Sequence Detail

ID/Version

P28700 (UniProt | EBI)

Last sequence update: 1992-12-01
Last annotation update: 2024-01-24

Sequence description from provider

RecName: Full=Retinoic acid receptor RXR-alpha;AltName: Full=Nuclear receptor subfamily 2 group B member 1;AltName: Full=Retinoid X receptor alpha;

Provider

SWISS-PROT

Sequence

Polypeptide 467 aa

Source

Organism mouse

See UniProt | EBI for source

Annotated genes and markers

Follow the symbol links to get more information on the GO terms, expression assays, orthologs, phenotypic alleles, and other information for the genes or markers below.

Type	Symbol	Name	GO Terms	Expression Assays	Orthologs	Phenotypic Alleles
Gene	Rxra	retinoid X receptor alpha	164	154	4	22

Sequence references in MGI

J:2326 Mangelsdorf DJ, et al., Characterization of three RXR genes that mediate the action of 9-cis retinoic acid. Genes Dev. 1992 Mar;6(3):329-44
J:17363 Leid M, et al., Purification, cloning, and RXR identity of the HeLa cell factor with which RAR or TR heterodimerizes to bind target sequences efficiently [published erratum appears in Cell 1992 Nov 27;71(5):following 886]. Cell. 1992 Jan 24;68(2):377-95
J:22537 Tontonoz P, et al., Adipocyte-specific transcription factor ARF6 is a heterodimeric complex of two nuclear hormone receptors, PPAR gamma and RXR alpha. Nucleic Acids Res. 1994 Dec 25;22(25):5628-34
J:62059 Zhu Y, et al., Isolation and characterization of peroxisome proliferator-activated receptor (PPAR) interacting protein (PRIP) as a coactivator for PPAR. J Biol Chem. 2000 May 5;275(18):13510-6
J:114350 Cho YS, et al., Additional sex comb-like 1 (ASXL1), in cooperation with SRC-1, acts as a ligand-dependent coactivator for retinoic acid receptor. J Biol Chem. 2006 Jun 30;281(26):17588-98
J:125396 Li D, et al., Constitutive Coactivator of Peroxisome Proliferator-Activated Receptor (PPAR{gamma}), a Novel Coactivator of PPAR{gamma} that Promotes Adipogenesis. Mol Endocrinol. 2007 Oct;21(10):2320-33
J:274785 Guyot R, et al., The transforming acidic coiled coil (TACC1) protein modulates the transcriptional activity of the nuclear receptors TR and RAR. BMC Mol Biol. 2010 Jan 15;11:3
J:292518 Huttlin EL, et al., A tissue-specific atlas of mouse protein phosphorylation and expression. Cell. 2010 Dec 23;143(7):1174-89
J:320125 Bourguet W, et al., Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains. Mol Cell. 2000 Feb;5(2):289-98