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HDAC10

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HDAC10
Identifiers
AliasesHDAC10, HD10, histone deacetylase 10
External IDsOMIM: 608544; MGI: 2158340; HomoloGene: 23749; GeneCards: HDAC10; OMA:HDAC10 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_032019
NM_001159286

NM_199198

RefSeq (protein)

NP_001152758
NP_114408

NP_954668

Location (UCSC)Chr 22: 50.25 – 50.25 MbChr 15: 89.01 – 89.01 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Histone deacetylase 10 is an enzyme that in humans is encoded by the HDAC10 gene.[5][6][7] HDAC10 is a class IIb HDAC. It specifically has selectivity for long, slender polyamines like N8-acetylspermidine. [8]

Acetylation of histone core particles modulates chromatin structure and gene expression. The opposing enzymatic activities of histone acetyltransferases and histone deacetylases, such as HDAC10, determine the acetylation status of histone tails (Kao et al., 2002).[supplied by OMIM][7]

Interactions

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HDAC10 has been shown to interact with Histone deacetylase 2[9] and Nuclear receptor co-repressor 2.[9]

See also

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References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000100429Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000062906Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Kao HY, Lee CH, Komarov A, Han CC, Evans RM (January 2002). "Isolation and characterization of mammalian HDAC10, a novel histone deacetylase". The Journal of Biological Chemistry. 277 (1): 187–193. doi:10.1074/jbc.M108931200. PMID 11677242.
  6. ^ Guardiola AR, Yao TP (February 2002). "Molecular cloning and characterization of a novel histone deacetylase HDAC10". The Journal of Biological Chemistry. 277 (5): 3350–3356. doi:10.1074/jbc.M109861200. PMID 11726666.
  7. ^ a b "Entrez Gene: HDAC10 histone deacetylase 10".
  8. ^ Lambona C, Zwergel C, Fioravanti R, Valente S, Mai A (October 2023). "Histone deacetylase 10: A polyamine deacetylase from the crystal structure to the first inhibitors". Current Opinion in Structural Biology. 82: 102668. doi:10.1016/j.sbi.2023.102668. PMID 37542907.
  9. ^ a b Fischer DD, Cai R, Bhatia U, Asselbergs FA, Song C, Terry R, et al. (February 2002). "Isolation and characterization of a novel class II histone deacetylase, HDAC10". The Journal of Biological Chemistry. 277 (8): 6656–6666. doi:10.1074/jbc.M108055200. PMID 11739383.

Further reading

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