Retinoid X receptor beta

mammalian protein found in Mus musculus
Protein protein Q21990071
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Retinoid X receptor beta

Summary

Retinoid X receptor beta is a protein[1].

Key Facts

  • Retinoid X receptor beta's instance of is recorded as protein[2].
  • Retinoid X receptor beta's subclass of is recorded as protein[3].
  • Retinoid X receptor beta's UniProt protein ID is recorded as P28704[4].
  • Retinoid X receptor beta's part of is recorded as Retinoid X receptor/HNF4[5].
  • Retinoid X receptor beta's part of is recorded as Zinc finger, NHR/GATA-type[6].
  • Retinoid X receptor beta's part of is recorded as Nuclear hormone receptor-like domain superfamily[7].
  • Retinoid X receptor beta's part of is recorded as Nuclear hormone receptor, ligand-binding domain, protein family[8].
  • Retinoid X receptor beta's part of is recorded as Zinc finger, nuclear hormone receptor-type, protein family[9].
  • Retinoid X receptor beta's has part is recorded as Nuclear hormone receptor, ligand-binding domain[10].
  • Retinoid X receptor beta's has part is recorded as nuclear hormone receptor-type zinc finger[11].
  • Retinoid X receptor beta's RefSeq protein ID is recorded as NP_001192143[12].
  • Retinoid X receptor beta's RefSeq protein ID is recorded as NP_001192144[13].
  • Retinoid X receptor beta's RefSeq protein ID is recorded as NP_001192145[14].
  • Retinoid X receptor beta's RefSeq protein ID is recorded as NP_035436[15].
  • Retinoid X receptor beta's molecular function is recorded as RNA polymerase II cis-regulatory region sequence-specific DNA binding[16].
  • Retinoid X receptor beta's molecular function is recorded as DNA binding[17].
  • Retinoid X receptor beta's molecular function is recorded as sequence-specific DNA binding[18].
  • Retinoid X receptor beta's molecular function is recorded as protein homodimerization activity[19].
  • Retinoid X receptor beta's molecular function is recorded as DNA-binding transcription factor activity[20].
  • Retinoid X receptor beta's molecular function is recorded as zinc ion binding[21].
  • Retinoid X receptor beta's molecular function is recorded as metal ion binding[22].
  • Retinoid X receptor beta's molecular function is recorded as steroid hormone receptor activity[23].
  • Retinoid X receptor beta's molecular function is recorded as protein binding[24].
  • Retinoid X receptor beta's molecular function is recorded as RNA polymerase II transcription regulatory region sequence-specific DNA binding[25].
  • Retinoid X receptor beta's molecular function is recorded as DNA-binding transcription activator activity, RNA polymerase II-specific[26].

References

Programmatic citations — every numbered marker resolves to a verifiable graph row below.

Direct Wikidata claims

  1. [2] . Q905695. Retrieved . wikidata.org.
  2. [3] . Q905695. Retrieved . wikidata.org.
  3. [4] . Q905695. Retrieved . wikidata.org.
  4. [5] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  5. [6] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  6. [7] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  7. [8] . wikidata.org.
  8. [9] . wikidata.org.
  9. [10] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  10. [11] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  11. [12] . Q20641742. Retrieved . wikidata.org.
  12. [13] . Q20641742. Retrieved . wikidata.org.
  13. [14] . Q20641742. Retrieved . wikidata.org.
  14. [15] . Q20641742. Retrieved . wikidata.org.
  15. [16] . H-2RIIBP, a member of the nuclear hormone receptor superfamily that binds to both the regulatory element of major histocompatibility class I genes and the estrogen response element. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] . A dynamic balance between ARP-1/COUP-TFII, EAR-3/COUP-TFI, and retinoic acid receptor:retinoid X receptor heterodimers regulates Oct-3/4 expression in embryonal carcinoma cells. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] . Cooperative formation of high-order oligomers by retinoid X receptors: an unexpected mode of DNA recognition. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] . Characterization of receptor-interacting protein 140 in retinoid receptor activities. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

  1. [1] . Wikidata. wikidata.org.

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Use these citations when quoting this entity in research, articles, AI prompts, or wherever provenance matters. We aggregate Wikidata + Wikipedia + authoritative open-data sources; the stitched, scored, cross-referenced view is what 4ort.xyz contributes.

APA 4ort.xyz Knowledge Graph. (2026). Retinoid X receptor beta. Retrieved May 3, 2026, from https://4ort.xyz/entity/retinoid-x-receptor-beta-q21990071
MLA “Retinoid X receptor beta.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/retinoid-x-receptor-beta-q21990071.
BibTeX @misc{4ortxyz_retinoid-x-receptor-beta-q21990071_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Retinoid X receptor beta}}, year = {2026}, url = {https://4ort.xyz/entity/retinoid-x-receptor-beta-q21990071}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Retinoid X receptor beta — https://4ort.xyz/entity/retinoid-x-receptor-beta-q21990071 (retrieved 2026-05-03)

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