Retinoid X receptor alpha

Retinoid X receptor, alpha
File:PBB Protein RXRA image.jpg PDB rendering based on 1by4.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1by4​, 1dkf​, 1dsz​, 1fby​, 1fm6​, 1fm9​, 1g1u​, 1g5y​, 1k74​, 1lbd​, 1mv9​, 1mvc​, 1mzn​, 1r0n​, 1rdt​, 1rxr​, 1xdk​, 1xls​, 1xv9​, 1xvp​, 1ynw​, 2acl​, 2nll​
Identifiers
Symbols	RXRA ; FLJ16020; FLJ16733; MGC102720; NR2B1
External IDs	Template:OMIM5 Template:MGI HomoloGene: 2220
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
File:PBB GE RXRA 202449 s at tn.png
File:PBB GE RXRA 202426 s 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 alpha (RXR-alpha), also known as NR2B1 (nuclear receptor subfamily 2, group B, member 1) is a nuclear receptor encoded by the RXRA gene.

Retinoid X receptors (RXRs) and retinoic acid receptors (RARs), are nuclear receptors that mediate the biological effects of retinoids by their involvement in retinoic acid-mediated gene activation. These receptors exert their action by binding, as homodimers or heterodimers, to specific sequences in the promoters of target genes and regulating their transcription. The protein encoded by this gene is a member of the steroid and thyroid hormone receptor superfamily of transcriptional regulators.

See also

• Retinoid X receptor

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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Heyman RA, Mangelsdorf DJ, Dyck JA; et al. (1992). "9-cis retinoic acid is a high affinity ligand for the retinoid X receptor". Cell. 68 (2): 397–406. PMID 1310260.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Kliewer SA, Umesono K, Mangelsdorf DJ, Evans RM (1992). "Retinoid X receptor interacts with nuclear receptors in retinoic acid, thyroid hormone and vitamin D3 signalling". Nature. 355 (6359): 446–9. doi:10.1038/355446a0. PMID 1310351.CS1 maint: Multiple names: authors list (link)
• Kliewer SA, Umesono K, Heyman RA; et al. (1992). "Retinoid X receptor-COUP-TF interactions modulate retinoic acid signaling". Proc. Natl. Acad. Sci. U.S.A. 89 (4): 1448–52. PMID 1311101.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Bugge TH, Pohl J, Lonnoy O, Stunnenberg HG (1992). "RXR alpha, a promiscuous partner of retinoic acid and thyroid hormone receptors". EMBO J. 11 (4): 1409–18. PMID 1314167.CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Mangelsdorf DJ, Umesono K, Kliewer SA; et al. (1991). "A direct repeat in the cellular retinol-binding protein type II gene confers differential regulation by RXR and RAR". Cell. 66 (3): 555–61. PMID 1651173.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Mangelsdorf DJ, Ong ES, Dyck JA, Evans RM (1990). "Nuclear receptor that identifies a novel retinoic acid response pathway". Nature. 345 (6272): 224–9. doi:10.1038/345224a0. PMID 2159111.CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Multiple names: authors list (link)
• Chen JD, Evans RM (1995). "A transcriptional co-repressor that interacts with nuclear hormone receptors". Nature. 377 (6548): 454–7. doi:10.1038/377454a0. PMID 7566127.
• Schulman IG, Chakravarti D, Juguilon H; et al. (1995). "Interactions between the retinoid X receptor and a conserved region of the TATA-binding protein mediate hormone-dependent transactivation". Proc. Natl. Acad. Sci. U.S.A. 92 (18): 8288–92. PMID 7667283.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.
• Rastinejad F, Perlmann T, Evans RM, Sigler PB (1995). "Structural determinants of nuclear receptor assembly on DNA direct repeats". Nature. 375 (6528): 203–11. doi:10.1038/375203a0. PMID 7746322.CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Multiple names: authors list (link)
• Seol W, Choi HS, Moore DD (1995). "Isolation of proteins that interact specifically with the retinoid X receptor: two novel orphan receptors". Mol. Endocrinol. 9 (1): 72–85. PMID 7760852.CS1 maint: Multiple names: authors list (link)
• Bourguet W, Ruff M, Chambon P; et al. (1995). "Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha". Nature. 375 (6530): 377–82. doi:10.1038/375377a0. PMID 7760929.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Lee JW, Choi HS, Gyuris J; et al. (1995). "Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor". Mol. Endocrinol. 9 (2): 243–54. PMID 7776974.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Tontonoz P, Graves RA, Budavari AI; et al. (1995). "Adipocyte-specific transcription factor ARF6 is a heterodimeric complex of two nuclear hormone receptors, PPAR gamma and RXR alpha". Nucleic Acids Res. 22 (25): 5628–34. PMID 7838715.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Lee JW, Ryan F, Swaffield JC; et al. (1995). "Interaction of thyroid-hormone receptor with a conserved transcriptional mediator". Nature. 374 (6517): 91–4. doi:10.1038/374091a0. PMID 7870181.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Lee MS, Sem DS, Kliewer SA; et al. (1994). "NMR assignments and secondary structure of the retinoid X receptor alpha DNA-binding domain. Evidence for the novel C-terminal helix". Eur. J. Biochem. 224 (2): 639–50. PMID 7925381.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)

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