SAS4_YEAST
ID SAS4_YEAST Reviewed; 481 AA.
AC Q04003; D6VSG4;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Something about silencing protein 4;
GN Name=SAS4; OrderedLocusNames=YDR181C; ORFNames=YD9395.15C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
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 [3]
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 [4]
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 [5]
RP INTERACTION WITH ASF1.
RX PubMed=11404324; DOI=10.1093/genetics/158.2.587;
RA Sutton A., Bucaria J., Osley M.A., Sternglanz R.;
RT "Yeast ASF1 protein is required for cell cycle regulation of histone gene
RT transcription.";
RL Genetics 158:587-596(2001).
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 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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, SAS4 is
CC essential for histone acetyltransferase (HAT) activity of the complex.
CC {ECO:0000269|PubMed:10471696, ECO:0000269|PubMed:10471697,
CC ECO:0000269|PubMed:12626510}.
CC -!- SUBUNIT: Interacts with ASF1. 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.
CC {ECO:0000269|PubMed:11404324}.
CC -!- INTERACTION:
CC Q04003; P32447: ASF1; NbExp=5; IntAct=EBI-38500, EBI-3003;
CC Q04003; Q12495: RLF2; NbExp=3; IntAct=EBI-38500, EBI-3913;
CC Q04003; P40963: SAS2; NbExp=7; IntAct=EBI-38500, EBI-16476;
CC Q04003; Q99314: SAS5; NbExp=3; IntAct=EBI-38500, EBI-31212;
CC -!- SUBCELLULAR LOCATION: Nucleus {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 800 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z46727; CAA86688.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12024.1; -; Genomic_DNA.
DR PIR; S49778; S49778.
DR RefSeq; NP_010467.1; NM_001180489.1.
DR AlphaFoldDB; Q04003; -.
DR SMR; Q04003; -.
DR BioGRID; 32235; 164.
DR ComplexPortal; CPX-777; SAS acetyltransferase complex.
DR DIP; DIP-6283N; -.
DR IntAct; Q04003; 5.
DR MINT; Q04003; -.
DR STRING; 4932.YDR181C; -.
DR iPTMnet; Q04003; -.
DR MaxQB; Q04003; -.
DR PaxDb; Q04003; -.
DR PRIDE; Q04003; -.
DR EnsemblFungi; YDR181C_mRNA; YDR181C; YDR181C.
DR GeneID; 851762; -.
DR KEGG; sce:YDR181C; -.
DR SGD; S000002589; SAS4.
DR VEuPathDB; FungiDB:YDR181C; -.
DR eggNOG; ENOG502RYH0; Eukaryota.
DR HOGENOM; CLU_035634_0_0_1; -.
DR InParanoid; Q04003; -.
DR OMA; PYHKKML; -.
DR BioCyc; YEAST:G3O-29770-MON; -.
DR PRO; PR:Q04003; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04003; protein.
DR GO; GO:0000785; C:chromatin; IDA:SGD.
DR GO; GO:0000781; C:chromosome, telomeric region; IC:SGD.
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:0016573; P:histone acetylation; IDA:ComplexPortal.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IDA:SGD.
DR InterPro; IPR016158; Cullin_homology.
DR InterPro; IPR038988; Sas4.
DR InterPro; IPR029184; Sas4_dom.
DR PANTHER; PTHR38422; PTHR38422; 1.
DR Pfam; PF15460; SAS4; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Coiled coil; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..481
FT /note="Something about silencing protein 4"
FT /id="PRO_0000097593"
FT REGION 319..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 90..120
FT /evidence="ECO:0000255"
FT COILED 139..160
FT /evidence="ECO:0000255"
SQ SEQUENCE 481 AA; 55409 MW; 71979C2084803CB2 CRC64;
MGIFQSIEEA NNTSERLLRS EIKNSHGEFE KFDFDTEEYE INPKRKLRLV SRINPNAGHL
RKSKSCFTVD EHVDETRCQK PVMKSPFMSN VDDEIKKKRE TITKMTLEIE HHELSQNIRK
PTDDLLPDST YQPYHKKMLK QENRMIQSDI VNGENEADRL SLISDRLGML NWEVTLQKVT
KINDPTDENE METKRYQTKE LIDSMLHKFE SMKKKSRNLA RRPASSDSLL KLVSGKDWPK
IYTRIDRTFI PDYASSSDEE EEKITVEEIR ERRLKKREQQ CGGSIIVLLS DHQSQKGMTR
FAIVAEPLRK PYLIKTSTKE RNSWKNKVPT NPKKFKKAPR ISTQIAVKRR REVIPLTMEV
EPEVIRDIRQ DTQKSMKLNV KAEEISVTET VKSKEMNALR NNAASISPTL SEKAPLGSIS
SCTASQISQR SSENVGAIIN NINPNLAIVP SCNEKTFVKT HNGMKTNSGI NILPVRKKKK
V
