HDAC9

HDAC9

Histone deacetylase 9, also known as HDAC9, is a human gene.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 = ]

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.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 = ]

ee also

* Histone deacetylase

References

Further reading

PBB_Further_reading
citations =
*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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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

External links

*

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes


Wikimedia Foundation. 2010.

Игры ⚽ Поможем написать курсовую

Look at other dictionaries:

  • Histona deacetilasa 9 — HUGO 14065 Símbolo HDAC9 Símbolos alt. DKFZp779K1053; HD7; HDAC; HDAC7; HDAC7B; HDAC9B; HDAC9FL; HDR …   Wikipedia Español

  • Autophagy network — consists of enzymes and substrates involved in the degradation of a cell s own components. Network membersThe Autophagy network members (gene name and aliases) as published in the last 500 newest PubMed entries (see below) are depicted… …   Wikipedia

  • Histon-Deacetylase — Vorhandene Strukturdaten …   Deutsch Wikipedia

  • Деацетилазы гистонов — Каталитический домен HDAC4, связанный с ингибитором (показан зелёным цветом). Деацетилазы гистонов (Histone deacetylases, HDACs), К. Ф. 3.5.1  ферменты катализирующие удаление ацетильной группы ε N ацетил лизина гистонов, внесенные… …   Википедия

  • Histone deacetylase — Histone deacetylases (HDAC) (EC number 3.5.1) are a class of enzymes that remove acetyl groups from an ε N acetyl lysine amino acid on a histone. Its action is opposite to that of histone acetyltransferase.ubtypesHDAC proteins are found in three… …   Wikipedia

  • Nuclear receptor co-repressor 1 — Nuclear receptor corepressor 1 Rendering based on PDB 2EQR …   Wikipedia

  • MEF2C — Myocyte enhancer factor 2C PDB rendering based on 1c7u …   Wikipedia

  • Myocyte-specific enhancer factor 2A — Myocyte enhancer factor 2A PDB rendering based on 1c7u …   Wikipedia

  • HDAC — Histon Deacetylase Vorhandene Strukturdaten: 1tyi …   Deutsch Wikipedia

  • Histondeacetylase — Histon Deacetylase Vorhandene Strukturdaten: 1tyi …   Deutsch Wikipedia

Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”