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P53686

- HST2_YEAST

UniProt

P53686 - HST2_YEAST

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Protein

NAD-dependent protein deacetylase HST2

Gene

HST2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

NAD-dependent histone deacetylase that is involved in nuclear silencing events. Derepresses subtelomeric silencing and increases repression in nucleolar (rDNA) silencing. Its function is negatively regulated by active nuclear export.5 Publications

Catalytic activityi

NAD+ + an acetylprotein = nicotinamide + O-acetyl-ADP-ribose + a protein.1 PublicationPROSITE-ProRule annotation

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Enzyme regulationi

Inhibited by ADP-ribose and nicotinamide.1 Publication

Kineticsi

  1. KM=10.2 µM for NAD+4 Publications
  2. KM=0.92 µM for acetylated poly-L-lysine4 Publications
  3. KM=0.5 µM for a synthetic histone H3K14 acetyllysine peptide4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei135 – 1351Proton acceptor1 PublicationPROSITE-ProRule annotation
Metal bindingi143 – 1431Zinc4 PublicationsPROSITE-ProRule annotation
Metal bindingi146 – 1461Zinc4 PublicationsPROSITE-ProRule annotation
Metal bindingi170 – 1701Zinc4 PublicationsPROSITE-ProRule annotation
Metal bindingi173 – 1731Zinc4 PublicationsPROSITE-ProRule annotation
Binding sitei270 – 2701NAD; via amide nitrogen2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi32 – 5221NAD2 PublicationsAdd
BLAST
Nucleotide bindingi115 – 1184NAD2 Publications
Nucleotide bindingi223 – 2253NAD2 Publications
Nucleotide bindingi248 – 2503NAD2 Publications

GO - Molecular functioni

  1. NAD+ binding Source: InterPro
  2. NAD-dependent histone deacetylase activity Source: SGD
  3. NAD-dependent histone deacetylase activity (H4-K16 specific) Source: UniProtKB
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. chromatin silencing at rDNA Source: SGD
  2. chronological cell aging Source: SGD
  3. histone H4 deacetylation Source: UniProtKB
  4. negative regulation of chromatin silencing at telomere Source: SGD
  5. negative regulation of mitotic recombination Source: SGD
  6. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-33934-MONOMER.
SABIO-RKP53686.

Names & Taxonomyi

Protein namesi
Recommended name:
NAD-dependent protein deacetylase HST2 (EC:3.5.1.-)
Alternative name(s):
Homologous to SIR2 protein 2
Regulatory protein SIR2 homolog 2
Gene namesi
Name:HST2
Ordered Locus Names:YPL015C
ORF Names:LPA2C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XVI

Organism-specific databases

CYGDiYPL015c.
SGDiS000005936. HST2.

Subcellular locationi

Cytoplasm. Nucleus
Note: Shuttles between the nucleus and cytoplasm, but is largely cytoplasmic owing to efficient nuclear export. Nuclear exclusion is mediated by the exportin CRM1.

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi117 – 1171I → A, D, H, W or Y: Nearly or completely catalytically inactive. 1 Publication
Mutagenesisi117 – 1171I → F or V: Near wild-type activity for deacetylation. Increases slightly the KM for NAD(+) to 25 uM. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 357356NAD-dependent protein deacetylase HST2PRO_0000110282Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei340 – 3401Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP53686.
PaxDbiP53686.

Expressioni

Gene expression databases

GenevestigatoriP53686.

Interactioni

Subunit structurei

Homotrimer. Monomer. Homotrimeric in its unliganded state. Undergoes a trimer-monomer transition upon acetyl-lysine substrate binding.4 Publications

Protein-protein interaction databases

BioGridi36162. 38 interactions.
IntActiP53686. 2 interactions.
MINTiMINT-4504340.
STRINGi4932.YPL015C.

Structurei

Secondary structure

1
357
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 64Combined sources
Helixi9 – 2113Combined sources
Beta strandi27 – 315Combined sources
Helixi33 – 397Combined sources
Beta strandi44 – 463Combined sources
Turni47 – 493Combined sources
Helixi51 – 533Combined sources
Helixi56 – 583Combined sources
Helixi63 – 675Combined sources
Helixi69 – 746Combined sources
Helixi77 – 8610Combined sources
Beta strandi88 – 903Combined sources
Helixi95 – 10511Combined sources
Beta strandi109 – 1146Combined sources
Helixi120 – 1234Combined sources
Helixi128 – 1303Combined sources
Beta strandi131 – 1333Combined sources
Beta strandi136 – 1438Combined sources
Turni144 – 1463Combined sources
Helixi153 – 1597Combined sources
Beta strandi161 – 1633Combined sources
Turni171 – 1733Combined sources
Beta strandi176 – 1816Combined sources
Helixi191 – 20818Combined sources
Beta strandi218 – 2236Combined sources
Turni230 – 2323Combined sources
Helixi233 – 2375Combined sources
Beta strandi242 – 2509Combined sources
Helixi254 – 2574Combined sources
Beta strandi264 – 2663Combined sources
Helixi270 – 28112Combined sources
Helixi284 – 2918Combined sources
Helixi304 – 31310Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q14X-ray2.50A1-357[»]
1Q17X-ray2.70A/B/C1-294[»]
1Q1AX-ray1.50A5-293[»]
1SZCX-ray1.75A1-294[»]
1SZDX-ray1.50A1-294[»]
2OD2X-ray2.00A1-294[»]
2OD7X-ray2.00A1-294[»]
2OD9X-ray2.05A1-294[»]
2QQFX-ray2.00A1-294[»]
2QQGX-ray2.05A1-294[»]
ProteinModelPortaliP53686.
SMRiP53686. Positions 5-293.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53686.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 286274Deacetylase sirtuin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the sirtuin family. Class I subfamily.Curated
Contains 1 deacetylase sirtuin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0846.
GeneTreeiENSGT00740000115546.
HOGENOMiHOG000085952.
InParanoidiP53686.
KOiK11121.
OMAiFRPTIAH.
OrthoDBiEOG7MWH64.

Family and domain databases

Gene3Di3.30.1600.10. 2 hits.
3.40.50.1220. 3 hits.
InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR003000. Sirtuin.
IPR026591. Sirtuin_cat_small_dom.
IPR017328. Sirtuin_class_I.
IPR026590. Ssirtuin_cat_dom.
[Graphical view]
PANTHERiPTHR11085. PTHR11085. 1 hit.
PfamiPF02146. SIR2. 1 hit.
[Graphical view]
PIRSFiPIRSF037938. SIR2_euk. 1 hit.
SUPFAMiSSF52467. SSF52467. 1 hit.
PROSITEiPS50305. SIRTUIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P53686-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSVSTASTEM SVRKIAAHMK SNPNAKVIFM VGAGISTSCG IPDFRSPGTG
60 70 80 90 100
LYHNLARLKL PYPEAVFDVD FFQSDPLPFY TLAKELYPGN FRPSKFHYLL
110 120 130 140 150
KLFQDKDVLK RVYTQNIDTL ERQAGVKDDL IIEAHGSFAH CHCIGCGKVY
160 170 180 190 200
PPQVFKSKLA EHPIKDFVKC DVCGELVKPA IVFFGEDLPD SFSETWLNDS
210 220 230 240 250
EWLREKITTS GKHPQQPLVI VVGTSLAVYP FASLPEEIPR KVKRVLCNLE
260 270 280 290 300
TVGDFKANKR PTDLIVHQYS DEFAEQLVEE LGWQEDFEKI LTAQGGMGDN
310 320 330 340 350
SKEQLLEIVH DLENLSLDQS EHESADKKDK KLQRLNGHDS DEDGASNSSS

SQKAAKE
Length:357
Mass (Da):39,979
Last modified:October 1, 1996 - v1
Checksum:iED281E5B8241A4D0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39063 Genomic DNA. Translation: AAA81035.1.
U33335 Genomic DNA. Translation: AAB68090.1.
AY693204 Genomic DNA. Translation: AAT93223.1.
BK006949 Genomic DNA. Translation: DAA11413.1.
PIRiS59678.
RefSeqiNP_015310.1. NM_001183829.1.

Genome annotation databases

EnsemblFungiiYPL015C; YPL015C; YPL015C.
GeneIDi856092.
KEGGisce:YPL015C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39063 Genomic DNA. Translation: AAA81035.1 .
U33335 Genomic DNA. Translation: AAB68090.1 .
AY693204 Genomic DNA. Translation: AAT93223.1 .
BK006949 Genomic DNA. Translation: DAA11413.1 .
PIRi S59678.
RefSeqi NP_015310.1. NM_001183829.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1Q14 X-ray 2.50 A 1-357 [» ]
1Q17 X-ray 2.70 A/B/C 1-294 [» ]
1Q1A X-ray 1.50 A 5-293 [» ]
1SZC X-ray 1.75 A 1-294 [» ]
1SZD X-ray 1.50 A 1-294 [» ]
2OD2 X-ray 2.00 A 1-294 [» ]
2OD7 X-ray 2.00 A 1-294 [» ]
2OD9 X-ray 2.05 A 1-294 [» ]
2QQF X-ray 2.00 A 1-294 [» ]
2QQG X-ray 2.05 A 1-294 [» ]
ProteinModelPortali P53686.
SMRi P53686. Positions 5-293.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 36162. 38 interactions.
IntActi P53686. 2 interactions.
MINTi MINT-4504340.
STRINGi 4932.YPL015C.

Chemistry

BindingDBi P53686.
ChEMBLi CHEMBL5933.

Proteomic databases

MaxQBi P53686.
PaxDbi P53686.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YPL015C ; YPL015C ; YPL015C .
GeneIDi 856092.
KEGGi sce:YPL015C.

Organism-specific databases

CYGDi YPL015c.
SGDi S000005936. HST2.

Phylogenomic databases

eggNOGi COG0846.
GeneTreei ENSGT00740000115546.
HOGENOMi HOG000085952.
InParanoidi P53686.
KOi K11121.
OMAi FRPTIAH.
OrthoDBi EOG7MWH64.

Enzyme and pathway databases

BioCyci YEAST:G3O-33934-MONOMER.
SABIO-RK P53686.

Miscellaneous databases

EvolutionaryTracei P53686.
NextBioi 981122.
PROi P53686.

Gene expression databases

Genevestigatori P53686.

Family and domain databases

Gene3Di 3.30.1600.10. 2 hits.
3.40.50.1220. 3 hits.
InterProi IPR029035. DHS-like_NAD/FAD-binding_dom.
IPR003000. Sirtuin.
IPR026591. Sirtuin_cat_small_dom.
IPR017328. Sirtuin_class_I.
IPR026590. Ssirtuin_cat_dom.
[Graphical view ]
PANTHERi PTHR11085. PTHR11085. 1 hit.
Pfami PF02146. SIR2. 1 hit.
[Graphical view ]
PIRSFi PIRSF037938. SIR2_euk. 1 hit.
SUPFAMi SSF52467. SSF52467. 1 hit.
PROSITEi PS50305. SIRTUIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: S288c / YPH1.
  2. "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 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases."
    Landry J., Sutton A., Tafrov S.T., Heller R.C., Stebbins J., Pillus L., Sternglanz R.
    Proc. Natl. Acad. Sci. U.S.A. 97:5807-5811(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Silent information regulator 2 family of NAD- dependent histone/protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose."
    Tanner K.G., Landry J., Sternglanz R., Denu J.M.
    Proc. Natl. Acad. Sci. U.S.A. 97:14178-14182(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
  7. "A cytosolic NAD-dependent deacetylase, Hst2p, can modulate nucleolar and telomeric silencing in yeast."
    Perrod S., Cockell M.M., Laroche T., Renauld H., Ducrest A.L., Bonnard C., Gasser S.M.
    EMBO J. 20:197-209(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  10. "Substrate specificity and kinetic mechanism of the Sir2 family of NAD+-dependent histone/protein deacetylases."
    Borra M.T., Langer M.R., Slama J.T., Denu J.M.
    Biochemistry 43:9877-9887(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
  11. "Nuclear export modulates the cytoplasmic Sir2 homologue Hst2."
    Wilson J.M., Le V.Q., Zimmerman C., Marmorstein R., Pillus L.
    EMBO Rep. 7:1247-1251(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  12. "Use of substrate analogs and mutagenesis to study substrate binding and catalysis in the Sir2 family of NAD-dependent protein deacetylases."
    Khan A.N., Lewis P.N.
    J. Biol. Chem. 281:11702-11711(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
  13. "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-340, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Investigation of the catalytic mechanism of Sir2 enzyme with QM/MM approach: SN1 vs SN2?"
    Liang Z., Shi T., Ouyang S., Li H., Yu K., Zhu W., Luo C., Jiang H.
    J. Phys. Chem. B 114:11927-11933(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE.
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  16. "Structure and autoregulation of the yeast Hst2 homolog of Sir2."
    Zhao K., Chai X., Clements A., Marmorstein R.
    Nat. Struct. Biol. 10:864-871(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH PEPTIDE SUBSTRATE; ZINC AND NAD.
  17. "Structure of the yeast Hst2 protein deacetylase in ternary complex with 2'-O-acetyl ADP ribose and histone peptide."
    Zhao K., Chai X., Marmorstein R.
    Structure 11:1403-1411(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 5-293 IN COMPLEX WITH SUBSTRATE ANALOG; PEPTIDE SUBSTRATE AND ZINC, SUBUNIT.
  18. "Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD(+)-dependent Sir2 histone/protein deacetylases."
    Zhao K., Harshaw R., Chai X., Marmorstein R.
    Proc. Natl. Acad. Sci. U.S.A. 101:8563-8568(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-294 IN COMPLEX WITH PEPTIDE SUBSTRATE; ZINC AND NAD.
  19. "Structural basis for nicotinamide inhibition and base exchange in Sir2 enzymes."
    Sanders B.D., Zhao K., Slama J.T., Marmorstein R.
    Mol. Cell 25:463-472(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-294 IN COMPLEX WITH PEPTIDE SUBSTRATE; NICOTINAMIDE AND ZINC, MUTAGENESIS OF 117, BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiHST2_YEAST
AccessioniPrimary (citable) accession number: P53686
Secondary accession number(s): D6W3Z7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 26, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 5260 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

External Data

Dasty 3