Histone deacetylase 2 - Mus musculus (Mouse)

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Reviewed, UniProtKB/Swiss-Prot P70288 (HDAC2_MOUSE)

Last modified November 3, 2009. Version 93. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Histone deacetylase 2
      Short name=HD2
    EC=3.5.1.98
Alternative name(s):
    YY1 transcription factor-binding protein

Gene names

Name:	Hdac2
Synonyms:	Yy1bp

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length	488 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes By similarity. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1.
Catalytic activity	Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.
Subunit structure	Part of the core histone deacetylase (HDAC) complex composed of HDAC1, HDAC2, RBBP4 and RBBP7. The core complex associates with MTA2, MBD3, MTA1L1, CHD3 and CHD4 to form the nucleosome remodeling and histone deacetylation (NuRD) complex, or with SIN3, SAP18 and SAP30 to form the SIN3 HDAC complex. Component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35, AOF2/LSD1, RCOR1/CoREST and PHF21A/BHC80. The BHC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. Part of a complex containing the core histones H2A, H2B, H3 and H4, DEK and unphosphorylated DAXX. Part of a complex containing ATR and CHD4. Forms a heterologous complex at least with YY1. Interacts with ATR, DNMT1, MINT, HDAC7, HDAC10, HCFC1, NRIP1, MJD2A/JHDM3A, PRDM6, SAP30, SETDB1 and SUV39H1. Interacts with the non-histone region of H2AFY. Interacts with PELP1. Component of a mSin3A corepressor complex that contains SIN3A, SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1 and HDAC2 By similarity. Interacts with CBFA2T3. Interacts with CHFR and SAP30L. Interacts (CK2 phosphorylated form) with SP3 By similarity.
Subcellular location	Nucleus.
Sequence similarities	Belongs to the histone deacetylase family. Type 1 subfamily.

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Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Molecular function	Chromatin regulator Hydrolase Repressor
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	hippocampus development Inferred from genetic interaction. Source: MGI histone deacetylation Inferred from genetic interaction. Source: MGI neuron differentiation Inferred from genetic interaction. Source: MGI regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Traceable author statement. Source: UniProtKB heterochromatin Inferred from direct assay. Source: MGI histone deacetylase complex Traceable author statement. Source: UniProtKB replication fork Inferred from direct assay. Source: MGI
Molecular function	histone deacetylase activity Traceable author statement. Source: UniProtKB transcription factor activity Inferred from direct assay. Source: MGI transcription factor binding Traceable author statement. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
Sap30	O88574	1	EBI-302251,EBI-593511

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 488

488

Histone deacetylase 2

PRO_0000114694

Regions

Region

9 – 322

314

Histone deacetylase

Compositional bias

300 – 303

Poly-Gly

Sites

Active site

142

By similarity

Amino acid modifications

Modified residue

N6-acetyllysine By similarity

Modified residue

N6-acetyllysine By similarity

Modified residue

394

Phosphoserine Ref.11 Ref.12 Ref.13

Modified residue

407

Phosphoserine By similarity

Modified residue

422

Phosphoserine Ref.11 Ref.13

Modified residue

424

Phosphoserine Ref.11 Ref.13

Experimental info

Sequence conflict

289

A → V in EDL04897. Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

P70288-1 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: B9843D24A775157C
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FASTA

488

55,302

        10         20         30         40         50         60 
MAYSQGGGKK KVCYYYDGDI GNYYYGQGHP MKPHRIRMTH NLLLNYGLYR KMEIYRPHKA 

        70         80         90        100        110        120 
TAEEMTKYHS DEYIKFLRSI RPDNMSEYSK QMQRFNVGED CPVFDGLFEF CQLSTGGSVA 

       130        140        150        160        170        180 
GAVKLNRQQT DMAVNWAGGL HHAKKSEASG FCYVNDIVLA ILELLKYHQR VLYIDIDIHH 

       190        200        210        220        230        240 
GDGVEEAFYT TDRVMTVSFH KYGEYFPGTG DLRDIGAGKG KYYAVNFPMR DGIDDESYGQ 

       250        260        270        280        290        300 
IFKPIISKVM EMYQPSAVVL QCGADSLSGD RLGCFNLTVK GHAKCVEVAK TFNLPLLMLG 

       310        320        330        340        350        360 
GGGYTIRNVA RCWTYETAVA LDCEIPNELP YNDYFEYFGP DFKLHISPSN MTNQNTPEYM 

       370        380        390        400        410        420 
EKIKQRLFEN LRMLPHAPGV QMQAIPEDAV HEDSGDEDGE DPDKRISIRA SDKRIACDEE 

       430        440        450        460        470        480 
FSDSEDEGEG GRRNVADHKK GAKKARIEED KKETEDKKTD VKEEDKSKDN SGEKTDPKGA 


KSEQLSNP

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global regulator RPD3." Yang W.-M., Inouye C.J., Zeng Y., Bearss D., Seto E. Proc. Natl. Acad. Sci. U.S.A. 93:12845-12850(1996) [PubMed: 8917507] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lymphoma.
[2]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	"SAP30, a component of the mSin3 corepressor complex involved in N-CoR-mediated repression by specific transcription factors." Laherty C.D., Billin A.N., Lavinsky R.M., Yochum G.S., Bush A.C., Sun J.-M., Mullen T.-M., Davie J.R., Rose D.W., Glass C.K., Rosenfeld M.G., Ayer D.E., Eisenman R.N. Mol. Cell 2:33-42(1998) [PubMed: 9702189] [Abstract] Cited for: INTERACTION WITH SAP30.
[5]	"Identification of a nuclear domain with deacetylase activity." Downes M., Ordentlich P., Kao H.-Y., Alvarez J.G.A., Evans R.M. Proc. Natl. Acad. Sci. U.S.A. 97:10330-10335(2000) [PubMed: 10984530] [Abstract] Cited for: INTERACTION WITH HDAC7.
[6]	"ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with multiple histone deacetylases and binds mSin3A through its oligomerization domain." Amann J.M., Nip J., Strom D.K., Lutterbach B., Harada H., Lenny N., Downing J.R., Meyers S., Hiebert S.W. Mol. Cell. Biol. 21:6470-6483(2001) [PubMed: 11533236] [Abstract] Cited for: INTERACTION WITH CBFA2T3.
[7]	"Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases." Vaute O., Nicolas E., Vandel L., Trouche D. Nucleic Acids Res. 30:475-481(2002) [PubMed: 11788710] [Abstract] Cited for: INTERACTION WITH SUV39H1.
[8]	"An ERG (ets-related gene)-associated histone methyltransferase interacts with histone deacetylases 1/2 and transcription co-repressors mSin3A/B." Yang L., Mei Q., Zielinska-Kwiatkowska A., Matsui Y., Blackburn M.L., Benedetti D., Krumm A.A., Taborsky G.J. Jr., Chansky H.A. Biochem. J. 369:651-657(2003) [PubMed: 12398767] [Abstract] Cited for: INTERACTION WITH SETDB1.
[9]	"Structural characterization of the histone variant macroH2A." Chakravarthy S., Gundimella S.K., Caron C., Perche P.-Y., Pehrson J.R., Khochbin S., Luger K. Mol. Cell. Biol. 25:7616-7624(2005) [PubMed: 16107708] [Abstract] Cited for: INTERACTION WITH H2AFY.
[10]	"PRISM/PRDM6, a transcriptional repressor that promotes the proliferative gene program in smooth muscle cells." Davis C.A., Haberland M., Arnold M.A., Sutherland L.B., McDonald O.G., Richardson J.A., Childs G., Harris S., Owens G.K., Olson E.N. Mol. Cell. Biol. 26:2626-2636(2006) [PubMed: 16537907] [Abstract] Cited for: INTERACTION WITH PRDM6.
[11]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 18973353] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND SER-424, MASS SPECTROMETRY.
[12]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed: 19144319] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, MASS SPECTROMETRY. Tissue: Macrophage.
[13]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed: 19131326] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND SER-424, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	U31758 mRNA. Translation: AAC52889.1. CH466540 Genomic DNA. Translation: EDL04897.1. BC138517 mRNA. Translation: AAI38518.1.
IPI	IPI00137668.
RefSeq	NP_032255.2.
UniGene	Mm.19806
3D structure databases
HSSP	HSSP built from PDB template 1C3P based on UniProtKB O67135.
ModBase	Search...
Protein-protein interaction databases
IntAct	P70288. 10 interactions.
STRING	P70288.
PTM databases
PhosphoSite	P70288.
Proteomic databases
PRIDE	P70288.
Genome annotation databases
Ensembl	ENSMUST00000019911; ENSMUSP00000019911; ENSMUSG00000019777; Mus musculus. [Genome view]
GeneID	15182.
KEGG	mmu:15182.
UCSC	uc007evf.1. mouse.
Organism-specific databases
MGI	MGI:1097691. Hdac2.
Phylogenomic databases
HOGENOM	P70288.
HOVERGEN	P70288.
Gene expression databases
ArrayExpress	P70288.
Bgee	P70288.
CleanEx	MM_HDAC2.
Genevestigator	P70288.
GermOnline	ENSMUSG00000019777. Mus musculus.
Family and domain databases
InterPro	IPR000286. His_deacetylse. IPR003084. His_deacetylse_1. [Graphical view]
Gene3D	G3DSA:3.40.800.20. His_deacetylse. 1 hit.
PANTHER	PTHR10625. His_deacetylse. 1 hit. PTHR10625:SF28. His_deacetylse_1. 1 hit.
Pfam	PF00850. Hist_deacetyl. 1 hit. [Graphical view]
PIRSF	PIRSF037913. His_deacetylse_1. 1 hit.
PRINTS	PR01270. HDASUPER. PR01271. HISDACETLASE.
ProtoNet	Search...
Other Resources
SOURCE	Search...

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Entry information

Entry name

HDAC2_MOUSE

Accession

Primary (citable) accession number: P70288
Secondary accession number(s): B2RRP3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	February 1, 1997
Last modified:	November 3, 2009
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents