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O94446

- ESA1_SCHPO

UniProt

O94446 - ESA1_SCHPO

Protein

Histone acetyltransferase mst1

Gene

mst1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z. Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, and histone H2A to form H2AK4ac and H2AK7ac. Acetylation of histone H4 is essential for DNA double-strand break repair through homologous recombination. Involved in cell cycle progression. Recruitment to promoters depends on H3K4me By similarity.By similarity

    Catalytic activityi

    Acetyl-CoA + [histone] = CoA + acetyl-[histone].

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei279 – 2791By similarity
    Active sitei321 – 3211NucleophileBy similarity
    Binding sitei324 – 3241Acetyl-CoABy similarity
    Binding sitei359 – 3591Acetyl-CoABy similarity

    GO - Molecular functioni

    1. H4 histone acetyltransferase activity Source: PomBase
    2. protein binding Source: PomBase

    GO - Biological processi

    1. centromere complex assembly Source: PomBase
    2. chromatin remodeling Source: PomBase
    3. double-strand break repair Source: PomBase
    4. histone H4 acetylation Source: PomBase
    5. mitotic sister chromatid segregation Source: PomBase
    6. regulation of transcription, DNA-templated Source: UniProtKB-KW
    7. replication fork protection Source: PomBase
    8. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Chromatin regulator, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone acetyltransferase mst1 (EC:2.3.1.48)
    Gene namesi
    Name:mst1
    Synonyms:esa1
    ORF Names:SPAC637.12c
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome I

    Organism-specific databases

    PomBaseiSPAC637.12c.

    Subcellular locationi

    Nucleus 2 Publications

    GO - Cellular componenti

    1. NuA4 histone acetyltransferase complex Source: PomBase
    2. nuclear chromatin Source: PomBase
    3. nucleus Source: PomBase

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 463463Histone acetyltransferase mst1PRO_0000051564Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei279 – 2791N6-acetyllysine; by autocatalysisBy similarity

    Post-translational modificationi

    Autoacetylation at Lys-279 is required for proper function.By similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO94446.

    Interactioni

    Subunit structurei

    Component of the NuA4 histone acetyltransferase complex By similarity. Interacts with arp4.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi279924. 29 interactions.
    IntActiO94446. 1 interaction.
    MINTiMINT-8210884.
    STRINGi4896.SPAC637.12c-1.

    Structurei

    3D structure databases

    ProteinModelPortaliO94446.
    SMRiO94446. Positions 179-452.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini33 – 8957ChromoAdd
    BLAST
    Domaini179 – 450272MYST-type HATAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni329 – 3357Acetyl-CoA bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi262 – 28322ESA1-RPD3 motifAdd
    BLAST

    Domaini

    The ESA1-RPD3 motif is common to ESA1 and RPD3 and is required for ESA1 histone acetyl-transferase (HAT) activity and RPD3 histone deacetylase (HDAC) activity.

    Sequence similaritiesi

    Belongs to the MYST (SAS/MOZ) family.Curated
    Contains 1 chromo domain.Curated

    Phylogenomic databases

    eggNOGiCOG5027.
    HOGENOMiHOG000182457.
    KOiK11304.
    OMAiNIYSICM.
    OrthoDBiEOG7RFTRR.
    PhylomeDBiO94446.

    Family and domain databases

    Gene3Di3.40.630.30. 1 hit.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR000953. Chromo_domain/shadow.
    IPR016197. Chromodomain-like.
    IPR002717. MOZ_SAS.
    IPR025995. Tudor-knot.
    [Graphical view]
    PfamiPF01853. MOZ_SAS. 1 hit.
    PF11717. Tudor-knot. 1 hit.
    [Graphical view]
    SMARTiSM00298. CHROMO. 1 hit.
    [Graphical view]
    SUPFAMiSSF54160. SSF54160. 1 hit.
    SSF55729. SSF55729. 1 hit.
    PROSITEiPS51726. MYST_HAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O94446-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNDVDDESK IETKSYEAKD IVYKSKVFAF KDGEYRKAEI LMIQKRTRGV    50
    VYYVHYNDYN KRLDEWITID NIDLSKGIEY PPPEKPKKAH GKGKSSKRPK 100
    AVDRRRSITA PSKTEPSTPS TEKPEPSTPS GESDHGSNAG NESLPLLEED 150
    HKPESLSKEQ EVERLRFSGS MVQNPHEIAR IRNINKICIG DHEIEPWYFS 200
    PYPKEFSEVD IVYICSFCFC YYGSERQFQR HREKCTLQHP PGNEIYRDDY 250
    ISFFEIDGRK QRTWCRNICL LSKLFLDHKM LYYDVDPFLF YCMCRRDEYG 300
    CHLVGYFSKE KESSENYNLA CILTLPQYQR HGYGKLLIQF SYELTKREHK 350
    HGSPEKPLSD LGLISYRAYW AEQIINLVLG MRTETTIDEL ANKTSMTTND 400
    VLHTLQALNM LKYYKGQFII CISDGIEQQY ERLKNKKRRR INGDLLADWQ 450
    PPVFHPSQLR FGW 463
    Length:463
    Mass (Da):54,390
    Last modified:May 1, 1999 - v1
    Checksum:iA5C6A4AEA1207902
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329670 Genomic DNA. Translation: CAA22591.1.
    AB027858 Genomic DNA. Translation: BAA87162.1.
    PIRiT39004.
    RefSeqiNP_594630.1. NM_001020058.2.

    Genome annotation databases

    EnsemblFungiiSPAC637.12c.1; SPAC637.12c.1:pep; SPAC637.12c.
    GeneIDi2543506.
    KEGGispo:SPAC637.12c.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329670 Genomic DNA. Translation: CAA22591.1 .
    AB027858 Genomic DNA. Translation: BAA87162.1 .
    PIRi T39004.
    RefSeqi NP_594630.1. NM_001020058.2.

    3D structure databases

    ProteinModelPortali O94446.
    SMRi O94446. Positions 179-452.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 279924. 29 interactions.
    IntActi O94446. 1 interaction.
    MINTi MINT-8210884.
    STRINGi 4896.SPAC637.12c-1.

    Proteomic databases

    MaxQBi O94446.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPAC637.12c.1 ; SPAC637.12c.1:pep ; SPAC637.12c .
    GeneIDi 2543506.
    KEGGi spo:SPAC637.12c.

    Organism-specific databases

    PomBasei SPAC637.12c.

    Phylogenomic databases

    eggNOGi COG5027.
    HOGENOMi HOG000182457.
    KOi K11304.
    OMAi NIYSICM.
    OrthoDBi EOG7RFTRR.
    PhylomeDBi O94446.

    Miscellaneous databases

    NextBioi 20804516.
    PROi O94446.

    Family and domain databases

    Gene3Di 3.40.630.30. 1 hit.
    InterProi IPR016181. Acyl_CoA_acyltransferase.
    IPR000953. Chromo_domain/shadow.
    IPR016197. Chromodomain-like.
    IPR002717. MOZ_SAS.
    IPR025995. Tudor-knot.
    [Graphical view ]
    Pfami PF01853. MOZ_SAS. 1 hit.
    PF11717. Tudor-knot. 1 hit.
    [Graphical view ]
    SMARTi SM00298. CHROMO. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54160. SSF54160. 1 hit.
    SSF55729. SSF55729. 1 hit.
    PROSITEi PS51726. MYST_HAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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.
    2. "Large-scale screening of intracellular protein localization in living fission yeast cells by the use of a GFP-fusion genomic DNA library."
      Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T., Hiraoka Y.
      Genes Cells 5:169-190(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 263-441, SUBCELLULAR LOCATION.
      Strain: ATCC 38364 / 968.
    3. "BAF53/Arp4 homolog Alp5 in fission yeast is required for histone H4 acetylation, kinetochore-spindle attachment, and gene silencing at centromere."
      Minoda A., Saitoh S., Takahashi K., Toda T.
      Mol. Biol. Cell 16:316-327(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARP4.
    4. "Schizosaccharomyces pombe mst2+ encodes a MYST family histone acetyltransferase that negatively regulates telomere silencing."
      Gomez E.B., Espinosa J.M., Forsburg S.L.
      Mol. Cell. Biol. 25:8887-8903(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiESA1_SCHPO
    AccessioniPrimary (citable) accession number: O94446
    Secondary accession number(s): Q9USC8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2004
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 97 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