SAS2_YEAST
ID SAS2_YEAST Reviewed; 338 AA.
AC P40963; D6VZV0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Histone acetyltransferase SAS2;
DE EC=2.3.1.48 {ECO:0000269|PubMed:22020126};
DE AltName: Full=Something about silencing protein 2;
GN Name=SAS2; Synonyms=ESO1; OrderedLocusNames=YMR127C; ORFNames=YM9553.03C;
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].
RX PubMed=9093847; DOI=10.1093/genetics/145.4.923;
RA Ehrenhofer-Murray A.E., Rivier D.H., Rine J.;
RT "The role of Sas2, an acetyltransferase homologue of Saccharomyces
RT cerevisiae, in silencing and ORC function.";
RL Genetics 145:923-934(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
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 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 [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, COMPONENT OF THE SAS COMPLEX WITH SAS2
RP AND SAS5, AND MUTAGENESIS OF 216-GLN-ARG-217; 219-GLY--GLY-221 AND
RP 224-LEU-ILE-225.
RX PubMed=11731479; DOI=10.1101/gad.907201;
RA Osada S., Sutton A., Muster N., Brown C.E., Yates J.R. III, Sternglanz R.,
RA Workman J.L.;
RT "The yeast SAS (something about silencing) protein complex contains a MYST-
RT type putative acetyltransferase and functions with chromatin assembly
RT factor ASF1.";
RL Genes Dev. 15:3155-3168(2001).
RN [7]
RP COMPONENT OF THE SAS COMPLEX WITH SAS2 AND SAS5, INTERACTION WITH CAC1, AND
RP MUTAGENESIS OF CYS-106 AND 213-PRO-PRO-214.
RX PubMed=11731480; DOI=10.1101/gad.929001;
RA Meijsing S.H., Ehrenhofer-Murray A.E.;
RT "The silencing complex SAS-I links histone acetylation to the assembly of
RT repressed chromatin by CAF-I and Asf1 in Saccharomyces cerevisiae.";
RL Genes Dev. 15:3169-3182(2001).
RN [8]
RP FUNCTION OF THE SAS COMPLEX.
RX PubMed=12626510; DOI=10.1074/jbc.m210709200;
RA Sutton A., Shia W.-J., Band D., Kaufman P.D., Osada S., Workman J.L.,
RA Sternglanz R.;
RT "Sas4 and Sas5 are required for the histone acetyltransferase activity of
RT Sas2 in the SAS complex.";
RL J. Biol. Chem. 278:16887-16892(2003).
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 DISRUPTION PHENOTYPE.
RX PubMed=16079223; DOI=10.1534/genetics.105.046938;
RA Jambunathan N., Martinez A.W., Robert E.C., Agochukwu N.B., Ibos M.E.,
RA Dugas S.L., Donze D.;
RT "Multiple bromodomain genes are involved in restricting the spread of
RT heterochromatic silencing at the Saccharomyces cerevisiae HMR-tRNA
RT boundary.";
RL Genetics 171:913-922(2005).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, ACETYLATION AT LYS-168, AND
RP MUTAGENESIS OF LYS-168.
RX PubMed=22020126; DOI=10.1038/emboj.2011.382;
RA Yuan H., Rossetto D., Mellert H., Dang W., Srinivasan M., Johnson J.,
RA Hodawadekar S., Ding E.C., Speicher K., Abshiru N., Perry R., Wu J.,
RA Yang C., Zheng Y.G., Speicher D.W., Thibault P., Verreault A.,
RA Johnson F.B., Berger S.L., Sternglanz R., McMahon S.B., Cote J.,
RA Marmorstein R.;
RT "MYST protein acetyltransferase activity requires active site lysine
RT autoacetylation.";
RL EMBO J. 31:58-70(2012).
CC -!- FUNCTION: Histone acetyltransferase (HAT) subunit of the SAS complex, a
CC multiprotein complex that acetylates 'Lys-16' of histone H4 and 'Lys-
CC 14' of histone H3. The SAS complex is however unable to acetylate
CC nucleosomal histones. The complex is involved in transcriptional
CC silencing at telomeres and at HML locus. Also involved in rDNA
CC silencing and G0 control. {ECO:0000269|PubMed:12626510,
CC ECO:0000269|PubMed:22020126}.
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:22020126};
CC -!- SUBUNIT: Interacts with CAC1. Component of the SAS complex, at least
CC composed of SAS2, SAS4 and SAS5. These three proteins constitute the
CC core of the complex and are sufficient to acetylate histones. SAS4 is
CC essential for HAT activity of the complex, while SAS5 is required for
CC maxiaml HAT activity. {ECO:0000269|PubMed:11731480,
CC ECO:0000303|PubMed:22020126}.
CC -!- INTERACTION:
CC P40963; P32447: ASF1; NbExp=4; IntAct=EBI-16476, EBI-3003;
CC P40963; Q12495: RLF2; NbExp=4; IntAct=EBI-16476, EBI-3913;
CC P40963; Q04003: SAS4; NbExp=7; IntAct=EBI-16476, EBI-38500;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- PTM: Autoacetylation at Lys-168 is required for proper function.
CC {ECO:0000303|PubMed:22020126}.
CC -!- DISRUPTION PHENOTYPE: Heterochromatin spreading downstream of the
CC silent mating-type locus HMR. {ECO:0000269|PubMed:16079223}.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}.
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DR EMBL; U14548; AAA21555.1; -; Genomic_DNA.
DR EMBL; Z48622; CAA88552.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10024.1; -; Genomic_DNA.
DR PIR; S48299; S48299.
DR RefSeq; NP_013846.1; NM_001182628.1.
DR AlphaFoldDB; P40963; -.
DR SMR; P40963; -.
DR BioGRID; 35304; 154.
DR ComplexPortal; CPX-777; SAS acetyltransferase complex.
DR DIP; DIP-4601N; -.
DR IntAct; P40963; 7.
DR MINT; P40963; -.
DR STRING; 4932.YMR127C; -.
DR ChEMBL; CHEMBL3832953; -.
DR iPTMnet; P40963; -.
DR PaxDb; P40963; -.
DR PRIDE; P40963; -.
DR EnsemblFungi; YMR127C_mRNA; YMR127C; YMR127C.
DR GeneID; 855157; -.
DR KEGG; sce:YMR127C; -.
DR SGD; S000004734; SAS2.
DR VEuPathDB; FungiDB:YMR127C; -.
DR eggNOG; KOG2747; Eukaryota.
DR HOGENOM; CLU_011815_0_2_1; -.
DR InParanoid; P40963; -.
DR OMA; LDNKSMY; -.
DR BioCyc; YEAST:G3O-32820-MON; -.
DR PRO; PR:P40963; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P40963; protein.
DR GO; GO:0000785; C:chromatin; IDA:SGD.
DR GO; GO:0000781; C:chromosome, telomeric region; IC:SGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033255; C:SAS acetyltransferase complex; IDA:SGD.
DR GO; GO:0016407; F:acetyltransferase activity; IDA:SGD.
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:ComplexPortal.
DR GO; GO:0043486; P:histone exchange; IMP:SGD.
DR GO; GO:0043966; P:histone H3 acetylation; IMP: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; IDA:SGD.
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; Cytoplasm;
KW Metal-binding; Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..338
FT /note="Histone acetyltransferase SAS2"
FT /id="PRO_0000051578"
FT DOMAIN 45..338
FT /note="MYST-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT ZN_FING 100..126
FT /note="C2HC MYST-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 242
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 209..211
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 216..222
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 246
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 323
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT MOD_RES 168
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000303|PubMed:22020126"
FT MUTAGEN 106
FT /note="C->L: Loss of function."
FT /evidence="ECO:0000269|PubMed:11731479,
FT ECO:0000269|PubMed:11731480"
FT MUTAGEN 168
FT /note="K->A,Q,R: Abolishes catalytic activity."
FT MUTAGEN 213..214
FT /note="PP->AV: Loss of function."
FT /evidence="ECO:0000269|PubMed:11731480"
FT MUTAGEN 216..217
FT /note="QR->AA: Abolishes silencing activity."
FT /evidence="ECO:0000269|PubMed:11731479"
FT MUTAGEN 219..221
FT /note="GLG->AAA: Does not affect silencing activity."
FT /evidence="ECO:0000269|PubMed:11731479"
FT MUTAGEN 224..225
FT /note="LI->AA: Does not affect silencing activity."
FT /evidence="ECO:0000269|PubMed:11731479"
SQ SEQUENCE 338 AA; 39206 MW; 22CBDC0D1B62A947 CRC64;
MARSLSQSLT ATTQKLKGKK NGGKGKNKPS AKIKKTQKEM LYGILNERNI RQIQFGLNKK
FSTWYGSAVY FDPETKRLGC SETKGQLSSV SNSQYWLDTL FVCEYCFKYT DDQTRFVGHV
ASCPFQYRVP GKIKYKSPEY TIRRVKGSKY QLFCQCLCLF TKLYLDNKSM YFKVDHYEFY
IVYETGSTKP MGFFSKDLVS YQQNNLACIL IFPPYQRRGL GLLLIEFSYK LSQLEGVISG
PEVPLSPFGL IGYLKYWSQI LCWHLIEGDL AHYDKVTLED LSIVTGMRVN DVILTLKHLN
CIGENNQIYL QSLNSWLKLH GTKRNWFKLK DEYLLIDD
