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Protein

Putative histone deacetylase 2

Gene

hda-2

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Probably responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (By similarity). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (By similarity). Histone deacetylases act via the formation of large multiprotein complexes (By similarity). As a likely component of a histone deacetylase complex, together with saeg-1 and hda-2, functions downstream of the cAMP-dependent kinase egl-4 to regulate the expression of genes required for egg-laying and forgaging (PubMed:21573134).By similarity1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei162 – 1621By similarity

GO - Molecular functioni

  • histone deacetylase activity Source: WormBase
  • NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
  • transcription corepressor activity Source: WormBase

GO - Biological processi

  • chromatin modification Source: WormBase
  • DNA protection Source: WormBase
  • histone deacetylation Source: WormBase
  • negative regulation of transcription from RNA polymerase II promoter Source: WormBase
  • nematode male tail tip morphogenesis Source: WormBase
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Hydrolase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-CEL-2467813. Separation of Sister Chromatids.
R-CEL-2500257. Resolution of Sister Chromatid Cohesion.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative histone deacetylase 2 (EC:3.5.1.98)
Gene namesi
Name:hda-2
ORF Names:C08B11.2
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome II

Organism-specific databases

WormBaseiC08B11.2; CE01472; WBGene00001835; hda-2.

Subcellular locationi

GO - Cellular componenti

  • histone deacetylase complex Source: WormBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 507507Putative histone deacetylase 2PRO_0000114720Add
BLAST

Proteomic databases

EPDiQ09440.
PaxDbiQ09440.
PRIDEiQ09440.

Interactioni

Subunit structurei

May be a component of a histone deacetylase complex containing saeg-2, saeg-1 and hda-2.1 Publication

Protein-protein interaction databases

BioGridi39617. 2 interactions.
IntActiQ09440. 1 interaction.
MINTiMINT-226304.
STRINGi6239.C08B11.2.

Structurei

3D structure databases

ProteinModelPortaliQ09440.
SMRiQ09440. Positions 29-395.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni29 – 342314Histone deacetylaseAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1342. Eukaryota.
COG0123. LUCA.
GeneTreeiENSGT00530000062889.
HOGENOMiHOG000225180.
InParanoidiQ09440.
KOiK06067.
OMAiRMIRGAP.
OrthoDBiEOG7VTDRR.
PhylomeDBiQ09440.

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.

Q09440-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSDKFKLDT LFDDNDEIIE PDGADVKKRN VAYYYHKDVG HFHYGQLHPM
60 70 80 90 100
KPQRLVVCND LVVSYEMPKY MTVVESPKLD AADISVFHTE DYVNFLQTVT
110 120 130 140 150
PKLGLTMPDD VLRQFNIGED CPIFAGLWDY CTLYAGGSVE GARRLNHKMN
160 170 180 190 200
DIVINWPGGL HHAKKSEASG FCYVNDIVLG ILELLKYHKR VLYIDIDIHH
210 220 230 240 250
GDGVQEAFNN SDRVMTVSFH RFGQYFPGSG SIMDKGVGPG KYFAINVPLM
260 270 280 290 300
AAIRDEPYLK LFESVISGVE ENFNPEAIVL QCGSDSLCED RLGQFALSFN
310 320 330 340 350
AHARAVKYVK SLGKPLMVLG GGGYTLRNVA RCWALETGVI LGLRMDDEIP
360 370 380 390 400
GTSLYSHYFT PRLLRPNLVP KMNDANSAAY LASIEKETLA CLRMIRGAPS
410 420 430 440 450
VQMQNIVGIR LDEIEQIEEN ERLQKSSKSS IEYEVGKVSE KMEEECFVEE
460 470 480 490 500
DSKPPSFPPG QDPRRIGQYW GYDRSGLAPP RSHSDVIEEA KYEDRDRRKD

LNIPGIP
Length:507
Mass (Da):57,138
Last modified:November 1, 1995 - v1
Checksum:iF500D405F7595BAF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46676 Genomic DNA. Translation: CAA86662.1.
PIRiT19067.
RefSeqiNP_495678.1. NM_063277.5.
UniGeneiCel.14857.

Genome annotation databases

EnsemblMetazoaiC08B11.2; C08B11.2; WBGene00001835.
GeneIDi174285.
KEGGicel:CELE_C08B11.2.
UCSCiC08B11.2. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46676 Genomic DNA. Translation: CAA86662.1.
PIRiT19067.
RefSeqiNP_495678.1. NM_063277.5.
UniGeneiCel.14857.

3D structure databases

ProteinModelPortaliQ09440.
SMRiQ09440. Positions 29-395.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi39617. 2 interactions.
IntActiQ09440. 1 interaction.
MINTiMINT-226304.
STRINGi6239.C08B11.2.

Proteomic databases

EPDiQ09440.
PaxDbiQ09440.
PRIDEiQ09440.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiC08B11.2; C08B11.2; WBGene00001835.
GeneIDi174285.
KEGGicel:CELE_C08B11.2.
UCSCiC08B11.2. c. elegans.

Organism-specific databases

CTDi174285.
WormBaseiC08B11.2; CE01472; WBGene00001835; hda-2.

Phylogenomic databases

eggNOGiKOG1342. Eukaryota.
COG0123. LUCA.
GeneTreeiENSGT00530000062889.
HOGENOMiHOG000225180.
InParanoidiQ09440.
KOiK06067.
OMAiRMIRGAP.
OrthoDBiEOG7VTDRR.
PhylomeDBiQ09440.

Enzyme and pathway databases

ReactomeiR-CEL-2467813. Separation of Sister Chromatids.
R-CEL-2500257. Resolution of Sister Chromatid Cohesion.

Miscellaneous databases

NextBioi883367.
PROiQ09440.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.
  2. "Nuclear cGMP-dependent kinase regulates gene expression via activity-dependent recruitment of a conserved histone deacetylase complex."
    Hao Y., Xu N., Box A.C., Schaefer L., Kannan K., Zhang Y., Florens L., Seidel C., Washburn M.P., Wiegraebe W., Mak H.Y.
    PLoS Genet. 7:E1002065-E1002065(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN HISTONE DEACETYLASE COMPLEX.

Entry informationi

Entry nameiHDA2_CAEEL
AccessioniPrimary (citable) accession number: Q09440
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 11, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. 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.