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P56519 (HDAC2_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 89. 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 2

Short name=HD2
EC=3.5.1.98
Gene names
Name:HDAC2
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length488 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.

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

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentESC/E(Z) complex

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Traceable author statement PubMed 12711221. Source: UniProtKB

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

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 – 488488Histone deacetylase 2
PRO_0000114695

Regions

Region9 – 322314Histone deacetylase
Compositional bias300 – 3034Poly-Gly

Sites

Active site1421 By similarity

Sequences

Sequence LengthMass (Da)Tools
P56519 [UniParc].

Last modified July 15, 1998. Version 1.
Checksum: 4F79B9C0D4A2D065

FASTA48855,153
        10         20         30         40         50         60 
MAYSQGGGKK KVCYYYDGDI GNYYYGQGHP MKPHRIRMTH NLLLNYGLYR KMEIYRPHKA 

        70         80         90        100        110        120 
TAEEMTKYHS DEYIKFLRSI RPDNMSEYSK QMQRFNVGED CPVFDGLFEF CQLSTGGSVA 

       130        140        150        160        170        180 
GAVKLNRQQT DMAVNWAGGL HHAKKSEASG FCYVNDIVLA ILELLKYHQR VLYIDIDIHH 

       190        200        210        220        230        240 
GDGVEEAFYT TDRVMTVSEV SMVNNFPGTG DLRDIGAGKG KYYAVNFPMR DGIDDESYGQ 

       250        260        270        280        290        300 
IFKPIISKVM EMYQPSAVVL QCGADSLSGD RLGCFNLTVK GHAKCVEVVK TFNLPLLMLG 

       310        320        330        340        350        360 
GGGYTIRNVA RCWTYETAVA LDCEIPNELP YNDYFEYFGP DFKLHISPSN MTNQNTPEYM 

       370        380        390        400        410        420 
EKIKQRLFEN LRMLPHAPGV QMQAIPEDAV HEDSGDEDGE DPDKRISIRA SDKRIACDEE 

       430        440        450        460        470        480 
FSDSEDEGEG GRRNVADHKK GAKKARIEED KKETEDKKAD VKEEDKSKDN SGEKTDTKGA 


KSEQLSNP 

« Hide

References

[1]Takami Y.
Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF039752 mRNA. Translation: AAB96924.1.
RefSeqNP_990162.1. NM_204831.1.
UniGeneGga.2951.

3D structure databases

ProteinModelPortalP56519.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid675914. 3 interactions.
IntActP56519. 1 interaction.
STRING9031.ENSGALP00000024133.

Chemistry

BindingDBP56519.

Proteomic databases

PaxDbP56519.
PRIDEP56519.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID395635.
KEGGgga:395635.

Organism-specific databases

CTD3066.

Phylogenomic databases

eggNOGCOG0123.
HOGENOMHOG000225180.
HOVERGENHBG057112.
InParanoidP56519.
KOK06067.
PhylomeDBP56519.

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

NextBio20815708.
PROP56519.

Entry information

Entry nameHDAC2_CHICK
AccessionPrimary (citable) accession number: P56519
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: April 16, 2014
This is version 89 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