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 27-MAR-2024, entry version 188. 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; GN 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 155. 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; 4932-YMR127C; -. DR PeptideAtlas; P40963; -. DR EnsemblFungi; YMR127C_mRNA; YMR127C; YMR127C. DR GeneID; 855157; -. DR KEGG; sce:YMR127C; -. DR AGR; SGD:S000004734; -. 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 OrthoDB; 118560at2759; -. DR BioCyc; YEAST:G3O-32820-MONOMER; -. DR BioGRID-ORCS; 855157; 0 hits in 10 CRISPR screens. 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; IEA:GOC. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; 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:0046972; F:histone H4K16 acetyltransferase activity; 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: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; IDA: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 PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1. DR PANTHER; PTHR10615:SF180; HISTONE ACETYLTRANSFERASE SAS2; 1. DR Pfam; PF01853; MOZ_SAS; 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; 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 //