MST2_SCHPO
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 03-AUG-2022, entry version 142.
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; 4896.SPAC17G8.13c.1; -.
DR MaxQB; Q10325; -.
DR PaxDb; Q10325; -.
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-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-SPO-5693548; Sensing of DNA Double Strand Breaks.
DR Reactome; R-SPO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-SPO-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-SPO-9018519; Estrogen-dependent gene expression.
DR PRO; PR:Q10325; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; NAS:PomBase.
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 acetyltransferase activity (H3-K14 specific); TAS:PomBase.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
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:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0031507; P:heterochromatin assembly; IGI:PomBase.
DR GO; GO:0033696; P:heterochromatin boundary formation; IGI:PomBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 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 Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SUPFAM; SSF55729; SSF55729; 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
