Q02959 (HOS3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone deacetylase HOS3
EC=3.5.1.98

Gene names

Name:	HOS3
Ordered Locus Names:	YPL116W
ORF Names:	LPH11W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	697 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes By similarity.
Catalytic activity	Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.
Subunit structure	Homodimer. Ref.4
Subcellular location	Nucleus By similarity.
Miscellaneous	Present with 4420 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the histone deacetylase family. HD type 1 subfamily.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Molecular function	Chromatin regulator Hydrolase Repressor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone H3 deacetylation Inferred from electronic annotation. Source: GOC histone H4 deacetylation Inferred from electronic annotation. Source: GOC positive regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 17706600. Source: SGD regulation of transcription involved in G1/S phase of mitotic cell cycle Inferred from genetic interaction PubMed 19823668. Source: SGD transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cellular bud neck Inferred from direct assay PubMed 14562095. Source: SGD cytoplasm Inferred from direct assay PubMed 11914276. Source: SGD nucleus Inferred from direct assay PubMed 11914276. Source: SGD
Molecular_function	NAD-dependent histone deacetylase activity (H3-K14 specific) Inferred from electronic annotation. Source: EC NAD-dependent histone deacetylase activity (H3-K18 specific) Inferred from electronic annotation. Source: EC NAD-dependent histone deacetylase activity (H3-K9 specific) Inferred from electronic annotation. Source: EC NAD-dependent histone deacetylase activity (H4-K16 specific) Inferred from electronic annotation. Source: EC histone deacetylase activity Inferred from direct assay Ref.4. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 697	697	Histone deacetylase HOS3		PRO_0000114727
Regions
	Region	40 – 440	401	Histone deacetylase
Sites
	Active site	196	1	By similarity
Amino acid modifications
	Modified residue	533	1	Phosphoserine Ref.7
	Modified residue	629	1	Phosphoserine Ref.6 Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Q02959 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: F2B5D09E87B097E5	FASTA	697	79,200
	10 20 30 40 50 60 MSSKHSDPLE RFYKQFQAFV QNNPNVISAA RAAAQIPESA KAVVVLSPYS LQHVFPREWV 70 80 90 100 110 120 TKSYRKTIVE RPERLLASSM GISAAITMYP SLFTLKSSHQ RKGSLMAPHV LKVHGSSWPA 130 140 150 160 170 180 ELIELCQMAD AKLLKGEIEV PDTWNSGDIY LSSKTIKALQ GTIGAIETGV DSIFKGPSAE 190 200 210 220 230 240 HISNRAFVAI RPPGHHCHYG TPSGFCLLNN AHVAIEYAYD TYNVTHVVVL DFDLHHGDGT 250 260 270 280 290 300 QDICWKRAGF KPEEEPEDSS YDDFGKKFAE FPKVGYFSMH DINSFPTESG FATKENIKNA 310 320 330 340 350 360 STCIMNSHDL NIWNIHLSKW TTEEEFNVLY RTKYRTLFAK ADEFFRSAKL EMNQQGRPFK 370 380 390 400 410 420 GLVVISAGFD ASEFEQTSMQ RHSVNVPTSF YTTFTKDALK LAQMHCHGKV LSLMEGGYSD 430 440 450 460 470 480 KAICSGVFAH LIGLQNQDWV KEWGSEQVVK EIVRGCKPAW KPYKTKRAKD VIRIWAEEVI 490 500 510 520 530 540 RLGRAMIPEF DDIIFKDAVN SAPSNSLLKA TVEPASTSTI AQRIIRSHRS NASPEKELHE 550 560 570 580 590 600 NKPRSTEKQE QREIRSDTKV KQLSSNNRAA ETQIPFLQQE FSSEDEDEEY VYDEELNKTF 610 620 630 640 650 660 NRTVEDITID DISRHLETLE IEKKGDEDSD HELKEKNWKN SHQRRLQGNG MYKIPSNTKP 670 680 690 HRIRQPQNAN TPTYDDSDIS MISHVSRKHT TRSGGRW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J. Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription." Rundlett S.E., Carmen A.A., Kobayashi R., Bavykin S., Turner B.M., Grunstein M. Proc. Natl. Acad. Sci. U.S.A. 93:14503-14508(1996) [PubMed] [Europe PMC] [Abstract] Cited for: GENE NAME.
[4]	"Yeast HOS3 forms a novel trichostatin A-insensitive homodimer with intrinsic histone deacetylase activity." Carmen A.A., Griffin P.R., Calaycay J.R., Rundlett S.E., Suka Y., Grunstein M. Proc. Natl. Acad. Sci. U.S.A. 96:12356-12361(1999) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, HOMODIMERIZATION.
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629, MASS SPECTROMETRY.
[7]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-533 AND SER-629, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U43503 Genomic DNA. Translation: AAB68246.1. BK006949 Genomic DNA. Translation: DAA11318.1.
PIR	S62006.
RefSeq	NP_015209.1. NM_001183930.1.
3D structure databases
ProteinModelPortal	Q02959.
SMR	Q02959. Positions 145-424.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-8047N.
IntAct	Q02959. 45 interactions.
MINT	MINT-2781063.
STRING	4932.YPL116W.
Proteomic databases
PaxDb	Q02959.
PeptideAtlas	Q02959.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YPL116W; YPL116W; YPL116W.
GeneID	855987.
KEGG	sce:YPL116W.
Organism-specific databases
CYGD	YPL116w.
SGD	S000006037. HOS3.
Phylogenomic databases
eggNOG	COG0123.
HOGENOM	HOG000246666.
KO	K11484.
OMA	AAITMYP.
OrthoDB	EOG4BZR9V.
Gene expression databases
Genevestigator	Q02959.
GermOnline	YPL116W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.40.800.20. 1 hit.
InterPro	IPR000286. His_deacetylse. IPR023801. His_deacetylse_dom. [Graphical view]
PANTHER	PTHR10625. PTHR10625. 1 hit.
Pfam	PF00850. Hist_deacetyl. 1 hit. [Graphical view]
PRINTS	PR01270. HDASUPER.
ProtoNet	Search...
Other
NextBio	980834.

Entry information

Entry name

HOS3_YEAST

Accession

Primary (citable) accession number: Q02959
Secondary accession number(s): D6W3Q2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program