HDAC11: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''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 | pmc =  | doi = 10.1074/jbc.M111871200 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: HDAC11 histone deacetylase 11| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=79885| accessdate = }}</ref>
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It is the only Class IV [[histone deacetylase|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.
{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Histone deacetylase 11
| HGNCid = 19086
| Symbol = HDAC11
| AltSymbols =; FLJ22237
| OMIM = 607226
| ECnumber = 
| Homologene = 11743
| MGIid = 2385252
| GeneAtlas_image1 = PBB_GE_HDAC11_219847_at_tn.png
| Function = {{GNF_GO|id=GO:0004407 |text = histone deacetylase activity}} {{GNF_GO|id=GO:0008134 |text = transcription factor binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0000118 |text = histone deacetylase complex}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0016568 |text = chromatin modification}} {{GNF_GO|id=GO:0016575 |text = histone deacetylation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 79885
    | Hs_Ensembl = ENSG00000163517
    | Hs_RefseqProtein = NP_079103
    | Hs_RefseqmRNA = NM_024827
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 3
    | Hs_GenLoc_start = 13496224
    | Hs_GenLoc_end = 13521834
    | Hs_Uniprot = Q96DB2
    | Mm_EntrezGene = 232232
    | Mm_Ensembl = ENSMUSG00000034245
    | Mm_RefseqmRNA = NM_144919
    | Mm_RefseqProtein = NP_659168
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 6
    | Mm_GenLoc_start = 91122308
    | Mm_GenLoc_end = 91140192
    | Mm_Uniprot = Q543U1
  }}
}}
'''Histone deacetylase 11''', also known as '''HDAC11''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HDAC11 histone deacetylase 11| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=79885| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{PBB_Summary
| section_title =  
| summary_text = 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">{{cite web | title = Entrez Gene: HDAC11 histone deacetylase 11| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=79885| accessdate = }}</ref>
}}


==See also==
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 [[Protein-protein interaction|interact]] with [[HDAC6]].<ref name=pmid11948178 />
 
== See also ==
* [[Histone deacetylase]]
* [[Histone deacetylase]]


==References==
== References ==
{{reflist|2}}
{{reflist}}


==Further reading==
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{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 }}
| citations =
* {{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 | author=Verdin E, Dequiedt F, Kasler HG |title=Class II histone deacetylases: versatile regulators. |journal=Trends Genet. |volume=19 |issue= 5 |pages= 286-93 |year= 2003 |pmid= 12711221 |doi= }}
* {{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 | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi= }}
* {{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 | author=Simpson JC, Wellenreuther R, Poustka A, ''et al.'' |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287-92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058 }}
* {{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 }}
*{{cite journal | author=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=J. Biol. Chem. |volume=277 |issue= 28 |pages= 25748-55 |year= 2002 |pmid= 11948178 |doi= 10.1074/jbc.M111871200 }}
* {{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 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{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  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
* {{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 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Wiemann S, Arlt D, Huber W, ''et al.'' |title=From ORFeome to biology: a functional genomics pipeline. |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136-44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704 }}
*{{cite journal | author=Voelter-Mahlknecht S, Ho AD, Mahlknecht U |title=Chromosomal organization and localization of the novel class IV human histone deacetylase 11 gene. |journal=Int. J. Mol. Med. |volume=16 |issue= 4 |pages= 589-98 |year= 2005 |pmid= 16142391 |doi= }}
*{{cite journal | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal | author=Mehrle A, Rosenfelder H, Schupp I, ''et al.'' |title=The LIFEdb database in 2006. |journal=Nucleic Acids Res. |volume=34 |issue= Database issue |pages= D415-8 |year= 2006 |pmid= 16381901 |doi= 10.1093/nar/gkj139 }}
*{{cite journal | author=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=Clin. Endocrinol. (Oxf) |volume=66 |issue= 1 |pages= 110-4 |year= 2007 |pmid= 17201809 |doi= 10.1111/j.1365-2265.2006.02694.x }}
}}
{{refend}}
{{refend}}


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* {{MeshName|HDAC11+protein,+human}}
* {{MeshName|HDAC11+protein,+human}}


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{{Carbon-nitrogen non-peptide hydrolases}}
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Latest revision as of 13:31, 31 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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.[1][2]

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.[3] 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][2]

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.[1]

See also

References

  1. ↑ 1.0 1.1 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". The Journal of Biological Chemistry. 277 (28): 25748–55. doi:10.1074/jbc.M111871200. PMID 11948178.
  2. ↑ 2.0 2.1 "Entrez Gene: HDAC11 histone deacetylase 11".
  3. ↑ Yang XJ, Seto E (Mar 2008). "The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men". Nature Reviews Molecular Cell Biology. 9 (3): 206–18. doi:10.1038/nrm2346. PMC 2667380. PMID 18292778.

Further reading

External links

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


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