ID   SAS3_YEAST              Reviewed;         831 AA.
AC   P34218; D6VPU7;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   27-MAR-2024, entry version 187.
DE   RecName: Full=Histone acetyltransferase SAS3;
DE            EC=2.3.1.48 {ECO:0000269|PubMed:10600516, ECO:0000269|PubMed:10817755};
DE   AltName: Full=Something about silencing protein 3 {ECO:0000303|PubMed:10817755};
GN   Name=SAS3; OrderedLocusNames=YBL052C; ORFNames=YBL0507, YBL0515;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8154187; DOI=10.1002/yea.320091210;
RA   Scherens B., el Bakkoury M., Vierendeels F., Dubois E., Messenguy F.;
RT   "Sequencing and functional analysis of a 32,560 bp segment on the left arm
RT   of yeast chromosome II. Identification of 26 open reading frames, including
RT   the KIP1 and SEC17 genes.";
RL   Yeast 9:1355-1371(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   PROTEIN SEQUENCE OF 799-813, FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH
RP   SPT16, AND MUTAGENESIS OF 426-GLN-ARG-427; 429-GLY--GLY-431 AND
RP   434-LEU-MET-435.
RX   PubMed=10817755;
RA   John S., Howe L., Tafrov S.T., Grant P.A., Sternglanz R., Workman J.L.;
RT   "The something about silencing protein, Sas3, is the catalytic subunit of
RT   NuA3, a yTAF(II)30-containing HAT complex that interacts with the Spt16
RT   subunit of the yeast CP (Cdc68/Pob3)-FACT complex.";
RL   Genes Dev. 14:1196-1208(2000).
RN   [5]
RP   CHARACTERIZATION.
RX   PubMed=8782818; DOI=10.1038/ng0996-42;
RA   Reifsnyder C., Lowell J., Clarke A., Pillus L.;
RT   "Yeast SAS silencing genes and human genes associated with AML and HIV-1
RT   Tat interactions are homologous with acetyltransferases.";
RL   Nat. Genet. 14:42-49(1996).
RN   [6]
RP   ERRATUM OF PUBMED:8782818.
RX   PubMed=9140406; DOI=10.1038/ng0597-106;
RA   Reifsnyder C., Lowell J., Clarke A., Pillus L.;
RL   Nat. Genet. 16:109-109(1997).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-303; CYS-306; HIS-319
RP   AND CYS-323.
RX   PubMed=10600516; DOI=10.1006/bbrc.1999.1836;
RA   Takechi S., Nakayama T.;
RT   "Sas3 is a histone acetyltransferase and requires a zinc finger motif.";
RL   Biochem. Biophys. Res. Commun. 266:405-410(1999).
RN   [8]
RP   FUNCTION.
RX   PubMed=11731478; DOI=10.1101/gad.931401;
RA   Howe L., Auston D., Grant P., John S., Cook R.G., Workman J.L., Pillus L.;
RT   "Histone H3 specific acetyltransferases are essential for cell cycle
RT   progression.";
RL   Genes Dev. 15:3144-3154(2001).
RN   [9]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [10]
RP   FUNCTION OF THE NUA3 COMPLEX.
RX   PubMed=16581777; DOI=10.1128/mcb.26.8.3018-3028.2006;
RA   Martin D.G., Grimes D.E., Baetz K., Howe L.;
RT   "Methylation of histone H3 mediates the association of the NuA3 histone
RT   acetyltransferase with chromatin.";
RL   Mol. Cell. Biol. 26:3018-3028(2006).
RN   [11]
RP   FUNCTION OF THE NUA3 COMPLEX, IDENTIFICATION IN THE NUA3 COMPLEX, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=17157260; DOI=10.1016/j.molcel.2006.10.026;
RA   Taverna S.D., Ilin S., Rogers R.S., Tanny J.C., Lavender H., Li H.,
RA   Baker L., Boyle J., Blair L.P., Chait B.T., Patel D.J., Aitchison J.D.,
RA   Tackett A.J., Allis C.D.;
RT   "Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT
RT   activity at K14 of H3 and transcription at a subset of targeted ORFs.";
RL   Mol. Cell 24:785-796(2006).
CC   -!- FUNCTION: Catalytic component of the histone acetyltransferase NuA3
CC       complex, that acetylates Lys-14 of histone H3. Recruitment of NuA3 to
CC       nucleosomes requires methylated histone H3. In conjunction with the
CC       FACT complex, NuA3 may be involved in transcriptional regulation. In
CC       vitro, SAS3 acetylates free histones H3 and H4. It is involved in
CC       silencing the HMR locus. {ECO:0000269|PubMed:10600516,
CC       ECO:0000269|PubMed:10817755, ECO:0000269|PubMed:11731478,
CC       ECO:0000269|PubMed:16581777, ECO:0000269|PubMed:17157260}.
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:10600516, ECO:0000269|PubMed:10817755};
CC   -!- SUBUNIT: Component of the NuA3 complex, composed of at least NTO1,
CC       SAS3, TAF14, YNG1 and EAF6. SAS3 interacts with CDC68/SPT16.
CC       {ECO:0000269|PubMed:10817755, ECO:0000269|PubMed:17157260}.
CC   -!- INTERACTION:
CC       P34218; P35189: TAF14; NbExp=3; IntAct=EBI-16484, EBI-18920;
CC       P34218; Q08465: YNG1; NbExp=5; IntAct=EBI-16484, EBI-31890;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC   -!- PTM: Autoacetylation at Lys-367 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; Z23261; CAA80794.1; -; Genomic_DNA.
DR   EMBL; Z35814; CAA84873.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07067.1; -; Genomic_DNA.
DR   PIR; S39835; S39835.
DR   RefSeq; NP_009501.1; NM_001178292.1.
DR   AlphaFoldDB; P34218; -.
DR   SMR; P34218; -.
DR   BioGRID; 32646; 207.
DR   ComplexPortal; CPX-1810; NuA3 histone acetyltransferase complex.
DR   DIP; DIP-4277N; -.
DR   IntAct; P34218; 25.
DR   MINT; P34218; -.
DR   STRING; 4932.YBL052C; -.
DR   iPTMnet; P34218; -.
DR   MaxQB; P34218; -.
DR   PaxDb; 4932-YBL052C; -.
DR   PeptideAtlas; P34218; -.
DR   DNASU; 852228; -.
DR   EnsemblFungi; YBL052C_mRNA; YBL052C; YBL052C.
DR   GeneID; 852228; -.
DR   KEGG; sce:YBL052C; -.
DR   AGR; SGD:S000000148; -.
DR   SGD; S000000148; SAS3.
DR   VEuPathDB; FungiDB:YBL052C; -.
DR   eggNOG; KOG2747; Eukaryota.
DR   HOGENOM; CLU_014892_1_0_1; -.
DR   InParanoid; P34218; -.
DR   OMA; TETHWEL; -.
DR   OrthoDB; 118560at2759; -.
DR   BioCyc; YEAST:G3O-28951-MONOMER; -.
DR   BioGRID-ORCS; 852228; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P34218; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P34218; Protein.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR   GO; GO:0033100; C:NuA3 histone acetyltransferase complex; IDA:SGD.
DR   GO; GO:1990467; C:NuA3a histone acetyltransferase complex; IDA:SGD.
DR   GO; GO:1990468; C:NuA3b histone acetyltransferase complex; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; NAS:ComplexPortal.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IDA:SGD.
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:0006351; P:DNA-templated transcription; NAS:ComplexPortal.
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   GO; GO:0030466; P:silent mating-type cassette heterochromatin formation; IMP:SGD.
DR   GO; GO:0031509; P:subtelomeric heterochromatin formation; IMP:SGD.
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:SF217; HISTONE ACETYLTRANSFERASE SAS3; 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; Acyltransferase; Chromatin regulator;
KW   Direct protein sequencing; Metal-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..831
FT                   /note="Histone acetyltransferase SAS3"
FT                   /id="PRO_0000051579"
FT   DOMAIN          267..573
FT                   /note="MYST-type HAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT   ZN_FING         300..325
FT                   /note="C2HC MYST-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT   REGION          614..639
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          719..813
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        621..636
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        719..735
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        736..791
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        792..813
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        452
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT   BINDING         419..421
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT   BINDING         426..432
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT   BINDING         456
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT   MOD_RES         367
FT                   /note="N6-acetyllysine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT   MUTAGEN         303
FT                   /note="C->A: Greatly diminishes HAT activity."
FT                   /evidence="ECO:0000269|PubMed:10600516,
FT                   ECO:0000269|PubMed:10817755"
FT   MUTAGEN         306
FT                   /note="C->A: Greatly diminishes HAT activity."
FT                   /evidence="ECO:0000269|PubMed:10600516,
FT                   ECO:0000269|PubMed:10817755"
FT   MUTAGEN         319
FT                   /note="H->A: Greatly diminishes HAT activity."
FT                   /evidence="ECO:0000269|PubMed:10600516,
FT                   ECO:0000269|PubMed:10817755"
FT   MUTAGEN         323
FT                   /note="C->A: Abolishes HAT activity."
FT                   /evidence="ECO:0000269|PubMed:10600516,
FT                   ECO:0000269|PubMed:10817755"
FT   MUTAGEN         426..427
FT                   /note="QR->AA: Loss of function."
FT                   /evidence="ECO:0000269|PubMed:10817755"
FT   MUTAGEN         429..431
FT                   /note="GYG->AAA: Loss of function."
FT                   /evidence="ECO:0000269|PubMed:10817755"
FT   MUTAGEN         434..435
FT                   /note="LM->AA: No effect."
FT                   /evidence="ECO:0000269|PubMed:10817755"
SQ   SEQUENCE   831 AA;  97582 MW;  ACF5B1B225CB4A71 CRC64;
     MSLTANDESP KPKKNALLKN LEIDDLIHSQ FVRSDTNGHR TTRRLFNSDA SISHRIRGSV
     RSDKGLNKIK KGLISQQSKL ASENSSQNIV NRDNKMGAVS FPIIEPNIEV SEELKVRIKY
     DSIKFFNFER LISKSSVIAP LVNKNITSSG PLIGFQRRVN RLKQTWDLAT ENMEYPYSSD
     NTPFRDNDSW QWYVPYGGTI KKMKDFSTKR TLPTWEDKIK FLTFLENSKS ATYINGNVSL
     CNHNETDQEN EDRKKRKGKV PRIKNKVWFS QIEYIVLRNY EIKPWYTSPF PEHINQNKMV
     FICEFCLKYM TSRYTFYRHQ LKCLTFKPPG NEIYRDGKLS VWEIDGRENV LYCQNLCLLA
     KCFINSKTLY YDVEPFIFYI LTEREDTENH PYQNAAKFHF VGYFSKEKFN SNDYNLSCIL
     TLPIYQRKGY GQFLMEFSYL LSRKESKFGT PEKPLSDLGL LTYRTFWKIK CAEVLLKLRD
     SARRRSNNKN EDTFQQVSLN DIAKLTGMIP TDVVFGLEQL QVLYRHKTRS LSSLDDFNYI
     IKIDSWNRIE NIYKTWSSKN YPRVKYDKLL WEPIILGPSF GINGMMNLEP TALADEALTN
     ETMAPVISNN THIENYNNSR AHNKRRRRRR RSSEHKTSKL HVNNIIEPEV PATDFFEDTV
     SSLTEYMCDY KNTNNDRLIY QAEKRVLESI HDRKGIPRSK FSTETHWELC FTIKNSETPL
     GNHAARRNDT GISSLEQDEV ENDVDTELYV GENAKEDEDE DEDFTLDDDI EDEQISEEND
     EEEDTYEEDS DDDEDGKRKG QEQDENDIES HIRKERVRKR RKITLIEDDE E
//