Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O13298

- PHD1_SCHPO

UniProt

O13298 - PHD1_SCHPO

Protein

Histone deacetylase phd1

Gene

phd1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.By similarity

    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 sitei158 – 1581By similarity

    GO - Molecular functioni

    1. histone deacetylase activity Source: PomBase
    2. histone deacetylase activity (H4-K16 specific) Source: PomBase
    3. NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
    4. NAD-dependent histone deacetylase activity (H3-K18 specific) Source: UniProtKB-EC
    5. NAD-dependent histone deacetylase activity (H3-K9 specific) Source: UniProtKB-EC
    6. NAD-dependent histone deacetylase activity (H4-K16 specific) Source: UniProtKB-EC

    GO - Biological processi

    1. chromatin remodeling Source: PomBase
    2. chromatin silencing at centromere Source: PomBase
    3. chromatin silencing at silent mating-type cassette Source: PomBase
    4. chromatin silencing at telomere Source: PomBase
    5. histone deacetylation Source: PomBase
    6. histone H4 deacetylation Source: GOC
    7. regulation of nucleosome density Source: PomBase
    8. regulation of transcription from RNA polymerase II promoter Source: PomBase
    9. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Hydrolase, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone deacetylase phd1 (EC:3.5.1.98)
    Gene namesi
    Name:phd1
    Synonyms:hda1
    ORF Names:SPAC3G9.07c
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome I

    Organism-specific databases

    PomBaseiSPAC3G9.07c.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. cytoplasm Source: PomBase
    2. cytosol Source: PomBase
    3. nucleus Source: PomBase
    4. Rpd3L-Expanded complex Source: PomBase
    5. Set3 complex Source: PomBase

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 434434Histone deacetylase phd1PRO_0000114725Add
    BLAST

    Proteomic databases

    MaxQBiO13298.

    Interactioni

    Protein-protein interaction databases

    BioGridi280057. 156 interactions.
    MINTiMINT-4666521.
    STRINGi4896.SPAC3G9.07c-1.

    Structurei

    3D structure databases

    ProteinModelPortaliO13298.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni26 – 339314Histone deacetylaseAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0123.
    HOGENOMiHOG000225180.
    KOiK11483.
    OMAiDKQIHHI.
    OrthoDBiEOG78M0B2.
    PhylomeDBiO13298.

    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.

    O13298-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDTPETSTPY EQVEKGSFFS FRPQKKRVTY HLDEQVGNYH YGDKHPMKPH    50
    RITITNHLVM GYGLHNKMSV FSPRMATFGE MSEFHREDYL DFLKRVTPDN 100
    AEQFADKFQQ FNIGDDCPVF DGTYEFSQRS AGASLDASRK LVQGQTDIAI 150
    NWSGGLHHAK RGEASGFCYV NDIVLAILNM LRFFPRVLYI DIDIHHGDGV 200
    QQAFYESDRV LTVSFHKYNG DFFPATGNFD ENGVKGGKYF ALNVPLEDGI 250
    GDEQYTSLFK SIIEPTINTF QPSAIVLQCG ADSLGYDRLG VFNLSIHAHG 300
    ECVRFTRSFN IPMLVVGGGG YTLRNVARAW CYETSICVNE QIPSELPRET 350
    LYYEFFAPDY TLHPRLTTKI ENKNTPKALE DLRIRALEQL RYLGGAPSVQ 400
    MQQIPPDLTG HLEEEDERLN DEYLDKAVDV RVRG 434
    Length:434
    Mass (Da):49,381
    Last modified:January 1, 1998 - v1
    Checksum:iCA2FF0D34CA536EA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB008888 Genomic DNA. Translation: BAA23598.1.
    CU329670 Genomic DNA. Translation: CAA15916.1.
    PIRiT11643.
    RefSeqiNP_594079.1. NM_001019506.2.

    Genome annotation databases

    EnsemblFungiiSPAC3G9.07c.1; SPAC3G9.07c.1:pep; SPAC3G9.07c.
    GeneIDi2543643.
    KEGGispo:SPAC3G9.07c.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB008888 Genomic DNA. Translation: BAA23598.1 .
    CU329670 Genomic DNA. Translation: CAA15916.1 .
    PIRi T11643.
    RefSeqi NP_594079.1. NM_001019506.2.

    3D structure databases

    ProteinModelPortali O13298.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 280057. 156 interactions.
    MINTi MINT-4666521.
    STRINGi 4896.SPAC3G9.07c-1.

    Proteomic databases

    MaxQBi O13298.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPAC3G9.07c.1 ; SPAC3G9.07c.1:pep ; SPAC3G9.07c .
    GeneIDi 2543643.
    KEGGi spo:SPAC3G9.07c.

    Organism-specific databases

    PomBasei SPAC3G9.07c.

    Phylogenomic databases

    eggNOGi COG0123.
    HOGENOMi HOG000225180.
    KOi K11483.
    OMAi DKQIHHI.
    OrthoDBi EOG78M0B2.
    PhylomeDBi O13298.

    Miscellaneous databases

    NextBioi 20804649.

    Family and domain databases

    Gene3Di 3.40.800.20. 1 hit.
    InterProi IPR000286. His_deacetylse.
    IPR003084. His_deacetylse_1.
    IPR023801. His_deacetylse_dom.
    [Graphical view ]
    PANTHERi PTHR10625. PTHR10625. 1 hit.
    Pfami PF00850. Hist_deacetyl. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037913. His_deacetylse_1. 1 hit.
    PRINTSi PR01270. HDASUPER.
    PR01271. HISDACETLASE.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiPHD1_SCHPO
    AccessioniPrimary (citable) accession number: O13298
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 107 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3