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InterPro: IPR000286 Histone deacetylase superfamily

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2720 proteins

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Accession

IPR000286 His_deacetylse

Type

Family

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:3.40.800.20	His_deacetylse	2475
Pfam	PF00850	Hist_deacetyl	2571
PRINTS	PR01270	HDASUPER	2348
PANTHER	PTHR10625	His_deacetylse	2648
Signatures in BioMart

InterPro Relationships Help

Children

IPR003084 Histone deacetylase
IPR003085 Acetoin utilisation ACUC protein
IPR017320 Histone deacetylase class II, eukaryotic
IPR017321 Histone deacetylase class II, yeast

InterPro annotation

Entry Details in BioMart

Abstract

Histones can be reversibly acetylated on several lysine residues. Regulation of transcription is caused in part by this mechanism. Histone deacetylases catalyse the removal of the acetyl group. Histone deacetylases, acetoin utilization proteins and acetylpolyamine amidohydrolases are all members of this ancient protein superfamily [1].

Structural links Help

PDB - click here

SCOP: c.42.1.2

CATH: 3.40.800.20

Database links Help

Enzyme: EC:3.5.1.98

PANDIT: PF00850

Blocks: IPB000286

Pfam Clan: CL0302.2

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR000286

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O17323 Histone deacetylase 4

P32561 Histone deacetylase RPD3

P56524 Histone deacetylase 4

Q94517 Histone deacetylase Rpd3

Q99N13 Histone deacetylase 9

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR017320	Histone deacetylase class II, eukaryotic
IPR003084	Histone deacetylase
IPR000286	Histone deacetylase superfamily
	SWISS-MODEL
	PDB Chain
	ModBase

Publications Open in usermanual
1.	Leipe DD, Landsman D. Histone deacetylases, acetoin utilization proteins and acetylpolyamine amidohydrolases are members of an ancient protein superfamily. Nucleic Acids Res. 25 3693-7 1997 [PubMed: 9278492] http://dx.doi.org/10.1093/nar/25.18.3693

Additional Reading Open in usermanual
	Thomson S, Mahadevan LC, Clayton AL. MAP kinase-mediated signalling to nucleosomes and immediate-early gene induction. Semin. Cell Dev. Biol. 10 1999 205-14 [PubMed: 10441074] http://dx.doi.org/10.1006/scdb.1999.0302
	Grant PA, Berger SL. Histone acetyltransferase complexes. Semin. Cell Dev. Biol. 10 1999 169-77 [PubMed: 10441070] http://dx.doi.org/10.1006/scdb.1999.0298
	Turner BM. Introduction: chromatin--a target for intracellular signalling pathways. Semin. Cell Dev. Biol. 10 1999 165-7 [PubMed: 10441069] http://dx.doi.org/10.1006/scdb.1999.0297
	Magnaghi-Jaulin L, Ait-Si-Ali S, Harel-Bellan A. Histone acetylation in signal transduction by growth regulatory signals. Semin. Cell Dev. Biol. 10 1999 197-203 [PubMed: 10441073] http://dx.doi.org/10.1006/scdb.1999.0301
	Muchardt C, Yaniv M. The mammalian SWI/SNF complex and the control of cell growth. Semin. Cell Dev. Biol. 10 1999 189-95 [PubMed: 10441072] http://dx.doi.org/10.1006/scdb.1999.0300
	Vannini A, Volpari C, Gallinari P, Jones P, Mattu M, Carfi A, De Francesco R, Steinkuhler C, Di Marco S. Substrate binding to histone deacetylases as shown by the crystal structure of the HDAC8-substrate complex. EMBO Rep. 8 2007 879-84 [PubMed: 17721440] http://dx.doi.org/10.1038/sj.embor.7401047
	Somoza JR, Skene RJ, Katz BA, Mol C, Ho JD, Jennings AJ, Luong C, Arvai A, Buggy JJ, Chi E, Tang J, Sang BC, Verner E, Wynands R, Leahy EM, Dougan DR, Snell G, Navre M, Knuth MW, Swanson RV, McRee DE, Tari LW. Structural snapshots of human HDAC8 provide insights into the class I histone deacetylases. Structure 12 2004 1325-34 [PubMed: 15242608] http://dx.doi.org/10.1016/j.str.2004.04.012
	Archer SY, Hodin RA. Histone acetylation and cancer. Curr. Opin. Genet. Dev. 9 1999 171-4 [PubMed: 10322142] http://dx.doi.org/10.1016/S0959-437X(99)80026-4
	Kouzarides T. Histone acetylases and deacetylases in cell proliferation. Curr. Opin. Genet. Dev. 9 1999 40-8 [PubMed: 10072350] http://dx.doi.org/10.1016/S0959-437X(99)80006-9
	Finnin MS, Donigian JR, Cohen A, Richon VM, Rifkind RA, Marks PA, Breslow R, Pavletich NP. Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors. Nature 401 1999 188-93 [PubMed: 10490031] http://dx.doi.org/10.1038/43710
	Ayer DE. Histone deacetylases: transcriptional repression with SINers and NuRDs. Trends Cell Biol. 9 1999 193-8 [PubMed: 10322454] http://dx.doi.org/10.1016/S0962-8924(99)01536-6
	Johnson CA, Turner BM. Histone deacetylases: complex transducers of nuclear signals. Semin. Cell Dev. Biol. 10 1999 179-88 [PubMed: 10441071] http://dx.doi.org/10.1006/scdb.1999.0299
	Minucci S, Pelicci PG. Retinoid receptors in health and disease: co-regulators and the chromatin connection. Semin. Cell Dev. Biol. 10 1999 215-25 [PubMed: 10441075] http://dx.doi.org/10.1006/scdb.1999.0303
	Jacobs JJ, van Lohuizen M. Cellular memory of transcriptional states by Polycomb-group proteins. Semin. Cell Dev. Biol. 10 1999 227-35 [PubMed: 10441076] http://dx.doi.org/10.1006/scdb.1999.0304

InterPro 23.1