ESA1_SCHPO
ID ESA1_SCHPO Reviewed; 463 AA.
AC O94446; Q9USC8;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Histone acetyltransferase mst1 {ECO:0000305};
DE EC=2.3.1.48 {ECO:0000269|PubMed:20299449};
DE AltName: Full=Protein 2-hydroxyisobutyryltransferase mst1 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:29192674};
DE AltName: Full=Protein acetyltransferase mst1 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q08649};
DE AltName: Full=Protein crotonyltransferase mst1 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q08649};
GN Name=mst1 {ECO:0000303|PubMed:16199868, ECO:0000303|PubMed:18505873,
GN ECO:0000312|PomBase:SPAC637.12c};
GN Synonyms=esa1, kat5 {ECO:0000303|PubMed:18505873}; ORFNames=SPAC637.12c;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 263-441, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP INTERACTION WITH ARP4.
RX PubMed=15483052; DOI=10.1091/mbc.e04-06-0519;
RA Minoda A., Saitoh S., Takahashi K., Toda T.;
RT "BAF53/Arp4 homolog Alp5 in fission yeast is required for histone H4
RT acetylation, kinetochore-spindle attachment, and gene silencing at
RT centromere.";
RL Mol. Biol. Cell 16:316-327(2005).
RN [4]
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 [5]
RP FUNCTION, AND MUTAGENESIS OF LEU-344.
RX PubMed=18505873; DOI=10.1534/genetics.107.085779;
RA Gomez E.B., Nugent R.L., Laria S., Forsburg S.L.;
RT "Schizosaccharomyces pombe histone acetyltransferase Mst1 (KAT5) is an
RT essential protein required for damage response and chromosome
RT segregation.";
RL Genetics 179:757-771(2008).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=20299449; DOI=10.1101/gad.1881710;
RA Xhemalce B., Kouzarides T.;
RT "A chromodomain switch mediated by histone H3 Lys 4 acetylation regulates
RT heterochromatin assembly.";
RL Genes Dev. 24:647-652(2010).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=29192674; DOI=10.1038/cr.2017.149;
RA Huang H., Luo Z., Qi S., Huang J., Xu P., Wang X., Gao L., Li F., Wang J.,
RA Zhao W., Gu W., Chen Z., Dai L., Dai J., Zhao Y.;
RT "Landscape of the regulatory elements for lysine 2-hydroxyisobutyrylation
RT pathway.";
RL Cell Res. 28:111-125(2018).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-344.
RX PubMed=33723569; DOI=10.1093/genetics/iyab042;
RA Li T., Petreaca R.C., Forsburg S.L.;
RT "Schizosaccharomyces pombe KAT5 contributes to resection and repair of a
RT DNA double-strand break.";
RL Genetics 218:0-0(2021).
CC -!- FUNCTION: Catalytic component of the NuA4 histone acetyltransferase
CC (HAT) complex which is involved in epigenetic transcriptional
CC activation of selected genes principally by acetylation of nucleosomal
CC histones H4, H3, H2B, H2A and H2A variant H2A.Z (PubMed:16199868).
CC Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac,
CC histone H3 to form H3K14ac, and histone H2A to form H2AK4ac and H2AK7ac
CC (By similarity). The NuA4 complex is involved in the DNA damage
CC response and is required for chromosome segregation (PubMed:18505873,
CC PubMed:33723569). The NuA4 complex plays a direct role in repair of DNA
CC double-strand breaks (DSBs) through homologous recombination
CC (PubMed:33723569). Recruitment to promoters depends on H3K4me (By
CC similarity). Also acetylates non-histone proteins (By similarity). In
CC addition to protein acetyltransferase, can use different acyl-CoA
CC substrates, such as 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA)
CC or (2E)-butenoyl-CoA (crotonyl-CoA), and is able to mediate protein 2-
CC hydroxyisobutyrylation and crotonylation, respectively
CC (PubMed:29192674). {ECO:0000250|UniProtKB:Q08649,
CC ECO:0000269|PubMed:16199868, ECO:0000269|PubMed:18505873,
CC ECO:0000269|PubMed:29192674, ECO:0000269|PubMed:33723569}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845,
CC Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000269|PubMed:20299449};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993;
CC Evidence={ECO:0000269|PubMed:20299449};
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;
CC Evidence={ECO:0000250|UniProtKB:Q08649};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949;
CC Evidence={ECO:0000250|UniProtKB:Q08649};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyisobutanoyl-CoA + L-lysyl-[protein] = CoA + H(+) +
CC N(6)-(2-hydroxyisobutanoyl)-L-lysyl-[protein]; Xref=Rhea:RHEA:24180,
CC Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15921, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:131780,
CC ChEBI:CHEBI:144968; Evidence={ECO:0000269|PubMed:29192674};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24181;
CC Evidence={ECO:0000269|PubMed:29192674};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-butenoyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-
CC (2E)-butenoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:53908, Rhea:RHEA-
CC COMP:9752, Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57332,
CC ChEBI:CHEBI:137954; Evidence={ECO:0000250|UniProtKB:Q08649};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53909;
CC Evidence={ECO:0000250|UniProtKB:Q08649};
CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex (By
CC similarity). Interacts with arp4 (PubMed:15483052).
CC {ECO:0000250|UniProtKB:Q08649, ECO:0000269|PubMed:15483052}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889,
CC ECO:0000269|PubMed:16199868}. Chromosome {ECO:0000269|PubMed:20299449,
CC ECO:0000269|PubMed:33723569}. Note=Localizes to pericentric
CC heterochromatin (PubMed:20299449). Following DNA damage, localizes to
CC sites of DNA damage, such as double stand breaks (DSBs)
CC (PubMed:33723569). {ECO:0000269|PubMed:20299449,
CC ECO:0000269|PubMed:33723569}.
CC -!- DOMAIN: The ESA1-RPD3 motif is common to ESA1 and RPD3 and is required
CC for ESA1 histone acetyl-transferase (HAT) activity and RPD3 histone
CC deacetylase (HDAC) activity. {ECO:0000250|UniProtKB:Q08649}.
CC -!- PTM: Autoacetylation at Lys-279 is required for proper function.
CC {ECO:0000250|UniProtKB:Q08649}.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}.
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DR EMBL; CU329670; CAA22591.1; -; Genomic_DNA.
DR EMBL; AB027858; BAA87162.1; -; Genomic_DNA.
DR PIR; T39004; T39004.
DR RefSeq; NP_594630.1; NM_001020058.2.
DR AlphaFoldDB; O94446; -.
DR SMR; O94446; -.
DR BioGRID; 279924; 31.
DR IntAct; O94446; 3.
DR MINT; O94446; -.
DR STRING; 4896.SPAC637.12c.1; -.
DR iPTMnet; O94446; -.
DR MaxQB; O94446; -.
DR PaxDb; O94446; -.
DR PRIDE; O94446; -.
DR EnsemblFungi; SPAC637.12c.1; SPAC637.12c.1:pep; SPAC637.12c.
DR GeneID; 2543506; -.
DR KEGG; spo:SPAC637.12c; -.
DR PomBase; SPAC637.12c; mst1.
DR VEuPathDB; FungiDB:SPAC637.12c; -.
DR eggNOG; KOG2747; Eukaryota.
DR HOGENOM; CLU_011815_2_0_1; -.
DR InParanoid; O94446; -.
DR OMA; SMTQNQT; -.
DR PhylomeDB; O94446; -.
DR Reactome; R-SPO-6804758; Regulation of TP53 Activity through Acetylation.
DR PRO; PR:O94446; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:PomBase.
DR GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; ISO:PomBase.
DR GO; GO:0004402; F:histone acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0044016; F:histone acetyltransferase activity (H3-K4 specific); IDA: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:0106226; F:peptide 2-hydroxyisobutyryltransferase activity; IEA:RHEA.
DR GO; GO:0140065; F:peptide butyryltransferase activity; IDA:UniProtKB.
DR GO; GO:0140064; F:peptide crotonyltransferase activity; IEA:RHEA.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0034508; P:centromere complex assembly; IGI:PomBase.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; IGI:PomBase.
DR GO; GO:0031452; P:negative regulation of heterochromatin assembly; IMP:PomBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IMP:PomBase.
DR GO; GO:0031453; P:positive regulation of heterochromatin assembly; IMP:PomBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0048478; P:replication fork protection; IGI:PomBase.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR002717; HAT_MYST-type.
DR InterPro; IPR025995; Tudor-knot.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR040706; Zf-MYST.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF11717; Tudor-knot; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Chromatin regulator; Chromosome; DNA damage;
KW DNA repair; Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..463
FT /note="Histone acetyltransferase mst1"
FT /id="PRO_0000051564"
FT DOMAIN 22..74
FT /note="Tudor-knot"
FT /evidence="ECO:0000255"
FT DOMAIN 179..451
FT /note="MYST-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT ZN_FING 212..237
FT /note="C2HC MYST-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT REGION 76..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 262..283
FT /note="ESA1-RPD3 motif"
FT COMPBIAS 111..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 355
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q08649"
FT BINDING 320..324
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q08649"
FT BINDING 329..335
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q08649"
FT BINDING 359
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q08649"
FT SITE 321
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q08649"
FT MOD_RES 279
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q08649"
FT MUTAGEN 344
FT /note="L->S: Temperature-sensitive mutation; sensitivity to
FT DNA damaging agents even at permissive temperatures.
FT Impaired repair of DNA double-strand breaks (DSBs) through
FT homologous recombination."
FT /evidence="ECO:0000269|PubMed:18505873,
FT ECO:0000269|PubMed:33723569"
SQ SEQUENCE 463 AA; 54390 MW; A5C6A4AEA1207902 CRC64;
MSNDVDDESK IETKSYEAKD IVYKSKVFAF KDGEYRKAEI LMIQKRTRGV VYYVHYNDYN
KRLDEWITID NIDLSKGIEY PPPEKPKKAH GKGKSSKRPK AVDRRRSITA PSKTEPSTPS
TEKPEPSTPS GESDHGSNAG NESLPLLEED HKPESLSKEQ EVERLRFSGS MVQNPHEIAR
IRNINKICIG DHEIEPWYFS PYPKEFSEVD IVYICSFCFC YYGSERQFQR HREKCTLQHP
PGNEIYRDDY ISFFEIDGRK QRTWCRNICL LSKLFLDHKM LYYDVDPFLF YCMCRRDEYG
CHLVGYFSKE KESSENYNLA CILTLPQYQR HGYGKLLIQF SYELTKREHK HGSPEKPLSD
LGLISYRAYW AEQIINLVLG MRTETTIDEL ANKTSMTTND VLHTLQALNM LKYYKGQFII
CISDGIEQQY ERLKNKKRRR INGDLLADWQ PPVFHPSQLR FGW
