GCN5_SCHPO
ID GCN5_SCHPO Reviewed; 454 AA.
AC Q9UUK2;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Histone acetyltransferase gcn5 {ECO:0000305};
DE EC=2.3.1.48 {ECO:0000269|PubMed:14988732};
DE AltName: Full=Histone crotonyltransferase gcn5 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q03330};
GN Name=gcn5; ORFNames=SPAC1952.05;
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 [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=14988732; DOI=10.1038/sj.emboj.7600138;
RA Yamada T., Mizuno K., Hirota K., Kon N., Wahls W.P., Hartsuiker E.,
RA Murofushi H., Shibata T., Ohta K.;
RT "Roles of histone acetylation and chromatin remodeling factor in a meiotic
RT recombination hotspot.";
RL EMBO J. 23:1792-1803(2004).
RN [2]
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 [3]
RP INTERACTION WITH TAF72.
RX PubMed=11279037; DOI=10.1074/jbc.m100248200;
RA Mitsuzawa H., Seino H., Yamao F., Ishihama A.;
RT "Two WD repeat-containing TATA-binding protein-associated factors in
RT fission yeast that suppress defects in the anaphase-promoting complex.";
RL J. Biol. Chem. 276:17117-17124(2001).
CC -!- FUNCTION: Histone acetyltransferase that acetylates histone H2B to form
CC H2BK11ac and H2BK16ac, histone H3 to form H3K14ac, with a lower
CC preference histone H4 to form H4K8ac and H4K16ac, and contributes to
CC H2A.Z acetylation (PubMed:14988732). Acetylation of histones gives a
CC specific tag for epigenetic transcription activation (PubMed:14988732).
CC In addition to histone acetyltransferase, can use different acyl-CoA
CC substrates, such as (2E)-butenoyl-CoA (crotonyl-CoA) and is able to
CC mediate histone crotonylation (By similarity).
CC {ECO:0000250|UniProtKB:Q03330, ECO:0000269|PubMed:14988732}.
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:0000269|PubMed:14988732};
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:Q03330};
CC -!- SUBUNIT: Interacts with taf72. {ECO:0000269|PubMed:11279037}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. GCN5 subfamily.
CC {ECO:0000305}.
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DR EMBL; AB162439; BAD11106.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB52569.1; -; Genomic_DNA.
DR PIR; T37933; T37933.
DR RefSeq; NP_594807.1; NM_001020236.2.
DR AlphaFoldDB; Q9UUK2; -.
DR SMR; Q9UUK2; -.
DR BioGRID; 278971; 290.
DR IntAct; Q9UUK2; 3.
DR MINT; Q9UUK2; -.
DR STRING; 4896.SPAC1952.05.1; -.
DR iPTMnet; Q9UUK2; -.
DR MaxQB; Q9UUK2; -.
DR PaxDb; Q9UUK2; -.
DR PRIDE; Q9UUK2; -.
DR EnsemblFungi; SPAC1952.05.1; SPAC1952.05.1:pep; SPAC1952.05.
DR GeneID; 2542513; -.
DR KEGG; spo:SPAC1952.05; -.
DR PomBase; SPAC1952.05; gcn5.
DR VEuPathDB; FungiDB:SPAC1952.05; -.
DR eggNOG; KOG1472; Eukaryota.
DR HOGENOM; CLU_015741_2_0_1; -.
DR InParanoid; Q9UUK2; -.
DR OMA; RWMGYIK; -.
DR PhylomeDB; Q9UUK2; -.
DR Reactome; R-SPO-5689880; Ub-specific processing proteases.
DR Reactome; R-SPO-9018519; Estrogen-dependent gene expression.
DR PRO; PR:Q9UUK2; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005721; C:pericentric heterochromatin; EXP:PomBase.
DR GO; GO:0000124; C:SAGA complex; IDA:PomBase.
DR GO; GO:0010484; F:H3 histone acetyltransferase activity; IDA:PomBase.
DR GO; GO:0036408; F:histone acetyltransferase activity (H3-K14 specific); IMP:PomBase.
DR GO; GO:0043993; F:histone acetyltransferase activity (H3-K18 specific); IDA:PomBase.
DR GO; GO:0043992; F:histone acetyltransferase activity (H3-K9 specific); IDA:PomBase.
DR GO; GO:0140064; F:peptide crotonyltransferase activity; IEA:RHEA.
DR GO; GO:1990841; F:promoter-specific chromatin binding; EXP:PomBase.
DR GO; GO:0006338; P:chromatin remodeling; IMP:PomBase.
DR GO; GO:0006310; P:DNA recombination; NAS:PomBase.
DR GO; GO:0043966; P:histone H3 acetylation; IBA:GO_Central.
DR GO; GO:0010515; P:negative regulation of induction of conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:1905533; P:negative regulation of leucine import across plasma membrane; IMP:PomBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:PomBase.
DR Gene3D; 1.20.920.10; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR037800; GCN5.
DR InterPro; IPR000182; GNAT_dom.
DR PANTHER; PTHR45750; PTHR45750; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Activator; Acyltransferase; Bromodomain; Chromatin regulator; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Transferase.
FT CHAIN 1..454
FT /note="Histone acetyltransferase gcn5"
FT /id="PRO_0000211199"
FT DOMAIN 118..273
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT DOMAIN 360..430
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 191
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 195..197
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 202..208
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 234..237
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT SITE 191
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 454 AA; 51976 MW; FF99039B00E8ECB3 CRC64;
MSNSLNDQTR PPDSSVVDST SSNFPNASND SVHDKPVKQD EQSNPNVREA IANSDGQESL
AVKENKDTES SSSHFVPNGV SNSKKRKLVA TDLDVDFDIS SVRVTEKPSV LEEKSGVIQF
RVVSNDDTAD SMIMLTGLKN IFMKQLPKMP KEYITRLIYD RNHLSMTIVK DNLHVVGGIT
YRPFEQRGFA EIVFCAIASN EQVRGYGSHL MNHLKDYVRG TTTIQHFLTY ADNYAIGYFK
KQGFTKEITL DKSIWVGYIK DYEGGTLMQC TMIPKIKYLE ANLILAIQKA AVVSKINRIT
RSNVVYPGLD VFKDGPAHIE PSQVPGLMEV GWCKEMEELS KKPRPKPFFA VLEMLFTEMQ
NHPSSWPFMQ PVSKEDVPDY YEVIEHPMDL STMEFRLRNN QYESVEEFIR DAKYIFDNCR
SYNDSNTTYY KNADRLEKFF QKKLRETEYS HLAD
