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Protein

Histone deacetylase 8

Gene

hdac8

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: Annotation score: 3 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.

Cofactori

a divalent metal cationNote: Binds 1 divalent metal cation per subunit.

Enzyme regulationi

Its activity is inhibited by trichostatin A (TSA) and butyrate, 2 well known histone deacetylase inhibitors.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei102SubstrateBy similarity1
Active sitei144Proton acceptorBy similarity1
Binding sitei152Substrate; via carbonyl oxygenBy similarity1
Metal bindingi179Divalent metal cationBy similarity1
Metal bindingi181Divalent metal cationBy similarity1
Metal bindingi268Divalent metal cationBy similarity1
Binding sitei307SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Hydrolase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone deacetylase 8 (EC:3.5.1.98)
Short name:
HD8
Gene namesi
Name:hdac8
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
Proteomesi
  • UP000000437 Componenti: Unplaced

Organism-specific databases

ZFINiZDB-GENE-040426-2772. hdac8.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003895091 – 378Histone deacetylase 8Add BLAST378

Proteomic databases

PaxDbiQ7SXM0.

Interactioni

Protein-protein interaction databases

STRINGi7955.ENSDARP00000077625.

Structurei

3D structure databases

ProteinModelPortaliQ7SXM0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni15 – 325Histone deacetylaseBy similarityAdd BLAST311

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1342. Eukaryota.
KOG3635. Eukaryota.
ENOG410XPJZ. LUCA.
HOGENOMiHOG000225180.
HOVERGENiHBG057112.
InParanoidiQ7SXM0.
KOiK11405.
PhylomeDBiQ7SXM0.

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.

Q7SXM0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEKSDSNDD KSRTRSVVYV YSPEYIQTCD SLSKVPNRAS MVHSLIEAYG
60 70 80 90 100
LLKYMRVVKP HVASIEEMAV FHTDSYLQHL HKISQDGDND DPQSADFGLG
110 120 130 140 150
YDCPVVEGIF DYAAAVGGAT LTAAQNLLDG KCDVAINWAG GWHHAKKDEA
160 170 180 190 200
SGSCYVNDAV LGILKLREKY DRVLYVDVDL HHGDGVEDAF SFTSKVMTVS
210 220 230 240 250
LHKFSPGFFP GTGDVTDTGL GKGRWYAVNV PFEDGVRDDR YCQTFTSVMQ
260 270 280 290 300
EVKALFNPEA VVMQLGADTM AGDPMCSFNM TPVGVAKCLT YILGWELPTL
310 320 330 340 350
LLGGGGYNLA NTARCWTYLT GTVLGQTLSS EIPDHEFFTE YGPDYSLEIS
360 370
PSCRPDRNES QHLERVISTI KGNLKNVV
Length:378
Mass (Da):41,583
Last modified:October 1, 2003 - v1
Checksum:iED4D6FD03D62C4DF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC055541 mRNA. Translation: AAH55541.1.
RefSeqiNP_998596.1. NM_213431.1.
UniGeneiDr.3849.

Genome annotation databases

GeneIDi406740.
KEGGidre:406740.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC055541 mRNA. Translation: AAH55541.1.
RefSeqiNP_998596.1. NM_213431.1.
UniGeneiDr.3849.

3D structure databases

ProteinModelPortaliQ7SXM0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7955.ENSDARP00000077625.

Proteomic databases

PaxDbiQ7SXM0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi406740.
KEGGidre:406740.

Organism-specific databases

CTDi55869.
ZFINiZDB-GENE-040426-2772. hdac8.

Phylogenomic databases

eggNOGiKOG1342. Eukaryota.
KOG3635. Eukaryota.
ENOG410XPJZ. LUCA.
HOGENOMiHOG000225180.
HOVERGENiHBG057112.
InParanoidiQ7SXM0.
KOiK11405.
PhylomeDBiQ7SXM0.

Miscellaneous databases

PROiQ7SXM0.

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 nameiHDAC8_DANRE
AccessioniPrimary (citable) accession number: Q7SXM0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 24, 2009
Last sequence update: October 1, 2003
Last modified: October 5, 2016
This is version 82 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.