Reviewed, UniProtKB/Swiss-Prot O13298 (PHD1_SCHPO)

Names and origin

Protein names

Recommended name:
    Histone deacetylase phd1
    EC=3.5.1.98

Gene names

Name:	phd1
Synonyms:	hda1
ORF Names:	SPAC3G9.07c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	434 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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. Type 1 subfamily.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Molecular function	Chromatin regulator Hydrolase Repressor
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	chromatin silencing at centromere Ref.3 Inferred from mutant phenotype. Source: GeneDB_SPombe chromatin silencing at silent mating-type cassette Ref.3 Inferred from mutant phenotype. Source: GeneDB_SPombe chromatin silencing at telomere Ref.3 Inferred from mutant phenotype. Source: GeneDB_SPombe histone deacetylation Inferred from direct assay. Source: GeneDB_SPombe regulation of nucleosome density Inferred from expression pattern. Source: GeneDB_SPombe regulation of transcription from RNA polymerase II promoter Inferred from expression pattern. Source: GeneDB_SPombe transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Rpd3L-Expanded complex Inferred from direct assay. Source: GeneDB_SPombe Set3 complex Inferred from direct assay. Source: GeneDB_SPombe cytosol Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	histone deacetylase activity (H3-K16 specific) Inferred from direct assay. Source: GeneDB_SPombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 434	434	Histone deacetylase phd1		PRO_0000114725
Regions
	Region	26 – 339	314	Histone deacetylase
Sites
	Active site	158	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	O13298-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: CA2FF0D34CA536EA	FASTA	434	49,381
	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

References

	« Hide 'large scale' referencesShow '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: 9781677] [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. , 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: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[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: 9628926] [Abstract] Cited for: CHARACTERIZATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB008888 Genomic DNA. Translation: BAA23598.1. CU329670 Genomic DNA. Translation: CAA15916.1.
PIR	T11643.
RefSeq	NP_594079.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	O13298.
Genome annotation databases
GeneID	2543643.
GenomeReviews	Gene locus phd1 in contig CU329670_GR.
KEGG	spo:SPAC3G9.07c.
NMPDR	fig|4896.1.peg.4049.
Organism-specific databases
GeneDB_Spombe	SPAC3G9.07c.
Phylogenomic databases
OMA	IHTATAL.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-001706-MON.
Gene expression databases
ArrayExpress	O13298.
Family and domain databases
InterPro	IPR000286. His_deacetylse. IPR003084. His_deacetylse_1. [Graphical view]
Gene3D	G3DSA:3.40.800.20. His_deacetylse. 1 hit.
PANTHER	PTHR10625. His_deacetylse. 1 hit. PTHR10625:SF28. His_deacetylse_1. 1 hit.
Pfam	PF00850. Hist_deacetyl. 1 hit. [Graphical view]
PIRSF	PIRSF037913. His_deacetylse_1. 1 hit.
PRINTS	PR01270. HDASUPER. PR01271. HISDACETLASE.
ProtoNet	Search...

Entry information

Entry name

PHD1_SCHPO

Accession

Primary (citable) accession number: O13298

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	November 3, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)