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Q13547 (HDAC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 174. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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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
Synonyms:RPD3L1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length482 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B. Component a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity. Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-ARNTL/BMAL1 heterodimer. Ref.20 Ref.34 Ref.35 Ref.40 Ref.44 Ref.49 Ref.54

Catalytic activity

Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.

Subunit structure

Interacts with C10orf90/FATS (via its N-terminal): the interaction prevents binding of HDAC1 to CDKN1A/p21 and facilitates the acetylation and stabilization of CDKN1A/p21. Interacts with CDKN1A/p21; the interaction is prevented by binding of C10orf90/FATS facilitating acetylation and stabilization of CDKN1A/p21. Component of a RCOR/GFI/KDM1A/HDAC complex. Interacts directly with GFI1 and GFI1B. 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, KDM1A, 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, SMYD2, SUV39H1, TGIF, TGIF2, UHRF1, UHRF2 and ZNF541. Interacts with the non-histone region of H2AFY. Interacts with HDAC9. Component of a mSin3A corepressor complex that contains SIN3A, SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1 and HDAC2. Interacts with BANP, CBFA2T3 and KDM5B. Interacts with SAP30L. Interacts with E4F1. Interacts with KFL1 and SAMSN1. Interacts with SV40 large T antigen. Interacts with CHFR, PRDM16 and SMAD3. Interacts with SP1; the interaction deacetylates SP1 and regulates its transcriptional activity. Interacts with SP3; the interaction deacetylates SP3 and regulates its transcriptional activity. In vitro, C18 ceramides increase this interaction and the subsequent SP3 deacetylation and SP3-mediated repression of the TERT promoter. Interacts with RB1 and SMARCA4/BRG1. Interacts with TRAF6. Interacts with TSHZ3 (via N-terminus); the interaction is direct. Found in a trimeric complex with APBB1 and TSHZ3; the interaction between HDAC1 and APBB1 is mediated by TSHZ3. Interacts with APEX1; the interaction is not dependent on the acetylated status of APEX1. Interacts with NR4A2/NURR1 and BRMS1. Interacts with TRIM28; the interaction recruits HDAC1 to E2F1 and inhibits its acetylation. Binds to CDK5 complexed to CDK5R1 (p25). Interacts with ZMYND15. Interacts with DDX5. Part of a complex composed of TRIM28, HDAC1, HDAC2 and EHMT2. Interacts with BCL6 and DDIT3/CHOP. Part of a complex containing at least CDYL, MIER1, MIER2, HDAC1 and HDAC2. Interacts with NR1D2 (via C-terminus). Interacts with ZNF431. Interacts with INSM1. Interacts with TSC22D3 isoform 1;this interaction affects HDAC1 activity on MYOG promoter and thus inhibits MYOD1 transcriptional activity By similarity. Interacts with BHLHE40/DEC1. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.28 Ref.30 Ref.31 Ref.32 Ref.34 Ref.35 Ref.36 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45 Ref.47 Ref.49 Ref.53 Ref.54 Ref.55 Ref.61 Ref.62

Subcellular location

Nucleus.

Tissue specificity

Ubiquitous, with higher levels in heart, pancreas and testis, and lower levels in kidney and brain.

Post-translational modification

Sumoylated on Lys-444 and Lys-476; which promotes enzymatic activity. Desumoylated by SENP1. Ref.15 Ref.16 Ref.27

Phosphorylation on Ser-421 and Ser-423 promotes enzymatic activity and interactions with NuRD and SIN3 complexes. Phosphorylated by CDK5. Ref.10

Ubiquitinated by CHFR, leading to its degradation by the proteasome By similarity. Ubiquitinated by KCTD11, leading to proteasomal degradation. Ref.55 Ref.58

Sequence similarities

Belongs to the histone deacetylase family. HD type 1 subfamily.

Ontologies

Keywords
   Biological processBiological rhythms
Host-virus interaction
Transcription
Transcription regulation
   Cellular componentNucleus
   Molecular functionChromatin regulator
Hydrolase
Repressor
   PTMAcetylation
Isopeptide bond
Methylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP-dependent chromatin remodeling

Inferred from direct assay PubMed 16217013. Source: UniProt

Notch signaling pathway

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

chromatin modification

Traceable author statement PubMed 12711221. Source: UniProtKB

chromatin remodeling

Inferred by curator PubMed 16762839PubMed 17827154. Source: BHF-UCL

circadian regulation of gene expression

Inferred from sequence or structural similarity. Source: UniProtKB

embryonic digit morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

epidermal cell differentiation

Inferred from sequence or structural similarity. Source: BHF-UCL

eyelid development in camera-type eye

Inferred from sequence or structural similarity. Source: BHF-UCL

fungiform papilla formation

Inferred from sequence or structural similarity. Source: BHF-UCL

gene expression

Traceable author statement. Source: Reactome

hair follicle placode formation

Inferred from sequence or structural similarity. Source: BHF-UCL

histone H3 deacetylation

Inferred from direct assay PubMed 12590135. Source: BHF-UCL

histone H4 deacetylation

Inferred from direct assay PubMed 12590135. Source: BHF-UCL

histone deacetylation

Inferred from mutant phenotype Ref.55. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation by host of viral transcription

Inferred from mutant phenotype PubMed 16540471. Source: UniProtKB

negative regulation of androgen receptor signaling pathway

Inferred from direct assay PubMed 15919722. Source: BHF-UCL

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of cell cycle

Traceable author statement. Source: Reactome

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 18854353. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 18974119. Source: UniProtKB

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

odontogenesis of dentin-containing tooth

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 18347167. Source: BHF-UCL

positive regulation of receptor biosynthetic process

Inferred from mutant phenotype PubMed 18316616. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 16762839. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 16762839. Source: BHF-UCL

protein deacetylation

Inferred from direct assay PubMed 17172643. Source: UniProtKB

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription, DNA-templated

Traceable author statement. Source: Reactome

transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentNuRD complex

Inferred from direct assay PubMed 19644445. Source: UniProtKB

Sin3 complex

Inferred from direct assay PubMed 17827154. Source: BHF-UCL

cytoplasm

Traceable author statement PubMed 12711221. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 18326024. Source: UniProtKB

histone deacetylase complex

Traceable author statement PubMed 12711221. Source: UniProtKB

nuclear chromatin

Inferred from direct assay PubMed 22926524. Source: BHF-UCL

nucleoplasm

Inferred from direct assay PubMed 22926524. Source: BHF-UCL

nucleus

Inferred from direct assay Ref.6. Source: UniProtKB

protein complex

Inferred from direct assay PubMed 16217013. Source: UniProt

   Molecular_functionNAD-dependent histone deacetylase activity (H3-K14 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H3-K18 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H3-K9 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H4-K16 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

RNA polymerase II repressing transcription factor binding

Inferred from physical interaction PubMed 22926524. Source: BHF-UCL

RNA polymerase II transcription corepressor activity

Inferred from direct assay PubMed 15919722. Source: BHF-UCL

activating transcription factor binding

Inferred from physical interaction PubMed 20590529. Source: UniProtKB

core promoter binding

Inferred from direct assay PubMed 18974119. Source: UniProtKB

deacetylase activity

Inferred from sequence or structural similarity. Source: UniProtKB

enzyme binding

Inferred from physical interaction PubMed 11062478PubMed 11136718PubMed 11641274. Source: UniProtKB

histone deacetylase activity

Inferred from mutant phenotype Ref.44Ref.55. Source: UniProtKB

histone deacetylase binding

Inferred from physical interaction PubMed 12590135. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.6Ref.5Ref.7PubMed 11259576PubMed 11553631PubMed 11641274PubMed 11863372PubMed 12176973PubMed 12202768Ref.18PubMed 14752048PubMed 15140878PubMed 16306601PubMed 16540471Ref.35PubMed 17172643PubMed 17636019Ref.40Ref.41Ref.44Ref.45PubMed 18722353Ref.53Ref.49Ref.55Ref.54PubMed 19505873PubMed 20363964Ref.61. Source: UniProtKB

protein deacetylase activity

Inferred from direct assay PubMed 17172643. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.2. Source: ProtInc

transcription factor binding

Inferred from physical interaction PubMed 15509593Ref.32PubMed 18974119. Source: UniProtKB

transcription regulatory region sequence-specific DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 482482Histone deacetylase 1
PRO_0000114687

Regions

Region9 – 321313Histone deacetylase

Sites

Active site1411

Amino acid modifications

Modified residue741N6-acetyllysine Ref.57
Modified residue2201N6-acetyllysine Ref.57
Modified residue3931Phosphoserine Ref.33 Ref.37 Ref.46 Ref.56 Ref.59 Ref.63
Modified residue4211Phosphoserine; by CK2 Ref.10 Ref.33 Ref.51 Ref.56 Ref.59 Ref.63
Modified residue4231Phosphoserine; by CK2 Ref.10 Ref.33 Ref.51 Ref.56 Ref.59 Ref.63
Modified residue4321N6-methylated lysine; by EHMT2 Ref.48
Cross-link444Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.16
Cross-link476Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.16

Experimental info

Mutagenesis1411H → A: Abolishes histone deacetylase activity. Ref.55
Mutagenesis2871F → Y: Abolishes interaction with CHFR; when associated with I-297. Ref.55
Mutagenesis2971M → I: Abolishes interaction with CHFR; when associated with Y-287. Ref.55
Mutagenesis391 – 48292Missing: Strongly decreases deacetylase activity, and disrupts interaction with NuRD and SIN3 complexes.
Mutagenesis4211S → A: Strongly decreases deacetylase activity, and disrupts interaction with NuRD and SIN3 complexes. Ref.10
Mutagenesis4211S → D or E: Slightly decreases deacetylase activity. Ref.10
Mutagenesis4231S → A: Strongly decreases deacetylase activity, and disrupts interaction with NuRD and SIN3 complexes. Ref.10
Mutagenesis4231S → D or E: Decreases deacetylase activity. Ref.10
Mutagenesis4241E → A: Slightly decreases deacetylase activity, no effect on interaction with NuRD and SIN3 complexes.
Mutagenesis4251E → A: No effect on deacetylase activity, no effect on interaction with NuRD and SIN3 complexes.
Mutagenesis4261E → A: Decreases deacetylase activity, and disrupts interaction with NuRD and SIN3 complexes.
Sequence conflict3121W → R in BAA08909. Ref.2

Secondary structure

............................................................... 482
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q13547 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 4D35B7C1ED7838D6

FASTA48255,103
        10         20         30         40         50         60 
MAQTQGTRRK 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 EESGDEDEDD PDKRISICSS DKRIACEEEF 

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


LA 

« Hide

References

« Hide 'large scale' references
[1]"A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p."
Taunton J., Hassig C.A., Schreiber S.L.
Science 272:408-411(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: T-cell.
[2]"Isolation and mapping of a human gene (RPD3L1) that is homologous to RPD3, a transcription factor in Saccharomyces cerevisiae."
Furukawa Y., Kawakami T., Sudo K., Inazawa J., Matsumine A., Akiyama T., Nakamura Y.
Cytogenet. Cell Genet. 73:130-133(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fetal lung.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[4]"MEF-2 function is modified by a novel co-repressor, MITR."
Sparrow D.B., Miska E.A., Langley E., Reynaud-Deonauth S., Kotecha S., Towers N., Spohr G., Kouzarides T., Mohun T.J.
EMBO J. 18:5085-5098(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HDAC9.
[5]"BCoR, a novel corepressor involved in BCL-6 repression."
Huynh K.D., Fischle W., Verdin E., Bardwell V.J.
Genes Dev. 14:1810-1823(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BCOR.
[6]"HDAC1, a histone deacetylase, forms a complex with Hus1 and Rad9, two G2/M checkpoint Rad proteins."
Cai R.L., Yan-Neale Y., Cueto M.A., Xu H., Cohen D.
J. Biol. Chem. 275:27909-27916(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH THE 9-1-1 COMPLEX AND HUS1.
[7]"Receptor-interacting protein 140 directly recruits histone deacetylases for gene silencing."
Wei L.-N., Hu X., Chandra D., Seto E., Farooqui M.
J. Biol. Chem. 275:40782-40787(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NRIP1.
[8]"Sequestration and inhibition of Daxx-mediated transcriptional repression by PML."
Li H., Leo C., Zhu J., Wu X., O'Neil J., Park E.-J., Chen J.D.
Mol. Cell. Biol. 20:1784-1796(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DAXX.
[9]"Identification of a transcriptional repressor related to the noncatalytic domain of histone deacetylases 4 and 5."
Zhou X., Richon V.M., Rifkind R.A., Marks P.A.
Proc. Natl. Acad. Sci. U.S.A. 97:1056-1061(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HDAC9.
[10]"Histone deacetylase 1 phosphorylation promotes enzymatic activity and complex formation."
Pflum M.K.H., Tong J.K., Lane W.S., Schreiber S.L.
J. Biol. Chem. 276:47733-47741(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-421 AND SER-423, MUTAGENESIS OF SER-421 AND SER-423, IDENTIFICATION BY MASS SPECTROMETRY.
[11]"Sharp, an inducible cofactor that integrates nuclear receptor repression and activation."
Shi Y., Downes M., Xie W., Kao H.-Y., Ordentlich P., Tsai C.-C., Hon M., Evans R.M.
Genes Dev. 15:1140-1151(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MINT.
[12]"Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1."
Humphrey G.W., Wang Y., Russanova V.R., Hirai T., Qin J., Nakatani Y., Howard B.H.
J. Biol. Chem. 276:6817-6824(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MBD2 AND MBD3.
[13]"TGIF2 interacts with histone deacetylase 1 and represses transcription."
Melhuish T.A., Gallo C.M., Wotton D.
J. Biol. Chem. 276:32109-32114(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TGIF2.
[14]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CBFA2T3.
[15]"The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase."
Kirsh O., Seeler J.-S., Pichler A., Gast A., Mueller S., Miska E., Mathieu M., Harel-Bellan A., Kouzarides T., Melchior F., Dejean A.
EMBO J. 21:2682-2691(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION.
[16]"SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its biological activities."
David G., Neptune M.A., DePinho R.A.
J. Biol. Chem. 277:23658-23663(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-444 AND LYS-476.
[17]"Role of acetylated human AP-endonuclease (APE1/Ref-1) in regulation of the parathyroid hormone gene."
Bhakat K.K., Izumi T., Yang S.H., Hazra T.K., Mitra S.
EMBO J. 22:6299-6309(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APEX1.
[18]"Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1."
Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W.
Genes Dev. 17:896-911(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HCFC1.
[19]"A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes."
Hakimi M.-A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R.
J. Biol. Chem. 278:7234-7239(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE BHC COMPLEX WITH PHF21A; HDAC2; HMG20B; KDM1A; RCOR1; ZMYM2; ZNF217; ZMYM3; KIAA0182 AND GTF2I.
[20]"Acetylated SP3 is a transcriptional activator."
Ammanamanchi S., Freeman J.W., Brattain M.G.
J. Biol. Chem. 278:35775-35780(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SP3, FUNCTION.
[21]"Human MI-ER1 alpha and beta function as transcriptional repressors by recruitment of histone deacetylase 1 to their conserved ELM2 domain."
Ding Z., Gillespie L.L., Paterno G.D.
Mol. Cell. Biol. 23:250-258(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MIER1.
[22]"Identification and characterization of three new components of the mSin3A corepressor complex."
Fleischer T.C., Yun U.J., Ayer D.E.
Mol. Cell. Biol. 23:3456-3467(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MSIN3A COREPRESSOR COMPLEX WITH SIN3A; SAP130; SUDS3; ARID4B; HDAC1 AND HDAC2.
[23]"Modulation of p120E4F transcriptional activity by the Gam1 adenoviral early protein."
Colombo R., Draetta G.F., Chiocca S.
Oncogene 22:2541-2547(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH E4F1.
[24]"Identification of a novel BRMS1-homologue protein p40 as a component of the mSin3A/p33(ING1b)/HDAC1 deacetylase complex."
Nikolaev A.Y., Papanikolaou N.A., Li M., Qin J., Gu W.
Biochem. Biophys. Res. Commun. 323:1216-1222(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BRMS1L.
[25]"MTA3 and the Mi-2/NuRD complex regulate cell fate during B lymphocyte differentiation."
Fujita N., Jaye D.L., Geigerman C., Akyildiz A., Mooney M.R., Boss J.M., Wade P.A.
Cell 119:75-86(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BCL6, IDENTIFICATION IN THE NURD COMPLEX.
[26]"Site-specific acetylation of the fetal globin activator NF-E4 prevents its ubiquitination and regulates its interaction with the histone deacetylase, HDAC1."
Zhao Q., Cumming H., Cerruti L., Cunningham J.M., Jane S.M.
J. Biol. Chem. 279:41477-41486(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NFE4.
[27]"SENP1 enhances androgen receptor-dependent transcription through desumoylation of histone deacetylase 1."
Cheng J., Wang D., Wang Z., Yeh E.T.H.
Mol. Cell. Biol. 24:6021-6028(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DESUMOYLATION BY SENP1.
[28]"ICBP90, an E2F-1 target, recruits HDAC1 and binds to methyl-CpG through its SRA domain."
Unoki M., Nishidate T., Nakamura Y.
Oncogene 23:7601-7610(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UHRF1 AND UHRF2.
[29]"NuRD and SIN3 histone deacetylase complexes in development."
Ahringer J.
Trends Genet. 16:351-356(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON DEACETYLASE COMPLEXES.
[30]"Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein."
Gray S.G., Iglesias A.H., Lizcano F., Villanueva R., Camelo S., Jingu H., Teh B.T., Koibuchi N., Chin W.W., Kokkotou E., Dangond F.
J. Biol. Chem. 280:28507-28518(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KDM4A.
[31]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BANP.
[32]"INSM1 functions as a transcriptional repressor of the neuroD/beta2 gene through the recruitment of cyclin D1 and histone deacetylases."
Liu W.D., Wang H.W., Muguira M., Breslin M.B., Lan M.S.
Biochem. J. 397:169-177(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH INSM1.
[33]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-421 AND SER-423, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[34]"Sp1 deacetylation induced by phorbol ester recruits p300 to activate 12(S)-lipoxygenase gene transcription."
Hung J.J., Wang Y.T., Chang W.C.
Mol. Cell. Biol. 26:1770-1785(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SP1, FUNCTION.
[35]"Breast cancer metastasis suppressor 1 functions as a corepressor by enhancing histone deacetylase 1-mediated deacetylation of RelA/p65 and promoting apoptosis."
Liu Y., Smith P.W., Jones D.R.
Mol. Cell. Biol. 26:8683-8696(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH BRMS1.
[36]"SAP30L interacts with members of the Sin3A corepressor complex and targets Sin3A to the nucleolus."
Viiri K.M., Korkeamaeki H., Kukkonen M.K., Nieminen L.K., Lindfors K., Peterson P., Maeki M., Kainulainen H., Lohi O.
Nucleic Acids Res. 34:3288-3298(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SAP30L.
[37]"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Prostate cancer.
[38]"Mechanisms of ceramide-mediated repression of the human telomerase reverse transcriptase promoter via deacetylation of Sp3 by histone deacetylase 1."
Wooten-Blanks L.G., Song P., Senkal C.E., Ogretmen B.
FASEB J. 21:3386-3397(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SP3.
[39]"Breast cancer associated transcriptional repressor PLU-1/JARID1B interacts directly with histone deacetylases."
Barrett A., Santangelo S., Tan K., Catchpole S., Roberts K., Spencer-Dene B., Hall D., Scibetta A., Burchell J., Verdin E., Freemont P., Taylor-Papadimitriou J.
Int. J. Cancer 121:265-275(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KDM5B.
[40]"Regulation of E2F1 function by the nuclear corepressor KAP1."
Wang C., Rauscher F.J. III, Cress W.D., Chen J.
J. Biol. Chem. 282:29902-29909(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRIM28, FUNCTION.
[41]"Critical and functional regulation of CHOP (C/EBP homologous protein) through the N-terminal portion."
Ohoka N., Hattori T., Kitagawa M., Onozaki K., Hayashi H.
J. Biol. Chem. 282:35687-35694(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DDIT3.
[42]"Involvement of chromatin and histone deacetylation in SV40 T antigen transcription regulation."
Valls E., Blanco-Garcia N., Aquizu N., Piedra D., Estaras C., de la Cruz X., Martinez-Balbas M.A.
Nucleic Acids Res. 35:1958-1968(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SV40 LARGE T ANTIGEN.
[43]"SUMO modification of the DEAD box protein p68 modulates its transcriptional activity and promotes its interaction with HDAC1."
Jacobs A.M., Nicol S.M., Hislop R.G., Jaffray E.G., Hay R.T., Fuller-Pace F.V.
Oncogene 26:5866-5876(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DDX5.
[44]"The orphan nuclear receptor Rev-erbbeta recruits Tip60 and HDAC1 to regulate apolipoprotein CIII promoter."
Wang J., Liu N., Liu Z., Li Y., Song C., Yuan H., Li Y.Y., Zhao X., Lu H.
Biochim. Biophys. Acta 1783:224-236(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NR1D2.
[45]"Nuclear tumor necrosis factor receptor-associated factor 6 in lymphoid cells negatively regulates c-Myb-mediated transactivation through small ubiquitin-related modifier-1 modification."
Pham L.V., Zhou H.J., Lin-Lee Y.C., Tamayo A.T., Yoshimura L.C., Fu L., Darnay B.G., Ford R.J.
J. Biol. Chem. 283:5081-5089(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRAF6.
[46]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[47]"CDYL bridges REST and histone methyltransferases for gene repression and suppression of cellular transformation."
Mulligan P., Westbrook T.F., Ottinger M., Pavlova N., Chang B., Macia E., Shi Y.J., Barretina J., Liu J., Howley P.M., Elledge S.J., Shi Y.
Mol. Cell 32:718-726(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH CDYL; MIER1; MIER2 AND HDAC2.
[48]"Protein lysine methyltransferase G9a acts on non-histone targets."
Rathert P., Dhayalan A., Murakami M., Zhang X., Tamas R., Jurkowska R., Komatsu Y., Shinkai Y., Cheng X., Jeltsch A.
Nat. Chem. Biol. 4:344-346(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-432.
[49]"A calcium-dependent switch in a CREST-BRG1 complex regulates activity-dependent gene expression."
Qiu Z., Ghosh A.
Neuron 60:775-787(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RB1 AND SMARCA4/BRG1.
[50]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[51]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421 AND SER-423, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[52]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[53]"SKI and MEL1 cooperate to inhibit transforming growth factor-beta signal in gastric cancer cells."
Takahata M., Inoue Y., Tsuda H., Imoto I., Koinuma D., Hayashi M., Ichikura T., Yamori T., Nagasaki K., Yoshida M., Matsuoka M., Morishita K., Yuki K., Hanyu A., Miyazawa K., Inazawa J., Miyazono K., Imamura T.
J. Biol. Chem. 284:3334-3344(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRDM16 AND SMAD3.
[54]"FE65 binds Teashirt, inhibiting expression of the primate-specific caspase-4."
Kajiwara Y., Akram A., Katsel P., Haroutunian V., Schmeidler J., Beecham G., Haines J.L., Pericak-Vance M.A., Buxbaum J.D.
PLoS ONE 4:E5071-E5071(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TSHZ3, IDENTIFICATION IN A TRIMERIC COMPLEX WITH APBB1 AND TSHZ3.
[55]"Chfr is linked to tumour metastasis through the downregulation of HDAC1."
Oh Y.M., Kwon Y.E., Kim J.M., Bae S.J., Lee B.K., Yoo S.J., Chung C.H., Deshaies R.J., Seol J.H.
Nat. Cell Biol. 11:295-302(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, INTERACTION WITH CHFR, MUTAGENESIS OF HIS-141; PHE-287 AND MET-297.
[56]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-421 AND SER-423, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[57]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-74 AND LYS-220, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[58]"Histone deacetylase and Cullin3-REN(KCTD11) ubiquitin ligase interplay regulates Hedgehog signalling through Gli acetylation."
Canettieri G., Di Marcotullio L., Greco A., Coni S., Antonucci L., Infante P., Pietrosanti L., De Smaele E., Ferretti E., Miele E., Pelloni M., De Simone G., Pedone E.M., Gallinari P., Giorgi A., Steinkuhler C., Vitagliano L., Pedone C. expand/collapse author list , Schinin M.E., Screpanti I., Gulino A.
Nat. Cell Biol. 12:132-142(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION BY KCTD11.
[59]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-421 AND SER-423, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[60]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[61]"Maintenance of silent chromatin through replication requires SWI/SNF-like chromatin remodeler SMARCAD1."
Rowbotham S.P., Barki L., Neves-Costa A., Santos F., Dean W., Hawkes N., Choudhary P., Will W.R., Webster J., Oxley D., Green C.M., Varga-Weisz P., Mermoud J.E.
Mol. Cell 42:285-296(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SMARCAD1.
[62]"SUMOylation of DEC1 protein regulates its transcriptional activity and enhances its stability."
Hong Y., Xing X., Li S., Bi H., Yang C., Zhao F., Liu Y., Ao X., Chang A.K., Wu H.
PLoS ONE 6:E23046-E23046(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BHLHE40/DEC1.
[63]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-421 AND SER-423, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U50079 mRNA. Translation: AAC50475.1.
D50405 mRNA. Translation: BAA08909.1.
BC000301 mRNA. Translation: AAH00301.1.
CCDSCCDS360.1.
RefSeqNP_004955.2. NM_004964.2.
UniGeneHs.88556.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TYImodel-A1-482[»]
4BKXX-ray3.00B1-482[»]
ProteinModelPortalQ13547.
SMRQ13547. Positions 8-376.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109315. 541 interactions.
DIPDIP-24184N.
IntActQ13547. 166 interactions.
MINTMINT-90475.
STRING9606.ENSP00000362649.

Chemistry

BindingDBQ13547.
ChEMBLCHEMBL2111429.
DrugBankDB02546. Vorinostat.
GuidetoPHARMACOLOGY2658.

PTM databases

PhosphoSiteQ13547.

Polymorphism databases

DMDM2498443.

Proteomic databases

MaxQBQ13547.
PaxDbQ13547.
PeptideAtlasQ13547.
PRIDEQ13547.

Protocols and materials databases

DNASU3065.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373548; ENSP00000362649; ENSG00000116478.
GeneID3065.
KEGGhsa:3065.
UCSCuc001bvb.1. human.

Organism-specific databases

CTD3065.
GeneCardsGC01P032757.
HGNCHGNC:4852. HDAC1.
HPACAB005017.
HPA029693.
MIM601241. gene.
neXtProtNX_Q13547.
PharmGKBPA29226.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0123.
HOGENOMHOG000225180.
HOVERGENHBG057112.
InParanoidQ13547.
KOK06067.
OMALTQGTKR.
OrthoDBEOG7DNNTW.
PhylomeDBQ13547.
TreeFamTF106171.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_604. Hemostasis.
REACT_71. Gene Expression.
SABIO-RKQ13547.

Gene expression databases

ArrayExpressQ13547.
BgeeQ13547.
CleanExHS_HDAC1.
GenevestigatorQ13547.

Family and domain databases

Gene3D3.40.800.20. 1 hit.
InterProIPR000286. His_deacetylse.
IPR003084. His_deacetylse_1.
IPR023801. His_deacetylse_dom.
[Graphical view]
PANTHERPTHR10625. PTHR10625. 1 hit.
PfamPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFPIRSF037913. His_deacetylse_1. 1 hit.
PRINTSPR01270. HDASUPER.
PR01271. HISDACETLASE.
ProtoNetSearch...

Other

ChiTaRSHDAC1. human.
GeneWikiHDAC1.
GenomeRNAi3065.
NextBio12125.
PROQ13547.
SOURCESearch...

Entry information

Entry nameHDAC1_HUMAN
AccessionPrimary (citable) accession number: Q13547
Secondary accession number(s): Q92534
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 174 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM