HOS1_YEAST
ID HOS1_YEAST Reviewed; 470 AA.
AC Q12214; D6W472;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Histone deacetylase HOS1;
DE EC=3.5.1.98;
GN Name=HOS1; OrderedLocusNames=YPR068C; ORFNames=YP9499.23C;
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 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, 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: 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 plays an important role in transcriptional regulation,
CC cell cycle progression and developmental events. Histone deacetylases
CC act via the formation of large multiprotein complexes (By similarity).
CC {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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 538 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; Z71255; CAA94976.1; -; Genomic_DNA.
DR EMBL; Z49219; CAA89185.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11488.1; -; Genomic_DNA.
DR PIR; S54089; S54089.
DR RefSeq; NP_015393.1; NM_001184165.1.
DR AlphaFoldDB; Q12214; -.
DR SMR; Q12214; -.
DR BioGRID; 36240; 99.
DR DIP; DIP-7974N; -.
DR IntAct; Q12214; 4.
DR STRING; 4932.YPR068C; -.
DR iPTMnet; Q12214; -.
DR MaxQB; Q12214; -.
DR PaxDb; Q12214; -.
DR PRIDE; Q12214; -.
DR EnsemblFungi; YPR068C_mRNA; YPR068C; YPR068C.
DR GeneID; 856181; -.
DR KEGG; sce:YPR068C; -.
DR SGD; S000006272; HOS1.
DR VEuPathDB; FungiDB:YPR068C; -.
DR eggNOG; KOG1342; Eukaryota.
DR GeneTree; ENSGT00940000157843; -.
DR HOGENOM; CLU_007727_7_8_1; -.
DR InParanoid; Q12214; -.
DR OMA; MSRFYTY; -.
DR BioCyc; YEAST:G3O-34216-MON; -.
DR Reactome; R-SCE-3214815; HDACs deacetylate histones.
DR Reactome; R-SCE-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-SCE-9018519; Estrogen-dependent gene expression.
DR PRO; PR:Q12214; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12214; protein.
DR GO; GO:0000118; C:histone deacetylase complex; IPI:SGD.
DR GO; GO:0004407; F:histone deacetylase activity; IBA:GO_Central.
DR GO; GO:0033558; F:protein lysine deacetylase activity; IDA:SGD.
DR GO; GO:0016575; P:histone deacetylation; IEA:UniProt.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0061587; P:transfer RNA gene-mediated silencing; IMP: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..470
FT /note="Histone deacetylase HOS1"
FT /id="PRO_0000114726"
FT REGION 47..392
FT /note="Histone deacetylase"
FT ACT_SITE 211
FT /evidence="ECO:0000250"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
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
