P28702 (RXRB_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 138.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Retinoic acid receptor RXR-beta Alternative name(s): Nuclear receptor subfamily 2 group B member 2 Retinoid X receptor beta | ||||
| Gene names |
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| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 533 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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 | |
| Tissue specificity | Expressed in a variety of tumor cell lines. Ref.8 |
| 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. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| CACNA1B | Q00975 | 3 | EBI-748576,EBI-1055161 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 533 | 533 | Retinoic acid receptor RXR-beta | PRO_0000053572 | |||||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||||
| DNA binding | 205 – 270 | 66 | Nuclear receptor | ||||||||||||||||||||||||||||||||||||
| Zinc finger | 205 – 225 | 21 | NR C4-type | ||||||||||||||||||||||||||||||||||||
| Zinc finger | 241 – 265 | 25 | NR C4-type | ||||||||||||||||||||||||||||||||||||
| Region | 1 – 204 | 204 | Modulating By similarity | ||||||||||||||||||||||||||||||||||||
| Region | 271 – 330 | 60 | Hinge | ||||||||||||||||||||||||||||||||||||
| Region | 331 – 533 | 203 | Ligand-binding By similarity | ||||||||||||||||||||||||||||||||||||
| Compositional bias | 61 – 198 | 138 | Pro-rich | ||||||||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 112 | 1 | S → T in AAA60293. Ref.1 | ||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||
| Helix | 301 – 309 | 9 | |||||||||||||||||||||||||||||||||||||
| Helix | 336 – 347 | 12 | |||||||||||||||||||||||||||||||||||||
| Helix | 350 – 355 | 6 | |||||||||||||||||||||||||||||||||||||
| Helix | 360 – 362 | 3 | |||||||||||||||||||||||||||||||||||||
| Helix | 365 – 387 | 23 | |||||||||||||||||||||||||||||||||||||
| Turn | 388 – 390 | 3 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 394 – 396 | 3 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 402 – 404 | 3 | |||||||||||||||||||||||||||||||||||||
| Helix | 405 – 411 | 7 | |||||||||||||||||||||||||||||||||||||
| Helix | 414 – 423 | 10 | |||||||||||||||||||||||||||||||||||||
| Helix | 425 – 431 | 7 | |||||||||||||||||||||||||||||||||||||
| Helix | 435 – 446 | 12 | |||||||||||||||||||||||||||||||||||||
| Helix | 457 – 478 | 22 | |||||||||||||||||||||||||||||||||||||
| Helix | 485 – 490 | 6 | |||||||||||||||||||||||||||||||||||||
| Helix | 493 – 513 | 21 | |||||||||||||||||||||||||||||||||||||
| Helix | 517 – 521 | 5 | |||||||||||||||||||||||||||||||||||||
Sequences
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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: 1310259] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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: 1330328] [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: 1315958] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [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] | "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]. |
| [6] | "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. Beck S.Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [7] | "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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain. |
| [8] | "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: 8381386] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 161-331, TISSUE SPECIFICITY. |
| [9] | "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: 11782480] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 299-522 IN COMPLEX WITH THE RXR-SPECIFIC AGONIST LG100268. |
| [10] | "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: 12970175] [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. AL031228 Genomic DNA. Translation: CAA20239.1. BC001167 mRNA. Translation: AAH01167.1. X66424 mRNA. No translation available. | ||||||||||||||||||
| IPI | IPI00426305. | ||||||||||||||||||
| PIR | S37781. | ||||||||||||||||||
| RefSeq | NP_068811.1. NM_021976.3. | ||||||||||||||||||
| UniGene | Hs.388034. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P28702. | ||||||||||||||||||
| SMR | P28702. Positions 202-532. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| IntAct | P28702. 30 interactions. | ||||||||||||||||||
| MINT | MINT-1365658. | ||||||||||||||||||
| STRING | P28702. | ||||||||||||||||||
PTM databases | |||||||||||||||||||
| PhosphoSite | P28702. | ||||||||||||||||||
Polymorphism databases | |||||||||||||||||||
| DMDM | 1350911. | ||||||||||||||||||
Proteomic databases | |||||||||||||||||||
| PRIDE | P28702. | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| Ensembl | ENST00000374680; ENSP00000363812; ENSG00000204231. ENST00000383217; ENSP00000372704; ENSG00000206289. ENST00000415157; ENSP00000402506; ENSG00000228333. ENST00000415909; ENSP00000410468; ENSG00000235712. ENST00000431820; ENSP00000411238; ENSG00000231321. ENST00000436753; ENSP00000415199; ENSG00000227322. | ||||||||||||||||||
| GeneID | 6257. | ||||||||||||||||||
| KEGG | hsa:6257. | ||||||||||||||||||
| UCSC | uc003odb.1. human. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| CTD | 6257. | ||||||||||||||||||
| GeneCards | GC06M033161. | ||||||||||||||||||
| HGNC | HGNC:10478. RXRB. | ||||||||||||||||||
| HPA | CAB002003. | ||||||||||||||||||
| MIM | 180246. gene. | ||||||||||||||||||
| neXtProt | NX_P28702. | ||||||||||||||||||
| PharmGKB | PA34891. | ||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| eggNOG | maNOG14823. | ||||||||||||||||||
| HOVERGEN | HBG005606. | ||||||||||||||||||
| OrthoDB | EOG4SJ5DV. | ||||||||||||||||||
| PhylomeDB | P28702. | ||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||
| Pathway_Interaction_DB | a6b1_a6b4_integrin_pathway. a6b1 and a6b4 Integrin signaling. ar_tf_pathway. Regulation of Androgen receptor activity. retinoic_acid_pathway. Retinoic acid receptors-mediated signaling. rxr_vdr_pathway. RXR and RAR hetrodimerization with other nuclear receptor. | ||||||||||||||||||
| Reactome | REACT_71. Gene Expression. | ||||||||||||||||||
Gene expression databases | |||||||||||||||||||
| CleanEx | HS_RXRB. | ||||||||||||||||||
| Genevestigator | P28702. | ||||||||||||||||||
| GermOnline | ENSG00000204231. Homo sapiens. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR008946. Nucl_hormone_rcpt_ligand-bd. IPR000536. Nucl_hrmn_rcpt_lig-bd_core. IPR000003. Retinoid-X_rcpt. IPR001723. Str_hrmn_rcpt. IPR001628. Znf_hrmn_rcpt. IPR013088. Znf_NHR/GATA. [Graphical view] | ||||||||||||||||||
| Gene3D | G3DSA:1.10.565.10. Nucl_hrmn_rcpt_lig_bd. 1 hit. G3DSA:3.30.50.10. Znf_NHR/GATA. 1 hit. | ||||||||||||||||||
| KO | K08525. | ||||||||||||||||||
| Pfam | PF00104. Hormone_recep. 1 hit. PF00105. zf-C4. 1 hit. [Graphical view] | ||||||||||||||||||
| PRINTS | PR00545. RETINOIDXR. PR00398. STRDHORMONER. PR00047. STROIDFINGER. | ||||||||||||||||||
| SMART | SM00430. HOLI. 1 hit. SM00399. ZnF_C4. 1 hit. [Graphical view] | ||||||||||||||||||
| SUPFAM | SSF48508. Str_ncl_receptor. 1 hit. | ||||||||||||||||||
| PROSITE | PS00031. NUCLEAR_REC_DBD_1. 1 hit. PS51030. NUCLEAR_REC_DBD_2. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other | |||||||||||||||||||
| DrugBank | DB00459. Acitretin. DB00210. Adapalene. DB00523. Alitretinoin. DB00307. Bexarotene. DB00926. Etretinate. DB00799. Tazarotene. DB00755. Tretinoin. | ||||||||||||||||||
| NextBio | 24299. | ||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||
Entry information
| Entry name | RXRB_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P28702 Secondary accession number(s): P28703 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any 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
| Human chromosome 6 Human chromosome 6: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with