SAS3_YEAST
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 03-AUG-2022, entry version 180.
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; 197.
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; P34218; -.
DR PRIDE; P34218; -.
DR DNASU; 852228; -.
DR EnsemblFungi; YBL052C_mRNA; YBL052C; YBL052C.
DR GeneID; 852228; -.
DR KEGG; sce:YBL052C; -.
DR SGD; S000000148; SAS3.
DR VEuPathDB; FungiDB:YBL052C; -.
DR eggNOG; KOG2747; Eukaryota.
DR HOGENOM; CLU_014892_1_0_1; -.
DR InParanoid; P34218; -.
DR OMA; REDTENH; -.
DR BioCyc; YEAST:G3O-28951-MON; -.
DR Reactome; R-SCE-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-SCE-5693548; Sensing of DNA Double Strand Breaks.
DR Reactome; R-SCE-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-SCE-9018519; Estrogen-dependent gene expression.
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; IC:ComplexPortal.
DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:SGD.
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:0016573; P:histone acetylation; IDA:SGD.
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 GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IMP:SGD.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR GO; GO:0006351; P:transcription, DNA-templated; IC:ComplexPortal.
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; 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
