ID HOS2_YEAST Reviewed; 452 AA.
AC P53096; D6VTW0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 27-MAR-2024, entry version 188.
DE RecName: Full=Probable histone deacetylase HOS2;
DE EC=3.5.1.98;
GN Name=HOS2; OrderedLocusNames=YGL194C; ORFNames=G1330;
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 [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9046087;
RX DOI=10.1002/(sici)1097-0061(199701)13:1<55::aid-yea48>3.0.co;2-9;
RA Coglievina M., Klima R., Bertani I., Delneri D., Zaccaria P., Bruschi C.V.;
RT "Sequencing of a 40.5 kb fragment located on the left arm of chromosome VII
RT from Saccharomyces cerevisiae.";
RL Yeast 13:55-64(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
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 [4]
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 [5]
RP IDENTIFICATION IN A COMPLEX WITH SET3; HST1; SNT1; SIF2; CPR1 AND YIL112W.
RX PubMed=11711434; DOI=10.1101/gad.207401;
RA Pijnappel W.W.M.P., Schaft D., Roguev A., Shevchenko A., Tekotte H.,
RA Wilm M., Rigaut G., Seraphin B., Aasland R., Stewart A.F.;
RT "The S. cerevisiae SET3 complex includes two histone deacetylases, Hos2 and
RT Hst1, and is a meiotic-specific repressor of the sporulation gene
RT program.";
RL Genes Dev. 15:2991-3004(2001).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF 195-HIS-HIS-196.
RX PubMed=12434058; DOI=10.1126/science.1077790;
RA Wang A., Kurdistani S.K., Grunstein M.;
RT "Requirement of Hos2 histone deacetylase for gene activity in yeast.";
RL Science 298:1412-1414(2002).
RN [7]
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).
CC -!- FUNCTION: Responsible for the deacetylation of lysine residues on the
CC N-terminal part of the core histones (H2A, H2B, H3 and H4). It is
CC apparently involved in transcriptional activation.
CC {ECO:0000269|PubMed:12434058}.
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 -!- SUBUNIT: Identified in a Set3C complex with SET3, HST1, SNT1, SIF2,
CC CPR1 and HOS4/YIL112W. {ECO:0000269|PubMed:11711434}.
CC -!- INTERACTION:
CC P53096; P14922: CYC8; NbExp=4; IntAct=EBI-8475, EBI-18215;
CC P53096; P61830: HHT2; NbExp=2; IntAct=EBI-8475, EBI-8098;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 4890 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; X91837; CAA62950.1; -; Genomic_DNA.
DR EMBL; Z72716; CAA96906.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07921.1; -; Genomic_DNA.
DR PIR; S64211; S64211.
DR RefSeq; NP_011321.1; NM_001181059.1.
DR AlphaFoldDB; P53096; -.
DR SMR; P53096; -.
DR BioGRID; 33063; 406.
DR ComplexPortal; CPX-1342; SET3C histone deacetylase complex.
DR DIP; DIP-6828N; -.
DR IntAct; P53096; 37.
DR STRING; 4932.YGL194C; -.
DR MaxQB; P53096; -.
DR PaxDb; 4932-YGL194C; -.
DR PeptideAtlas; P53096; -.
DR EnsemblFungi; YGL194C_mRNA; YGL194C; YGL194C.
DR GeneID; 852681; -.
DR KEGG; sce:YGL194C; -.
DR AGR; SGD:S000003162; -.
DR SGD; S000003162; HOS2.
DR VEuPathDB; FungiDB:YGL194C; -.
DR eggNOG; KOG1342; Eukaryota.
DR GeneTree; ENSGT00940000160487; -.
DR HOGENOM; CLU_007727_7_4_1; -.
DR InParanoid; P53096; -.
DR OMA; CYETSIC; -.
DR OrthoDB; 1327607at2759; -.
DR BioCyc; YEAST:G3O-30675-MONOMER; -.
DR Reactome; R-SCE-2500257; Resolution of Sister Chromatid Cohesion.
DR BioGRID-ORCS; 852681; 0 hits in 10 CRISPR screens.
DR PRO; PR:P53096; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53096; Protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0034399; C:nuclear periphery; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0070210; C:Rpd3L-Expanded complex; HDA:SGD.
DR GO; GO:0034967; C:Set3 complex; IDA:SGD.
DR GO; GO:0004407; F:histone deacetylase activity; IBA:GO_Central.
DR GO; GO:0045129; F:NAD-independent histone deacetylase activity; IDA:SGD.
DR GO; GO:0009267; P:cellular response to starvation; NAS:ComplexPortal.
DR GO; GO:0006974; P:DNA damage response; NAS:ComplexPortal.
DR GO; GO:0045835; P:negative regulation of meiotic nuclear division; IDA:ComplexPortal.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IMP:SGD.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:SGD.
DR CDD; cd11598; HDAC_Hos2; 1.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR003084; His_deacetylse_1.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR10625:SF25; HISTONE DEACETYLASE 3; 1.
DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PIRSF; PIRSF037913; His_deacetylse_1; 1.
DR PRINTS; PR01270; HDASUPER.
DR PRINTS; PR01271; HISDACETLASE.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE 1: Evidence at protein level;
KW Activator; Chromatin regulator; Hydrolase; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..452
FT /note="Probable histone deacetylase HOS2"
FT /id="PRO_0000114723"
FT REGION 26..340
FT /note="Histone deacetylase"
FT REGION 428..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 197
FT /evidence="ECO:0000250"
FT MUTAGEN 196..197
FT /note="HH->AA: Leads to hyperacetylation."
FT CONFLICT 352..364
FT /note="PFRDSFGPDYSLY -> HSGTHSGRIIHFI (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 452 AA; 51455 MW; 024E8AEA0A445A08 CRC64;
MSGTFSYDVK TKENEPLFEF NSAYSPRVSY HFNSKVSHYH YGVKHPMKPF RLMLTDHLVS
SYGLHKIMDL YETRSATRDE LLQFHSEDYV NFLSKVSPEN ANKLPRGTLE NFNIGDDCPI
FQNLYDYTTL YTGASLDATR KLINNQSDIA INWSGGLHHA KKNSPSGFCY VNDIVLSILN
LLRYHPRILY IDIDLHHGDG VQEAFYTTDR VFTLSFHKYN GEFFPGTGDL TEIGCDKGKH
FALNVPLEDG IDDDSYINLF KSIVDPLIMT FKPTLIVQQC GADSLGHDRL GCFNLNIKAH
GECVKFVKSF GLPMLVVGGG GYTPRNVSRL WTYETGILND VLLPEDIPED IPFRDSFGPD
YSLYPMLDDL YENKNSKKLL EDIRIRCLEN IRYLQGAPSV RMDAECIPTQ DISALTEEED
KIIQEMNEET EADSSNRLEE MEKENSGLIA FS
//
