{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q07794","secondaryAccessions":["D6VY01"],"uniProtkbId":"RT109_YEAST","entryAudit":{"firstPublicDate":"2006-12-12","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1996-11-01","entryVersion":180,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","commonName":"Baker's yeast","taxonId":559292,"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Histone acetyltransferase RTT109"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17272722"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17369253"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17690098"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18707894"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21256037"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29300933"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31194870"}],"value":"2.3.1.48"}]},"alternativeNames":[{"fullName":{"value":"Regulator of Ty1 transposition protein 109"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"17046836"}],"value":"RTT109"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"18568037"}],"value":"KAT11"},{"value":"KIM2"},{"value":"REM50"}],"orderedLocusNames":[{"value":"YLL002W"}],"orfNames":[{"value":"L1377"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11779788"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17046836"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17272723"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17320445"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17369253"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18568037"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18577595"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18707894"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18719104"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18723682"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19172748"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19683497"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20560668"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21256037"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29300933"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31194870"}],"value":"Histone chaperone-dependent acetylase that modifies 'Lys-9', 'Lys-14', 'Lys-23', 'Lys-27', and 'Lys-56' on histone H3 (H3K9Ac, H3K14Ac and H3K23Ac, H3K27Ac, and H3K56Ac) to promote nucleosome assembly, genomic stability, DNA repair and transcriptional regulation during mitotic S-phase (PubMed:17046836, PubMed:17272723, PubMed:17320445, PubMed:17369253, PubMed:18723682, PubMed:19172748, PubMed:19683497, PubMed:20560668, PubMed:21256037, PubMed:29300933, PubMed:31194870). Its residue selectivity is influenced by the acetylation status of histone H3, and also the presence of histone chaperone ASF1 that shifts selectivity to 'Lys-56' when H3K14Ac is already present (PubMed:31194870). H3K56 acetylation weakens the interaction between the histone core and the surrounding DNA in the nucleosomal particle and drives chromatin disassembly (PubMed:18577595). Autoacetylates (PubMed:18568037, PubMed:18707894, PubMed:18719104). Independently of acetyltransferase activity, stimulates histone deposition by VPS75 (PubMed:19172748). Involved in regulation of Ty1 transposition (PubMed:11779788)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] + CoA + 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ACTIVITY","reaction":{"name":"L-lysyl-[protein] + acetyl-CoA = N(6)-acetyl-L-lysyl-[protein] + CoA + 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PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":0.3,"unit":"uM","substrate":"acetyl-CoA (at pH 7.5, 25 degrees Celsius in the presence of VPS75 chaperone)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20560668"}]},{"constant":8.0,"unit":"uM","substrate":"acetyl-CoA (at pH 8, 30 degrees Celsius in the presence of VPS75 chaperone)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18568037"}]},{"constant":1.0,"unit":"uM","substrate":"acetyl-CoA (at pH 7.0, 25 degrees Celsius in the presence of VPS75 chaperone)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19172748"}]},{"constant":0.3,"unit":"uM","substrate":"acetyl-CoA (at pH 7.0, 25 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19172748"}]},{"constant":7.0,"unit":"uM","substrate":"histone H3 (at pH 7.5, 25 degrees Celsius in the presence of VPS75 chaperone)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20560668"}]},{"constant":8.5,"unit":"uM","substrate":"histone H3 (at pH 8, 30 degrees Celsius in the presence of VPS75 chaperone)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18568037"}]},{"constant":8.1,"unit":"uM","substrate":"histone H3 (at pH 7.0, 25 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19172748"}]},{"constant":1.4,"unit":"uM","substrate":"histone H3/H4 (at pH 7.0, 25 degrees Celsius in the presence of VPS75 chaperone)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19172748"}]},{"constant":2.9,"unit":"uM","substrate":"histone H3/H4 (at pH 7.0, 25 degrees Celsius)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19172748"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18568037"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19172748"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20560668"}],"value":"kcat is 0.11 sec(-1) with acetyl-CoA as substrate (at pH 7.5, 25 degrees Celsius in the presence of VPS75 chaperone) (PubMed:20560668). kcat is 0.19 sec(-1) with acetyl-CoA as substrate (at pH 7.0, 25 degrees Celsius in the presence of VPS75 chaperone) (PubMed:19172748). kcat is 0.0017 sec(-1) with acetyl-CoA as substrate (at pH 7.0, 25 degrees Celsius) (PubMed:19172748). kcat is 0.62 sec(-1) with histone H3 as substrate (at pH 7.5, 25 degrees Celsius in the presence of VPS75 chaperone) (PubMed:20560668). kcat is 22.5 min(-1) with histone H3 (at pH 8, 30 degrees Celsius in the presence of VPS75 chaperone) (PubMed:18568037). kcat is 0.0033 sec(-1) with acetyl-CoA as substrate (at pH 7.0, 25 degrees Celsius) (PubMed:19172748). kcat is 0.11 sec(-1) with histone H3/H4 as substrate (at pH 7.0, 25 degrees Celsius in the presence of VPS75 chaperone) (PubMed:19172748). kcat is 0.0033 sec(-1) with histone H3/H4 as substrate (at pH 7.0, 25 degrees Celsius) (PubMed:19172748)."}]}},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20560668"}],"value":"Optimum pH is >8.5."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17272723"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17320445"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17369253"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17690098"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18719104"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18723682"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19172748"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20560668"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21256037"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21454705"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29300933"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31387991"}],"value":"Forms a complex composed of two RTT109 subunits and one VPS75 homodimer; each RTT109 subunit interacts predominantly with VPS75 instead of interacting with the other RTT109 subunit (PubMed:17320445, PubMed:18719104, PubMed:20560668, PubMed:21256037, PubMed:31387991). Interacts with VPS75; the interaction is direct (PubMed:17272723, PubMed:17320445, PubMed:17369253, PubMed:17690098, PubMed:18719104, PubMed:18723682, PubMed:20560668, PubMed:21256037, PubMed:31387991). Interacts (via C-terminus) with ASF1; the interaction is direct (PubMed:17320445, PubMed:17690098, PubMed:29300933, PubMed:31387991). Interacts with histone H3/H4 heterodimers via histone H3 (PubMed:19172748, PubMed:21454705)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q07794","intActId":"EBI-2887026"},"interactantTwo":{"uniProtKBAccession":"P25293","geneName":"NAP1","intActId":"EBI-11850"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q07794","intActId":"EBI-2887026"},"interactantTwo":{"uniProtKBAccession":"P53853","geneName":"VPS75","intActId":"EBI-29225"},"numberOfExperiments":21,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14562095"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15282802"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15282802"}],"value":"Expression peaks in cell cycle G1"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18568037"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18719104"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19172748"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19683497"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21256037"}],"value":"Abolishes acetylation of histone H3 'Lys-56'; simultaneous disruption of GCN5 also abolishes acetylation of histone H3 'Lys-9' and 'Lys-27' (PubMed:21256037). Decreases acetylation of histone H3 'Lys-9' and 'Lys-23' (PubMed:19172748). Decreases HTA1 RNA level; simultaneous disruption of HIR1 or RTT106 alleviates the effect (PubMed:19683497). Increases sensitivity to methyl methane sulfonate, hydroxyurea, and camptothecin (genotoxic stress) (PubMed:18568037, PubMed:18719104)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14562106"}],"value":"Present with 1140 molecules/cell in log phase SD medium"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the RTT109 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":436,"modifier":"EXACT"}},"description":"Histone acetyltransferase RTT109","featureId":"PRO_0000268738"},{"type":"Domain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":404,"modifier":"EXACT"}},"description":"Rtt109-type 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