P53096 (HOS2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable histone deacetylase HOS2
EC=3.5.1.98

Gene names

Name:	HOS2
Ordered Locus Names:	YGL194C
ORF Names:	G1330

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	452 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). It is apparently involved in transcriptional activation. Ref.6
Catalytic activity	Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.
Subunit structure	Identified in a Set3C complex with SET3, HST1, SNT1, SIF2, CPR1 and HOS4/YIL112W. Ref.5
Subcellular location	Nucleus.
Miscellaneous	Present with 4890 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	Activator Chromatin regulator Hydrolase
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 negative regulation of meiosis Inferred from mutant phenotype Ref.5. Source: SGD positive regulation of stress-activated MAPK cascade Inferred from mutant phenotype PubMed 18487345. Source: SGD regulation of transcription, DNA-dependent Inferred from mutant phenotype PubMed 19379692. Source: SGD transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Rpd3L-Expanded complex Inferred from direct assay PubMed 19040720. Source: SGD Set3 complex Inferred from direct assay Ref.5. Source: SGD cytoplasm Inferred from direct assay PubMed 22842922. Source: SGD
Molecular_function	NAD-dependent histone deacetylase activity Inferred from direct assay Ref.5. Source: SGD 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 NAD-independent histone deacetylase activity Inferred from direct assay Ref.5. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CYC8	P14922	4	EBI-8475,EBI-18215
HHT2	P61830	2	EBI-8475,EBI-8098

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 452	452	Probable histone deacetylase HOS2		PRO_0000114723
Regions
	Region	26 – 340	315	Histone deacetylase
Sites
	Active site	197	1	By similarity
Experimental info
	Mutagenesis	196 – 197	2	HH → AA: Leads to hyperacetylation. Ref.6
	Sequence conflict	352 – 364	13	PFRDS…DYSLY → HSGTHSGRIIHFI Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P53096 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 024E8AEA0A445A08	FASTA	452	51,455
	10 20 30 40 50 60 MSGTFSYDVK TKENEPLFEF NSAYSPRVSY HFNSKVSHYH YGVKHPMKPF RLMLTDHLVS 70 80 90 100 110 120 SYGLHKIMDL YETRSATRDE LLQFHSEDYV NFLSKVSPEN ANKLPRGTLE NFNIGDDCPI 130 140 150 160 170 180 FQNLYDYTTL YTGASLDATR KLINNQSDIA INWSGGLHHA KKNSPSGFCY VNDIVLSILN 190 200 210 220 230 240 LLRYHPRILY IDIDLHHGDG VQEAFYTTDR VFTLSFHKYN GEFFPGTGDL TEIGCDKGKH 250 260 270 280 290 300 FALNVPLEDG IDDDSYINLF KSIVDPLIMT FKPTLIVQQC GADSLGHDRL GCFNLNIKAH 310 320 330 340 350 360 GECVKFVKSF GLPMLVVGGG GYTPRNVSRL WTYETGILND VLLPEDIPED IPFRDSFGPD 370 380 390 400 410 420 YSLYPMLDDL YENKNSKKLL EDIRIRCLEN IRYLQGAPSV RMDAECIPTQ DISALTEEED 430 440 450 KIIQEMNEET EADSSNRLEE MEKENSGLIA FS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequencing of a 40.5 kb fragment located on the left arm of chromosome VII from Saccharomyces cerevisiae." Coglievina M., Klima R., Bertani I., Delneri D., Zaccaria P., Bruschi C.V. Yeast 13:55-64(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"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.
[5]	"The S. cerevisiae SET3 complex includes two histone deacetylases, Hos2 and Hst1, and is a meiotic-specific repressor of the sporulation gene program." Pijnappel W.W.M.P., Schaft D., Roguev A., Shevchenko A., Tekotte H., Wilm M., Rigaut G., Seraphin B., Aasland R., Stewart A.F. Genes Dev. 15:2991-3004(2001) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH SET3; HST1; SNT1; SIF2; CPR1 AND YIL112W.
[6]	"Requirement of Hos2 histone deacetylase for gene activity in yeast." Wang A., Kurdistani S.K., Grunstein M. Science 298:1412-1414(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF 195-HIS-HIS-196.
[7]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X91837 Genomic DNA. Translation: CAA62950.1. Z72716 Genomic DNA. Translation: CAA96906.1. BK006941 Genomic DNA. Translation: DAA07921.1.
PIR	S64211.
RefSeq	NP_011321.1. NM_001181059.1.
3D structure databases
ProteinModelPortal	P53096.
SMR	P53096. Positions 28-394.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6828N.
IntAct	P53096. 37 interactions.
MINT	MINT-629670.
STRING	4932.YGL194C.
Proteomic databases
PaxDb	P53096.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YGL194C; YGL194C; YGL194C.
GeneID	852681.
KEGG	sce:YGL194C.
Organism-specific databases
CYGD	YGL194c.
SGD	S000003162. HOS2.
Phylogenomic databases
eggNOG	COG0123.
GeneTree	ENSGT00390000003411.
HOGENOM	HOG000225180.
KO	K11483.
OMA	PRVMYID.
OrthoDB	EOG4GJ2XR.
Gene expression databases
Genevestigator	P53096.
GermOnline	YGL194C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.40.800.20. 1 hit.
InterPro	IPR000286. His_deacetylse. IPR003084. His_deacetylse_1. IPR023801. His_deacetylse_dom. [Graphical view]
PANTHER	PTHR10625. PTHR10625. 1 hit.
Pfam	PF00850. Hist_deacetyl. 1 hit. [Graphical view]
PIRSF	PIRSF037913. His_deacetylse_1. 1 hit.
PRINTS	PR01270. HDASUPER. PR01271. HISDACETLASE.
ProtoNet	Search...
Other
NextBio	971996.

Entry information

Entry name

HOS2_YEAST

Accession

Primary (citable) accession number: P53096
Secondary accession number(s): D6VTW0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program