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Protein

Retinoic acid receptor RXR-alpha

Gene

RXRA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi135 – 20066Nuclear receptorPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri135 – 15521NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri171 – 19525NR C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • 9-cis retinoic acid receptor activity Source: ProtInc
  • chromatin DNA binding Source: Ensembl
  • DNA binding Source: MGI
  • enzyme binding Source: UniProtKB
  • ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: BHF-UCL
  • protein heterodimerization activity Source: UniProtKB
  • retinoic acid receptor activity Source: BHF-UCL
  • retinoic acid-responsive element binding Source: UniProtKB
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: MGI
  • sequence-specific DNA binding Source: AgBase
  • sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • steroid hormone receptor activity Source: InterPro
  • transcription coactivator activity Source: ProtInc
  • vitamin D receptor binding Source: BHF-UCL
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Host-virus interaction, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_11042. Recycling of bile acids and salts.
REACT_11048. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
REACT_11054. Synthesis of bile acids and bile salts.
REACT_11082. Import of palmitoyl-CoA into the mitochondrial matrix.
REACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_116145. PPARA activates gene expression.
REACT_118659. RORA activates gene expression.
REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
REACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_13812. Endogenous sterols.
REACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_15525. Nuclear Receptor transcription pathway.
REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
REACT_24941. Circadian Clock.
REACT_264212. Transcriptional activation of mitochondrial biogenesis.
REACT_267785. Signaling by Retinoic Acid.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinkiP19793.

Names & Taxonomyi

Protein namesi
Recommended name:
Retinoic acid receptor RXR-alpha
Alternative name(s):
Nuclear receptor subfamily 2 group B member 1
Retinoid X receptor alpha
Gene namesi
Name:RXRA
Synonyms:NR2B1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:10477. RXRA.

Subcellular locationi

GO - Cellular componenti

  • nuclear chromatin Source: BHF-UCL
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • receptor complex Source: BHF-UCL
  • RNA polymerase II transcription factor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi27 – 271S → A: Abolishes phosphorylation. No change in increase of RARA-mediated transcriptional activity. 2 Publications
Mutagenesisi27 – 271S → A: Increase in RARA-mediated transcriptional activity. 2 Publications

Organism-specific databases

PharmGKBiPA34890.

Chemistry

DrugBankiDB00459. Acitretin.
DB00210. Adapalene.
DB00523. Alitretinoin.
DB00307. Bexarotene.
DB00749. Etodolac.

Polymorphism and mutation databases

BioMutaiRXRA.
DMDMi133701.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 462462Retinoic acid receptor RXR-alphaPRO_0000053566Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211PhosphoserineBy similarity
Modified residuei27 – 271Phosphoserine1 Publication
Modified residuei56 – 561Phosphoserine; by MAPK8 and MAPK9By similarity
Modified residuei70 – 701Phosphoserine; by MAPK8 and MAPK9By similarity
Modified residuei82 – 821Phosphothreonine; by MAPK8 and MAPK9By similarity
Cross-linki108 – 108Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei259 – 2591Phosphoserine1 Publication
Modified residuei260 – 2601Phosphoserine; by MAPK8 and MAPK9By similarity

Post-translational modificationi

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.By similarity1 Publication
Sumoylation negatively regulates transcriptional activity. Desumoylated specifically by SENP6.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP19793.
PaxDbiP19793.
PRIDEiP19793.

PTM databases

PhosphoSiteiP19793.

Miscellaneous databases

PMAP-CutDBP19793.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP19793.
CleanExiHS_RXRA.
ExpressionAtlasiP19793. baseline and differential.
GenevestigatoriP19793.

Organism-specific databases

HPAiCAB004565.
CAB005352.

Interactioni

Subunit structurei

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.By similarity15 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q034633EBI-78598,EBI-9159704From a different organism.
MED25Q71SY54EBI-78598,EBI-394558
NCOA1Q157885EBI-78598,EBI-455189
Ncoa6Q9JLI42EBI-78598,EBI-286271From a different organism.
PIK3R1P279868EBI-78598,EBI-79464
RARAP102766EBI-78598,EBI-413374
STAT1P422242EBI-78598,EBI-1057697

Protein-protein interaction databases

BioGridi112168. 110 interactions.
DIPiDIP-641N.
IntActiP19793. 39 interactions.
MINTiMINT-98407.
STRINGi9606.ENSP00000419692.

Structurei

Secondary structure

1
462
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi131 – 1344Combined sources
Turni136 – 1383Combined sources
Beta strandi141 – 1466Combined sources
Beta strandi149 – 1513Combined sources
Helixi153 – 16513Combined sources
Beta strandi172 – 1754Combined sources
Turni181 – 1866Combined sources
Helixi188 – 19710Combined sources
Helixi202 – 2043Combined sources
Helixi226 – 2294Combined sources
Helixi232 – 24211Combined sources
Helixi246 – 2505Combined sources
Turni251 – 2533Combined sources
Beta strandi258 – 2614Combined sources
Helixi264 – 28421Combined sources
Helixi289 – 2913Combined sources
Helixi294 – 31623Combined sources
Turni317 – 3193Combined sources
Beta strandi320 – 3256Combined sources
Turni327 – 3293Combined sources
Beta strandi331 – 3333Combined sources
Helixi334 – 3385Combined sources
Turni339 – 3413Combined sources
Helixi343 – 35210Combined sources
Helixi354 – 3596Combined sources
Helixi364 – 37512Combined sources
Beta strandi380 – 3823Combined sources
Helixi386 – 40722Combined sources
Helixi414 – 4196Combined sources
Helixi422 – 44221Combined sources
Helixi449 – 4546Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4CN2X-ray2.07C/D130-212[»]
4CN3X-ray2.35A/B/C130-212[»]
D130-173[»]
D175-212[»]
4CN5X-ray2.00A/B130-212[»]
4CN7X-ray2.34A/B/E/F130-212[»]
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[»]
4OC7X-ray2.50A223-462[»]
4POHX-ray2.30A228-458[»]
4POJX-ray2.00A228-458[»]
4PP3X-ray2.00A228-458[»]
4PP5X-ray2.00A228-458[»]
DisProtiDP00062.
ProteinModelPortaliP19793.
SMRiP19793. Positions 127-459.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19793.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 134134ModulatingBy similarityAdd
BLAST
Regioni201 – 22424HingeAdd
BLAST
Regioni225 – 462238Ligand-bindingAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri135 – 15521NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri171 – 19525NR C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG327099.
GeneTreeiENSGT00760000118948.
HOVERGENiHBG005606.
InParanoidiP19793.
KOiK08524.
OMAiKHFLPLD.
OrthoDBiEOG72RMZ5.
PhylomeDBiP19793.
TreeFamiTF352097.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR021780. 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]
PfamiPF00104. Hormone_recep. 1 hit.
PF11825. Nuc_recep-AF1. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR00545. RETINOIDXR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P19793-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDTKHFLPLD FSTQVNSSLT SPTGRGSMAA PSLHPSLGPG IGSPGQLHSP
60 70 80 90 100
ISTLSSPING MGPPFSVISS PMGPHSMSVP TTPTLGFSTG SPQLSSPMNP
110 120 130 140 150
VSSSEDIKPP LGLNGVLKVP AHPSGNMASF TKHICAICGD RSSGKHYGVY
160 170 180 190 200
SCEGCKGFFK RTVRKDLTYT CRDNKDCLID KRQRNRCQYC RYQKCLAMGM
210 220 230 240 250
KREAVQEERQ RGKDRNENEV ESTSSANEDM PVERILEAEL AVEPKTETYV
260 270 280 290 300
EANMGLNPSS PNDPVTNICQ AADKQLFTLV EWAKRIPHFS ELPLDDQVIL
310 320 330 340 350
LRAGWNELLI ASFSHRSIAV KDGILLATGL HVHRNSAHSA GVGAIFDRVL
360 370 380 390 400
TELVSKMRDM QMDKTELGCL RAIVLFNPDS KGLSNPAEVE ALREKVYASL
410 420 430 440 450
EAYCKHKYPE QPGRFAKLLL RLPALRSIGL KCLEHLFFFK LIGDTPIDTF
460
LMEMLEAPHQ MT
Length:462
Mass (Da):50,811
Last modified:February 1, 1991 - v1
Checksum:i7F952B580AD84C42
GO
Isoform 2 (identifier: P19793-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-97: Missing.

Note: No experimental confirmation available.

Show »
Length:365
Mass (Da):41,060
Checksum:i6F0D30787329986D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti261 – 2611P → L.
Corresponds to variant rs2234960 [ dbSNP | Ensembl ].
VAR_014620
Natural varianti327 – 3271A → S.
Corresponds to variant rs1805345 [ dbSNP | Ensembl ].
VAR_050582
Natural varianti336 – 3361S → I.
Corresponds to variant rs1805345 [ dbSNP | Ensembl ].
VAR_014621
Natural varianti398 – 3981A → V.
Corresponds to variant rs11542209 [ dbSNP | Ensembl ].
VAR_050583

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9797Missing in isoform 2. 1 PublicationVSP_056565Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52773 mRNA. Translation: CAA36982.1.
AB307705 mRNA. Translation: BAH02296.1.
AK131192 mRNA. Translation: BAG54745.1.
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.
CCDSiCCDS35172.1. [P19793-1]
PIRiS09592.
RefSeqiNP_001278850.1. NM_001291921.1. [P19793-2]
NP_002948.1. NM_002957.5. [P19793-1]
UniGeneiHs.590886.

Genome annotation databases

EnsembliENST00000481739; ENSP00000419692; ENSG00000186350. [P19793-1]
GeneIDi6256.
KEGGihsa:6256.
UCSCiuc004cfb.2. human. [P19793-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

Retinoid X receptor entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52773 mRNA. Translation: CAA36982.1.
AB307705 mRNA. Translation: BAH02296.1.
AK131192 mRNA. Translation: BAG54745.1.
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.
CCDSiCCDS35172.1. [P19793-1]
PIRiS09592.
RefSeqiNP_001278850.1. NM_001291921.1. [P19793-2]
NP_002948.1. NM_002957.5. [P19793-1]
UniGeneiHs.590886.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4CN2X-ray2.07C/D130-212[»]
4CN3X-ray2.35A/B/C130-212[»]
D130-173[»]
D175-212[»]
4CN5X-ray2.00A/B130-212[»]
4CN7X-ray2.34A/B/E/F130-212[»]
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[»]
4OC7X-ray2.50A223-462[»]
4POHX-ray2.30A228-458[»]
4POJX-ray2.00A228-458[»]
4PP3X-ray2.00A228-458[»]
4PP5X-ray2.00A228-458[»]
DisProtiDP00062.
ProteinModelPortaliP19793.
SMRiP19793. Positions 127-459.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112168. 110 interactions.
DIPiDIP-641N.
IntActiP19793. 39 interactions.
MINTiMINT-98407.
STRINGi9606.ENSP00000419692.

Chemistry

BindingDBiP19793.
ChEMBLiCHEMBL2363071.
DrugBankiDB00459. Acitretin.
DB00210. Adapalene.
DB00523. Alitretinoin.
DB00307. Bexarotene.
DB00749. Etodolac.
GuidetoPHARMACOLOGYi610.

PTM databases

PhosphoSiteiP19793.

Polymorphism and mutation databases

BioMutaiRXRA.
DMDMi133701.

Proteomic databases

MaxQBiP19793.
PaxDbiP19793.
PRIDEiP19793.

Protocols and materials databases

DNASUi6256.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000481739; ENSP00000419692; ENSG00000186350. [P19793-1]
GeneIDi6256.
KEGGihsa:6256.
UCSCiuc004cfb.2. human. [P19793-1]

Organism-specific databases

CTDi6256.
GeneCardsiGC09P137208.
HGNCiHGNC:10477. RXRA.
HPAiCAB004565.
CAB005352.
MIMi180245. gene.
neXtProtiNX_P19793.
PharmGKBiPA34890.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG327099.
GeneTreeiENSGT00760000118948.
HOVERGENiHBG005606.
InParanoidiP19793.
KOiK08524.
OMAiKHFLPLD.
OrthoDBiEOG72RMZ5.
PhylomeDBiP19793.
TreeFamiTF352097.

Enzyme and pathway databases

ReactomeiREACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_11042. Recycling of bile acids and salts.
REACT_11048. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
REACT_11054. Synthesis of bile acids and bile salts.
REACT_11082. Import of palmitoyl-CoA into the mitochondrial matrix.
REACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_116145. PPARA activates gene expression.
REACT_118659. RORA activates gene expression.
REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
REACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_13812. Endogenous sterols.
REACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_15525. Nuclear Receptor transcription pathway.
REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
REACT_24941. Circadian Clock.
REACT_264212. Transcriptional activation of mitochondrial biogenesis.
REACT_267785. Signaling by Retinoic Acid.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinkiP19793.

Miscellaneous databases

ChiTaRSiRXRA. human.
EvolutionaryTraceiP19793.
GeneWikiiRetinoid_X_receptor_alpha.
GenomeRNAii6256.
NextBioi24295.
PMAP-CutDBP19793.
PROiP19793.
SOURCEiSearch...

Gene expression databases

BgeeiP19793.
CleanExiHS_RXRA.
ExpressionAtlasiP19793. baseline and differential.
GenevestigatoriP19793.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR021780. 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]
PfamiPF00104. Hormone_recep. 1 hit.
PF11825. Nuc_recep-AF1. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR00545. RETINOIDXR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1).
    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] (ISOFORM 1), DNA-BINDING.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Amygdala.
  4. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 1).
    Tissue: Ovary.
  7. NIEHS SNPs program
    Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-462.
  8. "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.
  9. "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.
  10. "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.
  11. "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.
  12. "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.
  13. "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.
  14. "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.
  15. "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.
  16. "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.
  17. "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.
  18. "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.
  19. "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.
  20. "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.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. "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.
  23. "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.
  24. "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.
  25. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  26. "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.
  27. "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.
  28. "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.
  29. "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.
  30. "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.
  31. "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.
  32. "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.
  33. Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 129-212 IN COMPLEX WITH DNA.
  34. "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.
  35. "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.
  36. "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.

Entry informationi

Entry nameiRXRA_HUMAN
AccessioniPrimary (citable) accession number: P19793
Secondary accession number(s): B3KY83, Q2NL52, Q2V504
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: May 27, 2015
This is version 184 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.