Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P28702 (RXRB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Retinoic acid receptor RXR-beta
Alternative name(s):
Nuclear receptor subfamily 2 group B member 2
Retinoid X receptor beta
Gene names
Name:RXRB
Synonyms:NR2B2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length533 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 By similarity. Specifically binds 9-cis retinoic acid (9C-RA).

Subunit structure

Homodimer By similarity. Heterodimer with a RAR molecule. Binds DNA preferentially as a RAR/RXR heterodimer. Ref.1

Subcellular location

Nucleus.

Tissue specificity

Expressed in a variety of tumor cell lines. Ref.10

Domain

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

Sequence similarities

Belongs to the nuclear hormone receptor family. NR2 subfamily.

Contains 1 nuclear receptor DNA-binding domain.

Sequence caution

The sequence BAD92481.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionReceptor
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcardiac muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

cellular response to retinoic acid

Inferred from electronic annotation. Source: Ensembl

gene expression

Traceable author statement. Source: Reactome

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

maternal placenta development

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

ventricular cardiac muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentnucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 7990953. Source: HGNC

   Molecular_function9-cis retinoic acid receptor activity

Traceable author statement PubMed 1662118. Source: ProtInc

ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from direct assay PubMed 7990953. Source: BHF-UCL

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding transcription factor activity

Non-traceable author statement PubMed 1662118. Source: ProtInc

steroid hormone receptor activity

Inferred from electronic annotation. Source: InterPro

transcription coactivator activity

Traceable author statement PubMed 1662118. Source: ProtInc

transcription regulatory region DNA binding

Inferred from electronic annotation. Source: Ensembl

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CACNA1BQ009753EBI-748576,EBI-1055161

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P28702-1)

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.
Isoform 2 (identifier: P28702-3)

The sequence of this isoform differs from the canonical sequence as follows:
     418-418: D → DRSLS

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 533533Retinoic acid receptor RXR-beta
PRO_0000053572

Regions

DNA binding205 – 27066Nuclear receptor
Zinc finger205 – 22521NR C4-type
Zinc finger241 – 26525NR C4-type
Region1 – 204204Modulating By similarity
Region271 – 33060Hinge
Region331 – 533203Ligand-binding By similarity
Compositional bias61 – 198138Pro-rich

Natural variations

Alternative sequence4181D → DRSLS in isoform 2.
VSP_045587

Experimental info

Sequence conflict1121S → T in AAA60293. Ref.1

Secondary structure

............................... 533
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: D0069FE93AC16A04

FASTA53356,922
        10         20         30         40         50         60 
MSWAARPPFL PQRHAAGQCG PVGVRKEMHC GVASRWRRRR PWLDPAAAAA AAVAGGEQQT 

        70         80         90        100        110        120 
PEPEPGEAGR DGMGDSGRDS RSPDSSSPNP LPQGVPPPSP PGPPLPPSTA PSLGGSGAPP 

       130        140        150        160        170        180 
PPPMPPPPLG SPFPVISSSM GSPGLPPPAP PGFSGPVSSP QINSTVSLPG GGSGPPEDVK 

       190        200        210        220        230        240 
PPVLGVRGLH CPPPPGGPGA GKRLCAICGD RSSGKHYGVY SCEGCKGFFK RTIRKDLTYS 

       250        260        270        280        290        300 
CRDNKDCTVD KRQRNRCQYC RYQKCLATGM KREAVQEERQ RGKDKDGDGE GAGGAPEEMP 

       310        320        330        340        350        360 
VDRILEAELA VEQKSDQGVE GPGGTGGSGS SPNDPVTNIC QAADKQLFTL VEWAKRIPHF 

       370        380        390        400        410        420 
SSLPLDDQVI LLRAGWNELL IASFSHRSID VRDGILLATG LHVHRNSAHS AGVGAIFDRV 

       430        440        450        460        470        480 
LTELVSKMRD MRMDKTELGC LRAIILFNPD AKGLSNPSEV EVLREKVYAS LETYCKQKYP 

       490        500        510        520        530 
EQQGRFAKLL LRLPALRSIG LKCLEHLFFF KLIGDTPIDT FLMEMLEAPH QLA 

« Hide

Isoform 2 [UniParc].

Checksum: E6789FB00428DA2C
Show »

FASTA53757,365

References

« Hide 'large scale' references
[1]"Purification, cloning, and RXR identity of the HeLa cell factor with which RAR or TR heterodimerizes to bind target sequences efficiently."
Leid M., Kastner P., Lyons R., Nakshatri H., Saunders M., Zacharewsi T., Chen J.Y., Staub A., Garnier J.-M., Mader S., Chambon P.
Cell 68:377-395(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), HETERODIMERIZATION.
Tissue: Mammary carcinoma.
[2]Erratum
Leid M., Kastner P., Lyons R., Nakshatri H., Saunders M., Zacharewsi T., Chen J.Y., Staub A., Garnier J.-M., Mader S., Chambon P.
Cell 71:887-887(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[3]"Isolation of a full-length cDNA clone encoding a N-terminally variant form of the human retinoid X receptor beta."
Fleischhauer K., Park J.H., Disanto J.P., Marks M.S., Ozato K., Yang S.Y.
Nucleic Acids Res. 20:1801-1801(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]Numasawa T., Koga H., Ueyama K., Maeda S., Sakou T., Harata S., Leppert M., Inoue I.
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Isolation of cDNA coding for putatively new variants of multiple human nuclear receptors."
Kaighin V.A., Martin A.L., Aronstam R.S.
Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Liver.
[6]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[7]"Molecular cloning and characterization of the human HRXRB gene and 5' flanking region."
Corella A., Vergara A., Paez G., de Miguel C., Encio I.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[10]"Cloning and chromosome mapping of human retinoid X receptor beta: selective amino acid sequence conservation of a nuclear hormone receptor in mammals."
Fleischhauer K., McBride O.W., DiSanto J.P., Ozato K., Yang S.Y.
Hum. Genet. 90:505-510(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 161-331 (ISOFORM 1), TISSUE SPECIFICITY.
[11]"The structural basis for the specificity of retinoid-X receptor-selective agonists: new insights into the role of helix H12."
Love J.D., Gooch J.T., Benko S., Li C., Nagy L., Chatterjee V.K., Evans R.M., Schwabe J.W.
J. Biol. Chem. 277:11385-11391(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 299-522 IN COMPLEX WITH THE RXR-SPECIFIC AGONIST LG100268.
[12]"Crystal structure of the heterodimeric complex of LXRalpha and RXRbeta ligand-binding domains in a fully agonistic conformation."
Svensson S., Ostberg T., Jacobsson M., Norstrom C., Stefansson K., Hallen D., Johansson I.C., Zachrisson K., Ogg D., Jendeberg L.
EMBO J. 22:4625-4633(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 298-533 IN COMPLEX WITH NR1H3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M84820 mRNA. Translation: AAA60293.1.
X63522 mRNA. Translation: CAA45087.1.
AF065396 Genomic DNA. Translation: AAC18599.1.
AF120161 Genomic DNA. Translation: AAD13794.1.
HQ709179 mRNA. Translation: ADZ17386.1.
AB209244 mRNA. Translation: BAD92481.1. Different initiation.
AL031228 Genomic DNA. Translation: CAA20239.1.
AL844527 Genomic DNA. Translation: CAI41836.2.
CR936877 Genomic DNA. Translation: CAQ09065.1.
CR759733 Genomic DNA. Translation: CAQ10299.1.
CR354565 Genomic DNA. Translation: CAQ11083.1.
AL645940 Genomic DNA. No translation available.
AL662824 Genomic DNA. No translation available.
BC001167 mRNA. Translation: AAH01167.1.
X66424 mRNA. No translation available.
PIRS37781.
RefSeqNP_001257330.1. NM_001270401.1.
NP_068811.1. NM_021976.4.
UniGeneHs.388034.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H9UX-ray2.70A/B/C/D299-522[»]
1UHLX-ray2.90A298-533[»]
ProteinModelPortalP28702.
SMRP28702. Positions 202-532.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112169. 29 interactions.
IntActP28702. 31 interactions.
MINTMINT-1365658.
STRING9606.ENSP00000363812.

Chemistry

BindingDBP28702.
ChEMBLCHEMBL2363071.
DrugBankDB00459. Acitretin.
DB00210. Adapalene.
DB00523. Alitretinoin.
DB00307. Bexarotene.
DB00926. Etretinate.
DB00799. Tazarotene.
DB00755. Tretinoin.
GuidetoPHARMACOLOGY611.

PTM databases

PhosphoSiteP28702.

Polymorphism databases

DMDM1350911.

Proteomic databases

PaxDbP28702.
PRIDEP28702.

Protocols and materials databases

DNASU6257.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374680; ENSP00000363812; ENSG00000204231. [P28702-1]
ENST00000374685; ENSP00000363817; ENSG00000204231. [P28702-3]
ENST00000383216; ENSP00000372703; ENSG00000206289. [P28702-3]
ENST00000383217; ENSP00000372704; ENSG00000206289. [P28702-1]
ENST00000415157; ENSP00000402506; ENSG00000228333. [P28702-1]
ENST00000415909; ENSP00000410468; ENSG00000235712. [P28702-1]
ENST00000431161; ENSP00000393286; ENSG00000235712. [P28702-3]
ENST00000431820; ENSP00000411238; ENSG00000231321. [P28702-1]
ENST00000436753; ENSP00000415199; ENSG00000227322. [P28702-1]
ENST00000443603; ENSP00000402590; ENSG00000227322. [P28702-3]
ENST00000455462; ENSP00000400104; ENSG00000228333. [P28702-3]
ENST00000456244; ENSP00000393870; ENSG00000231321. [P28702-3]
GeneID6257.
KEGGhsa:6257.
UCSCuc003odb.4. human. [P28702-1]
uc003odc.4. human.

Organism-specific databases

CTD6257.
GeneCardsGC06M033161.
GC06Mj33082.
GC06Mk33139.
GC06Ml33315.
GC06Mm33331.
GC06Mn33090.
HGNCHGNC:10478. RXRB.
HPACAB002003.
MIM180246. gene.
neXtProtNX_P28702.
PharmGKBPA34891.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG327099.
HOGENOMHOG000260821.
HOVERGENHBG005606.
KOK08525.
OMAFLPERHA.
PhylomeDBP28702.
TreeFamTF352097.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.
SignaLinkP28702.

Gene expression databases

ArrayExpressP28702.
BgeeP28702.
CleanExHS_RXRB.
GenevestigatorP28702.

Family and domain databases

Gene3D1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProIPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR000003. Retinoid-X_rcpt/HNF4.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSPR00545. RETINOIDXR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. SSF48508. 1 hit.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRXRB. human.
EvolutionaryTraceP28702.
GeneWikiRetinoid_X_receptor_beta.
GenomeRNAi6257.
NextBio24299.
PROP28702.
SOURCESearch...

Entry information

Entry nameRXRB_HUMAN
AccessionPrimary (citable) accession number: P28702
Secondary accession number(s): P28703 expand/collapse secondary AC list , Q59G65, Q5JP92, Q5STQ1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM