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O13298 (PHD1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 106. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone deacetylase phd1

EC=3.5.1.98
Gene names
Name:phd1
Synonyms:hda1
ORF Names:SPAC3G9.07c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length434 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 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. Is not essential.

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 remodeling

Inferred by curator. Source: PomBase

chromatin silencing at centromere

Inferred from mutant phenotype Ref.3. Source: PomBase

chromatin silencing at silent mating-type cassette

Inferred from mutant phenotype Ref.3. Source: PomBase

chromatin silencing at telomere

Inferred from mutant phenotype Ref.3. Source: PomBase

histone H4 deacetylation

Inferred from direct assay PubMed 16079916. Source: GOC

histone deacetylation

Inferred from direct assay PubMed 11884604. Source: PomBase

regulation of nucleosome density

Inferred from expression pattern PubMed 16079916. Source: PomBase

regulation of transcription from RNA polymerase II promoter

Inferred from expression pattern PubMed 16079916. Source: PomBase

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentRpd3L-Expanded complex

Inferred from direct assay PubMed 19040720. Source: PomBase

Set3 complex

Inferred from direct assay PubMed 19040720. Source: PomBase

cytoplasm

Inferred from direct assay PubMed 11884604. Source: PomBase

cytosol

Inferred from direct assay PubMed 16823372. Source: PomBase

nucleus

Inferred from direct assay PubMed 16823372. Source: PomBase

   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 11884604. Source: PomBase

histone deacetylase activity (H4-K16 specific)

Inferred from direct assay PubMed 16079916. Source: PomBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 434434Histone deacetylase phd1
PRO_0000114725

Regions

Region26 – 339314Histone deacetylase

Sites

Active site1581 By similarity

Sequences

Sequence LengthMass (Da)Tools
O13298 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: CA2FF0D34CA536EA

FASTA43449,381
        10         20         30         40         50         60 
MDTPETSTPY EQVEKGSFFS FRPQKKRVTY HLDEQVGNYH YGDKHPMKPH RITITNHLVM 

        70         80         90        100        110        120 
GYGLHNKMSV FSPRMATFGE MSEFHREDYL DFLKRVTPDN AEQFADKFQQ FNIGDDCPVF 

       130        140        150        160        170        180 
DGTYEFSQRS AGASLDASRK LVQGQTDIAI NWSGGLHHAK RGEASGFCYV NDIVLAILNM 

       190        200        210        220        230        240 
LRFFPRVLYI DIDIHHGDGV QQAFYESDRV LTVSFHKYNG DFFPATGNFD ENGVKGGKYF 

       250        260        270        280        290        300 
ALNVPLEDGI GDEQYTSLFK SIIEPTINTF QPSAIVLQCG ADSLGYDRLG VFNLSIHAHG 

       310        320        330        340        350        360 
ECVRFTRSFN IPMLVVGGGG YTLRNVARAW CYETSICVNE QIPSELPRET LYYEFFAPDY 

       370        380        390        400        410        420 
TLHPRLTTKI ENKNTPKALE DLRIRALEQL RYLGGAPSVQ MQQIPPDLTG HLEEEDERLN 

       430 
DEYLDKAVDV RVRG 

« Hide

References

« Hide 'large scale' references
[1]"phd1+, a histone deacetylase gene of Schizosaccharomyces pombe, is required for the meiotic cell cycle and resistance to trichostatin A."
Kim Y.B., Honda A., Yoshida M., Horinouchi S.
FEBS Lett. 436:193-196(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[3]"Genetic characterisation of hda1+, a putative fission yeast histone deacetylase gene."
Olsson T.G.S., Ekwall K., Allshire R.C., Sunnerhagen P., Partridge J.F., Richardson W.A.
Nucleic Acids Res. 26:3247-3254(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB008888 Genomic DNA. Translation: BAA23598.1.
CU329670 Genomic DNA. Translation: CAA15916.1.
PIRT11643.
RefSeqNP_594079.1. NM_001019506.2.

3D structure databases

ProteinModelPortalO13298.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid280057. 156 interactions.
MINTMINT-4666521.
STRING4896.SPAC3G9.07c-1.

Proteomic databases

MaxQBO13298.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC3G9.07c.1; SPAC3G9.07c.1:pep; SPAC3G9.07c.
GeneID2543643.
KEGGspo:SPAC3G9.07c.

Organism-specific databases

PomBaseSPAC3G9.07c.

Phylogenomic databases

eggNOGCOG0123.
HOGENOMHOG000225180.
KOK11483.
OMADKQIHHI.
OrthoDBEOG78M0B2.
PhylomeDBO13298.

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

NextBio20804649.

Entry information

Entry namePHD1_SCHPO
AccessionPrimary (citable) accession number: O13298
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: May 14, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names