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Protein HDAC6 PDB 3C5K.png
Available structures
PDBOrtholog search: PDBe RCSB
AliasesHDAC6, CPBHM, HD6, PPP1R90, JM21, histone deacetylase 6
External IDsMGI: 1333752 HomoloGene: 31353 GeneCards: HDAC6
Gene location (Human)
X chromosome (human)
Chr.X chromosome (human)[1]
X chromosome (human)
Genomic location for HDAC6
Genomic location for HDAC6
BandXp11.23Start48,801,377 bp[1]
End48,824,982 bp[1]
RNA expression pattern
PBB GE HDAC6 211722 s at fs.png

PBB GE HDAC6 206846 s at fs.png

PBB GE HDAC6 216224 s at fs.png
More reference expression data
RefSeq (mRNA)


RefSeq (protein)


Location (UCSC)Chr X: 48.8 – 48.82 MbChr X: 7.93 – 7.95 Mb
PubMed search[3][4]
View/Edit HumanView/Edit Mouse

Histone deacetylase 6 is an enzyme that in humans is encoded by the HDAC6 gene.[5][6]


Histones play a critical role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation alters chromatin structure and affects transcription. The protein encoded by this gene belongs to class II of the histone deacetylase/acuc/apha family. It contains an internal duplication of two catalytic domains that appear to function independently of each other. This protein possesses histone deacetylase activity and represses transcription.[7]

Clinical relevance[edit]

Mutations in this gene have been associated to Alzheimer's disease.[8]

Over expression of this protein correlates with tumorigenesis and cell survival. HDAC6 also encourages metastasis of cancer cells.[9]


Retracts the Cilium of the cell, which is necessary prior to mitosis of the cell.[10]

HDAC also encourages cell motility and catalyzes α-tubulin deacetylation.[11] as a result the enzyme also encourages cancer cell metastasis.[9]
HDAC6 also affects transcription and translation by regulating the heat-shock protein 90 (Hsp90) and stress granules (SGs), respectively.[9]

HDAC6 is also known to bond with high affinity to ubiquitinated proteins.[12] HDAC6 is also required in the formation of SG (Stress granule proteins and is instrumental in SG formation; pharmacological inhibition or genetic removal of HDAC6 abolished SG formation.


HDAC6 has been shown to interact with HDAC11[13] and Zinc finger and BTB domain-containing protein 16.[14]

HDAC6 interacts with SG (Stress granule) protein G3BP1.[12]

See also[edit]


  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000094631 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031161 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:".
  4. ^ "Mouse PubMed Reference:".
  5. ^ Grozinger CM, Hassig CA, Schreiber SL (Jun 1999). "Three proteins define a class of human histone deacetylases related to yeast Hda1p". Proc Natl Acad Sci U S A. 96 (9): 4868–73. doi:10.1073/pnas.96.9.4868. PMC 21783. PMID 10220385.
  6. ^ Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (May 1999). "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 5 (6): 355–64. doi:10.1093/dnares/5.6.355. PMID 10048485.
  7. ^ "Entrez Gene: HDAC6 histone deacetylase 6".
  8. ^ Cook C, Gendron TF, Scheffel K, Carlomagno Y, Dunmore J, DeTure M, Petrucelli L (5 April 2012). "Loss of HDAC6, a novel CHIP substrate, alleviates abnormal tau accumulation". Human Molecular Genetics. 21 (13): 2936–45. doi:10.1093/hmg/dds125. PMC 3373241. PMID 22492994.
  9. ^ a b c Aldana-Masangkay GI, Sakamoto KM (2011). "The role of HDAC6 in cancer". J. Biomed. Biotechnol. 2011: 1–10. doi:10.1155/2011/875824. PMC 2975074. PMID 21076528.
  10. ^ Krishnamurthy K, Wang G, Silva J, Condie BG, Bieberich E (February 2007). "Ceramide regulates atypical PKCzeta/lambda-mediated cell polarity in primitive ectoderm cells. A novel function of sphingolipids in morphogenesis". J. Biol. Chem. 282 (5): 3379–90. doi:10.1074/jbc.M607779200. PMID 17105725. Lay summaryphys.org/news.
  11. ^ Gao YS, Hubbert CC, Lu J, Lee YS, Lee JY, Yao TP (2007). "Histone deacetylase 6 regulates growth factor-induced actin remodeling and endocytosis". Mol. Cell. Biol. 27 (24): 8637–47. doi:10.1128/MCB.00393-07. PMC 2169396. PMID 17938201.
  12. ^ a b Kwon S, Zhang Y, Matthias P (December 2007). "The deacetylase HDAC6 is a novel critical component of stress granules involved in the stress response". Genes Dev. 21 (24): 3381–94. doi:10.1101/gad.461107. PMC 2113037. PMID 18079183.
  13. ^ Gao L, Cueto MA, Asselbergs F, Atadja P (Jul 2002). "Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family". J. Biol. Chem. 277 (28): 25748–55. doi:10.1074/jbc.M111871200. PMID 11948178.
  14. ^ Chauchereau A, Mathieu M, de Saintignon J, Ferreira R, Pritchard LL, Mishal Z, Dejean A, Harel-Bellan A (Nov 2004). "HDAC4 mediates transcriptional repression by the acute promyelocytic leukaemia-associated protein PLZF". Oncogene. 23 (54): 8777–84. doi:10.1038/sj.onc.1208128. PMID 15467736.

Further reading[edit]

External links[edit]

This article incorporates text from the United States National Library of Medicine, which is in the public domain.