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O17695 (HDA1_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone deacetylase 1

EC=3.5.1.98
Gene names
Name:hda-1
ORF Names:C53A5.3
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. Involved in the endoderm determination possibly by repressing end-1 expression. Also involved in vulval development, possibly by repressing lag-2 expression. Ref.2 Ref.3

Catalytic activity

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

Subunit structure

Interacts with pop-1. Ref.2

Subcellular location

Nucleus. Cytoplasm. Note: Except in the germ line where it is also cytoplasmic.

Tissue specificity

Ubiquitously expressed throughout embryonic and postembryonic development. Ref.3

Developmental stage

Expressed both maternally and zygotically. Ref.3

Post-translational modification

Sumoylated Probable. Ref.4

Sequence similarities

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

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Molecular functionChromatin regulator
Developmental protein
Hydrolase
Repressor
   PTMUbl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processembryo development ending in birth or egg hatching

Inferred from mutant phenotype PubMed 9531533PubMed 9875852. Source: WormBase

embryonic digestive tract morphogenesis

Inferred from genetic interaction PubMed 15196946. Source: WormBase

gonad development

Inferred from mutant phenotype Ref.3. Source: WormBase

histone deacetylation

Inferred from direct assay PubMed 12507426. Source: WormBase

negative regulation of Notch signaling pathway

Inferred from mutant phenotype Ref.3. Source: WormBase

negative regulation of Ras protein signal transduction

Inferred from genetic interaction PubMed 10704416PubMed 9875852. Source: WormBase

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.2Ref.3. Source: WormBase

negative regulation of vulval development

Inferred from mutant phenotype Ref.3. Source: WormBase

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 23229554. Source: WormBase

regulation of cell differentiation

Inferred from genetic interaction PubMed 9531533. Source: WormBase

tail tip morphogenesis

Inferred from mutant phenotype PubMed 17506990. Source: WormBase

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentNuRD complex

Inferred from physical interaction PubMed 12507426. Source: WormBase

cytoplasm

Inferred from direct assay Ref.3. Source: WormBase

germ cell nucleus

Inferred from direct assay Ref.3. Source: WormBase

histone deacetylase complex

Inferred from physical interaction PubMed 9875852. Source: WormBase

nucleus

Inferred from direct assay Ref.3. Source: WormBase

   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

Inferred from direct assay PubMed 12507426. Source: WormBase

protein binding

Inferred from physical interaction Ref.2PubMed 12507426PubMed 9875852. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

pie-1Q941313EBI-318045,EBI-300501
pop-1Q106663EBI-318045,EBI-317870

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 461461Histone deacetylase 1
PRO_0000114719

Regions

Region13 – 325313Histone deacetylase

Sites

Active site1451 By similarity

Experimental info

Mutagenesis1451H → F: Loss of function.
Mutagenesis1861G → E in gon-10; specific defects in gonadogenesis and vulval development. Ref.3

Sequences

Sequence LengthMass (Da)Tools
O17695 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 9A104E88C5A1C07A

FASTA46152,138
        10         20         30         40         50         60 
MNSNGPLMEH GKRRVAYYYD SNIGNYYYGQ GHVMKPHRIR MTHHLVLNYG LYRNLEIFRP 

        70         80         90        100        110        120 
FPASFEDMTR FHSDEYMTFL KSANPDNLKS FNKQMLKFNV GEDCPLFDGL YEFCQLSSGG 

       130        140        150        160        170        180 
SLAAATKLNK QKVDIAINWM GGLHHAKKSE ASGFCYTNDI VLGILELLKY HKRVLYVDID 

       190        200        210        220        230        240 
VHHGDGVEEA FYTTDRVMTV SFHKYGDFFP GTGDLKDIGA GKGKLYSVNV PLRDGITDVS 

       250        260        270        280        290        300 
YQSIFKPIMT KVMERFDPCA VVLQCGADSL NGDRLGPFNL TLKGHGECAR FFRSYNVPLM 

       310        320        330        340        350        360 
MVGGGGYTPR NVARCWTYET SIAVDKEVPN ELPYNDYFEY FGPNYRLHIE SSNAANENSS 

       370        380        390        400        410        420 
DMLAKLQTDV IANLEQLTFV PSVQMRPIPE DALSALNDDS LIADQANPDK RLPPQITDGM 

       430        440        450        460 
IQDDGDFYDG EREGDDRRNE SDAKRAAQFE SEGGEKRQKT E 

« Hide

References

« Hide 'large scale' references
[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]"A POP-1 repressor complex restricts inappropriate cell type-specific gene transcription during Caenorhabditis elegans embryogenesis."
Calvo D., Victor M., Gay F., Sui G., Luke M.P.-S., Dufourcq P., Wen G., Maduro M., Rothman J., Shi Y.
EMBO J. 20:7197-7208(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH POP-1.
[3]"Functional requirement for histone deacetylase 1 in Caenorhabditis elegans gonadogenesis."
Dufourcq P., Victor M., Gay F., Calvo D., Hodgkin J., Shi Y.
Mol. Cell. Biol. 22:3024-3034(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF GLY-186.
[4]"Chromatin regulation and sumoylation in the inhibition of Ras-induced vulval development in Caenorhabditis elegans."
Poulin G., Dong Y., Fraser A.G., Hopper N.A., Ahringer J.
EMBO J. 24:2613-2623(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z81486 Genomic DNA. Translation: CAB03984.1.
PIRT20163.
RefSeqNP_506599.1. NM_074198.7.
UniGeneCel.17341.

3D structure databases

ProteinModelPortalO17695.
SMRO17695. Positions 12-377.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid44961. 22 interactions.
DIPDIP-26427N.
IntActO17695. 11 interactions.
MINTMINT-226391.
STRING6239.C53A5.3.2.

Proteomic databases

PaxDbO17695.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaC53A5.3; C53A5.3; WBGene00001834.
GeneID179959.
KEGGcel:CELE_C53A5.3.
UCSCC53A5.3.1. c. elegans.

Organism-specific databases

CTD179959.
WormBaseC53A5.3; CE08952; WBGene00001834; hda-1.

Phylogenomic databases

eggNOGCOG0123.
GeneTreeENSGT00530000062889.
HOGENOMHOG000225180.
InParanoidO17695.
KOK06067.
OMAQIQPDNE.
PhylomeDBO17695.

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

NextBio907546.

Entry information

Entry nameHDA1_CAEEL
AccessionPrimary (citable) accession number: O17695
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: June 11, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Caenorhabditis elegans

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