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Reviewed, UniProtKB/Swiss-Prot O09106 (HDAC1_MOUSE)

Last modified February 9, 2010. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
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 namesRecommended name:
    Histone deacetylase 1
      Short name=HD1
    EC=3.5.1.98
Gene names
Name: Hdac1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length482 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Deacetylates SP proteins, SP1 and SP3, and regulates their function. Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons. Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation By similarity. Ref.15

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, MBD2, 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. Associates with the 9-1-1 complex; interacts with HUS1. Found in a complex with DNMT3A and HDAC7. Interacts with BAZ2A/TIP5, BCOR, BRMS1L, DAXX, DNMT1, EP300, HCFC1, NFE4, PCAF, PHB2, MIER1, KDM4A, MINT, NRIP1, PRDM6, RERE, SETDB1, SUV39H1, TGIF, TGIF2, UHRF1, UHRF2 and ZNF541. Interacts with the non-histone region of H2AFY. Component of a mSin3A corepressor complex that contains SIN3A, SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1 and HDAC2. Interacts with KDM5B By similarity. Interacts with BANP and CBFA2T3. Interacts with SAP30L and KLF1. Interacts with E4F1. Interacts with CHFR, PRDM16, SP1, SP3, and SMAD3. Interacts with RB1 and SMARCA4/BRG1. Interacts with TRAF6 By similarity. Ref.15 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23

Subcellular location

Nucleus.

Tissue specificity

Widely expressed with higher levels in thymus and testis and lower levels in liver. Present in muscle (at protein level). Ref.20

Induction

By interleukin-2.

Post-translational modification

Sumoylated on Lys-444 and Lys-476; which promotes enzymatic activity. Desumoylated by SENP1 By similarity.

Phosphorylation on Ser-421 and Ser-423 promotes enzymatic activity and interactions with NuRD and SIN3 complexes By similarity.

Ubiquitinated by CHFR, leading to its degradation by the proteasome By similarity.

Sequence similarities

Belongs to the histone deacetylase family. Type 1 subfamily.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 482482Histone deacetylase 1
PRO_0000114688

Regions

Region9 – 321313Histone deacetylase

Sites

Active site1411 By similarity

Amino acid modifications

Modified residue741N6-acetyllysine By similarity
Modified residue2201N6-acetyllysine By similarity
Modified residue2211Phosphotyrosine By similarity
Modified residue3931Phosphoserine Ref.24 Ref.25 Ref.26
Modified residue4061Phosphoserine By similarity
Modified residue4211Phosphoserine Ref.24 Ref.25 Ref.26
Modified residue4231Phosphoserine Ref.24 Ref.25 Ref.26
Cross-link444Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link476Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

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Sequences

Sequence LengthMass (Da)Tools
O09106-1 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 7F64D3C17F5E4844

FASTA48255,075
        10         20         30         40         50         60 
MAQTQGTKRK VCYYYDGDVG NYYYGQGHPM KPHRIRMTHN LLLNYGLYRK MEIYRPHKAN 

        70         80         90        100        110        120 
AEEMTKYHSD DYIKFLRSIR PDNMSEYSKQ MQRFNVGEDC PVFDGLFEFC QLSTGGSVAS 

       130        140        150        160        170        180 
AVKLNKQQTD IAVNWAGGLH HAKKSEASGF CYVNDIVLAI LELLKYHQRV LYIDIDIHHG 

       190        200        210        220        230        240 
DGVEEAFYTT DRVMTVSFHK YGEYFPGTGD LRDIGAGKGK YYAVNYPLRD GIDDESYEAI 

       250        260        270        280        290        300 
FKPVMSKVME MFQPSAVVLQ CGSDSLSGDR LGCFNLTIKG HAKCVEFVKS FNLPMLMLGG 

       310        320        330        340        350        360 
GGYTIRNVAR CWTYETAVAL DTEIPNELPY NDYFEYFGPD FKLHISPSNM TNQNTNEYLE 

       370        380        390        400        410        420 
KIKQRLFENL RMLPHAPGVQ MQAIPEDAIP EESGDEDEED PDKRISICSS DKRIACEEEF 

       430        440        450        460        470        480 
SDSDEEGEGG RKNSSNFKKA KRVKTEDEKE KDPEEKKEVT EEEKTKEEKP EAKGVKEEVK 


LA

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References

« Hide 'large scale' references
[1]"Identification of mouse histone deacetylase 1 as a growth factor-inducible gene."
Bartl S., Taplick J., Lagger G., Khier H., Kuchler K., Seiser C.
Mol. Cell. Biol. 17:5033-5043(1997) [PubMed: 9271381] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fibroblast.
[2]Johnson C.A.
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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.
[4]"DNA methyltransferase Dnmt1 associates with histone deacetylase activity."
Fuks F., Burgers W.A., Brehm A., Hughes-Davies L., Kouzarides T.
Nat. Genet. 24:88-91(2000) [PubMed: 10615135] [Abstract]
Cited for: INTERACTION WITH DNMT1.
[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]"Association of COOH-terminal-binding protein (CtBP) and MEF2-interacting transcription repressor (MITR) contributes to transcriptional repression of the MEF2 transcription factor."
Zhang C.L., McKinsey T.A., Lu J.R., Olson E.N.
J. Biol. Chem. 276:35-39(2001) [PubMed: 11022042] [Abstract]
Cited for: INTERACTION WITH HDAC9.
[7]"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.
[8]"The chromatin remodeling complex NoRC targets HDAC1 to the ribosomal gene promoter and represses RNA polymerase I transcription."
Zhou Y., Santoro R., Grummt I.
EMBO J. 21:4632-4640(2002) [PubMed: 12198165] [Abstract]
Cited for: INTERACTION WITH BAZ2A.
[9]"Identification of mammalian Sds3 as an integral component of the Sin3/histone deacetylase corepressor complex."
Alland L., David G., Shen-Li H., Potes J., Muhle R., Lee H.-C., Hou H. Jr., Chen K., DePinho R.A.
Mol. Cell. Biol. 22:2743-2750(2002) [PubMed: 11909966] [Abstract]
Cited for: INTERACTION WITH SIN3B.
[10]"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.
[11]"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.
[12]"Biochemical fractionation reveals association of DNA methyltransferase (Dnmt) 3b with Dnmt1 and that of Dnmt 3a with a histone H3 methyltransferase and Hdac1."
Datta J., Ghoshal K., Sharma S.M., Tajima S., Jacob S.T.
J. Cell. Biochem. 88:855-864(2003) [PubMed: 12616525] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH DNMT3A.
[13]"Atrophin 2 recruits histone deacetylase and is required for the function of multiple signaling centers during mouse embryogenesis."
Zoltewicz J.S., Stewart N.J., Leung R., Peterson A.S.
Development 131:3-14(2004) [PubMed: 14645126] [Abstract]
Cited for: INTERACTION WITH RERE.
[14]"Transcriptional regulation by the repressor of estrogen receptor activity via recruitment of histone deacetylases."
Kurtev V., Margueron R., Kroboth K., Ogris E., Cavailles V., Seiser C.
J. Biol. Chem. 279:24834-24843(2004) [PubMed: 15140878] [Abstract]
Cited for: INTERACTION WITH PHB2.
[15]"Stage-specific repression by the EKLF transcriptional activator."
Chen X., Bieker J.J.
Mol. Cell. Biol. 24:10416-10424(2004) [PubMed: 15542849] [Abstract]
Cited for: INTERACTION WITH KLF1, FUNCTION.
[16]"Multiple domains of the receptor-interacting protein 140 contribute to transcription inhibition."
Castet A., Boulahtouf A., Versini G., Bonnet S., Augereau P., Vignon F., Khochbin S., Jalaguier S., Cavailles V.
Nucleic Acids Res. 32:1957-1966(2004) [PubMed: 15060175] [Abstract]
Cited for: INTERACTION WITH NRIP1.
[17]"The PHD finger/bromodomain of NoRC interacts with acetylated histone H4K16 and is sufficient for rDNA silencing."
Zhou Y., Grummt I.
Curr. Biol. 15:1434-1438(2005) [PubMed: 16085498] [Abstract]
Cited for: INTERACTION WITH BAZ2A.
[18]"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.
[19]"Tumor suppressor SMAR1 mediates cyclin D1 repression by recruitment of the SIN3/histone deacetylase 1 complex."
Rampalli S., Pavithra L., Bhatt A., Kundu T.K., Chattopadhyay S.
Mol. Cell. Biol. 25:8415-8429(2005) [PubMed: 16166625] [Abstract]
Cited for: INTERACTION WITH BANP.
[20]"Histone deacetylase 9 couples neuronal activity to muscle chromatin acetylation and gene expression."
Mejat A., Ramond F., Bassel-Duby R., Khochbin S., Olson E.N., Schaeffer L.
Nat. Neurosci. 8:313-321(2005) [PubMed: 15711539] [Abstract]
Cited for: INTERACTION WITH HDAC9, TISSUE SPECIFICITY.
[21]"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.
[22]"Neuroprotection by histone deacetylase-related protein."
Morrison B.E., Majdzadeh N., Zhang X., Lyles A., Bassel-Duby R., Olson E.N., D'Mello S.R.
Mol. Cell. Biol. 26:3550-3564(2006) [PubMed: 16611996] [Abstract]
Cited for: INTERACTION WITH HDAC9.
[23]"A novel germ cell-specific protein, SHIP1, forms a complex with chromatin remodeling activity during spermatogenesis."
Choi E., Han C., Park I., Lee B., Jin S., Choi H., Kim do H., Park Z.Y., Eddy E.M., Cho C.
J. Biol. Chem. 283:35283-35294(2008) [PubMed: 18849567] [Abstract]
Cited for: INTERACTION WITH ZNF541.
[24]"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-393; SER-421 AND SER-423, MASS SPECTROMETRY.
[25]"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-393; SER-421 AND SER-423, MASS SPECTROMETRY.
Tissue: Macrophage.
[26]"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-393; SER-421 AND SER-423, MASS SPECTROMETRY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X98207 mRNA. Translation: CAA66870.1.
U80780 mRNA. Translation: AAB68398.1.
IPIIPI00114232.
RefSeqNP_032254.1.
UniGeneMm.202504
Mm.391033

3D structure databases

SMRO09106. Positions 12-373.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-31499N.
IntActO09106. 11 interactions.
STRINGO09106.

PTM databases

PhosphoSiteO09106.

Proteomic databases

PRIDEO09106.

Genome annotation databases

EnsemblENSMUST00000102597; ENSMUSP00000099657; ENSMUSG00000028800; Mus musculus. [Genome view]
GeneID433759.
KEGGmmu:433759.
UCSCuc008uxg.1. mouse.

Organism-specific databases

CTD433759.
MGIMGI:108086. Hdac1.

Phylogenomic databases

eggNOGroNOG14641.
HOGENOMHBG396919.
HOVERGENO09106.
InParanoidO09106.
OMAIFKPVIS.
OrthoDBEOG94XN2W.
PhylomeDBO09106.

Gene expression databases

ArrayExpressO09106.
BgeeO09106.
CleanExMM_HDAC1.
GenevestigatorO09106.
GermOnlineENSMUSG00000061062. Mus musculus.

Family and domain databases

InterProIPR000286. His_deacetylse.
IPR003084. His_deacetylse_1.
[Graphical view]
Gene3DG3DSA:3.40.800.20. His_deacetylse. 1 hit.
PANTHERPTHR10625. His_deacetylse. 1 hit.
PTHR10625:SF28. His_deacetylse_1. 1 hit.
PfamPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFPIRSF037913. His_deacetylse_1. 1 hit.
PRINTSPR01270. HDASUPER.
PR01271. HISDACETLASE.
ProtoNetSearch...

Other Resources

NextBio408961.
SOURCESearch...

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Entry information

Entry nameHDAC1_MOUSE
AccessionPrimary (citable) accession number: O09106
Secondary accession number(s): P97476
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: February 9, 2010
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents