HDAC11

{{Short description|Protein-coding gene in the species Homo sapiens}} {{Infobox_gene}} '''Histone deacetylase 11''' is a 39kDa histone deacetylase enzyme that in humans is encoded by the ''HDAC11'' gene on chromosome 3 in humans and chromosome 6 in mice.<ref name="pmid11948178">{{cite journal | vauthors = Gao L, Cueto MA, Asselbergs F, Atadja P | title = Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family | journal = The Journal of Biological Chemistry | volume = 277 | issue = 28 | pages = 25748–55 | date = Jul 2002 | pmid = 11948178 | doi = 10.1074/jbc.M111871200 | s2cid = 20332854 | doi-access = free }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: HDAC11 histone deacetylase 11| url = https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=79885}}</ref>

It is the only Class IV HDAC since it is not highly homologous with either Rpd3 or hda1 yeast enzymes and so does not fit into either Class I or Class II.<ref>{{cite journal | vauthors = Yang XJ, Seto E | title = The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men | journal = Nature Reviews Molecular Cell Biology | volume = 9 | issue = 3 | pages = 206–18 | date = Mar 2008 | pmid = 18292778 | doi = 10.1038/nrm2346 | pmc=2667380}}</ref> It is the smallest HDAC isoform and it was first described in 2002.

== Function ==

Histone deacetylases, such as HDAC11, control DNA expression by modifying the core histone octamers that package DNA into dense chromatin structures and repress gene expression.[supplied by OMIM]<ref name="entrez" />

HDAC11 expression is normally found in brain and testis tissue, but upregulation of HDAC11 expression has also been seen in various cancer cells.

HDAC11 has been shown to be a negative regulator of IL-10 production in antigen presenting cells. It has also been shown that inhibition of HDAC11 results in increased expression of OX40L in Hodgkin lymphoma cells.

== Interactions ==

HDAC11 has been shown to interact with HDAC6.<ref name=pmid11948178 />

== See also == * Histone deacetylase

== References == {{reflist}}

== Further reading == {{refbegin | 2}} * {{cite journal | vauthors = Verdin E, Dequiedt F, Kasler HG | title = Class II histone deacetylases: versatile regulators | journal = Trends in Genetics | volume = 19 | issue = 5 | pages = 286–93 | date = May 2003 | pmid = 12711221 | doi = 10.1016/S0168-9525(03)00073-8 | hdl = 2268/80861 | hdl-access = free }} * {{cite journal | vauthors = Hartley JL, Temple GF, Brasch MA | title = DNA cloning using in vitro site-specific recombination | journal = Genome Research | volume = 10 | issue = 11 | pages = 1788–95 | date = Nov 2000 | pmid = 11076863 | pmc = 310948 | doi = 10.1101/gr.143000 }} * {{cite journal | vauthors = Simpson JC, Wellenreuther R, Poustka A, Pepperkok R, Wiemann S | title = Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing | journal = EMBO Reports | volume = 1 | issue = 3 | pages = 287–92 | date = Sep 2000 | pmid = 11256614 | pmc = 1083732 | doi = 10.1093/embo-reports/kvd058 }} * {{cite journal | vauthors = Wiemann S, Arlt D, Huber W, Wellenreuther R, Schleeger S, Mehrle A, Bechtel S, Sauermann M, Korf U, Pepperkok R, Sültmann H, Poustka A | title = From ORFeome to biology: a functional genomics pipeline | journal = Genome Research | volume = 14 | issue = 10B | pages = 2136–44 | date = Oct 2004 | pmid = 15489336 | pmc = 528930 | doi = 10.1101/gr.2576704 }} * {{cite journal | vauthors = Voelter-Mahlknecht S, Ho AD, Mahlknecht U | title = Chromosomal organization and localization of the novel class IV human histone deacetylase 11 gene | journal = International Journal of Molecular Medicine | volume = 16 | issue = 4 | pages = 589–98 | date = Oct 2005 | pmid = 16142391 | doi = 10.3892/ijmm.16.4.589 | doi-broken-date = 12 July 2025 }} * {{cite journal | vauthors = Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M | title = Towards a proteome-scale map of the human protein-protein interaction network | journal = Nature | volume = 437 | issue = 7062 | pages = 1173–8 | date = Oct 2005 | pmid = 16189514 | doi = 10.1038/nature04209 | bibcode = 2005Natur.437.1173R | s2cid = 4427026 }} * {{cite journal | vauthors = Mehrle A, Rosenfelder H, Schupp I, del Val C, Arlt D, Hahne F, Bechtel S, Simpson J, Hofmann O, Hide W, Glatting KH, Huber W, Pepperkok R, Poustka A, Wiemann S | title = The LIFEdb database in 2006 | journal = Nucleic Acids Research | volume = 34 | issue = Database issue | pages = D415–8 | date = Jan 2006 | pmid = 16381901 | pmc = 1347501 | doi = 10.1093/nar/gkj139 }} * {{cite journal | vauthors = Lindberg D, Akerström G, Westin G | title = Mutational analyses of WNT7A and HDAC11 as candidate tumour suppressor genes in sporadic malignant pancreatic endocrine tumours | journal = Clinical Endocrinology | volume = 66 | issue = 1 | pages = 110–4 | date = Jan 2007 | pmid = 17201809 | doi = 10.1111/j.1365-2265.2006.02694.x | s2cid = 21975021 }} {{refend}}

== External links == * {{MeshName|HDAC11+protein,+human}}

Category:EC 3.5.1