RXRB_HUMAN
ID RXRB_HUMAN Reviewed; 533 AA.
AC P28702; P28703; Q59G65; Q5JP92; Q5STQ1;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 233.
DE RecName: Full=Retinoic acid receptor RXR-beta;
DE AltName: Full=Nuclear receptor subfamily 2 group B member 2;
DE AltName: Full=Retinoid X receptor beta;
GN Name=RXRB; Synonyms=NR2B2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), HETERODIMERIZATION, SUBCELLULAR
RP LOCATION, SUBUNIT, AND FUNCTION.
RC TISSUE=Mammary carcinoma;
RX PubMed=1310259; DOI=10.1016/0092-8674(92)90478-u;
RA Leid M., Kastner P., Lyons R., Nakshatri H., Saunders M., Zacharewsi T.,
RA Chen J.Y., Staub A., Garnier J.-M., Mader S., Chambon P.;
RT "Purification, cloning, and RXR identity of the HeLa cell factor with which
RT RAR or TR heterodimerizes to bind target sequences efficiently.";
RL Cell 68:377-395(1992).
RN [2]
RP ERRATUM OF PUBMED:1310259, AND SEQUENCE REVISION.
RX PubMed=1330328;
RA Leid M., Kastner P., Lyons R., Nakshatri H., Saunders M., Zacharewsi T.,
RA Chen J.Y., Staub A., Garnier J.-M., Mader S., Chambon P.;
RL Cell 71:887-887(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1315958; DOI=10.1093/nar/20.7.1801;
RA Fleischhauer K., Park J.H., Disanto J.P., Marks M.S., Ozato K., Yang S.Y.;
RT "Isolation of a full-length cDNA clone encoding a N-terminally variant form
RT of the human retinoid X receptor beta.";
RL Nucleic Acids Res. 20:1801-1801(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Numasawa T., Koga H., Ueyama K., Maeda S., Sakou T., Harata S., Leppert M.,
RA Inoue I.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Liver;
RA Kaighin V.A., Martin A.L., Aronstam R.S.;
RT "Isolation of cDNA coding for putatively new variants of multiple human
RT nuclear receptors.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Corella A., Vergara A., Paez G., de Miguel C., Encio I.;
RT "Molecular cloning and characterization of the human HRXRB gene and 5'
RT flanking region.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 161-331 (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=8381386; DOI=10.1007/bf00217449;
RA Fleischhauer K., McBride O.W., DiSanto J.P., Ozato K., Yang S.Y.;
RT "Cloning and chromosome mapping of human retinoid X receptor beta:
RT selective amino acid sequence conservation of a nuclear hormone receptor in
RT mammals.";
RL Hum. Genet. 90:505-510(1993).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-25, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [13]
RP TISSUE SPECIFICITY, AND REPRESSION BY AGING.
RX PubMed=26463675; DOI=10.1093/brain/awv289;
RA Natrajan M.S., de la Fuente A.G., Crawford A.H., Linehan E., Nunez V.,
RA Johnson K.R., Wu T., Fitzgerald D.C., Ricote M., Bielekova B.,
RA Franklin R.J.;
RT "Retinoid X receptor activation reverses age-related deficiencies in myelin
RT debris phagocytosis and remyelination.";
RL Brain 138:3581-3597(2015).
RN [14]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=28167758; DOI=10.1073/pnas.1621425114;
RA Lee D.Y., Lin T.E., Lee C.I., Zhou J., Huang Y.H., Lee P.L., Shih Y.T.,
RA Chien S., Chiu J.J.;
RT "MicroRNA-10a is crucial for endothelial response to different flow
RT patterns via interaction of retinoid acid receptors and histone
RT deacetylases.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:2072-2077(2017).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 299-522 IN COMPLEX WITH THE
RP RXR-SPECIFIC AGONIST LG100268, AND SUBUNIT.
RX PubMed=11782480; DOI=10.1074/jbc.m110869200;
RA Love J.D., Gooch J.T., Benko S., Li C., Nagy L., Chatterjee V.K.,
RA Evans R.M., Schwabe J.W.;
RT "The structural basis for the specificity of retinoid-X receptor-selective
RT agonists: new insights into the role of helix H12.";
RL J. Biol. Chem. 277:11385-11391(2002).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 298-533 IN COMPLEX WITH NR1H3.
RX PubMed=12970175; DOI=10.1093/emboj/cdg456;
RA Svensson S., Ostberg T., Jacobsson M., Norstrom C., Stefansson K.,
RA Hallen D., Johansson I.C., Zachrisson K., Ogg D., Jendeberg L.;
RT "Crystal structure of the heterodimeric complex of LXRalpha and RXRbeta
RT ligand-binding domains in a fully agonistic conformation.";
RL EMBO J. 22:4625-4633(2003).
CC -!- FUNCTION: Receptor for retinoic acid. Retinoic acid receptors bind as
CC heterodimers to their target response elements in response to their
CC ligands, all-trans or 9-cis retinoic acid, and regulate gene expression
CC in various biological processes. The RAR/RXR heterodimers bind to the
CC retinoic acid response elements (RARE). {ECO:0000269|PubMed:1310259}.
CC -!- SUBUNIT: Homodimer (in vitro) (PubMed:11782480). Heterodimer with other
CC retinoic acid receptor family members. Binds DNA preferentially as a
CC RAR/RXR heterodimer (PubMed:1310259). Interacts with NR1H3
CC (PubMed:12970175). Interacts with AKAP13 (By similarity).
CC {ECO:0000250|UniProtKB:P28704, ECO:0000269|PubMed:11782480,
CC ECO:0000269|PubMed:12970175, ECO:0000269|PubMed:1310259}.
CC -!- INTERACTION:
CC P28702; Q00975: CACNA1B; NbExp=3; IntAct=EBI-748576, EBI-1055161;
CC P28702; Q9HB07: MYG1; NbExp=3; IntAct=EBI-748576, EBI-709754;
CC P28702; F1D8P7: NR1H2; NbExp=6; IntAct=EBI-748576, EBI-10177172;
CC P28702; Q13133: NR1H3; NbExp=3; IntAct=EBI-748576, EBI-781356;
CC P28702; Q13133-3: NR1H3; NbExp=6; IntAct=EBI-748576, EBI-11952806;
CC P28702; Q96RI1-1: NR1H4; NbExp=7; IntAct=EBI-748576, EBI-12417284;
CC P28702; P04150: NR3C1; NbExp=4; IntAct=EBI-748576, EBI-493507;
CC P28702; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-748576, EBI-79165;
CC P28702; P37231: PPARG; NbExp=5; IntAct=EBI-748576, EBI-781384;
CC P28702; P10276: RARA; NbExp=16; IntAct=EBI-748576, EBI-413374;
CC P28702; P10276-2: RARA; NbExp=4; IntAct=EBI-748576, EBI-10197061;
CC P28702; P10826-2: RARB; NbExp=10; IntAct=EBI-748576, EBI-8583223;
CC P28702; P13631: RARG; NbExp=7; IntAct=EBI-748576, EBI-2568901;
CC P28702; Q6IQ16: SPOPL; NbExp=3; IntAct=EBI-748576, EBI-2822161;
CC P28702-3; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-16429492, EBI-739580;
CC P28702-3; Q96B26: EXOSC8; NbExp=3; IntAct=EBI-16429492, EBI-371922;
CC P28702-3; Q08379: GOLGA2; NbExp=6; IntAct=EBI-16429492, EBI-618309;
CC P28702-3; Q6A162: KRT40; NbExp=3; IntAct=EBI-16429492, EBI-10171697;
CC P28702-3; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-16429492, EBI-10172526;
CC P28702-3; Q13133-3: NR1H3; NbExp=3; IntAct=EBI-16429492, EBI-11952806;
CC P28702-3; Q96RI1-1: NR1H4; NbExp=3; IntAct=EBI-16429492, EBI-12417284;
CC P28702-3; O43586: PSTPIP1; NbExp=3; IntAct=EBI-16429492, EBI-1050964;
CC P28702-3; P10276: RARA; NbExp=3; IntAct=EBI-16429492, EBI-413374;
CC P28702-3; P10826-2: RARB; NbExp=3; IntAct=EBI-16429492, EBI-8583223;
CC P28702-3; Q8IUQ4-2: SIAH1; NbExp=3; IntAct=EBI-16429492, EBI-11522811;
CC P28702-3; O75528: TADA3; NbExp=3; IntAct=EBI-16429492, EBI-473249;
CC P28702-3; Q12800: TFCP2; NbExp=3; IntAct=EBI-16429492, EBI-717422;
CC P28702-3; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-16429492, EBI-1105213;
CC P28702-3; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-16429492, EBI-11952721;
CC P28702-3; P14373: TRIM27; NbExp=3; IntAct=EBI-16429492, EBI-719493;
CC P28702-3; O94972: TRIM37; NbExp=3; IntAct=EBI-16429492, EBI-741602;
CC P28702-3; Q96S82: UBL7; NbExp=3; IntAct=EBI-16429492, EBI-348604;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1310259,
CC ECO:0000269|PubMed:28167758}. Cytoplasm {ECO:0000269|PubMed:28167758}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P28702-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P28702-3; Sequence=VSP_045587;
CC -!- TISSUE SPECIFICITY: Expressed in aortic endothelial cells (at protein
CC level) (PubMed:28167758). Expressed in monocytes (PubMed:26463675).
CC Expressed in a variety of tumor cell lines.
CC {ECO:0000269|PubMed:26463675, ECO:0000269|PubMed:28167758,
CC ECO:0000269|PubMed:8381386}.
CC -!- INDUCTION: Down-regulated by aging. {ECO:0000269|PubMed:26463675}.
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC DNA-binding domain and a C-terminal ligand-binding domain.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92481.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M84820; AAA60293.1; -; mRNA.
DR EMBL; X63522; CAA45087.1; -; mRNA.
DR EMBL; AF065396; AAC18599.1; -; Genomic_DNA.
DR EMBL; AF120161; AAD13794.1; -; Genomic_DNA.
DR EMBL; HQ709179; ADZ17386.1; -; mRNA.
DR EMBL; AB209244; BAD92481.1; ALT_INIT; mRNA.
DR EMBL; AL031228; CAA20239.1; -; Genomic_DNA.
DR EMBL; AL844527; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR936877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR354565; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645940; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL662824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001167; AAH01167.1; -; mRNA.
DR EMBL; X66424; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS4768.1; -. [P28702-1]
DR CCDS; CCDS59007.1; -. [P28702-3]
DR PIR; S37781; S37781.
DR RefSeq; NP_001257330.1; NM_001270401.1. [P28702-3]
DR RefSeq; NP_068811.1; NM_021976.4. [P28702-1]
DR PDB; 1H9U; X-ray; 2.70 A; A/B/C/D=299-522.
DR PDB; 1UHL; X-ray; 2.90 A; A=298-533.
DR PDB; 5HJP; X-ray; 2.60 A; A/C=299-533.
DR PDB; 5I4V; X-ray; 2.61 A; B/F=293-528.
DR PDB; 5KYA; X-ray; 2.60 A; B/F=293-528.
DR PDB; 5KYJ; X-ray; 2.80 A; B/F=293-528.
DR PDB; 7A78; X-ray; 1.72 A; A=298-533.
DR PDBsum; 1H9U; -.
DR PDBsum; 1UHL; -.
DR PDBsum; 5HJP; -.
DR PDBsum; 5I4V; -.
DR PDBsum; 5KYA; -.
DR PDBsum; 5KYJ; -.
DR PDBsum; 7A78; -.
DR AlphaFoldDB; P28702; -.
DR SMR; P28702; -.
DR BioGRID; 112169; 57.
DR ComplexPortal; CPX-652; RXRbeta-LXRbeta nuclear hormone receptor complex.
DR ComplexPortal; CPX-716; RXRbeta-LXRalpha nuclear hormone receptor complex.
DR ComplexPortal; CPX-871; RXRbeta-VDR nuclear hormone receptor complex.
DR CORUM; P28702; -.
DR IntAct; P28702; 68.
DR MINT; P28702; -.
DR STRING; 9606.ENSP00000363817; -.
DR BindingDB; P28702; -.
DR ChEMBL; CHEMBL1870; -.
DR DrugBank; DB08175; (2E,4E)-11-METHOXY-3,7,11-TRIMETHYLDODECA-2,4-DIENOIC ACID.
DR DrugBank; DB00459; Acitretin.
DR DrugBank; DB00210; Adapalene.
DR DrugBank; DB00523; Alitretinoin.
DR DrugBank; DB00307; Bexarotene.
DR DrugBank; DB01393; Bezafibrate.
DR DrugBank; DB03756; Doconexent.
DR DrugBank; DB00926; Etretinate.
DR DrugBank; DB01941; LG-100268.
DR DrugBank; DB07929; N-(TERT-BUTYL)-3,5-DIMETHYL-N'-[(5-METHYL-2,3-DIHYDRO-1,4-BENZODIOXIN-6-YL)CARBONYL]BENZOHYDRAZIDE.
DR DrugBank; DB02746; Phthalic Acid.
DR DrugBank; DB00412; Rosiglitazone.
DR DrugBank; DB00799; Tazarotene.
DR DrugBank; DB07080; TO-901317.
DR DrugBank; DB00755; Tretinoin.
DR DrugCentral; P28702; -.
DR GuidetoPHARMACOLOGY; 611; -.
DR MoonDB; P28702; Predicted.
DR GlyGen; P28702; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P28702; -.
DR PhosphoSitePlus; P28702; -.
DR BioMuta; RXRB; -.
DR DMDM; 1350911; -.
DR EPD; P28702; -.
DR jPOST; P28702; -.
DR MassIVE; P28702; -.
DR PaxDb; P28702; -.
DR PeptideAtlas; P28702; -.
DR PRIDE; P28702; -.
DR ProteomicsDB; 54494; -. [P28702-1]
DR ProteomicsDB; 63911; -.
DR Antibodypedia; 28936; 341 antibodies from 43 providers.
DR DNASU; 6257; -.
DR Ensembl; ENST00000374680.4; ENSP00000363812.3; ENSG00000204231.11. [P28702-1]
DR Ensembl; ENST00000374685.8; ENSP00000363817.4; ENSG00000204231.11. [P28702-3]
DR Ensembl; ENST00000383216.8; ENSP00000372703.4; ENSG00000206289.11. [P28702-3]
DR Ensembl; ENST00000383217.8; ENSP00000372704.4; ENSG00000206289.11. [P28702-1]
DR Ensembl; ENST00000415157.6; ENSP00000402506.2; ENSG00000228333.9. [P28702-1]
DR Ensembl; ENST00000415909.6; ENSP00000410468.2; ENSG00000235712.10. [P28702-1]
DR Ensembl; ENST00000431161.6; ENSP00000393286.2; ENSG00000235712.10. [P28702-3]
DR Ensembl; ENST00000431820.6; ENSP00000411238.2; ENSG00000231321.9. [P28702-1]
DR Ensembl; ENST00000436753.6; ENSP00000415199.2; ENSG00000227322.11. [P28702-1]
DR Ensembl; ENST00000443603.6; ENSP00000402590.2; ENSG00000227322.11. [P28702-3]
DR Ensembl; ENST00000455462.6; ENSP00000400104.2; ENSG00000228333.9. [P28702-3]
DR Ensembl; ENST00000456244.6; ENSP00000393870.2; ENSG00000231321.9. [P28702-3]
DR GeneID; 6257; -.
DR KEGG; hsa:6257; -.
DR MANE-Select; ENST00000374680.4; ENSP00000363812.3; NM_021976.5; NP_068811.1.
DR UCSC; uc003odc.5; human. [P28702-1]
DR CTD; 6257; -.
DR DisGeNET; 6257; -.
DR GeneCards; RXRB; -.
DR HGNC; HGNC:10478; RXRB.
DR HPA; ENSG00000204231; Low tissue specificity.
DR MIM; 180246; gene.
DR neXtProt; NX_P28702; -.
DR OpenTargets; ENSG00000204231; -.
DR PharmGKB; PA34891; -.
DR VEuPathDB; HostDB:ENSG00000204231; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000159208; -.
DR HOGENOM; CLU_007368_5_4_1; -.
DR InParanoid; P28702; -.
DR OMA; DEHCRQE; -.
DR PhylomeDB; P28702; -.
DR TreeFam; TF352097; -.
DR PathwayCommons; P28702; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-HSA-5362517; Signaling by Retinoic Acid.
DR Reactome; R-HSA-9029558; NR1H2 & NR1H3 regulate gene expression linked to lipogenesis.
DR Reactome; R-HSA-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR Reactome; R-HSA-9031525; NR1H2 & NR1H3 regulate gene expression to limit cholesterol uptake.
DR Reactome; R-HSA-9031528; NR1H2 & NR1H3 regulate gene expression linked to triglyceride lipolysis in adipose.
DR Reactome; R-HSA-9623433; NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis.
DR Reactome; R-HSA-9632974; NR1H2 & NR1H3 regulate gene expression linked to gluconeogenesis.
DR SignaLink; P28702; -.
DR SIGNOR; P28702; -.
DR BioGRID-ORCS; 6257; 35 hits in 1109 CRISPR screens.
DR ChiTaRS; RXRB; human.
DR EvolutionaryTrace; P28702; -.
DR GeneWiki; Retinoid_X_receptor_beta; -.
DR GenomeRNAi; 6257; -.
DR Pharos; P28702; Tclin.
DR PRO; PR:P28702; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P28702; protein.
DR Bgee; ENSG00000204231; Expressed in right lobe of thyroid gland and 94 other tissues.
DR ExpressionAtlas; P28702; baseline and differential.
DR Genevisible; P28702; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:GO_Central.
DR GO; GO:0003707; F:nuclear steroid receptor activity; IEA:InterPro.
DR GO; GO:0044323; F:retinoic acid-responsive element binding; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0032526; P:response to retinoic acid; IBA:GO_Central.
DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; IBA:GO_Central.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR IDEAL; IID00368; -.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR000003; Retinoid-X_rcpt/HNF4.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR00545; RETINOIDXR.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; DNA-binding; Metal-binding;
KW Methylation; Nucleus; Receptor; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..533
FT /note="Retinoic acid receptor RXR-beta"
FT /id="PRO_0000053572"
FT DOMAIN 296..529
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189,
FT ECO:0000269|PubMed:11782480"
FT DNA_BIND 205..270
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 205..225
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 241..265
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..204
FT /note="Modulating"
FT /evidence="ECO:0000250"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 36..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..295
FT /note="Hinge"
FT REGION 276..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..133
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..155
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 25
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 418
FT /note="D -> DRSLS (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5, ECO:0000303|Ref.6"
FT /id="VSP_045587"
FT CONFLICT 112
FT /note="S -> T (in Ref. 1; AAA60293)"
FT /evidence="ECO:0000305"
FT HELIX 301..310
FT /evidence="ECO:0007829|PDB:7A78"
FT HELIX 335..355
FT /evidence="ECO:0007829|PDB:7A78"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:7A78"
FT HELIX 365..387
FT /evidence="ECO:0007829|PDB:7A78"
FT TURN 388..390
FT /evidence="ECO:0007829|PDB:7A78"
FT STRAND 391..396
FT /evidence="ECO:0007829|PDB:7A78"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:7A78"
FT HELIX 405..410
FT /evidence="ECO:0007829|PDB:7A78"
FT HELIX 414..423
FT /evidence="ECO:0007829|PDB:7A78"
FT HELIX 425..431
FT /evidence="ECO:0007829|PDB:7A78"
FT HELIX 435..446
FT /evidence="ECO:0007829|PDB:7A78"
FT HELIX 457..478
FT /evidence="ECO:0007829|PDB:7A78"
FT HELIX 485..490
FT /evidence="ECO:0007829|PDB:7A78"
FT HELIX 493..513
FT /evidence="ECO:0007829|PDB:7A78"
FT HELIX 520..525
FT /evidence="ECO:0007829|PDB:7A78"
SQ SEQUENCE 533 AA; 56922 MW; D0069FE93AC16A04 CRC64;
MSWAARPPFL PQRHAAGQCG PVGVRKEMHC GVASRWRRRR PWLDPAAAAA AAVAGGEQQT
PEPEPGEAGR DGMGDSGRDS RSPDSSSPNP LPQGVPPPSP PGPPLPPSTA PSLGGSGAPP
PPPMPPPPLG SPFPVISSSM GSPGLPPPAP PGFSGPVSSP QINSTVSLPG GGSGPPEDVK
PPVLGVRGLH CPPPPGGPGA GKRLCAICGD RSSGKHYGVY SCEGCKGFFK RTIRKDLTYS
CRDNKDCTVD KRQRNRCQYC RYQKCLATGM KREAVQEERQ RGKDKDGDGE GAGGAPEEMP
VDRILEAELA VEQKSDQGVE GPGGTGGSGS SPNDPVTNIC QAADKQLFTL VEWAKRIPHF
SSLPLDDQVI LLRAGWNELL IASFSHRSID VRDGILLATG LHVHRNSAHS AGVGAIFDRV
LTELVSKMRD MRMDKTELGC LRAIILFNPD AKGLSNPSEV EVLREKVYAS LETYCKQKYP
EQQGRFAKLL LRLPALRSIG LKCLEHLFFF KLIGDTPIDT FLMEMLEAPH QLA
