Histone deacetylase 4

mammalian protein found in Homo sapiens
Protein protein Q21173206
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Histone deacetylase 4

Summary

Histone deacetylase 4 is a protein[1]. It draws 14 Wikipedia views per month (protein category, ranking #153 of 987).[2]

Key Facts

  • Histone deacetylase 4's instance of is recorded as protein[3].
  • Histone deacetylase 4's physically interacts with is recorded as tasquinimod[4].
  • Histone deacetylase 4's physically interacts with is recorded as belinostat[5].
  • Histone deacetylase 4's physically interacts with is recorded as givinostat[6].
  • Histone deacetylase 4's physically interacts with is recorded as panobinostat[7].
  • Histone deacetylase 4's physically interacts with is recorded as quisinostat[8].
  • Histone deacetylase 4's physically interacts with is recorded as romidepsin[9].
  • Histone deacetylase 4's physically interacts with is recorded as trichostatin A[10].
  • Histone deacetylase 4 is a type of protein[11].
  • Histone deacetylase 4 is part of Histone deacetylase domain superfamily[12].
  • Histone deacetylase 4 is part of Ureohydrolase domain superfamily[13].
  • Histone deacetylase 4 is part of Histone deacetylase 4[14].
  • Histone deacetylase 4 is part of Histone deacetylase, glutamine rich N-terminal domain, protein family[15].
  • Histone deacetylase 4 is part of histone deacetylases[16].
  • Histone deacetylase 4 comprises Histone deacetylase domain[17].
  • Histone deacetylase 4 comprises Histone deacetylase, glutamine rich N-terminal domain[18].
  • Histone deacetylase 4's molecular function is recorded as NAD-dependent histone deacetylase activity (H3-K14 specific)[19].
  • Histone deacetylase 4's molecular function is recorded as sequence-specific DNA binding[20].
  • Histone deacetylase 4's molecular function is recorded as DNA binding[21].
  • Histone deacetylase 4's molecular function is recorded as transcription corepressor activity[22].
  • Histone deacetylase 4's molecular function is recorded as histone deacetylase activity[23].
  • Histone deacetylase 4's molecular function is recorded as zinc ion binding[24].
  • Histone deacetylase 4's molecular function is recorded as transcription factor binding[25].
  • Histone deacetylase 4's molecular function is recorded as histone deacetylase binding[26].
  • Histone deacetylase 4's molecular function is recorded as potassium ion binding[27].

Why It Matters

Histone deacetylase 4 draws 14 Wikipedia views per month (protein category, ranking #153 of 987).[2] It has Wikipedia articles in 8 language editions, a strong signal of global cultural recognition.[28] It is known by 3 alternative names across languages and contexts.[29]

References

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

Direct Wikidata claims

  1. [3] . Q905695. Retrieved . wikidata.org.
  2. [4] . IUPHAR/BPS Guide to PHARMACOLOGY. Retrieved . wikidata.org.
  3. [5] . IUPHAR/BPS Guide to PHARMACOLOGY. Retrieved . wikidata.org.
  4. [6] . IUPHAR/BPS Guide to PHARMACOLOGY. Retrieved . wikidata.org.
  5. [7] . IUPHAR/BPS Guide to PHARMACOLOGY. Retrieved . wikidata.org.
  6. [8] . IUPHAR/BPS Guide to PHARMACOLOGY. Retrieved . wikidata.org.
  7. [9] . IUPHAR/BPS Guide to PHARMACOLOGY. Retrieved . wikidata.org.
  8. [10] . IUPHAR/BPS Guide to PHARMACOLOGY. Retrieved . wikidata.org.
  9. [11] . Q905695. Retrieved . wikidata.org.
  10. [12] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  11. [13] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  12. [14] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  13. [15] . wikidata.org.
  14. [16] . wikidata.org.
  15. [17] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  16. [18] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  17. [19] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [20] . FOXP3 up-regulates p21 expression by site-specific inhibition of histone deacetylase 2/histone deacetylase 4 association to the locus. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [21] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [22] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [23] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [24] . Structural and functional analysis of the human HDAC4 catalytic domain reveals a regulatory structural zinc-binding domain. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [25] . HDAC4 represses p21(WAF1/Cip1) expression in human cancer cells through a Sp1-dependent, p53-independent mechanism. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [26] . The histone deacetylase 9 gene encodes multiple protein isoforms. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [27] . Structural and functional analysis of the human HDAC4 catalytic domain reveals a regulatory structural zinc-binding domain. Retrieved . ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

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

Aggregate / graph-position facts

  1. [2] . Wikimedia Foundation. dumps.wikimedia.org.
  2. [28] . Wikidata sitelinks. wikidata.org.
  3. [29] . Wikidata aliases. wikidata.org.

📑 Cite this page

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). Histone deacetylase 4. Retrieved May 3, 2026, from https://4ort.xyz/entity/histone-deacetylase-4
MLA “Histone deacetylase 4.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/histone-deacetylase-4.
BibTeX @misc{4ortxyz_histone-deacetylase-4_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Histone deacetylase 4}}, year = {2026}, url = {https://4ort.xyz/entity/histone-deacetylase-4}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Histone deacetylase 4 — https://4ort.xyz/entity/histone-deacetylase-4 (retrieved 2026-05-03)

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Edit History

Rolling log of changes to this entity's Wikidata record. Values shown reflect the current state of each edited property — follow the history link to see the precise diff for any edit.

  1. 9h ago · Boghog · 2026-07-24 view diff on Wikidata ↗
    Subclass of protein
    Found in taxon Homo sapiens
    Physically interacts with tasquinimod, belinostat, givinostat +4
    Instance of
    + 12 other properties edited (see Wikidata diff for full list)
    "/* wbcreateclaim-create:1| */ [[Property:P591]]: 3.5.1.98, [[:toollabs:quickstatements/#/batch/261491|batch #261491]]"
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