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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Histone deacetylase 9''' is an [[enzyme]] that in humans is encoded by the ''HDAC9'' [[gene]].<ref name="pmid10523670">{{cite journal | vauthors = Wang AH, Bertos NR, Vezmar M, Pelletier N, Crosato M, Heng HH, Th'ng J, Han J, Yang XJ | title = HDAC4, a human histone deacetylase related to yeast HDA1, is a transcriptional corepressor | journal = Molecular and Cellular Biology | volume = 19 | issue = 11 | pages = 7816–27 | date = November 1999 | pmid = 10523670 | pmc = 84849 | doi = 10.1128/mcb.19.11.7816 }}</ref><ref name="pmid10487760">{{cite journal | vauthors = Sparrow DB, Miska EA, Langley E, Reynaud-Deonauth S, Kotecha S, Towers N, Spohr G, Kouzarides T, Mohun TJ | title = MEF-2 function is modified by a novel co-repressor, MITR | journal = The EMBO Journal | volume = 18 | issue = 18 | pages = 5085–98 | date = September 1999 | pmid = 10487760 | pmc = 1171579 | doi = 10.1093/emboj/18.18.5085 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: HDAC9 histone deacetylase 9| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9734| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Histone deacetylase 9
| HGNCid = 14065
| Symbol = HDAC9
| AltSymbols =; DKFZp779K1053; HD7; HDAC; HDAC7; HDAC7B; HDAC9B; HDAC9FL; HDRP; KIAA0744; MITR
| OMIM = 606543
| ECnumber = 
| Homologene = 64351
| MGIid = 1931221
| Function = {{GNF_GO|id=GO:0003714 |text = transcription corepressor activity}} {{GNF_GO|id=GO:0004407 |text = histone deacetylase activity}} {{GNF_GO|id=GO:0008134 |text = transcription factor binding}} {{GNF_GO|id=GO:0016566 |text = specific transcriptional repressor activity}} {{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:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0000122 |text = negative regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0007507 |text = heart development}} {{GNF_GO|id=GO:0016568 |text = chromatin modification}} {{GNF_GO|id=GO:0016575 |text = histone deacetylation}} {{GNF_GO|id=GO:0030183 |text = B cell differentiation}} {{GNF_GO|id=GO:0045843 |text = negative regulation of striated muscle development}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 9734
    | Hs_Ensembl = ENSG00000048052
    | Hs_RefseqProtein = NP_055522
    | Hs_RefseqmRNA = NM_014707
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 7
    | Hs_GenLoc_start = 18501894
    | Hs_GenLoc_end = 19002210
    | Hs_Uniprot = Q9UKV0
    | Mm_EntrezGene = 79221
    | Mm_Ensembl = ENSMUSG00000004698
    | Mm_RefseqmRNA = NM_024124
    | Mm_RefseqProtein = NP_077038
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 12
    | Mm_GenLoc_start = 34663701
    | Mm_GenLoc_end = 35022647
    | Mm_Uniprot = Q4QQN7
  }}
}}
'''Histone deacetylase 9''', also known as '''HDAC9''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HDAC9 histone deacetylase 9| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9734| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Histones play a critical role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation alters chromosome structure and affects transcription factor access to DNA. The protein encoded by this gene has sequence homology to members of the histone deacetylase family. This gene is orthologous to the Xenopus and mouse MITR genes. The MITR protein lacks the histone deacetylase catalytic domain. It represses MEF2 activity through recruitment of multicomponent corepressor complexes that include CtBP and HDACs. This encoded protein may play a role in hematopoiesis. Multiple alternatively spliced transcripts have been described for this gene but the full-length nature of some of them has not been determined.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = Histones play a critical role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation alters chromosome structure and affects transcription factor access to DNA. The protein encoded by this gene has sequence homology to members of the histone deacetylase family. This gene is orthologous to the Xenopus and mouse MITR genes. The MITR protein lacks the histone deacetylase catalytic domain. It represses MEF2 activity through recruitment of multicomponent corepressor complexes that include CtBP and HDACs. This encoded protein may play a role in hematopoiesis. Multiple alternatively spliced transcripts have been described for this gene but the full-length nature of some of them has not been determined.<ref name="entrez">{{cite web | title = Entrez Gene: HDAC9 histone deacetylase 9| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9734| accessdate = }}</ref>
}}


==See also==
== Interactions ==
 
HDAC9 has been shown to [[Protein-protein interaction|interact]] with:
{{div col|colwidth=20em}}
* [[CBX5 (gene)|CBX5]],<ref name = pmid12242305>{{cite journal | vauthors = Zhang CL, McKinsey TA, Olson EN | title = Association of class II histone deacetylases with heterochromatin protein 1: potential role for histone methylation in control of muscle differentiation | journal = Molecular and Cellular Biology | volume = 22 | issue = 20 | pages = 7302–12 | date = October 2002 | pmid = 12242305 | pmc = 139799 | doi = 10.1128/mcb.22.20.7302-7312.2002 }}</ref>
* [[HDAC3]],<ref name = pmid12590135/><ref name = pmid10655483>{{cite journal | vauthors = Zhou X, Richon VM, Rifkind RA, Marks PA | title = Identification of a transcriptional repressor related to the noncatalytic domain of histone deacetylases 4 and 5 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 97 | issue = 3 | pages = 1056–61 | date = February 2000 | pmid = 10655483 | pmc = 15519 | doi = 10.1073/pnas.97.3.1056 }}</ref>
* [[BTG2]], <ref>{{cite journal | vauthors = Micheli L, D'Andrea G, Leonardi L, Tirone F | title = HDAC1, HDAC4, and HDAC9 Bind to PC3/Tis21/Btg2 and Are Required for Its Inhibition of Cell Cycle Progression and Cyclin D1 Expression | journal = Journal of Cellular Physiology | volume = 232 | issue = 7 | pages = 1696–1707 | date = July 2017 | pmid = 27333946 | doi = 10.1002/jcp.25467 | url = http://www.inmm.cnr.it/tirone/pdfs/Micheli_et_al-2017-J_Cell_Physiol%20PC3-HDACs.pdf }}</ref>
* [[Myocyte-specific enhancer factor 2A]]<ref name = pmid10487761>{{cite journal | vauthors = Miska EA, Karlsson C, Langley E, Nielsen SJ, Pines J, Kouzarides T | title = HDAC4 deacetylase associates with and represses the MEF2 transcription factor | journal = The EMBO Journal | volume = 18 | issue = 18 | pages = 5099–107 | date = September 1999 | pmid = 10487761 | pmc = 1171580 | doi = 10.1093/emboj/18.18.5099 }}</ref><ref name = pmid10748098>{{cite journal | vauthors = Lemercier C, Verdel A, Galloo B, Curtet S, Brocard MP, Khochbin S | title = mHDA1/HDAC5 histone deacetylase interacts with and represses MEF2A transcriptional activity | journal = The Journal of Biological Chemistry | volume = 275 | issue = 20 | pages = 15594–9 | date = May 2000 | pmid = 10748098 | doi = 10.1074/jbc.M908437199 }}</ref>
* [[Nuclear receptor co-repressor 1]],<ref name = pmid12590135/>
* [[SIN3A]],<ref name = pmid12590135>{{cite journal | vauthors = Petrie K, Guidez F, Howell L, Healy L, Waxman S, Greaves M, Zelent A | title = The histone deacetylase 9 gene encodes multiple protein isoforms | journal = The Journal of Biological Chemistry | volume = 278 | issue = 18 | pages = 16059–72 | date = May 2003 | pmid = 12590135 | doi = 10.1074/jbc.M212935200 }}</ref><ref name = pmid11959865>{{cite journal | vauthors = Koipally J, Georgopoulos K | title = Ikaros-CtIP interactions do not require C-terminal binding protein and participate in a deacetylase-independent mode of repression | journal = The Journal of Biological Chemistry | volume = 277 | issue = 26 | pages = 23143–9 | date = June 2002 | pmid = 11959865 | doi = 10.1074/jbc.M202079200 }}</ref>  and
* [[SUV39H1]].<ref name = pmid12242305/>
{{Div col end}}
 
== See also ==
* [[Histone deacetylase]]
* [[Histone deacetylase]]
{{Clear}}


==References==
== References ==
{{reflist|2}}
{{reflist|33em}}


==Further reading==
== Further reading ==
{{refbegin | 2}}
{{refbegin|33em}}
{{PBB_Further_reading
* {{cite journal | vauthors = Marks PA, Richon VM, Rifkind RA | title = Histone deacetylase inhibitors: inducers of differentiation or apoptosis of transformed cells | journal = Journal of the National Cancer Institute | volume = 92 | issue = 15 | pages = 1210–6 | date = August 2000 | pmid = 10922406 | doi = 10.1093/jnci/92.15.1210 }}
| citations =
* {{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 }}
*{{cite journal | author=Marks PA, Richon VM, Rifkind RA |title=Histone deacetylase inhibitors: inducers of differentiation or apoptosis of transformed cells. |journal=J. Natl. Cancer Inst. |volume=92 |issue= 15 |pages= 1210-6 |year= 2000 |pmid= 10922406 |doi= }}
* {{cite journal | vauthors = | title = Toward a complete human genome sequence | journal = Genome Research | volume = 8 | issue = 11 | pages = 1097–108 | date = November 1998 | pmid = 9847074 | doi = 10.1101/gr.8.11.1097 }}
*{{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 = Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O | title = Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro | journal = DNA Research | volume = 5 | issue = 5 | pages = 277–86 | date = October 1998 | pmid = 9872452 | doi = 10.1093/dnares/5.5.277 }}
*{{cite journal | author= |title=Toward a complete human genome sequence. |journal=Genome Res. |volume=8 |issue= 11 |pages= 1097-108 |year= 1999 |pmid= 9847074 |doi= }}
* {{cite journal | vauthors = Miska EA, Karlsson C, Langley E, Nielsen SJ, Pines J, Kouzarides T | title = HDAC4 deacetylase associates with and represses the MEF2 transcription factor | journal = The EMBO Journal | volume = 18 | issue = 18 | pages = 5099–107 | date = September 1999 | pmid = 10487761 | pmc = 1171580 | doi = 10.1093/emboj/18.18.5099 }}
*{{cite journal | author=Nagase T, Ishikawa K, Suyama M, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. |journal=DNA Res. |volume=5 |issue= 5 |pages= 277-86 |year= 1999 |pmid= 9872452 |doi=  }}
* {{cite journal | vauthors = Zhou X, Richon VM, Rifkind RA, Marks PA | title = Identification of a transcriptional repressor related to the noncatalytic domain of histone deacetylases 4 and 5 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 97 | issue = 3 | pages = 1056–61 | date = February 2000 | pmid = 10655483 | pmc = 15519 | doi = 10.1073/pnas.97.3.1056 }}
*{{cite journal  | author=Sparrow DB, Miska EA, Langley E, ''et al.'' |title=MEF-2 function is modified by a novel co-repressor, MITR. |journal=EMBO J. |volume=18 |issue= 18 |pages= 5085-98 |year= 1999 |pmid= 10487760 |doi= 10.1093/emboj/18.18.5085 }}
* {{cite journal | vauthors = Youn HD, Grozinger CM, Liu JO | title = Calcium regulates transcriptional repression of myocyte enhancer factor 2 by histone deacetylase 4 | journal = The Journal of Biological Chemistry | volume = 275 | issue = 29 | pages = 22563–7 | date = July 2000 | pmid = 10825153 | doi = 10.1074/jbc.C000304200 }}
*{{cite journal | author=Miska EA, Karlsson C, Langley E, ''et al.'' |title=HDAC4 deacetylase associates with and represses the MEF2 transcription factor. |journal=EMBO J. |volume=18 |issue= 18 |pages= 5099-107 |year= 1999 |pmid= 10487761 |doi= 10.1093/emboj/18.18.5099 }}
* {{cite journal | vauthors = Zhang CL, McKinsey TA, Lu JR, Olson EN | title = Association of COOH-terminal-binding protein (CtBP) and MEF2-interacting transcription repressor (MITR) contributes to transcriptional repression of the MEF2 transcription factor | journal = The Journal of Biological Chemistry | volume = 276 | issue = 1 | pages = 35–9 | date = January 2001 | pmid = 11022042 | doi = 10.1074/jbc.M007364200 }}
*{{cite journal | author=Wang AH, Bertos NR, Vezmar M, ''et al.'' |title=HDAC4, a human histone deacetylase related to yeast HDA1, is a transcriptional corepressor. |journal=Mol. Cell. Biol. |volume=19 |issue= 11 |pages= 7816-27 |year= 1999 |pmid= 10523670 |doi=  }}
* {{cite journal | vauthors = Fischle W, Dequiedt F, Fillion M, Hendzel MJ, Voelter W, Verdin E | title = Human HDAC7 histone deacetylase activity is associated with HDAC3 in vivo | journal = The Journal of Biological Chemistry | volume = 276 | issue = 38 | pages = 35826–35 | date = September 2001 | pmid = 11466315 | doi = 10.1074/jbc.M104935200 }}
*{{cite journal  | author=Zhou X, Richon VM, Rifkind RA, Marks PA |title=Identification of a transcriptional repressor related to the noncatalytic domain of histone deacetylases 4 and 5. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 3 |pages= 1056-61 |year= 2000 |pmid= 10655483 |doi= }}
* {{cite journal | vauthors = Zhou X, Marks PA, Rifkind RA, Richon VM | title = Cloning and characterization of a histone deacetylase, HDAC9 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 98 | issue = 19 | pages = 10572–7 | date = September 2001 | pmid = 11535832 | pmc = 58507 | doi = 10.1073/pnas.191375098 }}
*{{cite journal | author=Youn HD, Grozinger CM, Liu JO |title=Calcium regulates transcriptional repression of myocyte enhancer factor 2 by histone deacetylase 4. |journal=J. Biol. Chem. |volume=275 |issue= 29 |pages= 22563-7 |year= 2000 |pmid= 10825153 |doi= 10.1074/jbc.C000304200 }}
* {{cite journal | vauthors = Koipally J, Georgopoulos K | title = Ikaros-CtIP interactions do not require C-terminal binding protein and participate in a deacetylase-independent mode of repression | journal = The Journal of Biological Chemistry | volume = 277 | issue = 26 | pages = 23143–9 | date = June 2002 | pmid = 11959865 | doi = 10.1074/jbc.M202079200 }}
*{{cite journal | author=Zhang CL, McKinsey TA, Lu JR, Olson EN |title=Association of COOH-terminal-binding protein (CtBP) and MEF2-interacting transcription repressor (MITR) contributes to transcriptional repression of the MEF2 transcription factor. |journal=J. Biol. Chem. |volume=276 |issue= 1 |pages= 35-9 |year= 2001 |pmid= 11022042 |doi= 10.1074/jbc.M007364200 }}
* {{cite journal | vauthors = Kirsh O, Seeler JS, Pichler A, Gast A, Müller S, Miska E, Mathieu M, Harel-Bellan A, Kouzarides T, Melchior F, Dejean A | title = The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase | journal = The EMBO Journal | volume = 21 | issue = 11 | pages = 2682–91 | date = June 2002 | pmid = 12032081 | pmc = 125385 | doi = 10.1093/emboj/21.11.2682 }}
*{{cite journal | author=Fischle W, Dequiedt F, Fillion M, ''et al.'' |title=Human HDAC7 histone deacetylase activity is associated with HDAC3 in vivo. |journal=J. Biol. Chem. |volume=276 |issue= 38 |pages= 35826-35 |year= 2001 |pmid= 11466315 |doi= 10.1074/jbc.M104935200 }}
* {{cite journal | vauthors = Mahlknecht U, Schnittger S, Will J, Cicek N, Hoelzer D | title = Chromosomal organization and localization of the human histone deacetylase 9 gene (HDAC9) | journal = Biochemical and Biophysical Research Communications | volume = 293 | issue = 1 | pages = 182–91 | date = April 2002 | pmid = 12054582 | doi = 10.1016/S0006-291X(02)00193-6 }}
*{{cite journal | author=Zhou X, Marks PA, Rifkind RA, Richon VM |title=Cloning and characterization of a histone deacetylase, HDAC9. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 19 |pages= 10572-7 |year= 2001 |pmid= 11535832 |doi= 10.1073/pnas.191375098 }}
* {{cite journal | vauthors = Zhang CL, McKinsey TA, Olson EN | title = Association of class II histone deacetylases with heterochromatin protein 1: potential role for histone methylation in control of muscle differentiation | journal = Molecular and Cellular Biology | volume = 22 | issue = 20 | pages = 7302–12 | date = October 2002 | pmid = 12242305 | pmc = 139799 | doi = 10.1128/MCB.22.20.7302-7312.2002 }}
*{{cite journal | author=Koipally J, Georgopoulos K |title=Ikaros-CtIP interactions do not require C-terminal binding protein and participate in a deacetylase-independent mode of repression. |journal=J. Biol. Chem. |volume=277 |issue= 26 |pages= 23143-9 |year= 2002 |pmid= 11959865 |doi= 10.1074/jbc.M202079200 }}
* {{cite journal | vauthors = Hoogeveen AT, Rossetti S, Stoyanova V, Schonkeren J, Fenaroli A, Schiaffonati L, van Unen L, Sacchi N | title = The transcriptional corepressor MTG16a contains a novel nucleolar targeting sequence deranged in t (16; 21)-positive myeloid malignancies | journal = Oncogene | volume = 21 | issue = 43 | pages = 6703–12 | date = September 2002 | pmid = 12242670 | doi = 10.1038/sj.onc.1205882 }}
*{{cite journal | author=Kirsh O, Seeler JS, Pichler A, ''et al.'' |title=The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase. |journal=EMBO J. |volume=21 |issue= 11 |pages= 2682-91 |year= 2002 |pmid= 12032081 |doi= 10.1093/emboj/21.11.2682 }}
* {{cite journal | vauthors = Petrie K, Guidez F, Howell L, Healy L, Waxman S, Greaves M, Zelent A | title = The histone deacetylase 9 gene encodes multiple protein isoforms | journal = The Journal of Biological Chemistry | volume = 278 | issue = 18 | pages = 16059–72 | date = May 2003 | pmid = 12590135 | doi = 10.1074/jbc.M212935200 }}
*{{cite journal | author=Mahlknecht U, Schnittger S, Will J, ''et al.'' |title=Chromosomal organization and localization of the human histone deacetylase 9 gene (HDAC9). |journal=Biochem. Biophys. Res. Commun. |volume=293 |issue= 1 |pages= 182-91 |year= 2002 |pmid= 12054582 |doi= 10.1016/S0006-291X(02)00193-6 }}
*{{cite journal | author=Zhang CL, McKinsey TA, Olson EN |title=Association of class II histone deacetylases with heterochromatin protein 1: potential role for histone methylation in control of muscle differentiation. |journal=Mol. Cell. Biol. |volume=22 |issue= 20 |pages= 7302-12 |year= 2002 |pmid= 12242305 |doi= }}
*{{cite journal | author=Hoogeveen AT, Rossetti S, Stoyanova V, ''et al.'' |title=The transcriptional corepressor MTG16a contains a novel nucleolar targeting sequence deranged in t (16; 21)-positive myeloid malignancies. |journal=Oncogene |volume=21 |issue= 43 |pages= 6703-12 |year= 2002 |pmid= 12242670 |doi= 10.1038/sj.onc.1205882 }}
*{{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  | author=Petrie K, Guidez F, Howell L, ''et al.'' |title=The histone deacetylase 9 gene encodes multiple protein isoforms. |journal=J. Biol. Chem. |volume=278 |issue= 18 |pages= 16059-72 |year= 2003 |pmid= 12590135 |doi= 10.1074/jbc.M212935200 }}
}}
{{refend}}
{{refend}}


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* {{MeshName|HDAC9+protein,+human}}
* {{MeshName|HDAC9+protein,+human}}


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Latest revision as of 15:08, 3 April 2018

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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 9 is an enzyme that in humans is encoded by the HDAC9 gene.[1][2][3]

Function

Histones play a critical role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation alters chromosome structure and affects transcription factor access to DNA. The protein encoded by this gene has sequence homology to members of the histone deacetylase family. This gene is orthologous to the Xenopus and mouse MITR genes. The MITR protein lacks the histone deacetylase catalytic domain. It represses MEF2 activity through recruitment of multicomponent corepressor complexes that include CtBP and HDACs. This encoded protein may play a role in hematopoiesis. Multiple alternatively spliced transcripts have been described for this gene but the full-length nature of some of them has not been determined.[3]

Interactions

HDAC9 has been shown to interact with:

See also

References

  1. ↑ Wang AH, Bertos NR, Vezmar M, Pelletier N, Crosato M, Heng HH, Th'ng J, Han J, Yang XJ (November 1999). "HDAC4, a human histone deacetylase related to yeast HDA1, is a transcriptional corepressor". Molecular and Cellular Biology. 19 (11): 7816–27. doi:10.1128/mcb.19.11.7816. PMC 84849. PMID 10523670.
  2. ↑ Sparrow DB, Miska EA, Langley E, Reynaud-Deonauth S, Kotecha S, Towers N, Spohr G, Kouzarides T, Mohun TJ (September 1999). "MEF-2 function is modified by a novel co-repressor, MITR". The EMBO Journal. 18 (18): 5085–98. doi:10.1093/emboj/18.18.5085. PMC 1171579. PMID 10487760.
  3. ↑ 3.0 3.1 "Entrez Gene: HDAC9 histone deacetylase 9".
  4. ↑ 4.0 4.1 Zhang CL, McKinsey TA, Olson EN (October 2002). "Association of class II histone deacetylases with heterochromatin protein 1: potential role for histone methylation in control of muscle differentiation". Molecular and Cellular Biology. 22 (20): 7302–12. doi:10.1128/mcb.22.20.7302-7312.2002. PMC 139799. PMID 12242305.
  5. ↑ 5.0 5.1 5.2 Petrie K, Guidez F, Howell L, Healy L, Waxman S, Greaves M, Zelent A (May 2003). "The histone deacetylase 9 gene encodes multiple protein isoforms". The Journal of Biological Chemistry. 278 (18): 16059–72. doi:10.1074/jbc.M212935200. PMID 12590135.
  6. ↑ Zhou X, Richon VM, Rifkind RA, Marks PA (February 2000). "Identification of a transcriptional repressor related to the noncatalytic domain of histone deacetylases 4 and 5". Proceedings of the National Academy of Sciences of the United States of America. 97 (3): 1056–61. doi:10.1073/pnas.97.3.1056. PMC 15519. PMID 10655483.
  7. ↑ Micheli L, D'Andrea G, Leonardi L, Tirone F (July 2017). "HDAC1, HDAC4, and HDAC9 Bind to PC3/Tis21/Btg2 and Are Required for Its Inhibition of Cell Cycle Progression and Cyclin D1 Expression" (PDF). Journal of Cellular Physiology. 232 (7): 1696–1707. doi:10.1002/jcp.25467. PMID 27333946.
  8. ↑ Miska EA, Karlsson C, Langley E, Nielsen SJ, Pines J, Kouzarides T (September 1999). "HDAC4 deacetylase associates with and represses the MEF2 transcription factor". The EMBO Journal. 18 (18): 5099–107. doi:10.1093/emboj/18.18.5099. PMC 1171580. PMID 10487761.
  9. ↑ Lemercier C, Verdel A, Galloo B, Curtet S, Brocard MP, Khochbin S (May 2000). "mHDA1/HDAC5 histone deacetylase interacts with and represses MEF2A transcriptional activity". The Journal of Biological Chemistry. 275 (20): 15594–9. doi:10.1074/jbc.M908437199. PMID 10748098.
  10. ↑ Koipally J, Georgopoulos K (June 2002). "Ikaros-CtIP interactions do not require C-terminal binding protein and participate in a deacetylase-independent mode of repression". The Journal of Biological Chemistry. 277 (26): 23143–9. doi:10.1074/jbc.M202079200. PMID 11959865.

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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