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Database: UniProt/SWISS-PROT
Entry: HOS3_YEAST
LinkDB: HOS3_YEAST
Original site: 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   13-FEB-2019, entry version 155.
DE   RecName: Full=Histone deacetylase HOS3;
DE            EC=3.5.1.98;
GN   Name=HOS3; OrderedLocusNames=YPL116W; ORFNames=LPH11W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; 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.,
RA   Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
RA   Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
RA   Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
RA   Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
RA   Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
RA   Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
RA   Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
RA   Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
RA   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.,
RA   Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
RA   Zollner A., 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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   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
RT   complexes that regulate silencing and transcription.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:14503-14508(1996).
RN   [4]
RP   CHARACTERIZATION, AND HOMODIMERIZATION.
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.,
RA   Dephoure N., 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
RP   BY 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
RT   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
RP   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
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582; SER-583 AND
RP   SER-613, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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
RT   insights into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Responsible for the deacetylation of lysine residues on
CC       the N-terminal part of the core histones (H2A, H2B, H3 and H4).
CC       Histone deacetylation gives a tag for epigenetic repression and
CC       plays an important role in transcriptional regulation, cell cycle
CC       progression and developmental events. Histone deacetylases act via
CC       the formation of large multiprotein complexes (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of an N(6)-acetyl-lysine residue of a histone
CC         to yield a deacetylated histone.; EC=3.5.1.98;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- MISCELLANEOUS: Present with 4420 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC       subfamily. {ECO:0000305}.
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   ProteinModelPortal; Q02959; -.
DR   SMR; Q02959; -.
DR   BioGrid; 36065; 93.
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_mRNA; YPL116W.
DR   GeneID; 855987; -.
DR   KEGG; sce:YPL116W; -.
DR   EuPathDB; FungiDB:YPL116W; -.
DR   SGD; S000006037; HOS3.
DR   HOGENOM; HOG000246666; -.
DR   InParanoid; Q02959; -.
DR   KO; K11484; -.
DR   OMA; NASTCIM; -.
DR   BioCyc; YEAST:G3O-34016-MONOMER; -.
DR   PRO; PR:Q02959; -.
DR   Proteomes; UP000002311; Chromosome XVI.
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:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
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   PANTHER; PTHR10625; PTHR10625; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   SUPFAM; SSF52768; SSF52768; 1.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Complete proteome; Hydrolase; Nucleus;
KW   Phosphoprotein; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    697       Histone deacetylase HOS3.
FT                                /FTId=PRO_0000114727.
FT   REGION       40    440       Histone deacetylase.
FT   ACT_SITE    196    196       {ECO:0000250}.
FT   MOD_RES     582    582       Phosphoserine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   MOD_RES     583    583       Phosphoserine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   MOD_RES     613    613       Phosphoserine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   MOD_RES     629    629       Phosphoserine.
FT                                {ECO:0000244|PubMed:17287358,
FT                                ECO:0000244|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
//
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