SAS5_YEAST
ID SAS5_YEAST Reviewed; 248 AA.
AC Q99314; D6W2R9;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Something about silencing protein 5;
GN Name=SAS5; OrderedLocusNames=YOR213C;
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 96604 / S288c / FY1679;
RX PubMed=8840505;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<877::aid-yea969>3.0.co;2-s;
RA Galisson F., Dujon B.;
RT "Sequence and analysis of a 33 kb fragment from the right arm of chromosome
RT XV of the yeast Saccharomyces cerevisiae.";
RL Yeast 12:877-885(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 FUNCTION.
RX PubMed=10471696; DOI=10.1093/genetics/153.1.13;
RA Xu E.Y., Kim S., Replogle K., Rine J., Rivier D.H.;
RT "Identification of SAS4 and SAS5, two genes that regulate silencing in
RT Saccharomyces cerevisiae.";
RL Genetics 153:13-23(1999).
RN [5]
RP FUNCTION.
RX PubMed=10471697; DOI=10.1093/genetics/153.1.25;
RA Xu E.Y., Kim S., Rivier D.H.;
RT "SAS4 and SAS5 are locus-specific regulators of silencing in Saccharomyces
RT cerevisiae.";
RL Genetics 153:25-33(1999).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND COMPONENT OF THE SAS COMPLEX WITH
RP SAS2 AND SAS5.
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 SUBCELLULAR LOCATION, AND COMPONENT OF THE SAS COMPLEX WITH SAS2 AND SAS5.
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 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Component of the SAS complex, a multiprotein complex that
CC acetylates 'Lys-16' of histone H4 and 'Lys-14' of histone H3. The SAS
CC complex is however unable to acetylate nucleosomal histones. The
CC complex is involved in transcriptional silencing at telomeres and at
CC HML locus. Also involved in rDNA silencing. In the complex, SAS5 is
CC required for maximal histone acetyltransferase (HAT) activity of the
CC complex, suggesting that it may be required to stabilize the complex or
CC help in substrate recognition. {ECO:0000269|PubMed:10471696,
CC ECO:0000269|PubMed:10471697, ECO:0000269|PubMed:12626510}.
CC -!- SUBUNIT: Component of the SAS complex, at least composed of SAS2, SAS4
CC and SAS5. These three proteins constitute the core of the complex, and
CC are sufficient to acetylate histones.
CC -!- INTERACTION:
CC Q99314; Q04003: SAS4; NbExp=3; IntAct=EBI-31212, EBI-38500;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00376,
CC ECO:0000269|PubMed:11731480}.
CC -!- DISRUPTION PHENOTYPE: Heterochromatin spreading downstream of the
CC silent mating-type locus HMR. {ECO:0000269|PubMed:16079223}.
CC -!- MISCELLANEOUS: Present with 1800 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X92441; CAA63176.1; -; Genomic_DNA.
DR EMBL; Z75121; CAA99429.1; -; Genomic_DNA.
DR EMBL; Z75122; CAA99431.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10985.1; -; Genomic_DNA.
DR PIR; S60940; S60940.
DR RefSeq; NP_014856.1; NM_001183632.1.
DR PDB; 7F5M; X-ray; 2.40 A; A/B=2-139.
DR PDBsum; 7F5M; -.
DR AlphaFoldDB; Q99314; -.
DR SMR; Q99314; -.
DR BioGRID; 34608; 84.
DR ComplexPortal; CPX-777; SAS acetyltransferase complex.
DR DIP; DIP-2945N; -.
DR IntAct; Q99314; 7.
DR MINT; Q99314; -.
DR STRING; 4932.YOR213C; -.
DR iPTMnet; Q99314; -.
DR MaxQB; Q99314; -.
DR PaxDb; Q99314; -.
DR PRIDE; Q99314; -.
DR EnsemblFungi; YOR213C_mRNA; YOR213C; YOR213C.
DR GeneID; 854388; -.
DR KEGG; sce:YOR213C; -.
DR SGD; S000005739; SAS5.
DR VEuPathDB; FungiDB:YOR213C; -.
DR eggNOG; KOG3149; Eukaryota.
DR GeneTree; ENSGT00940000176465; -.
DR HOGENOM; CLU_078004_0_0_1; -.
DR InParanoid; Q99314; -.
DR OMA; NDIPTHE; -.
DR BioCyc; YEAST:G3O-33715-MON; -.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-75955; RNA Polymerase II Transcription Elongation.
DR PRO; PR:Q99314; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q99314; protein.
DR GO; GO:0000785; C:chromatin; IDA:SGD.
DR GO; GO:0000781; C:chromosome, telomeric region; IC:SGD.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0033255; C:SAS acetyltransferase complex; IDA:SGD.
DR GO; GO:0000812; C:Swr1 complex; IBA:GO_Central.
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:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0016573; P:histone acetylation; IDA:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IDA:SGD.
DR Gene3D; 2.60.40.1970; -; 1.
DR InterPro; IPR016665; Sas5/TAF14.
DR InterPro; IPR038704; YEAST_sf.
DR InterPro; IPR005033; YEATS.
DR PANTHER; PTHR23195; PTHR23195; 1.
DR PANTHER; PTHR23195:SF2; PTHR23195:SF2; 1.
DR Pfam; PF03366; YEATS; 1.
DR PIRSF; PIRSF016551; SAS5/TFIID_14; 1.
DR PROSITE; PS51037; YEATS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..248
FT /note="Something about silencing protein 5"
FT /id="PRO_0000097596"
FT DOMAIN 1..139
FT /note="YEATS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00376"
FT REGION 223..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 248 AA; 29018 MW; 9E2F68A040A19E0D CRC64;
MDHSIEVTFR VKTQQVIIPE QNIRGNELPL RRWQMELLML DATGKEVEPT ILSKCIYHLH
SSFKQPKRRL NSLPFFIKET GWGEFNLKIE CFFIGNAGKF SIEHDLTFED DAYAVDYTVD
VPHEFSHLNS ELSKYFDLPW KVVSPEEEMS LRIADLPWIK SLALIDEDMM TDVVQMILND
PAVQRAIENH PRREQFFMFI TQLPDDLLMK IQAFLKLPNK NSTKQERTNF GSDAIHKDEP
VKAHNKLK
