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P19793 (RXRA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 174. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Retinoic acid receptor RXR-alpha
Alternative name(s):
Nuclear receptor subfamily 2 group B member 1
Retinoid X receptor alpha
Gene names
Name:RXRA
Synonyms:NR2B1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length462 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. The high affinity ligand for RXRs is 9-cis retinoic acid. RXRA serves as a common heterodimeric partner for a number of nuclear receptors. The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone acetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation. The RXRA/PPARA heterodimer is required for PPARA transcriptional activity on fatty acid oxidation genes such as ACOX1 and the P450 system genes. Ref.10 Ref.11 Ref.13 Ref.22

Subunit structure

Homodimer. Heterodimer with RARA; required for ligand-dependent retinoic acid receptor transcriptional activity. Heterodimer with PPARA (via the leucine-like zipper in the LBD); the interaction is required for PPARA transcriptional activity. Also heterodimerizes with PPARG. Interacts with NCOA3 and NCOA6 coactivators. Interacts with FAM120B By similarity. Interacts with PELP1, SENP6, SFPQ, DNTTIP2 and RNF8. Interacts (via the DNA binding domain) with HCV core protein; the interaction enhances the transcriptional activities of the RXRA/RARA and the RXRA/PPARA heterodimers. Interacts with PRMT2. Interacts with ASXL1 By similarity. Interacts with BHLHE40/DEC1, BHLHE41/DEC2, NCOR1 and NCOR2. Interacts in a ligand-dependent fashion with MED1 and NCOA1. Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.22

Subcellular location

Nucleus Ref.13.

Tissue specificity

Highly expressed in liver, also found in lung, kidney and heart.

Domain

Composed of three domains: a modulating N-terminal domain (AF1 domain), a DNA-binding domain and a C-terminal ligand-binding domain (AF2 domain).

Post-translational modification

Phosphorylated on serine and threonine residues mainly in the N-terminal modulating domain. Constiutively phosphorylated on Ser-21 in the presence or absence of ligand. Under stress conditions, hyperphosphorylated by activated JNK on Ser-56, Ser-70, Thr-82 and Ser-260 By similarity. Phosphorylated on Ser-27, in vitro, by PKA. This phosphorylation is required for repression of cAMP-mediated transcriptional activity of RARA. Ref.11

Sumoylation negatively regulates transcriptional activity. Desumoylated specifically by SENP6. Ref.18

Sequence similarities

Belongs to the nuclear hormone receptor family. NR2 subfamily.

Contains 1 nuclear receptor DNA-binding domain.

Ontologies

Keywords
   Biological processHost-virus interaction
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionReceptor
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcardiac muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

cellular lipid metabolic process

Traceable author statement. Source: Reactome

cholesterol metabolic process

Traceable author statement PubMed 18544046. Source: BHF-UCL

embryo implantation

Inferred from electronic annotation. Source: Ensembl

gene expression

Traceable author statement. Source: Reactome

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

maternal placenta development

Inferred from electronic annotation. Source: Ensembl

modulation by virus of host morphology or physiology

Inferred from direct assay Ref.13. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 17426122. Source: BHF-UCL

peroxisome proliferator activated receptor signaling pathway

Inferred from direct assay Ref.10. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 20219900. Source: UniProtKB

regulation of branching involved in prostate gland morphogenesis

Inferred from electronic annotation. Source: Ensembl

response to retinoic acid

Inferred from mutant phenotype PubMed 17538076. Source: BHF-UCL

retinoic acid receptor signaling pathway

Inferred from mutant phenotype PubMed 17538076. Source: BHF-UCL

secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

ventricular cardiac muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

ventricular cardiac muscle tissue morphogenesis

Inferred from electronic annotation. Source: Ensembl

vitamin metabolic process

Traceable author statement PubMed 1651173. Source: ProtInc

   Cellular_componentnuclear chromatin

Inferred from direct assay PubMed 18511497. Source: BHF-UCL

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 19917671. Source: UniProtKB

   Molecular_function9-cis retinoic acid receptor activity

Traceable author statement Ref.7. Source: ProtInc

DNA binding

Inferred from direct assay PubMed 12037571. Source: MGI

chromatin DNA binding

Inferred from electronic annotation. Source: Ensembl

enzyme binding

Inferred from physical interaction Ref.14. Source: UniProtKB

ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from direct assay PubMed 7990953. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 10428834Ref.13PubMed 12040021PubMed 14701856Ref.21PubMed 19917671PubMed 20219900PubMed 9653119. Source: UniProtKB

protein heterodimerization activity

Inferred from direct assay PubMed 19917671. Source: UniProtKB

retinoic acid receptor activity

Traceable author statement PubMed 18544046. Source: BHF-UCL

retinoic acid-responsive element binding

Inferred from direct assay PubMed 19917671. Source: UniProtKB

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 20219900. Source: UniProtKB

steroid hormone receptor activity

Inferred from electronic annotation. Source: InterPro

transcription coactivator activity

Traceable author statement PubMed 1651173. Source: ProtInc

vitamin D receptor binding

Inferred from physical interaction PubMed 17426122. Source: BHF-UCL

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 462462Retinoic acid receptor RXR-alpha
PRO_0000053566

Regions

DNA binding135 – 20066Nuclear receptor Ref.2
Zinc finger135 – 15521NR C4-type
Zinc finger171 – 19525NR C4-type
Region1 – 134134Modulating By similarity
Region201 – 22424Hinge
Region225 – 462238Ligand-binding

Amino acid modifications

Modified residue211Phosphoserine By similarity
Modified residue271Phosphoserine Ref.11
Modified residue561Phosphoserine; by MAPK8 and MAPK9 By similarity
Modified residue701Phosphoserine; by MAPK8 and MAPK9 By similarity
Modified residue821Phosphothreonine; by MAPK8 and MAPK9 By similarity
Modified residue2601Phosphoserine; by MAPK8 and MAPK9 By similarity
Cross-link108Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.18

Natural variations

Natural variant2611P → L.
Corresponds to variant rs2234960 [ dbSNP | Ensembl ].
VAR_014620
Natural variant3271A → S.
Corresponds to variant rs1805345 [ dbSNP | Ensembl ].
VAR_050582
Natural variant3361S → I.
Corresponds to variant rs1805345 [ dbSNP | Ensembl ].
VAR_014621
Natural variant3981A → V.
Corresponds to variant rs11542209 [ dbSNP | Ensembl ].
VAR_050583

Experimental info

Mutagenesis271S → A: Abolishes phosphorylation. No change in increase of RARA-mediated transcriptional activity. Ref.11 Ref.22
Mutagenesis271S → A: Increase in RARA-mediated transcriptional activity. Ref.11 Ref.22

Secondary structure

......................................................... 462
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P19793 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 7F952B580AD84C42

FASTA46250,811
        10         20         30         40         50         60 
MDTKHFLPLD FSTQVNSSLT SPTGRGSMAA PSLHPSLGPG IGSPGQLHSP ISTLSSPING 

        70         80         90        100        110        120 
MGPPFSVISS PMGPHSMSVP TTPTLGFSTG SPQLSSPMNP VSSSEDIKPP LGLNGVLKVP 

       130        140        150        160        170        180 
AHPSGNMASF TKHICAICGD RSSGKHYGVY SCEGCKGFFK RTVRKDLTYT CRDNKDCLID 

       190        200        210        220        230        240 
KRQRNRCQYC RYQKCLAMGM KREAVQEERQ RGKDRNENEV ESTSSANEDM PVERILEAEL 

       250        260        270        280        290        300 
AVEPKTETYV EANMGLNPSS PNDPVTNICQ AADKQLFTLV EWAKRIPHFS ELPLDDQVIL 

       310        320        330        340        350        360 
LRAGWNELLI ASFSHRSIAV KDGILLATGL HVHRNSAHSA GVGAIFDRVL TELVSKMRDM 

       370        380        390        400        410        420 
QMDKTELGCL RAIVLFNPDS KGLSNPAEVE ALREKVYASL EAYCKHKYPE QPGRFAKLLL 

       430        440        450        460 
RLPALRSIGL KCLEHLFFFK LIGDTPIDTF LMEMLEAPHQ MT 

« Hide

References

« Hide 'large scale' references
[1]"Nuclear receptor that identifies a novel retinoic acid response pathway."
Mangelsdorf D.J., Ong E.S., Dyck J.A., Evans R.M.
Nature 345:224-229(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[2]"DNA-binding profiling of human hormone nuclear receptors via fluorescence correlation spectroscopy in a cell-free system."
Kobayashi T., Kodani Y., Nozawa A., Endo Y., Sawasaki T.
FEBS Lett. 582:2737-2744(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], DNA-BINDING.
[3]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Ovary.
[6]NIEHS SNPs program
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-462.
[7]"9-cis retinoic acid is a high affinity ligand for the retinoid X receptor."
Heyman R.A., Mangelsdorf D.J., Dyck J.A., Stein R.B., Eichele G., Evans R.M., Thaller C.
Cell 68:397-406(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF LIGAND.
[8]"Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300."
Chen H., Lin R.J., Schiltz R.L., Chakravarti D., Nash A., Nagy L., Privalsky M.L., Nakatani Y., Evans R.M.
Cell 90:569-580(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NCOA3.
[9]"A nuclear factor ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo."
Lee S.-K., Anzick S.L., Choi J.-E., Bubendorf L., Guan X.-Y., Jung Y.-K., Kallioniemi O.-P., Kononen J., Trent J.M., Azorsa D., Jhun B.-H., Cheong J.H., Lee Y.C., Meltzer P.S., Lee J.W.
J. Biol. Chem. 274:34283-34293(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NCOA6.
[10]"Conserved amino acids in the ligand-binding and tau(i) domains of the peroxisome proliferator-activated receptor alpha are necessary for heterodimerization with RXR."
Gorla-Bajszczak A., Juge-Aubry C., Pernin A., Burger A.G., Meier C.A.
Mol. Cell. Endocrinol. 147:37-47(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: HETERODIMERIZATION WITH PPARA, FUNCTION.
[11]"Serine 27, a human retinoid X receptor alpha residue, phosphorylated by protein kinase A is essential for cyclicAMP-mediated downregulation of RXRalpha function."
Harish S., Ashok M.S., Khanam T., Rangarajan P.N.
Biochem. Biophys. Res. Commun. 279:853-857(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-27, FUNCTION, MUTAGENESIS OF SER-27.
[12]"PSF is a novel corepressor that mediates its effect through Sin3A and the DNA binding domain of nuclear hormone receptors."
Mathur M., Tucker P.W., Samuels H.H.
Mol. Cell. Biol. 21:2298-2311(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SFPQ.
[13]"Interaction of hepatitis C virus core protein with retinoid X receptor alpha modulates its transcriptional activity."
Tsutsumi T., Suzuki T., Shimoike T., Suzuki R., Moriya K., Shintani Y., Fujie H., Matsuura Y., Koike K., Miyamura T.
Hepatology 35:937-946(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HCV CORE PROTEIN AND PPARA, SUBCELLULAR LOCATION, FUNCTION.
[14]"Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha."
Qi C., Chang J., Zhu Y., Yeldandi A.V., Rao S.M., Zhu Y.-J.
J. Biol. Chem. 277:28624-28630(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRMT2.
[15]"ERBP, a novel estrogen receptor binding protein enhancing the activity of estrogen receptor."
Bu H., Kashireddy P., Chang J., Zhu Y.T., Zhang Z., Zheng W., Rao S.M., Zhu Y.-J.
Biochem. Biophys. Res. Commun. 317:54-59(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DNTTIP2.
[16]"The RING finger protein, RNF8, interacts with retinoid X receptor alpha and enhances its transcription-stimulating activity."
Takano Y., Adachi S., Okuno M., Muto Y., Yoshioka T., Matsushima-Nishiwaki R., Tsurumi H., Ito K., Friedman S.L., Moriwaki H., Kojima S., Okano Y.
J. Biol. Chem. 279:18926-18934(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNF8.
[17]"9-cis-retinoic acid up-regulates expression of transcriptional coregulator PELP1, a novel coactivator of the retinoid X receptor alpha pathway."
Singh R.R., Gururaj A.E., Vadlamudi R.K., Kumar R.
J. Biol. Chem. 281:15394-15404(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PELP1.
[18]"Negative modulation of RXRalpha transcriptional activity by small ubiquitin-related modifier (SUMO) modification and its reversal by SUMO-specific protease SUSP1."
Choi S.J., Chung S.S., Rho E.J., Lee H.W., Lee M.H., Choi H.S., Seol J.H., Baek S.H., Bang O.S., Chung C.H.
J. Biol. Chem. 281:30669-30677(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-108, INTERACTION WITH SENP6.
[19]"Lysine trimethylation of retinoic acid receptor-alpha: a novel means to regulate receptor function."
Huq M.D., Tsai N.-P., Khan S.A., Wei L.-N.
Mol. Cell. Proteomics 6:677-688(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: HETERODIMERIZATION WITH RARA.
[20]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"The basic helix-loop-helix proteins differentiated embryo chondrocyte (DEC) 1 and DEC2 function as corepressors of retinoid X receptors."
Cho Y., Noshiro M., Choi M., Morita K., Kawamoto T., Fujimoto K., Kato Y., Makishima M.
Mol. Pharmacol. 76:1360-1369(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BHLHE40/DEC1; BHLHE41/DEC2; NCOA1; MED1; NCOR1 AND NCOR2.
[22]"Activity of retinoic acid receptor-alpha is directly regulated at its protein kinase A sites in response to follicle-stimulating hormone signaling."
Santos N.C., Kim K.H.
Endocrinology 151:2361-2372(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: HETERODIMERIZATION WITH RARA, FUNCTION, MUTAGENESIS OF SER-27.
[23]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"NMR assignments and secondary structure of the retinoid X receptor alpha DNA-binding domain. Evidence for the novel C-terminal helix."
Lee M.S., Sem D.S., Kliewer S.A., Provencal J., Evans R.M., Wright P.E.
Eur. J. Biochem. 224:639-650(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 130-223.
[25]"Structural determinants of nuclear receptor assembly on DNA direct repeats."
Rastinejad F., Perlmann T., Evans R.M., Sigler P.B.
Nature 375:203-211(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 130-209.
[26]"Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha."
Bourguet W., Ruff M., Chambon P., Gronemeyer H., Moras D.
Nature 375:377-382(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 225-462.
[27]"High-resolution solution structure of the retinoid X receptor DNA-binding domain."
Holmbeck S.M., Foster M.P., Casimiro D.R., Sem D.S., Dyson H.J., Wright P.E.
J. Mol. Biol. 281:271-284(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 130-212.
[28]"Structure of the RXR-RAR DNA-binding complex on the retinoic acid response element DR1."
Rastinejad F., Wagner T., Zhao Q., Khorasanizadeh S.
EMBO J. 19:1045-1054(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 129-209 IN COMPLEX WITH RARA AND DNA.
[29]"Crystal structure of the human RXRalpha ligand-binding domain bound to its natural ligand: 9-cis retinoic acid."
Egea P.F., Mitschler A., Rochel N., Ruff M., Chambon P., Moras D.
EMBO J. 19:2592-2601(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 224-462 OF APO AND HOLO FORMS.
[30]"Structural basis for autorepression of retinoid X receptor by tetramer formation and the AF-2 helix."
Gampe R.T. Jr., Montana V.G., Lambert M.H., Wisely G.B., Milburn M.V., Xu H.E.
Genes Dev. 14:2229-2241(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 225-462 OF APO AND HOLO FORMS.
[31]"Structural basis of RXR-DNA interactions."
Zhao Q., Chasse S.A., Devarakonda S., Sierk M.L., Ahvazi B., Rastinejad F.
J. Mol. Biol. 296:509-520(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 129-212 IN COMPLEX WITH DNA.
[32]"Asymmetry in the PPARgamma/RXRalpha crystal structure reveals the molecular basis of heterodimerization among nuclear receptors."
Gampe R.T. Jr., Montana V.G., Lambert M.H., Miller A.B., Bledsoe R.K., Milburn M.V., Kliewer S.A., Willson T.M., Xu H.E.
Mol. Cell 5:545-555(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 225-462 IN COMPLEX WITH PPARG; COACTIVATOR NCOA1; RETINOIC ACID AND SYNTHETIC ANTIDIABETIC AGONISTS ROSIGLITAZONE AND GI262570.
[33]"Structural determinants of ligand binding selectivity between the peroxisome proliferator-activated receptors."
Xu H.E., Lambert M.H., Montana V.G., Plunket K.D., Moore L.B., Collins J.L., Oplinger J.A., Kliewer S.A., Gampe R.T. Jr., McKee D.D., Moore J.T., Willson T.M.
Proc. Natl. Acad. Sci. U.S.A. 98:13919-13924(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 225-462 IN COMPLEX WITH PPARA OR PPARG; 9-CIS RETINOIC ACID; COACTIVATOR NCOA1 AND PPAR SYNTHETIC AGONIST GW409544.
[34]"The nuclear xenobiotic receptor CAR: structural determinants of constitutive activation and heterodimerization."
Suino K., Peng L., Reynolds R., Li Y., Cha J.Y., Repa J.J., Kliewer S.A., Xu H.E.
Mol. Cell 16:893-905(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) OF 227-458 IN COMPLEX WITH M.MUSCULUS NR1I13; R.NORVEGICUS NCOA2 AND AGONIST INSECTICIDE CONTAMINANT TCPOBOP.
+Additional computationally mapped references.

Web resources

NIEHS-SNPs
Wikipedia

Retinoid X receptor entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52773 mRNA. Translation: CAA36982.1.
AB307705 mRNA. Translation: BAH02296.1.
AC156789 Genomic DNA. No translation available.
AL354796, AL669970 Genomic DNA. Translation: CAH70571.1.
AL669970, AL354796 Genomic DNA. Translation: CAM45733.1.
AL683798 Genomic DNA. No translation available.
CH471090 Genomic DNA. Translation: EAW88123.1.
BC110998 mRNA. Translation: AAI10999.1.
DQ303444 Genomic DNA. Translation: ABB96254.1.
CCDSCCDS35172.1.
PIRS09592.
RefSeqNP_002948.1. NM_002957.5.
UniGeneHs.590886.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BY4X-ray2.10A/B/C/D129-209[»]
1DSZX-ray1.70B129-212[»]
1FBYX-ray2.25A/B224-462[»]
1FM6X-ray2.10A/U225-462[»]
1FM9X-ray2.10A225-462[»]
1G1UX-ray2.50A/B/C/D225-462[»]
1G5YX-ray2.00A/B/C/D225-462[»]
1K74X-ray2.30A225-462[»]
1LBDX-ray2.70A201-460[»]
1MV9X-ray1.90A223-462[»]
1MVCX-ray1.90A223-462[»]
1MZNX-ray1.90A/C/E/G223-462[»]
1R0NX-ray2.60A130-206[»]
1RDTX-ray2.40A225-462[»]
1RXRNMR-A130-212[»]
1XLSX-ray2.96A/B/C/D227-458[»]
1XV9X-ray2.70A/C227-462[»]
1XVPX-ray2.60A/C227-462[»]
1YNWX-ray3.00B130-228[»]
2ACLX-ray2.80A/C/E/G225-462[»]
2NLLX-ray1.90A135-200[»]
2P1TX-ray1.80A223-462[»]
2P1UX-ray2.20A223-462[»]
2P1VX-ray2.20A223-462[»]
2ZXZX-ray3.00A223-462[»]
2ZY0X-ray2.90A/C223-462[»]
3DZUX-ray3.20A11-462[»]
3DZYX-ray3.10A11-462[»]
3E00X-ray3.10A11-462[»]
3E94X-ray1.90A223-462[»]
3FALX-ray2.36A/C225-462[»]
3FC6X-ray2.06A/C225-462[»]
3FUGX-ray2.00A223-462[»]
3H0AX-ray2.10A228-455[»]
3KWYX-ray2.30A223-462[»]
3NSPX-ray2.90A/B223-462[»]
3NSQX-ray2.60A/B223-462[»]
3OAPX-ray2.05A228-458[»]
3OZJX-ray2.10A/C225-462[»]
3PCUX-ray2.00A229-458[»]
3R29X-ray2.90A/B223-462[»]
3R2AX-ray3.00A/B/C/D223-462[»]
3R5MX-ray2.80A/C223-462[»]
3UVVX-ray2.95B225-462[»]
4J5WX-ray2.80C/D227-462[»]
4J5XX-ray2.80C/D227-462[»]
4K4JX-ray2.00A228-458[»]
4K6IX-ray2.10A228-458[»]
4M8EX-ray2.40A228-458[»]
4M8HX-ray2.20A228-458[»]
4N5GX-ray2.11A/B/C/D223-462[»]
4N8RX-ray2.03A/B/C/D223-462[»]
4NQAX-ray3.10A/H98-462[»]
DisProtDP00062.
ProteinModelPortalP19793.
SMRP19793. Positions 127-459.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112168. 107 interactions.
DIPDIP-641N.
IntActP19793. 35 interactions.
MINTMINT-98407.
STRING9606.ENSP00000419692.

Chemistry

BindingDBP19793.
ChEMBLCHEMBL2363071.
DrugBankDB00459. Acitretin.
DB00210. Adapalene.
DB00523. Alitretinoin.
DB00926. Etretinate.
GuidetoPHARMACOLOGY610.

PTM databases

PhosphoSiteP19793.

Polymorphism databases

DMDM133701.

Proteomic databases

MaxQBP19793.
PaxDbP19793.
PRIDEP19793.

Protocols and materials databases

DNASU6256.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000481739; ENSP00000419692; ENSG00000186350.
ENST00000594882; ENSP00000470812; ENSG00000269571.
GeneID6256.
KEGGhsa:6256.
UCSCuc004cfb.2. human.

Organism-specific databases

CTD6256.
GeneCardsGC09P137208.
HGNCHGNC:10477. RXRA.
HPACAB004565.
CAB005352.
MIM180245. gene.
neXtProtNX_P19793.
PharmGKBPA34890.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG327099.
HOVERGENHBG005606.
InParanoidP19793.
KOK08524.
OMAKHFLPLD.
PhylomeDBP19793.
TreeFamTF352097.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111217. Metabolism.
REACT_71. Gene Expression.
SignaLinkP19793.

Gene expression databases

ArrayExpressP19793.
BgeeP19793.
CleanExHS_RXRA.
GenevestigatorP19793.

Family and domain databases

Gene3D1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProIPR021780. Nuc_recep-AF1.
IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR000003. Retinoid-X_rcpt/HNF4.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamPF00104. Hormone_recep. 1 hit.
PF11825. Nuc_recep-AF1. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSPR00545. RETINOIDXR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. SSF48508. 1 hit.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP19793.
GeneWikiRetinoid_X_receptor_alpha.
GenomeRNAi6256.
NextBio24295.
PMAP-CutDBP19793.
PROP19793.
SOURCESearch...

Entry information

Entry nameRXRA_HUMAN
AccessionPrimary (citable) accession number: P19793
Secondary accession number(s): Q2NL52, Q2V504
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: July 9, 2014
This is version 174 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM