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P56517 (HDAC1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone deacetylase 1

Short name=HD1
EC=3.5.1.98
Gene names
Name:HDAC1
Synonyms:HDAC1A
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length480 AA.
Sequence statusComplete.
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

Forms a complex with RBAP48 By similarity.

Subcellular location

Nucleus Potential.

Sequence similarities

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

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Molecular functionChromatin regulator
Hydrolase
Repressor
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin modification

Traceable author statement PubMed 12711221. Source: UniProtKB

negative regulation by host of viral transcription

Inferred from electronic annotation. Source: Ensembl

negative regulation of androgen receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of receptor biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentNuRD complex

Inferred from electronic annotation. Source: Ensembl

Sin3 complex

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Traceable author statement PubMed 12711221. Source: UniProtKB

cytosol

Inferred from electronic annotation. Source: Ensembl

histone deacetylase complex

Traceable author statement PubMed 12711221. Source: UniProtKB

nucleus

Traceable author statement PubMed 12711221. Source: UniProtKB

   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 transcription corepressor activity

Inferred from electronic annotation. Source: Ensembl

core promoter binding

Inferred from electronic annotation. Source: Ensembl

histone deacetylase activity

Traceable author statement PubMed 12711221. Source: UniProtKB

transcription factor binding

Traceable author statement PubMed 12711221. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 480480Histone deacetylase 1
PRO_0000114689

Regions

Region9 – 321313Histone deacetylase
Compositional bias299 – 3024Poly-Gly
Compositional bias396 – 3994Poly-Glu
Compositional bias446 – 4538Poly-Glu

Sites

Active site1411 By similarity

Experimental info

Sequence conflict3 – 42LT → VM in AAB99850. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P56517 [UniParc].

Last modified July 15, 1998. Version 1.
Checksum: 82C78CE285C779D9

FASTA48054,939
        10         20         30         40         50         60 
MALTQGTKRK VCYYYDGDVG NYYYGQGHPM KPHRIRMTHN LLLNYGLYRK MEIYRPHKAN 

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

       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 
FKPVISKVME TFQPSAVVLQ CGSDSLSGDR LGCFNLTIKG HAKCVEFVKS FNLPMLMLGG 

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

       370        380        390        400        410        420 
KIKQRLFENL RMLPHAPGVQ MQPIPEDAVQ EDSGDEEEED PEKRISIRNS DKRISCDEEF 

       430        440        450        460        470        480 
SDSEDEGEGG RKNVANFKKA KRVKTEEEKE EEEKKDEKEE EKAKEEKAEP KGVKEETKST 

« Hide

References

[1]Takami Y.
Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Sun J.M., Chen H.Y., Davie J.R.
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF039751 mRNA. Translation: AAB96923.1.
AF043328 mRNA. Translation: AAB99850.1.
AF044169 mRNA. Translation: AAC00504.1.
RefSeqNP_989487.1. NM_204156.1.
UniGeneGga.10603.

3D structure databases

ProteinModelPortalP56517.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid675010. 2 interactions.
STRING9031.ENSGALP00000005212.

Chemistry

BindingDBP56517.

Proteomic databases

PaxDbP56517.
PRIDEP56517.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSGALT00000005221; ENSGALP00000005212; ENSGALG00000003297.
GeneID373961.
KEGGgga:373961.

Organism-specific databases

CTD3065.

Phylogenomic databases

eggNOGCOG0123.
GeneTreeENSGT00530000062889.
HOGENOMHOG000225180.
HOVERGENHBG057112.
InParanoidP56517.
KOK06067.
OMALTQGTKR.
OrthoDBEOG7DNNTW.
PhylomeDBP56517.
TreeFamTF106171.

Enzyme and pathway databases

BRENDA3.5.1.98. 1306.

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

NextBio20813492.
PROP56517.

Entry information

Entry nameHDAC1_CHICK
AccessionPrimary (citable) accession number: P56517
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: April 16, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families