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)

Q10325

- MST2_SCHPO

UniProt

Q10325 - MST2_SCHPO

Protein

Histone acetyltransferase mst2

Gene

mst2

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 98 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Component of the mst2 complex which is a highly specific H3 lysine 14 (H3K14) acetyltransferase that functions together with gcn5 to regulate global levels of H3K14 acetylation (H3K14ac), critical for DNA damage checkpoint activation. Negatively regulates telomere silencing. Telomere silencing is increased due to histone hypoacetylation and/or an increase in the ratio of methylated histones to acetylated histones. Telomeric histone acetylation contributes to normal meiotic progression.2 Publications

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei198 – 1981By similarity
    Active sitei240 – 2401NucleophileBy similarity
    Binding sitei243 – 2431Acetyl-CoABy similarity
    Binding sitei278 – 2781Acetyl-CoABy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri132 – 15423C2HC-typeAdd
    BLAST

    GO - Molecular functioni

    1. histone acetyltransferase activity (H3-K14 specific) Source: PomBase
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: UniProtKB-KW
    2. heterochromatin maintenance involved in chromatin silencing at centromere outer repeat region Source: PomBase
    3. histone H3-K14 acetylation Source: GOC
    4. negative regulation of chromatin silencing at telomere Source: PomBase
    5. regulation of meiotic cell cycle Source: PomBase

    Keywords - Molecular functioni

    Chromatin regulator, Transferase

    Keywords - Biological processi

    DNA damage

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone acetyltransferase mst2 (EC:2.3.1.48)
    Gene namesi
    Name:mst2
    ORF Names:SPAC17G8.13c
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome I

    Organism-specific databases

    PomBaseiSPAC17G8.13c.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: PomBase
    2. histone acetyltransferase complex Source: PomBase
    3. Mst2 histone acetyltransferase complex Source: PomBase
    4. nuclear chromatin Source: PomBase
    5. nucleus Source: PomBase

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 407407Histone acetyltransferase mst2PRO_0000051565Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei198 – 1981N6-acetyllysine; by autocatalysisBy similarity

    Post-translational modificationi

    Autoacetylation at Lys-198 is required for proper function.By similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ10325.

    Interactioni

    Subunit structurei

    Component of the mst2 complex composed of at least eaf6, mst2, nto1, pdp3, ptf1, ptf2 and tfg3.1 Publication

    Protein-protein interaction databases

    BioGridi278645. 97 interactions.
    MINTiMINT-4698771.
    STRINGi4896.SPAC17G8.13c-1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ10325.
    SMRiQ10325. Positions 102-372.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini98 – 372275MYST-type HATAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni248 – 2547Acetyl-CoA bindingBy similarity

    Sequence similaritiesi

    Belongs to the MYST (SAS/MOZ) family.Curated
    Contains 1 C2HC-type zinc finger.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri132 – 15423C2HC-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5027.
    KOiK11378.
    OMAiYICESCL.
    OrthoDBiEOG7RFTRR.
    PhylomeDBiQ10325.

    Family and domain databases

    Gene3Di3.40.630.30. 1 hit.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR002717. MOZ_SAS.
    [Graphical view]
    PfamiPF01853. MOZ_SAS. 1 hit.
    [Graphical view]
    SUPFAMiSSF55729. SSF55729. 1 hit.
    PROSITEiPS51726. MYST_HAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q10325-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPATILKSTA SSKTLLIIKF DTNSSRYPFY KKHLLELNSE STFLGLLTKG    50
    QADTSITRLN QDDVRLFEKA KTVADRTKDV AYSFSDPILS TQLRTPPPQP 100
    TSIRYLYFGT YRIKPWYTSP YPEEYSCAKN LYICESCLKY MNSDHVLQRH 150
    KMKCSWSYPP GDEIYRDKNI SIFEVDGQRQ PIYCQNLCLL AKMFLHSKML 200
    YYDVEPFLFY VLTEFDGQEC KVIGYFSKEK RSASDYNVSC ILTLPIYQRR 250
    GYGVFLIDFS YLLTQVEGKL GSPEKPLSDL GLVTYRSYWK MRVAKALLEI 300
    TTPISINAIA KSTSMVCDDV ISTLESLSVF KYDPLKKKYV LQLKRDELEN 350
    VYKAWNIKHP QRVNPKLLRW TPYLGEEQIS NLLLKENILI PLPQKRLLDN 400
    SHHLDSV 407
    Length:407
    Mass (Da):47,275
    Last modified:October 1, 1996 - v1
    Checksum:i27B70EB7AB947102
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329670 Genomic DNA. Translation: CAA93696.1.
    PIRiT37865.
    RefSeqiNP_593736.1. NM_001019167.2.

    Genome annotation databases

    EnsemblFungiiSPAC17G8.13c.1; SPAC17G8.13c.1:pep; SPAC17G8.13c.
    GeneIDi2542170.
    KEGGispo:SPAC17G8.13c.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329670 Genomic DNA. Translation: CAA93696.1 .
    PIRi T37865.
    RefSeqi NP_593736.1. NM_001019167.2.

    3D structure databases

    ProteinModelPortali Q10325.
    SMRi Q10325. Positions 102-372.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 278645. 97 interactions.
    MINTi MINT-4698771.
    STRINGi 4896.SPAC17G8.13c-1.

    Proteomic databases

    MaxQBi Q10325.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPAC17G8.13c.1 ; SPAC17G8.13c.1:pep ; SPAC17G8.13c .
    GeneIDi 2542170.
    KEGGi spo:SPAC17G8.13c.

    Organism-specific databases

    PomBasei SPAC17G8.13c.

    Phylogenomic databases

    eggNOGi COG5027.
    KOi K11378.
    OMAi YICESCL.
    OrthoDBi EOG7RFTRR.
    PhylomeDBi Q10325.

    Miscellaneous databases

    NextBioi 20803241.

    Family and domain databases

    Gene3Di 3.40.630.30. 1 hit.
    InterProi IPR016181. Acyl_CoA_acyltransferase.
    IPR002717. MOZ_SAS.
    [Graphical view ]
    Pfami PF01853. MOZ_SAS. 1 hit.
    [Graphical view ]
    SUPFAMi 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. "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.
    3. "Histone H3 lysine 14 acetylation is required for activation of a DNA damage checkpoint in fission yeast."
      Wang Y., Kallgren S.P., Reddy B.D., Kuntz K., Lopez-Maury L., Thompson J., Watt S., Ma C., Hou H., Shi Y., Yates J.R. III, Bahler J., O'Connell M.J., Jia S.
      J. Biol. Chem. 287:4386-4393(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MST2 COMPLEX, FUNCTION.
    4. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
      Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
      Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMST2_SCHPO
    AccessioniPrimary (citable) accession number: Q10325
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 98 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