P19793 (RXRA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	462 AA.
Sequence status	Complete.
Protein existence	Evidence 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.20
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. Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20
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 process	Host-virus interaction Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Receptor
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Uncategorized	ligand-regulated transcription factor activity Inferred from direct assay. Source: HGNC regulation of transcription from RNA polymerase II promoter by nuclear hormone receptor Traceable author statement. Source: Reactome
Biological process	cellular lipid metabolic process Traceable author statement. Source: Reactome cholesterol metabolic process Traceable author statement. Source: BHF-UCL negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay. 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. Source: MGI response to retinoic acid Inferred from mutant phenotype. Source: BHF-UCL transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW virus-host interaction Inferred from direct assay Ref.13. Source: UniProtKB vitamin metabolic process Traceable author statement. Source: ProtInc
Cellular component	nuclear chromatin Inferred from direct assay. Source: BHF-UCL nucleoplasm Traceable author statement. Source: Reactome
Molecular function	9-cis retinoic acid receptor activity Traceable author statement. Source: ProtInc enzyme binding Inferred from physical interaction Ref.14. Source: UniProtKB protein heterodimerization activity Inferred from direct assay. Source: UniProtKB retinoic acid-responsive element binding Inferred from direct assay. Source: UniProtKB sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding transcription factor activity Inferred from direct assay. Source: MGI steroid binding Inferred from electronic annotation. Source: InterPro steroid hormone receptor activity Inferred from electronic annotation. Source: InterPro transcription coactivator activity Traceable author statement. Source: ProtInc vitamin D receptor binding Inferred from physical interaction. Source: BHF-UCL zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Ncoa6	Q9JLI4	2	EBI-78598,EBI-286271	From a different organism.
PIK3R1	P27986	8	EBI-78598,EBI-79464
RARA	P10276	3	EBI-78598,EBI-413374
STAT1	P42224	2	EBI-78598,EBI-1057697

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 462

462

Retinoic acid receptor RXR-alpha

PRO_0000053566

Regions

DNA binding

135 – 200

66

Nuclear receptor Ref.2

Zinc finger

135 – 155

21

NR C4-type

Zinc finger

171 – 195

25

NR C4-type

Region

1 – 134

134

Modulating By similarity

Region

201 – 224

24

Hinge

Region

225 – 462

238

Ligand-binding

Amino acid modifications

Modified residue

21

1

Phosphoserine By similarity

Modified residue

27

1

Phosphoserine Ref.11

Modified residue

56

1

Phosphoserine; by MAPK8 and MAPK9 By similarity

Modified residue

70

1

Phosphoserine; by MAPK8 and MAPK9 By similarity

Modified residue

82

1

Phosphothreonine; by MAPK8 and MAPK9 By similarity

Modified residue

260

1

Phosphoserine; by MAPK8 and MAPK9 By similarity

Cross-link

108

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.18

Natural variations

Natural variant

261

1

P → L.
Corresponds to variant rs2234960 [ dbSNP | Ensembl ].

VAR_014620

Natural variant

327

1

A → S.
Corresponds to variant rs1805345 [ dbSNP | Ensembl ].

VAR_050582

Natural variant

336

1

S → I.
Corresponds to variant rs1805345 [ dbSNP | Ensembl ].

VAR_014621

Natural variant

398

1

A → V.
Corresponds to variant rs11542209 [ dbSNP | Ensembl ].

VAR_050583

Experimental info

Mutagenesis

27

1

S → A: Abolishes phosphorylation. No change in increase of RARA-mediated transcriptional activity. Ref.11 Ref.20

Mutagenesis

27

1

S → A: Increase in RARA-mediated transcriptional activity. Ref.11 Ref.20

Secondary structure

1

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462

Helix Strand Turn

Details...

Turn

136 – 138

3

Beta strand

147 – 150

4

Helix

153 – 164

12

Beta strand

184 – 186

3

Helix

188 – 196

9

Turn

197 – 199

3

Helix

202 – 204

3

Helix

226 – 229

4

Helix

232 – 242

11

Helix

264 – 284

21

Helix

289 – 291

3

Helix

294 – 316

23

Helix

317 – 319

3

Beta strand

320 – 325

6

Beta strand

331 – 333

3

Helix

334 – 340

7

Helix

343 – 352

10

Helix

354 – 360

7

Helix

364 – 375

12

Helix

386 – 407

22

Helix

414 – 419

6

Helix

421 – 441

21

Helix

452 – 455

4

Sequences

	Sequence		Length	Mass (Da)
	P19793 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: 7F952B580AD84C42	FASTA	462	50,811
	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

References

	« Hide 'large scale' referencesShow '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: 2159111] [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: 18619963] [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. , 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: 15164053] [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. , 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: 15489334] [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: 1310260] [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: 9267036] [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: 10567404] [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: 10195690] [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: 11162439] [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: 11259580] [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: 11915042] [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: 12039952] [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: 15047147] [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: 14981089] [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: 16574651] [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: 16912044] [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: 17205979] [Abstract] Cited for: HETERODIMERIZATION WITH RARA.
[20]	"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: 20215566] [Abstract] Cited for: HETERODIMERIZATION WITH RARA, FUNCTION, MUTAGENESIS OF SER-27.
[21]	"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: 7925381] [Abstract] Cited for: STRUCTURE BY NMR OF 130-223.
[22]	"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: 7746322] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 130-209.
[23]	"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: 7760929] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 225-462.
[24]	"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: 9698548] [Abstract] Cited for: STRUCTURE BY NMR OF 130-212.
[25]	"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: 10698945] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 129-209 IN COMPLEX WITH RARA AND DNA.
[26]	"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: 10835357] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 224-462 OF APO AND HOLO FORMS.
[27]	"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: 10970886] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 225-462 OF APO AND HOLO FORMS.
[28]	"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: 10669605] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 129-212 IN COMPLEX WITH DNA.
[29]	"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: 10882139] [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.
[30]	"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: 11698662] [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.
[31]	"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: 15610733] [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.

IPI

IPI00418394.

PIR

S09592.

RefSeq

NP_002948.1. NM_002957.4.

UniGene

Hs.590886.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BY4	X-ray	2.10	A/B/C/D	129-209	[»]
1DSZ	X-ray	1.70	B	129-212	[»]
1FBY	X-ray	2.25	A/B	224-462	[»]
1FM6	X-ray	2.10	A/U	225-462	[»]
1FM9	X-ray	2.10	A	225-462	[»]
1G1U	X-ray	2.50	A/B/C/D	225-462	[»]
1G5Y	X-ray	2.00	A/B/C/D	225-462	[»]
1K74	X-ray	2.30	A	225-462	[»]
1LBD	X-ray	2.70	A	201-462	[»]
1MV9	X-ray	1.90	A	223-462	[»]
1MVC	X-ray	1.90	A	223-462	[»]
1MZN	X-ray	1.90	A/C/E/G	223-462	[»]
1R0N	X-ray	2.60	A	130-206	[»]
1RDT	X-ray	2.40	A	225-462	[»]
1RXR	NMR	-	A	130-212	[»]
1XLS	X-ray	2.96	A/B/C/D	227-458	[»]
1XV9	X-ray	2.70	A/C	227-462	[»]
1XVP	X-ray	2.60	A/C	227-462	[»]
1YNW	X-ray	3.00	B	130-228	[»]
2ACL	X-ray	2.80	A/C/E/G	225-462	[»]
2NLL	X-ray	1.90	A	135-200	[»]
2P1T	X-ray	1.80	A	223-462	[»]
2P1U	X-ray	2.20	A	223-462	[»]
2P1V	X-ray	2.20	A	223-462	[»]
2ZXZ	X-ray	3.00	A	223-462	[»]
2ZY0	X-ray	2.90	A/C	223-462	[»]
3DZU	X-ray	3.20	A	11-462	[»]
3DZY	X-ray	3.10	A	11-462	[»]
3E00	X-ray	3.10	A	11-462	[»]
3E94	X-ray	1.90	A	223-462	[»]
3FAL	X-ray	2.36	A/C	225-462	[»]
3FC6	X-ray	2.06	A/C	225-462	[»]
3FUG	X-ray	2.00	A	223-462	[»]
3H0A	X-ray	2.10	A	228-455	[»]
3KWY	X-ray	2.30	A	223-462	[»]
3NSP	X-ray	2.90	A/B	223-462	[»]
3NSQ	X-ray	2.60	A/B	223-462	[»]
3OAP	X-ray	2.05	A	228-458	[»]
3OZJ	X-ray	2.10	A/C	225-462	[»]
3PCU	X-ray	2.00	A	229-458	[»]
3R29	X-ray	2.90	A/B	223-462	[»]
3R2A	X-ray	3.00	A/B/C/D	223-462	[»]

ProteinModelPortal

P19793.

SMR

P19793. Positions 129-459.

DisProt

DP00062.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-641N.

IntAct

P19793. 15 interactions.

MINT

MINT-98407.

STRING

P19793.

PTM databases

PhosphoSite

P19793.

Polymorphism databases

DMDM

133701.

Proteomic databases

PRIDE

P19793.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000481739; ENSP00000419692; ENSG00000186350.

GeneID

6256.

KEGG

hsa:6256.

UCSC

uc004cfb.1. human.

Organism-specific databases

CTD

6256.

GeneCards

GC09P137208.

H-InvDB

HIX0008518.

HGNC

HGNC:10477. RXRA.

HPA

CAB004565.
CAB005352.

MIM

180245. gene.

neXtProt

NX_P19793.

PharmGKB

PA34890.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG08166.

HOVERGEN

HBG005606.

InParanoid

P19793.

OMA

PNSPNDP.

OrthoDB

EOG4SJ5DV.

PhylomeDB

P19793.

Enzyme and pathway databases

Pathway_Interaction_DB

a6b1_a6b4_integrin_pathway. a6b1 and a6b4 Integrin signaling.
ar_tf_pathway. Regulation of Androgen receptor activity.
retinoic_acid_pathway. Retinoic acid receptors-mediated signaling.
rxr_vdr_pathway. RXR and RAR hetrodimerization with other nuclear receptor.

Reactome

REACT_111045. Developmental Biology.
REACT_22258. Metabolism of lipids and lipoproteins.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P19793.

Bgee

P19793.

CleanEx

HS_RXRA.

Genevestigator

P19793.

GermOnline

ENSG00000186350. Homo sapiens.

Family and domain databases

InterPro

IPR021780. DUF3345.
IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR000003. Retinoid-X_rcpt.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]

Gene3D

G3DSA:1.10.565.10. Nucl_hrmn_rcpt_lig_bd. 1 hit.
G3DSA:3.30.50.10. Znf_NHR/GATA. 1 hit.

KO

K08524.

Pfam

PF00104. Hormone_recep. 1 hit.
PF11825. Nuc_recep-AF1. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]

PRINTS

PR00545. RETINOIDXR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.

SMART

SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]

SUPFAM

SSF48508. Str_ncl_receptor. 1 hit.

PROSITE

PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00459. Acitretin.
DB00210. Adapalene.
DB00523. Alitretinoin.
DB00926. Etretinate.

NextBio

24295.

PMAP-CutDB

P19793.

SOURCE

Search...

Entry information

Entry name

RXRA_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 146 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.