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HDAC10

From Wikipedia, the free encyclopedia
Protein-coding gene in the species Homo sapiens
HDAC10
Identifiers
Aliases HDAC10 , HD10, histone deacetylase 10
External IDsOMIM: 608544; MGI: 2158340; HomoloGene: 23749; GeneCards: HDAC10; OMA:HDAC10 - orthologs
Gene location (Human)
Chromosome 22 (human)
Chr. Chromosome 22 (human) [1]
Band 22q13.33Start50,245,183 bp [1]
End50,251,405 bp [1]
Gene location (Mouse)
Chromosome 15 (mouse)
Chr. Chromosome 15 (mouse)[2]
Band 15|15 E3Start89,007,510 bp [2]
End89,012,903 bp [2]
RNA expression pattern
Bgee
Human Mouse (ortholog)
  • granulocyte

  • right uterine tube

  • right hemisphere of cerebellum

  • anterior pituitary

  • mucosa of transverse colon

  • spleen

  • right ovary

  • canal of the cervix

  • right frontal lobe

  • left ovary
  • granulocyte

  • right kidney

  • muscle of thigh

  • esophagus

  • lip

  • proximal tubule

  • neural layer of retina

  • lacrimal gland

  • mesenteric lymph nodes

  • neural tube
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

83933

170787

Ensembl

ENSG00000100429

ENSMUSG00000062906

UniProt

Q969S8
Q08AP5

Q6P3E7

RefSeq (mRNA)

NM_032019
NM_001159286

NM_199198

RefSeq (protein)

NP_001152758
NP_114408

NP_954668

Location (UCSC)Chr 22: 50.25 – 50.25 Mb Chr 15: 89.01 – 89.01 Mb
PubMed search[3] [4]
Wikidata

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. hdl:11573/1685964 . 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.

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