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P48443 (RXRG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 145. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Retinoic acid receptor RXR-gamma
Alternative name(s):
Nuclear receptor subfamily 2 group B member 3
Retinoid X receptor gamma
Gene names
Name:RXRG
Synonyms:NR2B3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length463 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. The high affinity ligand for RXRs is 9-cis retinoic acid By similarity.

Subunit structure

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

Subcellular location

Nucleus By similarity.

Domain

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

Sequence similarities

Belongs to the nuclear hormone receptor family. NR2 subfamily.

Contains 1 nuclear receptor DNA-binding domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionReceptor
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processgene expression

Traceable author statement. Source: Reactome

heart development

Inferred from electronic annotation. Source: Ensembl

neuron differentiation

Inferred from electronic annotation. Source: Ensembl

peripheral nervous system development

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

regulation of myelination

Inferred from electronic annotation. Source: Ensembl

response to retinoic acid

Inferred from electronic annotation. Source: Ensembl

skeletal muscle tissue development

Inferred from electronic annotation. Source: Ensembl

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

   Cellular_componentnucleoplasm

Traceable author statement. Source: Reactome

   Molecular_function9-cis retinoic acid receptor activity

Traceable author statement PubMed 8034312. Source: ProtInc

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

steroid hormone receptor activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RARAP102763EBI-712405,EBI-413374

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 463463Retinoic acid receptor RXR-gamma
PRO_0000053576

Regions

DNA binding136 – 21176Nuclear receptor
Zinc finger139 – 15921NR C4-type
Zinc finger175 – 19925NR C4-type
Region1 – 138138Modulating By similarity
Region205 – 26056Hinge
Region261 – 463203Ligand-binding By similarity

Secondary structure

.......................... 463
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P48443 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: AED5C94BB62A3157

FASTA46350,871
        10         20         30         40         50         60 
MYGNYSHFMK FPAGYGGSPG HTGSTSMSPS AALSTGKPMD SHPSYTDTPV SAPRTLSAVG 

        70         80         90        100        110        120 
TPLNALGSPY RVITSAMGPP SGALAAPPGI NLVAPPSSQL NVVNSVSSSE DIKPLPGLPG 

       130        140        150        160        170        180 
IGNMNYPSTS PGSLVKHICA ICGDRSSGKH YGVYSCEGCK GFFKRTIRKD LIYTCRDNKD 

       190        200        210        220        230        240 
CLIDKRQRNR CQYCRYQKCL VMGMKREAVQ EERQRSRERA ESEAECATSG HEDMPVERIL 

       250        260        270        280        290        300 
EAELAVEPKT ESYGDMNMEN STNDPVTNIC HAADKQLFTL VEWAKRIPHF SDLTLEDQVI 

       310        320        330        340        350        360 
LLRAGWNELL IASFSHRSVS VQDGILLATG LHVHRSSAHS AGVGSIFDRV LTELVSKMKD 

       370        380        390        400        410        420 
MQMDKSELGC LRAIVLFNPD AKGLSNPSEV ETLREKVYAT LEAYTKQKYP EQPGRFAKLL 

       430        440        450        460 
LRLPALRSIG LKCLEHLFFF KLIGDTPIDT FLMEMLETPL QIT 

« Hide

References

« Hide 'large scale' references
[1]Cooke T.A., Allegretto E.A., Heyman R.A., Lamph W.W.
Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart.
[2]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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].
Tissue: Eye.
[6]"Human retinoic acid receptor Rxr-gamma ligand-binding domain."
Structural genomics consortium (SGC)
Submitted (APR-2006) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 227-463.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U38480 mRNA. Translation: AAA80681.1.
CR456705 mRNA. Translation: CAG32986.1.
AL160058 Genomic DNA. Translation: CAC00596.1.
CH471067 Genomic DNA. Translation: EAW90745.1.
BC012063 mRNA. Translation: AAH12063.1.
RefSeqNP_001243500.1. NM_001256571.1.
NP_008848.1. NM_006917.4.
UniGeneHs.26550.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GL8X-ray2.40A/B/C/D227-463[»]
ProteinModelPortalP48443.
SMRP48443. Positions 136-456.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112170. 26 interactions.
DIPDIP-56220N.
IntActP48443. 9 interactions.
MINTMINT-1378806.
STRING9606.ENSP00000352900.

Chemistry

BindingDBP48443.
ChEMBLCHEMBL2363070.
DrugBankDB00459. Acitretin.
DB00210. Adapalene.
DB00523. Alitretinoin.
DB00926. Etretinate.
DB00755. Tretinoin.
GuidetoPHARMACOLOGY612.

PTM databases

PhosphoSiteP48443.

Polymorphism databases

DMDM1350913.

Proteomic databases

PaxDbP48443.
PRIDEP48443.

Protocols and materials databases

DNASU6258.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359842; ENSP00000352900; ENSG00000143171.
GeneID6258.
KEGGhsa:6258.
UCSCuc001gda.3. human.

Organism-specific databases

CTD6258.
GeneCardsGC01M165370.
HGNCHGNC:10479. RXRG.
HPACAB002615.
MIM180247. gene.
neXtProtNX_P48443.
PharmGKBPA34892.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG327099.
HOGENOMHOG000260821.
HOVERGENHBG005606.
InParanoidP48443.
KOK08526.
OMACASGGHE.
OrthoDBEOG72RMZ5.
PhylomeDBP48443.
TreeFamTF352097.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.
SignaLinkP48443.

Gene expression databases

ArrayExpressP48443.
BgeeP48443.
CleanExHS_RXRG.
GenevestigatorP48443.

Family and domain databases

Gene3D1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProIPR021780. Nuc_recep-AF1.
IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR000003. Retinoid-X_rcpt/HNF4.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamPF00104. Hormone_recep. 1 hit.
PF11825. Nuc_recep-AF1. 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

EvolutionaryTraceP48443.
GeneWikiRetinoid_X_receptor_gamma.
GenomeRNAi6258.
NextBio24303.
PROP48443.
SOURCESearch...

Entry information

Entry nameRXRG_HUMAN
AccessionPrimary (citable) accession number: P48443
Secondary accession number(s): A6NIP1, Q6IBU7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 145 of the entry and version 1 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 1

Human chromosome 1: entries, gene names and cross-references to MIM