Histone deacetylase 1 - Rattus norvegicus (Rat)

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Q4QQW4 (HDAC1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 73. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Histone deacetylase 1
Short name=HD1
EC=3.5.1.98

Gene names

Name:

Hdac1

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	482 AA.
Sequence status	Complete.
Protein existence	Evidence 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. 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 of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development 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, 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. 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, SAMSN1 and KLF1. Interacts with CHFR, PRDM16, SP1, SP3, and SMAD3. 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 By similarity. Interacts with NR4A2/NURR1 and BRMS1. Interacts with C10orf90/FATS (via its N-terminal); the interaction prevents binding of HDAC1 to the 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. Binds to CDK5 complexed to CDK5R (p25). Component of a RCOR/GFI/KDM1A/HDAC complex. Interacts with GFI1 and GFI1B By similarity. Interacts with ZMYND15. Interacts with DDX5 By similarity. Part of a complex composed of TRIM28, HDAC1, HDAC2 and EHMT2 By similarity. Interacts with DDIT3/CHOP 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. Phosphorylated by CDK5 By similarity. Ubiquitinated by CHFR and KCTD11, leading to its degradation by the proteasome By similarity.
Sequence similarities	Belongs to the histone deacetylase family. HD type 1 subfamily.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Molecular function	Chromatin regulator Hydrolase Repressor
PTM	Acetylation Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone H3 deacetylation Inferred from electronic annotation. Source: GOC histone H4 deacetylation Inferred from electronic annotation. Source: GOC regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	NAD-dependent histone deacetylase activity (H3-K14 specific) Inferred from electronic annotation. Source: EC NAD-dependent histone deacetylase activity (H3-K18 specific) Inferred from electronic annotation. Source: EC NAD-dependent histone deacetylase activity (H3-K9 specific) Inferred from electronic annotation. Source: EC NAD-dependent histone deacetylase activity (H4-K16 specific) Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 482

482

Histone deacetylase 1

PRO_0000304731

Regions

Region

9 – 321

313

Histone deacetylase

Sites

Active site

141

By similarity

Amino acid modifications

Modified residue

N6-acetyllysine By similarity

Modified residue

220

N6-acetyllysine By similarity

Modified residue

393

Phosphoserine By similarity

Modified residue

421

Phosphoserine By similarity

Modified residue

423

Phosphoserine By similarity

Modified residue

432

N6-methylated lysine; by EHMT2 By similarity

Cross-link

444

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Cross-link

476

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q4QQW4 [UniParc].

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

482

55,093

        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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC097943 mRNA. Translation: AAH97943.1. BC107476 mRNA. Translation: AAI07477.1.
IPI	IPI00364813.
RefSeq	NP_001020580.1. NM_001025409.1.
UniGene	Rn.1863.
3D structure databases
HSSP	HSSP built from PDB template 1T67 based on UniProtKB Q9BY41.
ProteinModelPortal	Q4QQW4.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000012854.
PTM databases
PhosphoSite	Q4QQW4.
Proteomic databases
PaxDb	Q4QQW4.
PRIDE	Q4QQW4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000012854; ENSRNOP00000012854; ENSRNOG00000009568.
GeneID	297893.
KEGG	rno:297893.
UCSC	RGD:619975. rat.
Organism-specific databases
CTD	3065.
RGD	619975. Hdac1.
Phylogenomic databases
eggNOG	COG0123.
GeneTree	ENSGT00530000062889.
HOGENOM	HOG000225180.
HOVERGEN	HBG057112.
InParanoid	Q4QQW4.
KO	K06067.
OrthoDB	EOG4868CH.
Enzyme and pathway databases
Reactome	REACT_111984. Signal Transduction.
Gene expression databases
Genevestigator	Q4QQW4.
Family and domain databases
Gene3D	3.40.800.20. 1 hit.
InterPro	IPR000286. His_deacetylse. IPR003084. His_deacetylse_1. IPR023801. His_deacetylse_dom. [Graphical view]
PANTHER	PTHR10625. PTHR10625. 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
BindingDB	Q4QQW4.
ChEMBL	CHEMBL2915.
NextBio	642799.

Entry information

Entry name

HDAC1_RAT

Accession

Primary (citable) accession number: Q4QQW4

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	July 19, 2005
Last modified:	April 3, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents