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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)DescriptionActionsGraphical viewLength
DNA bindingi135 – 200Nuclear receptorPROSITE-ProRule annotationAdd BLAST66
Zinc fingeri135 – 155NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri171 – 195NR C4-typePROSITE-ProRule annotationAdd BLAST25

GO - Molecular functioni

  • 9-cis retinoic acid receptor activity Source: ProtInc
  • chromatin DNA binding Source: Ensembl
  • DNA binding Source: MGI
  • enzyme binding Source: UniProtKB
  • 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
  • RNA polymerase II transcription factor activity, ligand-activated sequence-specific DNA binding Source: BHF-UCL
  • sequence-specific DNA binding Source: AgBase
  • steroid hormone receptor activity Source: InterPro
  • transcription coactivator activity Source: ProtInc
  • transcription factor activity, sequence-specific DNA binding Source: UniProtKB
  • 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

BioCyciZFISH:ENSG00000078380-MONOMER.
ReactomeiR-HSA-1368082. RORA activates gene expression.
R-HSA-1368108. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
R-HSA-159418. Recycling of bile acids and salts.
R-HSA-192105. Synthesis of bile acids and bile salts.
R-HSA-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
R-HSA-193807. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
R-HSA-1989781. PPARA activates gene expression.
R-HSA-200425. Import of palmitoyl-CoA into the mitochondrial matrix.
R-HSA-2032785. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
R-HSA-204174. Regulation of pyruvate dehydrogenase (PDH) complex.
R-HSA-211976. Endogenous sterols.
R-HSA-2151201. Transcriptional activation of mitochondrial biogenesis.
R-HSA-2426168. Activation of gene expression by SREBF (SREBP).
R-HSA-381340. Transcriptional regulation of white adipocyte differentiation.
R-HSA-383280. Nuclear Receptor transcription pathway.
R-HSA-400206. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
R-HSA-400253. Circadian Clock.
R-HSA-5362517. Signaling by Retinoic Acid.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
SignaLinkiP19793.
SIGNORiP19793.

Chemistry databases

SwissLipidsiSLP:000001552.

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
Proteomesi
  • UP000005640 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)DescriptionActionsGraphical viewLength
Mutagenesisi27S → A: Abolishes phosphorylation. No change in increase of RARA-mediated transcriptional activity. 2 Publications1
Mutagenesisi27S → A: Increase in RARA-mediated transcriptional activity. 2 Publications1

Organism-specific databases

DisGeNETi6256.
OpenTargetsiENSG00000186350.
PharmGKBiPA34890.

Chemistry databases

ChEMBLiCHEMBL2061.
DrugBankiDB00459. Acitretin.
DB00210. Adapalene.
DB00523. Alitretinoin.
DB00307. Bexarotene.
DB00749. Etodolac.
GuidetoPHARMACOLOGYi610.

Polymorphism and mutation databases

BioMutaiRXRA.
DMDMi133701.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000535661 – 462Retinoic acid receptor RXR-alphaAdd BLAST462

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei21PhosphoserineBy similarity1
Modified residuei27Phosphoserine1 Publication1
Modified residuei56Phosphoserine; by MAPK8 and MAPK9By similarity1
Modified residuei70Phosphoserine; by MAPK8 and MAPK9By similarity1
Modified residuei82Phosphothreonine; by MAPK8 and MAPK9By similarity1
Cross-linki108Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei129PhosphoserineCombined sources1
Modified residuei259PhosphoserineCombined sources1
Modified residuei260Phosphoserine; by MAPK8 and MAPK9By similarity1

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

EPDiP19793.
MaxQBiP19793.
PaxDbiP19793.
PeptideAtlasiP19793.
PRIDEiP19793.

PTM databases

iPTMnetiP19793.
PhosphoSitePlusiP19793.

Miscellaneous databases

PMAP-CutDBP19793.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000186350.
CleanExiHS_RXRA.
ExpressionAtlasiP19793. baseline and differential.
GenevisibleiP19793. HS.

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

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • vitamin D receptor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi112168. 115 interactors.
DIPiDIP-641N.
IntActiP19793. 41 interactors.
MINTiMINT-98407.
STRINGi9606.ENSP00000419692.

Chemistry databases

BindingDBiP19793.

Structurei

Secondary structure

1462
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi131 – 134Combined sources4
Turni136 – 138Combined sources3
Beta strandi141 – 146Combined sources6
Beta strandi149 – 151Combined sources3
Helixi153 – 165Combined sources13
Beta strandi172 – 175Combined sources4
Turni181 – 186Combined sources6
Helixi188 – 197Combined sources10
Helixi202 – 204Combined sources3
Helixi226 – 229Combined sources4
Helixi232 – 242Combined sources11
Helixi246 – 250Combined sources5
Turni251 – 253Combined sources3
Beta strandi258 – 261Combined sources4
Helixi264 – 284Combined sources21
Helixi289 – 291Combined sources3
Helixi294 – 316Combined sources23
Turni317 – 319Combined sources3
Beta strandi320 – 325Combined sources6
Turni327 – 329Combined sources3
Beta strandi331 – 333Combined sources3
Helixi334 – 338Combined sources5
Turni339 – 341Combined sources3
Helixi343 – 352Combined sources10
Helixi354 – 359Combined sources6
Helixi364 – 375Combined sources12
Beta strandi380 – 382Combined sources3
Helixi386 – 407Combined sources22
Helixi414 – 419Combined sources6
Helixi422 – 442Combined sources21
Beta strandi444 – 447Combined sources4
Helixi449 – 454Combined sources6
Helixi457 – 459Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4RFWX-ray2.40A228-458[»]
4RMCX-ray2.70A228-458[»]
4RMDX-ray1.90A228-462[»]
4RMEX-ray2.30A228-462[»]
4ZO1X-ray3.22B231-455[»]
4ZSHX-ray1.80A223-462[»]
5EC9X-ray2.30A229-456[»]
DisProtiDP00062.
ProteinModelPortaliP19793.
SMRiP19793.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19793.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 134ModulatingBy similarityAdd BLAST134
Regioni201 – 224HingeAdd BLAST24
Regioni225 – 462Ligand-bindingAdd BLAST238

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)DescriptionActionsGraphical viewLength
Zinc fingeri135 – 155NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri171 – 195NR C4-typePROSITE-ProRule annotationAdd BLAST25

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
GeneTreeiENSGT00760000118948.
HOVERGENiHBG005606.
InParanoidiP19793.
KOiK08524.
OMAiMDTKHFL.
OrthoDBiEOG091G0YX6.
PhylomeDBiP19793.
TreeFamiTF352097.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR021780. Nuc_recep-AF1.
IPR000536. Nucl_hrmn_rcpt_lig-bd.
IPR001723. Nuclear_hrmn_rcpt.
IPR000003. Retinoid-X_rcpt/HNF4.
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_014620261P → L.Corresponds to variant rs2234960dbSNPEnsembl.1
Natural variantiVAR_050582327A → S.Corresponds to variant rs1805345dbSNPEnsembl.1
Natural variantiVAR_014621336S → I.Corresponds to variant rs1805345dbSNPEnsembl.1
Natural variantiVAR_050583398A → V.Corresponds to variant rs11542209dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0565651 – 97Missing in isoform 2. 1 PublicationAdd BLAST97

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.3. 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
PDB 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[»]
4RFWX-ray2.40A228-458[»]
4RMCX-ray2.70A228-458[»]
4RMDX-ray1.90A228-462[»]
4RMEX-ray2.30A228-462[»]
4ZO1X-ray3.22B231-455[»]
4ZSHX-ray1.80A223-462[»]
5EC9X-ray2.30A229-456[»]
DisProtiDP00062.
ProteinModelPortaliP19793.
SMRiP19793.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112168. 115 interactors.
DIPiDIP-641N.
IntActiP19793. 41 interactors.
MINTiMINT-98407.
STRINGi9606.ENSP00000419692.

Chemistry databases

BindingDBiP19793.
ChEMBLiCHEMBL2061.
DrugBankiDB00459. Acitretin.
DB00210. Adapalene.
DB00523. Alitretinoin.
DB00307. Bexarotene.
DB00749. Etodolac.
GuidetoPHARMACOLOGYi610.
SwissLipidsiSLP:000001552.

PTM databases

iPTMnetiP19793.
PhosphoSitePlusiP19793.

Polymorphism and mutation databases

BioMutaiRXRA.
DMDMi133701.

Proteomic databases

EPDiP19793.
MaxQBiP19793.
PaxDbiP19793.
PeptideAtlasiP19793.
PRIDEiP19793.

Protocols and materials databases

DNASUi6256.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000481739; ENSP00000419692; ENSG00000186350. [P19793-1]
GeneIDi6256.
KEGGihsa:6256.
UCSCiuc004cfb.3. human. [P19793-1]

Organism-specific databases

CTDi6256.
DisGeNETi6256.
GeneCardsiRXRA.
HGNCiHGNC:10477. RXRA.
HPAiCAB004565.
CAB005352.
MIMi180245. gene.
neXtProtiNX_P19793.
OpenTargetsiENSG00000186350.
PharmGKBiPA34890.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
GeneTreeiENSGT00760000118948.
HOVERGENiHBG005606.
InParanoidiP19793.
KOiK08524.
OMAiMDTKHFL.
OrthoDBiEOG091G0YX6.
PhylomeDBiP19793.
TreeFamiTF352097.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000078380-MONOMER.
ReactomeiR-HSA-1368082. RORA activates gene expression.
R-HSA-1368108. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
R-HSA-159418. Recycling of bile acids and salts.
R-HSA-192105. Synthesis of bile acids and bile salts.
R-HSA-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
R-HSA-193807. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
R-HSA-1989781. PPARA activates gene expression.
R-HSA-200425. Import of palmitoyl-CoA into the mitochondrial matrix.
R-HSA-2032785. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
R-HSA-204174. Regulation of pyruvate dehydrogenase (PDH) complex.
R-HSA-211976. Endogenous sterols.
R-HSA-2151201. Transcriptional activation of mitochondrial biogenesis.
R-HSA-2426168. Activation of gene expression by SREBF (SREBP).
R-HSA-381340. Transcriptional regulation of white adipocyte differentiation.
R-HSA-383280. Nuclear Receptor transcription pathway.
R-HSA-400206. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
R-HSA-400253. Circadian Clock.
R-HSA-5362517. Signaling by Retinoic Acid.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
SignaLinkiP19793.
SIGNORiP19793.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000186350.
CleanExiHS_RXRA.
ExpressionAtlasiP19793. baseline and differential.
GenevisibleiP19793. HS.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR021780. Nuc_recep-AF1.
IPR000536. Nucl_hrmn_rcpt_lig-bd.
IPR001723. Nuclear_hrmn_rcpt.
IPR000003. Retinoid-X_rcpt/HNF4.
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...

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: November 30, 2016
This is version 201 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

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 one 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.