1073/pnas.95.14.7939. PMID 9653119. Bibcode1998PNAS...95.7939Y. 
  9. 9.0 9.1 9.2 "Identity between TRAP and SMCC complexes indicates novel pathways for the function of nuclear receptors and diverse mammalian activators". Molecular Cell 3 (3): 361–70. Mar 1999. doi:10.1016/S1097-2765(00)80463-3. PMID 10198638. 
  10. "A nuclear factor, ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo". The Journal of Biological Chemistry 274 (48): 34283–93. Nov 1999. doi:10.1074/jbc.274.48.34283. PMID 10567404. 
  11. "Activating protein-1, nuclear factor-kappaB, and serum response factor as novel target molecules of the cancer-amplified transcription coactivator ASC-2". Molecular Endocrinology 14 (6): 915–25. Jun 2000. doi:10.1210/mend.14.6.0471. PMID 10847592. 
  12. "A thyroid hormone receptor coactivator negatively regulated by the retinoblastoma protein". Proceedings of the National Academy of Sciences of the United States of America 94 (17): 9040–5. Aug 1997. doi:10.1073/pnas.94.17.9040. PMID 9256431. Bibcode1997PNAS...94.9040C. 
  13. "Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell line Chang liver cells". Proteomics 8 (14): 2885–96. Jul 2008. doi:10.1002/pmic.200700887. PMID 18655026. 

Further reading

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