ID   HOS1_YEAST              Reviewed;         470 AA.
AC   Q12214;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 65.
DE   RecName: Full=Histone deacetylase HOS1;
DE            EC=3.5.1.98;
GN   Name=HOS1; OrderedLocusNames=YPR068C; ORFNames=YP9499.23C;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   MEDLINE=97313271; 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   GENE NAME.
RX   MEDLINE=97121415; 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   [3]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; 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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND MASS
RP   SPECTROMETRY.
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).
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 plays an important role in transcriptional
CC       regulation, cell cycle progression and developmental events.
CC       Histone deacetylases act via the formation of large multiprotein
CC       complexes (By similarity).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC       a histone to yield a deacetylated histone.
CC   -!- INTERACTION:
CC       P14922:CYC8; NbExp=1; IntAct=EBI-8471, EBI-18215;
CC       P16649:TUP1; NbExp=1; IntAct=EBI-8471, EBI-19654;
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- MISCELLANEOUS: Present with 538 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. Type 1
CC       subfamily.
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DR   EMBL; Z71255; CAA94976.1; -; Genomic_DNA.
DR   EMBL; Z49219; CAA89185.1; -; Genomic_DNA.
DR   PIR; S54089; S54089.
DR   RefSeq; NP_015393.1; -.
DR   IntAct; Q12214; 2.
DR   Ensembl; YPR068C; Saccharomyces cerevisiae.
DR   GeneID; 856181; -.
DR   GenomeReviews; U00094_GR; YPR068C.
DR   KEGG; sce:YPR068C; -.
DR   NMPDR; fig|4932.3.peg.6529; -.
DR   CYGD; YPR068c; -.
DR   SGD; S000006272; HOS1.
DR   HOGENOM; Q12214; -.
DR   OMA; Q12214; NWDGGRH.
DR   NextBio; 981352; -.
DR   GermOnline; YPR068C; Saccharomyces cerevisiae.
DR   GO; GO:0000118; C:histone deacetylase complex; TAS:SGD.
DR   GO; GO:0004407; F:histone deacetylase activity; TAS:SGD.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0010552; P:positive regulation of specific transcripti...; IMP:SGD.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR000286; His_deacetylse.
DR   Gene3D; G3DSA:3.40.800.20; His_deacetylse; 1.
DR   PANTHER; PTHR10625; His_deacetylse; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PRINTS; PR01270; HDASUPER.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Complete proteome; Hydrolase; Nucleus;
KW   Phosphoprotein; Repressor; Transcription; Transcription regulation.
FT   CHAIN         1    470       Histone deacetylase HOS1.
FT                                /FTId=PRO_0000114726.
FT   REGION       47    392       Histone deacetylase.
FT   ACT_SITE    211    211       By similarity.
FT   MOD_RES     110    110       Phosphoserine.
SQ   SEQUENCE   470 AA;  54764 MW;  5DCFF35D8F6AC87D CRC64;
     MSKLVISTSI FQSQVADLLP CNNHQKSQLT YSLINAYDLL QHFDEVLTFP YARKDDLLEF
     HSKSYIDYLI NGRFNKMMAQ DVNNPMVESK WSELSELADN WNEKIDYNPS QDLQRFTTRE
     NLYNYYLNHS QALENNMDCI NNSEVPTNDK PTDTYILNSE TKQYNLEGDC PIFSYLPMYC
     QVITGATLNL LDHLSPTERL IGINWDGGRH HAFKQRASGF CYINDVVLLI QRLRKAKLNK
     ITYVDFDLHH GDGVEKAFQY SKQIQTISVH LYEPGFFPGT GSLSDSRKDK NVVNIPLKHG
     CDDNYLELIA SKIVNPLIER HEPEALIIEC GGDGLLGDRF NEWQLTIRGL SRIIINIMKS
     YPRAHIFLLG GGGYNDLLMS RFYTYLTWCV TKQFSNLRCG DNNSFQIDPF DVCDGDDSEQ
     FIREHDLVEM YNEENYQYWI YEMEGSSRMK MLRNDNKDRD MVELMKFYEL
//