Retinoid X receptor beta

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Retinoid X receptor, beta
File:PBB Protein RXRB image.jpg
PDB rendering based on 1by4.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols RXRB ; DAUDI6; H-2RIIBP; MGC1831; NR2B2; RCoR-1
External IDs Template:OMIM5 Template:MGI HomoloGene7923
RNA expression pattern
File:PBB GE RXRB 209148 at tn.png
File:PBB GE RXRB 215099 s at tn.png
File:PBB GE RXRB 215098 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Retinoid X receptor beta (RXR-beta), also known as NR2B2 (nuclear receptor subfamily 2, group B, member 2) is a nuclear receptor encoded by the RXRB gene.[1]

This gene encodes a member of the retinoid X receptor (RXR) family of nuclear receptors which are involved in mediating the effects of retinoic acid (RA). This receptor forms homodimers with the retinoic acid, thyroid hormone, and vitamin D receptors, increasing both DNA binding and transcriptional function on their respective response elements. The gene lies within the major histocompatibility complex (MHC) class II region on chromosome 6. An alternatively spliced transcript variant has been described, but its full length sequence has not been determined.[1]

See also

References

  1. 1.0 1.1 "Entrez Gene: RXRB retinoid X receptor, beta".

Further reading

  • Szanto A, Narkar V, Shen Q; et al. (2005). "Retinoid X receptors: X-ploring their (patho)physiological functions". Cell Death Differ. 11 Suppl 2: S126–43. doi:10.1038/sj.cdd.4401533. PMID 15608692.
  • Leid M, Kastner P, Lyons R; et al. (1992). "Purification, cloning, and RXR identity of the HeLa cell factor with which RAR or TR heterodimerizes to bind target sequences efficiently". Cell. 68 (2): 377–95. PMID 1310259.
  • Fleischhauer K, Park JH, DiSanto JP; et al. (1992). "Isolation of a full-length cDNA clone encoding a N-terminally variant form of the human retinoid X receptor beta". Nucleic Acids Res. 20 (7): 1801. PMID 1315958.
  • Berrodin TJ, Marks MS, Ozato K; et al. (1992). "Heterodimerization among thyroid hormone receptor, retinoic acid receptor, retinoid X receptor, chicken ovalbumin upstream promoter transcription factor, and an endogenous liver protein". Mol. Endocrinol. 6 (9): 1468–78. PMID 1331778.
  • Epplen C, Epplen JT (1992). "The human cDNA sequence homologous to the mouse MHC class I promoter-binding protein gene contains four additional codons in lymphocytes". Mamm. Genome. 3 (8): 472–5. PMID 1514958.
  • Yu VC, Delsert C, Andersen B; et al. (1992). "RXR beta: a coregulator that enhances binding of retinoic acid, thyroid hormone, and vitamin D receptors to their cognate response elements". Cell. 67 (6): 1251–66. PMID 1662118.
  • Oñate SA, Tsai SY, Tsai MJ, O'Malley BW (1995). "Sequence and characterization of a coactivator for the steroid hormone receptor superfamily". Science. 270 (5240): 1354–7. PMID 7481822.
  • Kooistra T, Lansink M, Arts J; et al. (1995). "Involvement of retinoic acid receptor alpha in the stimulation of tissue-type plasminogen-activator gene expression in human endothelial cells". Eur. J. Biochem. 232 (2): 425–32. PMID 7556191.
  • Perlmann T, Jansson L (1995). "A novel pathway for vitamin A signaling mediated by RXR heterodimerization with NGFI-B and NURR1". Genes Dev. 9 (7): 769–82. PMID 7705655.
  • Forman BM, Umesono K, Chen J, Evans RM (1995). "Unique response pathways are established by allosteric interactions among nuclear hormone receptors". Cell. 81 (4): 541–50. PMID 7758108.
  • Zanaria E, Muscatelli F, Bardoni B; et al. (1995). "An unusual member of the nuclear hormone receptor superfamily responsible for X-linked adrenal hypoplasia congenita". Nature. 372 (6507): 635–41. doi:10.1038/372635a0. PMID 7990953.
  • Almasan A, Mangelsdorf DJ, Ong ES; et al. (1994). "Chromosomal localization of the human retinoid X receptors". Genomics. 20 (3): 397–403. doi:10.1006/geno.1994.1193. PMID 8034312.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. PMID 8125298.
  • Fitzgibbon J, Gillett GT, Woodward KJ; et al. (1994). "Mapping of RXRB to human chromosome 6p21.3". Ann. Hum. Genet. 57 (Pt 3): 203–9. PMID 8257090.
  • Fleischhauer K, McBride OW, DiSanto JP; et al. (1993). "Cloning and chromosome mapping of human retinoid X receptor beta: selective amino acid sequence conservation of a nuclear hormone receptor in mammals". Hum. Genet. 90 (5): 505–10. PMID 8381386.
  • May M, Mengus G, Lavigne AC; et al. (1996). "Human TAF(II28) promotes transcriptional stimulation by activation function 2 of the retinoid X receptors". EMBO J. 15 (12): 3093–104. PMID 8670810.
  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. PMID 8889548.
  • Joyeux A, Cavaillès V, Balaguer P, Nicolas JC (1997). "RIP 140 enhances nuclear receptor-dependent transcription in vivo in yeast". Mol. Endocrinol. 11 (2): 193–202. PMID 9013766.
  • Xu XC, Sozzi G, Lee JS; et al. (1997). "Suppression of retinoic acid receptor beta in non-small-cell lung cancer in vivo: implications for lung cancer development". J. Natl. Cancer Inst. 89 (9): 624–9. PMID 9150186.
  • Chen H, Lin RJ, Schiltz RL; et al. (1997). "Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300". Cell. 90 (3): 569–80. PMID 9267036.

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