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Protein

Retinoic acid receptor RXR-alpha

Gene

Rxra

Organism
Mus musculus (Mouse)
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.3 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 bindingi140 – 205Nuclear 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 fingeri140 – 160NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri176 – 200NR 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 processTranscription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-159418 Recycling of bile acids and salts
R-MMU-192105 Synthesis of bile acids and bile salts
R-MMU-193368 Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol
R-MMU-193807 Synthesis of bile acids and bile salts via 27-hydroxycholesterol
R-MMU-200425 Import of palmitoyl-CoA into the mitochondrial matrix
R-MMU-204174 Regulation of pyruvate dehydrogenase (PDH) complex
R-MMU-211976 Endogenous sterols
R-MMU-381340 Transcriptional regulation of white adipocyte differentiation
R-MMU-383280 Nuclear Receptor transcription pathway
R-MMU-400206 Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha)
R-MMU-4090294 SUMOylation of intracellular receptors
R-MMU-5362517 Signaling by Retinoic Acid

<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 2

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:98214 Rxra

<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>Mutagenesisi22S → A: Loss of constituitive phosphorylation. No effect on RXRA transcriptional activity. 2 Publications1
Mutagenesisi44S → A: No effect on constituitive phosphorylation. 1 Publication1
Mutagenesisi48S → A: No effect on constituitive phosphorylation. 1 Publication1
Mutagenesisi54S → A: No effect on constituitive phosphorylation. 1 Publication1
Mutagenesisi61S → A: No effect on constituitive phosphorylation, decreased stress-induced phosphorylation but no effect on RXRA transcriptional activity. Abolishes stress-induced phosphorylation but no effect on RXRA transcriptional activity; when associated with A-75 and A-87. No effect on RXRA transcriptional activity. 1 Publication1
Mutagenesisi75S → A: No effect on constituitive phosphorylation, decreased stress-induced phosphorylation but no effect on RXRA transcriptional activity. Abolishes stress-induced phosphorylation but no effect on RXRA transcriptional activity; when associated with A-61 and A-87. 1 Publication1
Mutagenesisi87T → A: No effect on constituitive phosphorylation, decreased stress-induced phosphorylation but no effect on RXRA transcriptional activity. Abolishes stress-induced phosphorylation but no effect on RXRA transcriptional activity; when associated with A-61 and A-75. phosphorylation. No effect on RXRA transcriptional activity. 1 Publication1
Mutagenesisi96S → A: No effect on constituitive phosphorylation. 1 Publication1
Mutagenesisi101S → A: No effect on constituitive phosphorylation. 1 Publication1
Mutagenesisi265S → A: No effect on constiuitive phosphorylation but loss of stress-induced phosphorylation. No effect on RXRA transcriptional activity. 1 Publication1
Mutagenesisi455 – 456FL → AA: Abolishes interaction with ASXL1 and NCOA1. 1 Publication2
Mutagenesisi459 – 460ML → AA: Abolishes interaction with ASXL1 and NCOA1. 1 Publication2

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3084

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
610

<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_00000535671 – 467Retinoic acid receptor RXR-alphaAdd BLAST467

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)By similarity
<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 residuei22PhosphoserineCombined sources2 Publications1
Modified residuei28PhosphoserineBy similarity1
Modified residuei61Phosphoserine; by MAPK8 and MAPK91 Publication1
Modified residuei75Phosphoserine; by MAPK8 and MAPK91 Publication1
Modified residuei87Phosphothreonine; by MAPK8 and MAPK91 Publication1
Cross-linki113Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei134PhosphoserineBy similarity1
Modified residuei264PhosphoserineBy similarity1
Modified residuei265Phosphoserine; by MAPK8 and MAPK91 Publication1

<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. Phosphorylated on Ser-28, in vitro, by PKA. This phosphorylation is required for repression of cAMP-mediated transcriptional activity of RARA (By similarity). Constiutively phosphorylated on Ser-22 in the presence or absence of ligand. Under stress conditions, hyperphosphorylated by activated JNK on Ser-61, Ser-75, Thr-87 and Ser-265.By similarity2 Publications
Sumoylation negatively regulates transcriptional activity. Desumoylated specifically by SENP6 (By similarity).By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P28700

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

More...
PaxDbi
P28700

PRoteomics IDEntifications database

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PRIDEi
P28700

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P28700

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

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PhosphoSitePlusi
P28700

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000015846 Expressed in 296 organ(s), highest expression level in head

CleanEx database of gene expression profiles

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CleanExi
MM_RXRA

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P28700 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P28700 MM

<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 (By similarity). 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 (By similarity). Interacts with coactivator NCOA3, PELP1, SENP6, SFPQ, DNTTIP2 and RNF8. Interacts with PRMT2. Interacts with BHLHE40/DEC1, BHLHE41/DEC2, NCOR1 and NCOR2. Interacts in a ligand-dependent fashion with MED1 (By similarity). Interacts with coactivator NCOA6, and FAM120B. Interacts with ASXL1. Interacts in a ligand-dependent fashion with NCOA1. Interacts with VDR (By similarity).By similarity6 Publications

<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
203038, 16 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-505 Rxralpha-Pxr retinoic acid receptor complex
CPX-584 RXRalpha-RARalpha retinoic acid receptor complex
CPX-672 RXRalpha-RXRalpha retinoic acid receptor complex
CPX-673 RXRalpha-VDR nuclear hormone receptor complex
CPX-679 RXRalpha-LXRbeta nuclear hormone receptor complex
CPX-708 RXRalpha-LXRalpha nuclear hormone receptor complex
CPX-710 RXRalpha-TRbeta nuclear hormone receptor complex
CPX-713 RXRalpha-TRalpha nuclear hormone receptor complex
CPX-818 RXRalpha-RARalpha-NCOA2 retinoic acid receptor complex

Protein interaction database and analysis system

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IntActi
P28700, 18 interactors

Molecular INTeraction database

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MINTi
P28700

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000076491

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P28700

<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

1467
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P28700

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

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SMRi
P28700

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P28700

<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>Domaini232 – 463NR 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 – 139Modulating domainBy similarityAdd BLAST139
Regioni206 – 229HingeAdd 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 or AF1 domain, a DNA-binding domain and a C-terminal ligand-binding or 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 fingeri140 – 160NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri176 – 200NR C4-typePROSITE-ProRule annotationAdd BLAST25

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3575 Eukaryota
ENOG410XRZC LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000159789

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000260821

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG005606

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P28700

KEGG Orthology (KO)

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KOi
K08524

Database of Orthologous Groups

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OrthoDBi
EOG091G0YX6

Database for complete collections of gene phylogenies

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PhylomeDBi
P28700

TreeFam database of animal gene trees

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TreeFami
TF352097

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.50.10, 1 hit

Integrated resource of protein families, domains and functional sites

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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

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PRINTSi
PR00545 RETINOIDXR
PR00398 STRDHORMONER
PR00047 STROIDFINGER

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48508 SSF48508, 1 hit

PROSITE; a protein domain and family database

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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>Sequence (1+)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 has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P28700-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDTKHFLPLD FSTQVNSSSL NSPTGRGSMA VPSLHPSLGP GIGSPLGSPG
60 70 80 90 100
QLHSPISTLS SPINGMGPPF SVISSPMGPH SMSVPTTPTL GFGTGSPQLN
110 120 130 140 150
SPMNPVSSTE DIKPPLGLNG VLKVPAHPSG NMASFTKHIC AICGDRSSGK
160 170 180 190 200
HYGVYSCEGC KGFFKRTVRK DLTYTCRDNK DCLIDKRQRN RCQYCRYQKC
210 220 230 240 250
LAMGMKREAV QEERQRGKDR NENEVESTSS ANEDMPVEKI LEAELAVEPK
260 270 280 290 300
TETYVEANMG LNPSSPNDPV TNICQAADKQ LFTLVEWAKR IPHFSELPLD
310 320 330 340 350
DQVILLRAGW NELLIASFSH RSIAVKDGIL LATGLHVHRN SAHSAGVGAI
360 370 380 390 400
FDRVLTELVS KMRDMQMDKT ELGCLRAIVL FNPDSKGLSN PAEVEALREK
410 420 430 440 450
VYASLEAYCK HKYPEQPGRF AKLLLRLPAL RSIGLKCLEH LFFFKLIGDT
460
PIDTFLMEML EAPHQAT
Length:467
Mass (Da):51,217
Last modified:December 1, 1992 - 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:i0AF62396BCDC87DB
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 are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q6LC96Q6LC96_MOUSE
RXR alpha 2
Rxra RXR alpha
439Annotation score:

Annotation score:2 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>
A2AJP2A2AJP2_MOUSE
Retinoic acid receptor RXR-alpha
Rxra
165Annotation 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>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M84817 mRNA Translation: AAA40080.1
X66223 mRNA Translation: CAA46962.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS15830.1

Protein sequence database of the Protein Information Resource

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PIRi
S26668

NCBI Reference Sequences

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RefSeqi
NP_035435.1, NM_011305.3

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.24624

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000077257; ENSMUSP00000076491; ENSMUSG00000015846
ENSMUST00000166775; ENSMUSP00000133044; ENSMUSG00000015846

Database of genes from NCBI RefSeq genomes

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GeneIDi
20181

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:20181

UCSC genome browser

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UCSCi
uc008ixs.1 mouse

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84817 mRNA Translation: AAA40080.1
X66223 mRNA Translation: CAA46962.1
CCDSiCCDS15830.1
PIRiS26668
RefSeqiNP_035435.1, NM_011305.3
UniGeneiMm.24624

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
1DKFX-ray2.50A230-462[»]
1XDKX-ray2.90A/E230-467[»]
3A9EX-ray2.75A228-467[»]
ProteinModelPortaliP28700
SMRiP28700
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203038, 16 interactors
ComplexPortaliCPX-505 Rxralpha-Pxr retinoic acid receptor complex
CPX-584 RXRalpha-RARalpha retinoic acid receptor complex
CPX-672 RXRalpha-RXRalpha retinoic acid receptor complex
CPX-673 RXRalpha-VDR nuclear hormone receptor complex
CPX-679 RXRalpha-LXRbeta nuclear hormone receptor complex
CPX-708 RXRalpha-LXRalpha nuclear hormone receptor complex
CPX-710 RXRalpha-TRbeta nuclear hormone receptor complex
CPX-713 RXRalpha-TRalpha nuclear hormone receptor complex
CPX-818 RXRalpha-RARalpha-NCOA2 retinoic acid receptor complex
IntActiP28700, 18 interactors
MINTiP28700
STRINGi10090.ENSMUSP00000076491

Chemistry databases

BindingDBiP28700
ChEMBLiCHEMBL3084
GuidetoPHARMACOLOGYi610

PTM databases

iPTMnetiP28700
PhosphoSitePlusiP28700

Proteomic databases

MaxQBiP28700
PaxDbiP28700
PRIDEiP28700

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000077257; ENSMUSP00000076491; ENSMUSG00000015846
ENSMUST00000166775; ENSMUSP00000133044; ENSMUSG00000015846
GeneIDi20181
KEGGimmu:20181
UCSCiuc008ixs.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
6256
MGIiMGI:98214 Rxra

Phylogenomic databases

eggNOGiKOG3575 Eukaryota
ENOG410XRZC LUCA
GeneTreeiENSGT00940000159789
HOGENOMiHOG000260821
HOVERGENiHBG005606
InParanoidiP28700
KOiK08524
OrthoDBiEOG091G0YX6
PhylomeDBiP28700
TreeFamiTF352097

Enzyme and pathway databases

ReactomeiR-MMU-159418 Recycling of bile acids and salts
R-MMU-192105 Synthesis of bile acids and bile salts
R-MMU-193368 Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol
R-MMU-193807 Synthesis of bile acids and bile salts via 27-hydroxycholesterol
R-MMU-200425 Import of palmitoyl-CoA into the mitochondrial matrix
R-MMU-204174 Regulation of pyruvate dehydrogenase (PDH) complex
R-MMU-211976 Endogenous sterols
R-MMU-381340 Transcriptional regulation of white adipocyte differentiation
R-MMU-383280 Nuclear Receptor transcription pathway
R-MMU-400206 Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha)
R-MMU-4090294 SUMOylation of intracellular receptors
R-MMU-5362517 Signaling by Retinoic Acid

Miscellaneous databases

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

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ChiTaRSi
Rxra mouse
EvolutionaryTraceiP28700

Protein Ontology

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PROi
PR:P28700

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSMUSG00000015846 Expressed in 296 organ(s), highest expression level in head
CleanExiMM_RXRA
ExpressionAtlasiP28700 baseline and differential
GenevisibleiP28700 MM

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

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ProtoNeti
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<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_MOUSE
<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: P28700
<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: December 1, 1992
Last sequence update: December 1, 1992
Last modified: December 5, 2018
This is version 193 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

<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, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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