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Reviewed, UniProtKB/Swiss-Prot Q4QQW4 (HDAC1_RAT)

Last modified June 16, 2009. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Histone deacetylase 1
      Short name=HD1
    EC=3.5.1.98
Gene names
Name: Hdac1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length482 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript 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 By similarity.

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 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 BANP, CBFA2T3 and KDM5B. Interacts with E4F1 and KLF1 By similarity.

Subcellular location

Nucleus By similarity.

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.

Sequence similarities

Belongs to the histone deacetylase family. Type 1 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 482482Histone deacetylase 1
PRO_0000304731

Regions

Region9 – 321313Histone deacetylase

Sites

Active site1411 By similarity

Amino acid modifications

Modified residue2211Phosphotyrosine By similarity
Modified residue3931Phosphoserine By similarity
Modified residue4211Phosphoserine By similarity
Modified residue4231Phosphoserine By similarity
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

Sequences

Sequence LengthMass (Da)Tools
Q4QQW4-1 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: 7F6563C17F5E4844

FASTA48255,093
        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 


MA 

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References

[1]"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: Placenta.

Cross-references

Sequence databases

BC097943 mRNA. Translation: AAH97943.1.
BC107476 mRNA. Translation: AAI07477.1.
IPIIPI00364813.
RefSeqNP_001020580.1.
UniGeneRn.1863

3D structure databases

ModBaseSearch...

PTM databases

PhosphoSiteQ4QQW4.

Genome annotation databases

EnsemblENSRNOG00000009568. Rattus norvegicus. [Contig view]
GeneID297893.
KEGGrno:297893.
NMPDRfig|10116.3.peg.24004.

Organism-specific databases

RGD619975. Hdac1.

Phylogenomic databases

HOVERGENQ4QQW4.

Gene expression databases

ArrayExpressQ4QQW4.

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

NextBio642799.

Entry information

Entry nameHDAC1_RAT
AccessionPrimary (citable) accession number: Q4QQW4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: July 19, 2005
Last modified: June 16, 2009
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

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