HOS3_YEAST
ID HOS3_YEAST Reviewed; 697 AA.
AC Q02959; D6W3Q2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Histone deacetylase HOS3;
DE EC=3.5.1.98 {ECO:0000269|PubMed:10535926};
GN Name=HOS3; OrderedLocusNames=YPL116W; ORFNames=LPH11W;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 GENE NAME.
RX PubMed=8962081; DOI=10.1073/pnas.93.25.14503;
RA Rundlett S.E., Carmen A.A., Kobayashi R., Bavykin S., Turner B.M.,
RA Grunstein M.;
RT "HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes
RT that regulate silencing and transcription.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:14503-14508(1996).
RN [4]
RP CHARACTERIZATION, HOMODIMERIZATION, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10535926; DOI=10.1073/pnas.96.22.12356;
RA Carmen A.A., Griffin P.R., Calaycay J.R., Rundlett S.E., Suka Y.,
RA Grunstein M.;
RT "Yeast HOS3 forms a novel trichostatin A-insensitive homodimer with
RT intrinsic histone deacetylase activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:12356-12361(1999).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629, 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).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582; SER-583 AND SER-613, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Responsible for the deacetylation of lysine residues on the
CC N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone
CC deacetylation gives a tag for epigenetic repression and plays an
CC important role in transcriptional regulation, cell cycle progression
CC and developmental events. Histone deacetylases act via the formation of
CC large multiprotein complexes (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-
CC [histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-
CC COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:61930; EC=3.5.1.98;
CC Evidence={ECO:0000269|PubMed:10535926};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10535926}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10535926}.
CC -!- MISCELLANEOUS: Present with 4420 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC subfamily. {ECO:0000305}.
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DR EMBL; U43503; AAB68246.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11318.1; -; Genomic_DNA.
DR PIR; S62006; S62006.
DR RefSeq; NP_015209.1; NM_001183930.1.
DR AlphaFoldDB; Q02959; -.
DR SMR; Q02959; -.
DR BioGRID; 36065; 99.
DR DIP; DIP-8047N; -.
DR IntAct; Q02959; 47.
DR MINT; Q02959; -.
DR STRING; 4932.YPL116W; -.
DR iPTMnet; Q02959; -.
DR MaxQB; Q02959; -.
DR PaxDb; Q02959; -.
DR PRIDE; Q02959; -.
DR EnsemblFungi; YPL116W_mRNA; YPL116W; YPL116W.
DR GeneID; 855987; -.
DR KEGG; sce:YPL116W; -.
DR SGD; S000006037; HOS3.
DR VEuPathDB; FungiDB:YPL116W; -.
DR eggNOG; KOG1343; Eukaryota.
DR GeneTree; ENSGT01000000220060; -.
DR HOGENOM; CLU_024583_0_0_1; -.
DR InParanoid; Q02959; -.
DR OMA; GTQDICW; -.
DR BioCyc; YEAST:G3O-34016-MON; -.
DR PRO; PR:Q02959; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q02959; protein.
DR GO; GO:0005935; C:cellular bud neck; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005628; C:prospore membrane; HDA:SGD.
DR GO; GO:0004407; F:histone deacetylase activity; IDA:SGD.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016575; P:histone deacetylation; IDA:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IGI:SGD.
DR Gene3D; 3.40.800.20; -; 1.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; SSF52768; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Hydrolase; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..697
FT /note="Histone deacetylase HOS3"
FT /id="PRO_0000114727"
FT REGION 40..440
FT /note="Histone deacetylase"
FT REGION 525..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..559
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 196
FT /evidence="ECO:0000250"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 629
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956"
SQ SEQUENCE 697 AA; 79200 MW; F2B5D09E87B097E5 CRC64;
MSSKHSDPLE RFYKQFQAFV QNNPNVISAA RAAAQIPESA KAVVVLSPYS LQHVFPREWV
TKSYRKTIVE RPERLLASSM GISAAITMYP SLFTLKSSHQ RKGSLMAPHV LKVHGSSWPA
ELIELCQMAD AKLLKGEIEV PDTWNSGDIY LSSKTIKALQ GTIGAIETGV DSIFKGPSAE
HISNRAFVAI RPPGHHCHYG TPSGFCLLNN AHVAIEYAYD TYNVTHVVVL DFDLHHGDGT
QDICWKRAGF KPEEEPEDSS YDDFGKKFAE FPKVGYFSMH DINSFPTESG FATKENIKNA
STCIMNSHDL NIWNIHLSKW TTEEEFNVLY RTKYRTLFAK ADEFFRSAKL EMNQQGRPFK
GLVVISAGFD ASEFEQTSMQ RHSVNVPTSF YTTFTKDALK LAQMHCHGKV LSLMEGGYSD
KAICSGVFAH LIGLQNQDWV KEWGSEQVVK EIVRGCKPAW KPYKTKRAKD VIRIWAEEVI
RLGRAMIPEF DDIIFKDAVN SAPSNSLLKA TVEPASTSTI AQRIIRSHRS NASPEKELHE
NKPRSTEKQE QREIRSDTKV KQLSSNNRAA ETQIPFLQQE FSSEDEDEEY VYDEELNKTF
NRTVEDITID DISRHLETLE IEKKGDEDSD HELKEKNWKN SHQRRLQGNG MYKIPSNTKP
HRIRQPQNAN TPTYDDSDIS MISHVSRKHT TRSGGRW
