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Protein

Histone deacetylase 1

Gene

HDAC1

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei141By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Hydrolase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BRENDAi3.5.1.98. 1306.
ReactomeiR-GGA-1538133. G0 and Early G1.
R-GGA-201722. Formation of the beta-catenin:TCF transactivating complex.
R-GGA-3214815. HDACs deacetylate histones.
R-GGA-3769402. Deactivation of the beta-catenin transactivating complex.
R-GGA-73762. RNA Polymerase I Transcription Initiation.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone deacetylase 1 (EC:3.5.1.98)
Short name:
HD1
Gene namesi
Name:HDAC1
Synonyms:HDAC1A
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 23

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Ensembl
  • histone deacetylase complex Source: UniProtKB
  • nucleus Source: UniProtKB
  • NuRD complex Source: Ensembl
  • Sin3 complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001146891 – 480Histone deacetylase 1Add BLAST480

Proteomic databases

PaxDbiP56517.
PRIDEiP56517.

Expressioni

Gene expression databases

BgeeiENSGALG00000003297.

Interactioni

Subunit structurei

Forms a complex with RBAP48.By similarity

GO - Molecular functioni

  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi675010. 2 interactors.
STRINGi9031.ENSGALP00000005212.

Structurei

3D structure databases

ProteinModelPortaliP56517.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni9 – 321Histone deacetylaseAdd BLAST313

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi299 – 302Poly-Gly4
Compositional biasi396 – 399Poly-Glu4
Compositional biasi446 – 453Poly-Glu8

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1342. Eukaryota.
COG0123. LUCA.
GeneTreeiENSGT00530000062889.
HOGENOMiHOG000225180.
HOVERGENiHBG057112.
InParanoidiP56517.
KOiK06067.
OMAiHASCVKF.
OrthoDBiEOG091G067J.
PhylomeDBiP56517.
TreeFamiTF106171.

Family and domain databases

Gene3Di3.40.800.20. 1 hit.
InterProiIPR000286. His_deacetylse.
IPR003084. His_deacetylse_1.
IPR023801. His_deacetylse_dom.
[Graphical view]
PANTHERiPTHR10625. PTHR10625. 1 hit.
PfamiPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFiPIRSF037913. His_deacetylse_1. 1 hit.
PRINTSiPR01270. HDASUPER.
PR01271. HISDACETLASE.

Sequencei

Sequence statusi: Complete.

P56517-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALTQGTKRK VCYYYDGDVG NYYYGQGHPM KPHRIRMTHN LLLNYGLYRK
60 70 80 90 100
MEIYRPHKAN AEEMTKYHSD DYIKFLRSIR PDNMSEYSKQ MQRFNVGEDC
110 120 130 140 150
PVFDGLFEFC QLSAGGSVAS AVKLNKQQTD IAVNWAGGLH HAKKSEASGF
160 170 180 190 200
CYVNDIVLAI LELLKYHQRV LYIDIDIHHG DGVEEAFYTT DRVMTVSFHK
210 220 230 240 250
YGEYFPGTGD LRDIGAGKGK YYAVNYPLRD GIDDESYEAI FKPVISKVME
260 270 280 290 300
TFQPSAVVLQ CGSDSLSGDR LGCFNLTIKG HAKCVEFVKS FNLPMLMLGG
310 320 330 340 350
GGYTIRNVAR CWTYETAVAL DTEIPNELPY NDYFEYFGPD FKLHISPSNM
360 370 380 390 400
TNQNTNEYLE KIKQRLFENL RMLPHAPGVQ MQPIPEDAVQ EDSGDEEEED
410 420 430 440 450
PEKRISIRNS DKRISCDEEF SDSEDEGEGG RKNVANFKKA KRVKTEEEKE
460 470 480
EEEKKDEKEE EKAKEEKAEP KGVKEETKST
Length:480
Mass (Da):54,939
Last modified:July 15, 1998 - v1
Checksum:i82C78CE285C779D9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti3 – 4LT → VM in AAB99850 (Ref. 2) Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF039751 mRNA. Translation: AAB96923.1.
AF043328 mRNA. Translation: AAB99850.1.
AF044169 mRNA. Translation: AAC00504.1.
RefSeqiNP_989487.1. NM_204156.1.
UniGeneiGga.10603.

Genome annotation databases

EnsembliENSGALT00000005221; ENSGALP00000005212; ENSGALG00000003297.
GeneIDi373961.
KEGGigga:373961.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF039751 mRNA. Translation: AAB96923.1.
AF043328 mRNA. Translation: AAB99850.1.
AF044169 mRNA. Translation: AAC00504.1.
RefSeqiNP_989487.1. NM_204156.1.
UniGeneiGga.10603.

3D structure databases

ProteinModelPortaliP56517.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi675010. 2 interactors.
STRINGi9031.ENSGALP00000005212.

Proteomic databases

PaxDbiP56517.
PRIDEiP56517.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000005221; ENSGALP00000005212; ENSGALG00000003297.
GeneIDi373961.
KEGGigga:373961.

Organism-specific databases

CTDi3065.

Phylogenomic databases

eggNOGiKOG1342. Eukaryota.
COG0123. LUCA.
GeneTreeiENSGT00530000062889.
HOGENOMiHOG000225180.
HOVERGENiHBG057112.
InParanoidiP56517.
KOiK06067.
OMAiHASCVKF.
OrthoDBiEOG091G067J.
PhylomeDBiP56517.
TreeFamiTF106171.

Enzyme and pathway databases

BRENDAi3.5.1.98. 1306.
ReactomeiR-GGA-1538133. G0 and Early G1.
R-GGA-201722. Formation of the beta-catenin:TCF transactivating complex.
R-GGA-3214815. HDACs deacetylate histones.
R-GGA-3769402. Deactivation of the beta-catenin transactivating complex.
R-GGA-73762. RNA Polymerase I Transcription Initiation.

Miscellaneous databases

PROiP56517.

Gene expression databases

BgeeiENSGALG00000003297.

Family and domain databases

Gene3Di3.40.800.20. 1 hit.
InterProiIPR000286. His_deacetylse.
IPR003084. His_deacetylse_1.
IPR023801. His_deacetylse_dom.
[Graphical view]
PANTHERiPTHR10625. PTHR10625. 1 hit.
PfamiPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFiPIRSF037913. His_deacetylse_1. 1 hit.
PRINTSiPR01270. HDASUPER.
PR01271. HISDACETLASE.
ProtoNetiSearch...

Entry informationi

Entry nameiHDAC1_CHICK
AccessioniPrimary (citable) accession number: P56517
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: November 30, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.