Thyroid hormone receptor alpha

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THRA
Protein THRA PDB 1nav.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases THRA, AR7, CHNG6, EAR7, ERB-T-1, ERBA, ERBA1, NR1A1, THRA1, THRA2, c-ERBA-1, thyroid hormone receptor, alpha
External IDs MGI: 98742 HomoloGene: 37747 GeneCards: 7067
RNA expression pattern
PBB GE THRA 204100 at tn.png

PBB GE THRA 35846 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_199334
NM_001190918
NM_001190919
NM_003250

NM_178060
NM_001313983

RefSeq (protein)

NP_001177847.1
NP_001177848.1
NP_003241.2
NP_955366.1

NP_001300912.1
NP_835161.1

Location (UCSC) Chr 17: 40.06 – 40.09 Mb Chr 11: 98.74 – 98.77 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

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.[3][4][5]

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.[3]

Interactions[edit]

THR1 has been shown to interact with:

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ a b "Entrez Gene: THRA thyroid hormone receptor, alpha (erythroblastic leukemia viral (v-erb-a) oncogene homolog, avian)". 
  4. ^ Spurr NK, Solomon E, Jansson M, Sheer D, Goodfellow PN, Bodmer WF, Vennstrom B (Jan 1984). "Chromosomal localisation of the human homologues to the oncogenes erbA and B". The EMBO Journal. 3 (1): 159–63. PMC 557313free to read. PMID 6323162. 
  5. ^ Dayton AI, Selden JR, Laws G, Dorney DJ, Finan J, Tripputi P, Emanuel BS, Rovera G, Nowell PC, Croce CM (Jul 1984). "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. doi:10.1073/pnas.81.14.4495. PMC 345617free to read. PMID 6589608. 
  6. ^ 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". Molecular and Cellular Biology. 19 (5): 3383–94. doi:10.1128/mcb.19.5.3383. PMC 84131free to read. PMID 10207062. 
  7. ^ a b De Luca A, Severino A, De Paolis P, Cottone G, De Luca L, De Falco M, Porcellini A, Volpe M, Condorelli G (Feb 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". The Biochemical Journal. 369 (Pt 3): 477–84. doi:10.1042/BJ20020057. PMC 1223100free to read. PMID 12371907. 
  8. ^ Li D, Wang F, Samuels HH (Dec 2001). "Domain structure of the NRIF3 family of coregulators suggests potential dual roles in transcriptional regulation". Molecular and Cellular Biology. 21 (24): 8371–84. doi:10.1128/MCB.21.24.8371-8384.2001. PMC 100002free to read. PMID 11713274. 
  9. ^ Li D, Desai-Yajnik V, Lo E, Schapira M, Abagyan R, Samuels HH (Oct 1999). "NRIF3 is a novel coactivator mediating functional specificity of nuclear hormone receptors". Molecular and Cellular Biology. 19 (10): 7191–202. doi:10.1128/mcb.19.10.7191. PMC 84712free to read. PMID 10490654. 
  10. ^ Yuan CX, Ito M, Fondell JD, Fu ZY, Roeder RG (Jul 1998). "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. doi:10.1073/pnas.95.14.7939. PMC 20908free to read. PMID 9653119. 
  11. ^ a b c Ito M, Yuan CX, Malik S, Gu W, Fondell JD, Yamamura S, Fu ZY, Zhang X, Qin J, Roeder RG (Mar 1999). "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. doi:10.1016/S1097-2765(00)80463-3. PMID 10198638. 
  12. ^ 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 (Nov 1999). "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. doi:10.1074/jbc.274.48.34283. PMID 10567404. 
  13. ^ Lee SK, Na SY, Jung SY, Choi JE, Jhun BH, Cheong J, Meltzer PS, Lee YC, Lee JW (Jun 2000). "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. doi:10.1210/mend.14.6.0471. PMID 10847592. 
  14. ^ Chang KH, Chen Y, Chen TT, Chou WH, Chen PL, Ma YY, Yang-Feng TL, Leng X, Tsai MJ, O'Malley BW, Lee WH (Aug 1997). "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. doi:10.1073/pnas.94.17.9040. PMC 23019free to read. PMID 9256431. 
  15. ^ 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 (Jul 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.