Reviewed, UniProtKB/Swiss-Prot P53096 (HOS2_YEAST)

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 (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	452 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
Subcellular location	Nucleus.
Miscellaneous	Present with 4890 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the histone deacetylase family. Type 1 subfamily.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Molecular function	Activator Chromatin regulator Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	histone deacetylation Ref.4 Inferred from direct assay. Source: SGD negative regulation of meiosis Ref.4 Inferred from mutant phenotype. Source: SGD
Cellular component	histone deacetylase complex Ref.4 Inferred from physical interaction. Source: SGD
Molecular function	NAD-dependent histone deacetylase activity Ref.4 Inferred from direct assay. Source: SGD NAD-independent histone deacetylase activity Ref.4 Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CYC8	P14922	4	EBI-8475,EBI-18215

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 452	452	Probable histone deacetylase HOS2
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
	Sequence conflict	352 – 364	13	PFRDS…DYSLY → HSGTHSGRIIHFI Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P53096-1 [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: 9046087] [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: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[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: 8962081] [Abstract] Cited for: GENE NAME.
[4]	"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: 11711434] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH SET3; HST1; SNT1; SIF2; CPR1 AND YIL112W.
[5]	"Requirement of Hos2 histone deacetylase for gene activity in yeast." Wang A., Kurdistani S.K., Grunstein M. Science 298:1412-1414(2002) [PubMed: 12434058] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF 195-HIS-HIS-196.
[6]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X91837 Genomic DNA. Translation: CAA62950.1. Z72716 Genomic DNA. Translation: CAA96906.1.
PIR	S64211.
RefSeq	NP_011321.1.
3D structure databases
HSSP	HSSP built from PDB template 1C3P based on UniProtKB O67135.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:6828N.
IntAct	P53096.
Genome annotation databases
Ensembl	YGL194C. Saccharomyces cerevisiae. [Contig view]
GeneID	852681.
GenomeReviews	Gene locus YGL194C in contig Y13135_GR.
KEGG	sce:YGL194C.
NMPDR	fig|4932.3.peg.2424.
Organism-specific databases
CYGD	YGL194c.
SGD	S000003162. HOS2.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P53096.
Gene expression databases
GermOnline	YGL194C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000286. His_deacetylse. IPR003084. His_deacetylse_1. [Graphical view]
Gene3D	G3DSA:3.40.800.20. His_deacetylse. 1 hit.
PANTHER	PTHR10625. His_deacetylse. 1 hit. PTHR10625:SF28. His_deacetylse_1. 1 hit.
Pfam	PF00850. Hist_deacetyl. 1 hit. [Graphical view]
PIRSF	PIRSF037913. His_deacetylse_1. 1 hit.
PRINTS	PR01270. HDASUPER. PR01271. HISDACETLASE.
ProDom	P53096. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
LinkHub	P53096.
ProtoNet	Search...

Entry information

Entry name

HOS2_YEAST

Accession

Primary (citable) accession number: P53096

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	July 22, 2008
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)