ID   MST2_SCHPO              Reviewed;         407 AA.
AC   Q10325;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   24-JAN-2024, entry version 149.
DE   RecName: Full=Histone acetyltransferase mst2;
DE            EC=2.3.1.48 {ECO:0000250|UniProtKB:Q9H7Z6};
GN   Name=mst2; ORFNames=SPAC17G8.13c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=16199868; DOI=10.1128/mcb.25.20.8887-8903.2005;
RA   Gomez E.B., Espinosa J.M., Forsburg S.L.;
RT   "Schizosaccharomyces pombe mst2+ encodes a MYST family histone
RT   acetyltransferase that negatively regulates telomere silencing.";
RL   Mol. Cell. Biol. 25:8887-8903(2005).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MST2 COMPLEX,
RP   AND FUNCTION.
RX   PubMed=22184112; DOI=10.1074/jbc.m111.329417;
RA   Wang Y., Kallgren S.P., Reddy B.D., Kuntz K., Lopez-Maury L., Thompson J.,
RA   Watt S., Ma C., Hou H., Shi Y., Yates J.R. III, Bahler J., O'Connell M.J.,
RA   Jia S.;
RT   "Histone H3 lysine 14 acetylation is required for activation of a DNA
RT   damage checkpoint in fission yeast.";
RL   J. Biol. Chem. 287:4386-4393(2012).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Component of the mst2 complex which is a highly specific H3
CC       lysine 14 (H3K14) acetyltransferase that functions together with gcn5
CC       to regulate global levels of H3K14 acetylation (H3K14ac), critical for
CC       DNA damage checkpoint activation. Negatively regulates telomere
CC       silencing. Telomere silencing is increased due to histone
CC       hypoacetylation and/or an increase in the ratio of methylated histones
CC       to acetylated histones. Telomeric histone acetylation contributes to
CC       normal meiotic progression. {ECO:0000269|PubMed:16199868,
CC       ECO:0000269|PubMed:22184112}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC         lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC         Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC         Evidence={ECO:0000250|UniProtKB:Q9H7Z6};
CC   -!- SUBUNIT: Component of the mst2 complex composed of at least eaf6, mst2,
CC       nto1, pdp3, ptf1, ptf2 and tfg3. {ECO:0000269|PubMed:22184112}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- PTM: Autoacetylation at Lys-198 is required for proper function.
CC       {ECO:0000250|UniProtKB:Q9H7Z6}.
CC   -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}.
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DR   EMBL; CU329670; CAA93696.1; -; Genomic_DNA.
DR   PIR; T37865; T37865.
DR   RefSeq; NP_593736.1; NM_001019167.2.
DR   AlphaFoldDB; Q10325; -.
DR   SMR; Q10325; -.
DR   BioGRID; 278645; 110.
DR   STRING; 284812.Q10325; -.
DR   iPTMnet; Q10325; -.
DR   MaxQB; Q10325; -.
DR   PaxDb; 4896-SPAC17G8-13c-1; -.
DR   EnsemblFungi; SPAC17G8.13c.1; SPAC17G8.13c.1:pep; SPAC17G8.13c.
DR   GeneID; 2542170; -.
DR   KEGG; spo:SPAC17G8.13c; -.
DR   PomBase; SPAC17G8.13c; mst2.
DR   VEuPathDB; FungiDB:SPAC17G8.13c; -.
DR   eggNOG; KOG2747; Eukaryota.
DR   HOGENOM; CLU_011815_2_2_1; -.
DR   InParanoid; Q10325; -.
DR   PhylomeDB; Q10325; -.
DR   Reactome; R-SPO-6804758; Regulation of TP53 Activity through Acetylation.
DR   PRO; PR:Q10325; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0036410; C:Mst2 histone acetyltransferase complex; TAS:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0036408; F:histone H3K14 acetyltransferase activity; TAS:PomBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR   GO; GO:0006974; P:DNA damage response; IEA:UniProtKB-KW.
DR   GO; GO:0033696; P:heterochromatin boundary formation; IGI:PomBase.
DR   GO; GO:0031507; P:heterochromatin formation; IGI:PomBase.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.30.60.60; N-acetyl transferase-like; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR002717; HAT_MYST-type.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR040706; Zf-MYST.
DR   PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR10615:SF102; HISTONE ACETYLTRANSFERASE; 1.
DR   Pfam; PF01853; MOZ_SAS; 1.
DR   Pfam; PF17772; zf-MYST; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   PROSITE; PS51726; MYST_HAT; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chromatin regulator; Cytoplasm; DNA damage; Metal-binding;
KW   Nucleus; Reference proteome; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..407
FT                   /note="Histone acetyltransferase mst2"
FT                   /id="PRO_0000051565"
FT   DOMAIN          98..372
FT                   /note="MYST-type HAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT   ZN_FING         131..156
FT                   /note="C2HC MYST-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT   ACT_SITE        274
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT   BINDING         241..243
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT   BINDING         243
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250"
FT   BINDING         248..254
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT   BINDING         278
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT   BINDING         287
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT   MOD_RES         198
FT                   /note="N6-acetyllysine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
SQ   SEQUENCE   407 AA;  47275 MW;  27B70EB7AB947102 CRC64;
     MPATILKSTA SSKTLLIIKF DTNSSRYPFY KKHLLELNSE STFLGLLTKG QADTSITRLN
     QDDVRLFEKA KTVADRTKDV AYSFSDPILS TQLRTPPPQP TSIRYLYFGT YRIKPWYTSP
     YPEEYSCAKN LYICESCLKY MNSDHVLQRH KMKCSWSYPP GDEIYRDKNI SIFEVDGQRQ
     PIYCQNLCLL AKMFLHSKML YYDVEPFLFY VLTEFDGQEC KVIGYFSKEK RSASDYNVSC
     ILTLPIYQRR GYGVFLIDFS YLLTQVEGKL GSPEKPLSDL GLVTYRSYWK MRVAKALLEI
     TTPISINAIA KSTSMVCDDV ISTLESLSVF KYDPLKKKYV LQLKRDELEN VYKAWNIKHP
     QRVNPKLLRW TPYLGEEQIS NLLLKENILI PLPQKRLLDN SHHLDSV
//