NAD-dependent deacetylase HST1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P53685 (HST1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 111. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
NAD-dependent deacetylase HST1
EC=3.5.1.-

Alternative name(s):
Homologous to SIR2 protein 1

Gene names

Name:	HST1
Ordered Locus Names:	YOL068C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	503 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	NAD-dependent histone deacetylase involved in telomeric silencing. Histone deacetylase proteins act via the formation of large multiprotein complexes that are 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. Restores silencing at HMR in SIR2 mutants when overexpressed. Required to repress middle sporulation genes during vegetative growth. Acts as a sensor of NAD⁺ levels and regulator of NAD⁺ biosynthesis. Regulates the gene expression of de novo NAD⁺ biosynthesis genes. Ref.6 Ref.7
Catalytic activity	NAD⁺ + an acetylprotein = nicotinamide + O-acetyl-ADP-ribose + a protein. Ref.7 Ref.8
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subunit structure	Identified in the Set3C complex with HOS2, SIF2, SNT1, CPR1, HOS4/YIL112W and SET3. Its presence is however not essential for meiotic repression by the Set3C complex. Interacts with SUM1 and RFM1. The interaction with SUM1 is mediated by RFM1. Ref.10
Subcellular location	Nucleus. Note: But not nucleolar, and cytoplasmic. Ref.11
Miscellaneous	Present with 1440 molecules/cell in log phase SD medium. Ref.12
Sequence similarities	Belongs to the sirtuin family. Contains 1 deacetylase sirtuin-type domain.
Biophysicochemical properties	Kinetic parameters: K_M=94.2 µM for NAD⁺ Ref.7

Ontologies

Keywords
Biological process	Sporulation Transcription Transcription regulation
Cellular component	Nucleus
Ligand	Metal-binding NAD Zinc
Molecular function	Chromatin regulator Hydrolase Repressor
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	chromatin silencing Inferred from genetic interaction. Source: SGD negative regulation of mitotic recombination Inferred from mutant phenotype. Source: SGD sporulation resulting in formation of a cellular spore Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Set3 complex Inferred from direct assay Ref.9. Source: SGD
Molecular function	NAD+ binding Inferred from electronic annotation. Source: InterPro NAD-dependent histone deacetylase activity Inferred from direct assay Ref.9. Source: SGD NAD-independent histone deacetylase activity Inferred from direct assay Ref.9. Source: SGD protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SIF2	P38262	2	EBI-8691,EBI-17136

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 503

503

NAD-dependent deacetylase HST1

PRO_0000110281

Regions

Domain

191 – 470

280

Deacetylase sirtuin-type

Nucleotide binding

208 – 227

NAD By similarity

Nucleotide binding

290 – 294

NAD By similarity

Sites

Active site

310

Proton acceptor By similarity

Metal binding

318

Zinc By similarity

Metal binding

321

Zinc By similarity

Metal binding

342

Zinc By similarity

Metal binding

345

Zinc By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P53685 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 4CDF2799E4135ABB
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FASTA

503

57,702

        10         20         30         40         50         60 
MNILLMQRIV SFILVVSQGR YFHVGELTMT MLKRPQEEES DNNATKKLKT RLTYPCILGK 

        70         80         90        100        110        120 
DKVTGKFIFP AITKDDVMNA RLFLKDNDLK TFLEYFLPVE VNSIYIYFMI KLLGFDVKDK 

       130        140        150        160        170        180 
ELFMALNSNI TSNKERSSAE LSSIHAKAED EDELTDPLEK KHAVKLIKDL QKAINKVLST 

       190        200        210        220        230        240 
RLRLPNFNTI DHFTATLRNA KKILVLTGAG VSTSLGIPDF RSSEGFYSKI RHLGLEDPQD 

       250        260        270        280        290        300 
VFNLDIFLQD PSVFYNIAHM VLPPENMYSP LHSFIKMLQD KGKLLRNYTQ NIDNLESYAG 

       310        320        330        340        350        360 
IDPDKLVQCH GSFATASCVT CHWQIPGEKI FENIRNLELP LCPYCYQKRK QYFPMSNGNN 

       370        380        390        400        410        420 
TVQTNINFNS PILKSYGVLK PDMTFFGEAL PSRFHKTIRK DILECDLLIC IGTSLKVAPV 

       430        440        450        460        470        480 
SEIVNMVPSH VPQILINRDM VTHAEFDLNL LGFCDDVASL VAKKCHWDIP HKKWQDLKKI 

       490        500 
DYNCTEIDKG TYKIKKQPRK KQQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The SIR2 gene family, conserved from bacteria to humans, functions in silencing, cell cycle progression, and chromosome stability." Brachmann C.B., Sherman J.M., Devine S.E., Cameron E.E., Pillus L., Boeke J.D. Genes Dev. 9:2888-2902(1995) [PubMed: 7498786] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: S288c / YPH1.
[2]	"HST1, a new member of the SIR2 family of genes." Derbyshire M.K., Weinstock K.G., Strathern J.N. Yeast 12:631-640(1996) [PubMed: 8810037] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: GRY 668.
[3]	"Sequence analysis of a 33.2 kb segment from the left arm of yeast chromosome XV reveals eight known genes and ten new open reading frames including homologues of ABC transporters, inositol phosphatases and human expressed sequence tags." Tzermia M., Katsoulou C., Alexandraki D. Yeast 13:583-589(1997) [PubMed: 9178509] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. Kleine K. Nature 387:98-102(1997) [PubMed: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[5]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[6]	"Sum1 and Hst1 repress middle sporulation-specific gene expression during mitosis in Saccharomyces cerevisiae." Xie J., Pierce M., Gailus-Durner V., Wagner M., Winter E., Vershon A.K. EMBO J. 18:6448-6454(1999) [PubMed: 10562556] [Abstract] Cited for: FUNCTION.
[7]	"NAD+-dependent deacetylase Hst1p controls biosynthesis and cellular NAD+ levels in Saccharomyces cerevisiae." Bedalov A., Hirao M., Posakony J., Nelson M., Simon J.A. Mol. Cell. Biol. 23:7044-7054(2003) [PubMed: 12972620] [Abstract] Cited for: FUNCTION, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[8]	"A phylogenetically conserved NAD+-dependent protein deacetylase activity in the Sir2 protein family." Smith J.S., Brachmann C.B., Celic I., Kenna M.A., Muhammad S., Starai V.J., Avalos J.L., Escalante-Semerena J.C., Grubmeyer C., Wolberger C., Boeke J.D. Proc. Natl. Acad. Sci. U.S.A. 97:6658-6663(2000) [PubMed: 10841563] [Abstract] Cited for: ENZYME ACTIVITY.
[9]	"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 HOS2; SIF2; SNT1; CPR1; YIL112W AND SET3.
[10]	"Rfm1, a novel tethering factor required to recruit the hst1 histone deacetylase for repression of middle sporulation genes." McCord R., Pierce M., Xie J., Wonkatal S., Mickel C., Vershon A.K. Mol. Cell. Biol. 23:2009-2016(2003) [PubMed: 12612074] [Abstract] Cited for: INTERACTION WITH RFM1.
[11]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[12]	"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
EMBL GenBank DDBJ	U39041 Genomic DNA. Translation: AAA81033.1. L47120 Genomic DNA. Translation: AAB38430.1. Z74810 Genomic DNA. Translation: CAA99078.1. BK006948 Genomic DNA. Translation: DAA10715.1.
PIR	S59698.
RefSeq	NP_014573.1. NM_001183323.1.
3D structure databases
ProteinModelPortal	P53685.
SMR	P53685. Positions 157-494.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6757N.
IntAct	P53685. 5 interactions.
MINT	MINT-639447.
STRING	P53685.
Proteomic databases
PeptideAtlas	P53685.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YOL068C; YOL068C; YOL068C.
GeneID	854086.
KEGG	sce:YOL068C.
NMPDR	fig\|4932.3.peg.5665.
Organism-specific databases
CYGD	YOL068c.
SGD	S000005429. HST1.
Phylogenomic databases
eggNOG	fuNOG07733.
GeneTree	EFGT00050000002392.
HOGENOM	HBG203103.
OrthoDB	EOG4DZ53T.
Gene expression databases
ArrayExpress	P53685.
Genevestigator	P53685.
GermOnline	YOL068C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR003000. NAD-dep_deAcase_sirtuin. IPR007654. NAD-dep_histone_deAcase_SIR2_N. [Graphical view]
KO	K11121.
PANTHER	PTHR11085. SIR2. 1 hit.
Pfam	PF04574. DUF592. 1 hit. PF02146. SIR2. 1 hit. [Graphical view]
PROSITE	PS50305. SIRTUIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	975731.

Entry information

Entry name

HST1_YEAST

Accession

Primary (citable) accession number: P53685
Secondary accession number(s): D6W1Z9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents