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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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. 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
<p>This subsection of the ‘Function’ section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi135 – 200Nuclear receptorPROSITE-ProRule annotationAdd BLAST66
<p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri135 – 155NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri171 – 195NR C4-typePROSITE-ProRule annotationAdd BLAST25

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding, Receptor
Biological processHost-virus interaction, Transcription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-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-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-4090294 SUMOylation of intracellular receptors
R-HSA-5362517 Signaling by Retinoic Acid
R-HSA-5617472 Activation of anterior HOX genes in hindbrain development during early embryogenesis

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P19793

SIGNOR Signaling Network Open Resource

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SIGNORi
P19793

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

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MoonDBi
P19793 Predicted

Chemistry databases

SwissLipids knowledge resource for lipid biology

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SwissLipidsi
SLP:000001552

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Retinoic acid receptor RXR-alpha
Alternative name(s):
Nuclear receptor subfamily 2 group B member 1
Retinoid X receptor alpha
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:RXRA
Synonyms:NR2B1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 9

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000186350.9

Human Gene Nomenclature Database

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HGNCi
HGNC:10477 RXRA

Online Mendelian Inheritance in Man (OMIM)

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MIMi
180245 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P19793

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

DisGeNET

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DisGeNETi
6256

Open Targets

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OpenTargetsi
ENSG00000186350

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA34890

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2061

Drug and drug target database

More...
DrugBanki
DB07863 2-chloro-5-nitro-N-phenylbenzamide
DB00459 Acitretin
DB00210 Adapalene
DB00523 Alitretinoin
DB00307 Bexarotene
DB00749 Etodolac
DB00926 Etretinate
DB08601 tributylstannanyl

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
610

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
RXRA

Domain mapping of disease mutations (DMDM)

More...
DMDMi
133701

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000535661 – 462Retinoic acid receptor RXR-alphaAdd BLAST462

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki4Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

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EPDi
P19793

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P19793

MaxQB - The MaxQuant DataBase

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MaxQBi
P19793

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P19793

PeptideAtlas

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PeptideAtlasi
P19793

PRoteomics IDEntifications database

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PRIDEi
P19793

ProteomicsDB human proteome resource

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ProteomicsDBi
53687

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P19793

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P19793

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P19793

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000186350 Expressed in 231 organ(s), highest expression level in liver

CleanEx database of gene expression profiles

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CleanExi
HS_RXRA

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P19793 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P19793 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB004565
CAB005352

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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 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. Interacts with VDR.By similarity16 Publications
(Microbial infection) 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.1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
112168, 131 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-496 RXRalpha-PXR retinoic acid receptor complex
CPX-508 RXRalpha-RARalpha retinoic acid receptor complex
CPX-631 RXRalpha-VDR nuclear hormone receptor complex
CPX-632 RXRalpha-LXRalpha nuclear hormone receptor complex
CPX-654 RXRalpha-TRbeta nuclear hormone receptor complex
CPX-662 RXRalpha-TRalpha nuclear hormone receptor complex
CPX-664 RXRalpha-RXRalpha retinoic acid receptor complex
CPX-678 RXRalpha-LXRbeta nuclear hormone receptor complex
CPX-816 RXRalpha-RARalpha-NCOA2 retinoic acid receptor complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P19793

Database of interacting proteins

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DIPi
DIP-641N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P19793

Protein interaction database and analysis system

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IntActi
P19793, 50 interactors

Molecular INTeraction database

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MINTi
P19793

STRING: functional protein association networks

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STRINGi
9606.ENSP00000419692

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P19793

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1462
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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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[»]
5GYMX-ray2.60A/B/C/D/E/F/G/H227-462[»]
5JI0X-ray1.98A223-462[»]
5LYQX-ray2.17A223-462[»]
5MJ5X-ray1.90A229-457[»]
5MK4X-ray2.00A/C229-457[»]
5MKJX-ray2.50A229-458[»]
5MKUX-ray1.78A229-456[»]
5MMWX-ray2.70A229-457[»]
5TBPX-ray2.60A/B/C/D223-462[»]
5UANX-ray3.51A98-462[»]
5Z12X-ray2.75B/C228-458[»]
6A5YX-ray2.10D225-462[»]
6A5ZX-ray2.95D/L225-462[»]
6A60X-ray3.05D225-462[»]

Database of protein disorder

More...
DisProti
DP00062

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P19793

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P19793

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P19793

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini227 – 458NR LBDPROSITE-ProRule annotationAdd BLAST232

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 134ModulatingBy similarityAdd BLAST134
Regioni201 – 224HingeAdd BLAST24

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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).

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3575 Eukaryota
ENOG410XRZC LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000159789

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG005606

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P19793

KEGG Orthology (KO)

More...
KOi
K08524

Identification of Orthologs from Complete Genome Data

More...
OMAi
LTCGMKR

Database of Orthologous Groups

More...
OrthoDBi
912470at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P19793

TreeFam database of animal gene trees

More...
TreeFami
TF352097

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.50.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR035500 NHR_like_dom_sf
IPR021780 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

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00104 Hormone_recep, 1 hit
PF11825 Nuc_recep-AF1, 1 hit
PF00105 zf-C4, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00545 RETINOIDXR
PR00398 STRDHORMONER
PR00047 STROIDFINGER

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00430 HOLI, 1 hit
SM00399 ZnF_C4, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48508 SSF48508, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51843 NR_LBD, 1 hit
PS00031 NUCLEAR_REC_DBD_1, 1 hit
PS51030 NUCLEAR_REC_DBD_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A3B3IS44A0A3B3IS44_HUMAN
Retinoic acid receptor RXR-alpha
RXRA
123Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_014620261P → L. Corresponds to variant dbSNP:rs2234960Ensembl.1
Natural variantiVAR_050582327A → S. Corresponds to variant dbSNP:rs1805345Ensembl.1
Natural variantiVAR_014621336S → I. Corresponds to variant dbSNP:rs1805345Ensembl.1
Natural variantiVAR_050583398A → V. Corresponds to variant dbSNP:rs11542209Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0565651 – 97Missing in isoform 2. 1 PublicationAdd BLAST97

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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 Genomic DNA No translation available.
AL669970 Genomic DNA No translation available.
AL683798 Genomic DNA No translation available.
CH471090 Genomic DNA Translation: EAW88123.1
BC110998 mRNA Translation: AAI10999.1
DQ303444 Genomic DNA Translation: ABB96254.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS35172.1 [P19793-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
S09592

NCBI Reference Sequences

More...
RefSeqi
NP_001278850.1, NM_001291921.1 [P19793-2]
NP_002948.1, NM_002957.5 [P19793-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.590886

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000481739; ENSP00000419692; ENSG00000186350 [P19793-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
6256

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:6256

UCSC genome browser

More...
UCSCi
uc004cfb.3 human [P19793-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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 Genomic DNA No translation available.
AL669970 Genomic DNA No translation available.
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[»]
5GYMX-ray2.60A/B/C/D/E/F/G/H227-462[»]
5JI0X-ray1.98A223-462[»]
5LYQX-ray2.17A223-462[»]
5MJ5X-ray1.90A229-457[»]
5MK4X-ray2.00A/C229-457[»]
5MKJX-ray2.50A229-458[»]
5MKUX-ray1.78A229-456[»]
5MMWX-ray2.70A229-457[»]
5TBPX-ray2.60A/B/C/D223-462[»]
5UANX-ray3.51A98-462[»]
5Z12X-ray2.75B/C228-458[»]
6A5YX-ray2.10D225-462[»]
6A5ZX-ray2.95D/L225-462[»]
6A60X-ray3.05D225-462[»]
DisProtiDP00062
ProteinModelPortaliP19793
SMRiP19793
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112168, 131 interactors
ComplexPortaliCPX-496 RXRalpha-PXR retinoic acid receptor complex
CPX-508 RXRalpha-RARalpha retinoic acid receptor complex
CPX-631 RXRalpha-VDR nuclear hormone receptor complex
CPX-632 RXRalpha-LXRalpha nuclear hormone receptor complex
CPX-654 RXRalpha-TRbeta nuclear hormone receptor complex
CPX-662 RXRalpha-TRalpha nuclear hormone receptor complex
CPX-664 RXRalpha-RXRalpha retinoic acid receptor complex
CPX-678 RXRalpha-LXRbeta nuclear hormone receptor complex
CPX-816 RXRalpha-RARalpha-NCOA2 retinoic acid receptor complex
CORUMiP19793
DIPiDIP-641N
ELMiP19793
IntActiP19793, 50 interactors
MINTiP19793
STRINGi9606.ENSP00000419692

Chemistry databases

BindingDBiP19793
ChEMBLiCHEMBL2061
DrugBankiDB07863 2-chloro-5-nitro-N-phenylbenzamide
DB00459 Acitretin
DB00210 Adapalene
DB00523 Alitretinoin
DB00307 Bexarotene
DB00749 Etodolac
DB00926 Etretinate
DB08601 tributylstannanyl
GuidetoPHARMACOLOGYi610
SwissLipidsiSLP:000001552

Protein family/group databases

MoonDBiP19793 Predicted

PTM databases

iPTMnetiP19793
PhosphoSitePlusiP19793

Polymorphism and mutation databases

BioMutaiRXRA
DMDMi133701

Proteomic databases

EPDiP19793
jPOSTiP19793
MaxQBiP19793
PaxDbiP19793
PeptideAtlasiP19793
PRIDEiP19793
ProteomicsDBi53687

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
6256
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
6256
DisGeNETi6256
EuPathDBiHostDB:ENSG00000186350.9

GeneCards: human genes, protein and diseases

More...
GeneCardsi
RXRA
HGNCiHGNC:10477 RXRA
HPAiCAB004565
CAB005352
MIMi180245 gene
neXtProtiNX_P19793
OpenTargetsiENSG00000186350
PharmGKBiPA34890

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3575 Eukaryota
ENOG410XRZC LUCA
GeneTreeiENSGT00940000159789
HOVERGENiHBG005606
InParanoidiP19793
KOiK08524
OMAiLTCGMKR
OrthoDBi912470at2759
PhylomeDBiP19793
TreeFamiTF352097

Enzyme and pathway databases

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-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-4090294 SUMOylation of intracellular receptors
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

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
RXRA human
EvolutionaryTraceiP19793

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Retinoid_X_receptor_alpha

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
6256
PMAP-CutDBiP19793

Protein Ontology

More...
PROi
PR:P19793

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000186350 Expressed in 231 organ(s), highest expression level in liver
CleanExiHS_RXRA
ExpressionAtlasiP19793 baseline and differential
GenevisibleiP19793 HS

Family and domain databases

Gene3Di3.30.50.10, 1 hit
InterProiView protein in InterPro
IPR035500 NHR_like_dom_sf
IPR021780 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
PfamiView protein in Pfam
PF00104 Hormone_recep, 1 hit
PF11825 Nuc_recep-AF1, 1 hit
PF00105 zf-C4, 1 hit
PRINTSiPR00545 RETINOIDXR
PR00398 STRDHORMONER
PR00047 STROIDFINGER
SMARTiView protein in SMART
SM00430 HOLI, 1 hit
SM00399 ZnF_C4, 1 hit
SUPFAMiSSF48508 SSF48508, 1 hit
PROSITEiView protein in PROSITE
PS51843 NR_LBD, 1 hit
PS00031 NUCLEAR_REC_DBD_1, 1 hit
PS51030 NUCLEAR_REC_DBD_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRXRA_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P19793
Secondary accession number(s): B3KY83, Q2NL52, Q2V504
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: January 16, 2019
This is version 223 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  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. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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