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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: -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

Miscellaneous

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

Catalytic activityi

NAD+ + an acetylprotein = nicotinamide + O-acetyl-ADP-ribose + a protein.PROSITE-ProRule annotation1 Publication

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Activity 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)DescriptionActionsGraphical viewLength
    Active sitei135Proton acceptorPROSITE-ProRule annotation1 Publication1
    Metal bindingi143ZincPROSITE-ProRule annotation4 Publications1
    Metal bindingi146ZincPROSITE-ProRule annotation4 Publications1
    Metal bindingi170ZincPROSITE-ProRule annotation4 Publications1
    Metal bindingi173ZincPROSITE-ProRule annotation4 Publications1
    Binding sitei270NAD; via amide nitrogen2 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi32 – 52NAD2 PublicationsAdd BLAST21
    Nucleotide bindingi115 – 118NAD2 Publications4
    Nucleotide bindingi223 – 225NAD2 Publications3
    Nucleotide bindingi248 – 250NAD2 Publications3

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionHydrolase, Repressor
    Biological processTranscription, Transcription regulation
    LigandMetal-binding, NAD, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33934-MONOMER
    ReactomeiR-SCE-2151201 Transcriptional activation of mitochondrial biogenesis
    SABIO-RKiP53686

    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
    Proteomesi
    • UP000002311 Componenti: Chromosome XVI

    Organism-specific databases

    EuPathDBiFungiDB:YPL015C
    SGDiS000005936 HST2

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi117I → A, D, H, W or Y: Nearly or completely catalytically inactive. 1 Publication1
    Mutagenesisi117I → F or V: Near wild-type activity for deacetylation. Increases slightly the KM for NAD(+) to 25 uM. 1 Publication1

    Chemistry databases

    ChEMBLiCHEMBL5933

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedCombined sources
    ChainiPRO_00001102822 – 357NAD-dependent protein deacetylase HST2Add BLAST356

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylserineCombined sources1
    Modified residuei340PhosphoserineCombined sources1

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP53686
    PaxDbiP53686
    PRIDEiP53686

    PTM databases

    iPTMnetiP53686

    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, 52 interactors
    IntActiP53686, 3 interactors
    MINTiP53686
    STRINGi4932.YPL015C

    Chemistry databases

    BindingDBiP53686

    Structurei

    Secondary structure

    1357
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    ProteinModelPortaliP53686
    SMRiP53686
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP53686

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini13 – 286Deacetylase sirtuin-typePROSITE-ProRule annotationAdd BLAST274

    Sequence similaritiesi

    Belongs to the sirtuin family. Class I subfamily.Curated

    Phylogenomic databases

    GeneTreeiENSGT00870000136486
    HOGENOMiHOG000085952
    InParanoidiP53686
    KOiK11121
    OMAiLYPGSFI
    OrthoDBiEOG092C1NXT

    Family and domain databases

    Gene3Di3.30.1600.10, 2 hits
    InterProiView protein in InterPro
    IPR029035 DHS-like_NAD/FAD-binding_dom
    IPR003000 Sirtuin
    IPR026591 Sirtuin_cat_small_dom_sf
    IPR017328 Sirtuin_class_I
    IPR026590 Ssirtuin_cat_dom
    PfamiView protein in Pfam
    PF02146 SIR2, 1 hit
    PIRSFiPIRSF037938 SIR2_euk, 1 hit
    SUPFAMiSSF52467 SSF52467, 1 hit
    PROSITEiView protein in PROSITE
    PS50305 SIRTUIN, 1 hit

    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

    Similar proteinsi

    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
    PIRiS59678
    RefSeqiNP_015310.1, NM_001183829.1

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi36162, 52 interactors
    IntActiP53686, 3 interactors
    MINTiP53686
    STRINGi4932.YPL015C

    Chemistry databases

    BindingDBiP53686
    ChEMBLiCHEMBL5933

    PTM databases

    iPTMnetiP53686

    Proteomic databases

    MaxQBiP53686
    PaxDbiP53686
    PRIDEiP53686

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYPL015C; YPL015C; YPL015C
    GeneIDi856092
    KEGGisce:YPL015C

    Organism-specific databases

    EuPathDBiFungiDB:YPL015C
    SGDiS000005936 HST2

    Phylogenomic databases

    GeneTreeiENSGT00870000136486
    HOGENOMiHOG000085952
    InParanoidiP53686
    KOiK11121
    OMAiLYPGSFI
    OrthoDBiEOG092C1NXT

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33934-MONOMER
    ReactomeiR-SCE-2151201 Transcriptional activation of mitochondrial biogenesis
    SABIO-RKiP53686

    Miscellaneous databases

    EvolutionaryTraceiP53686
    PROiPR:P53686

    Family and domain databases

    Gene3Di3.30.1600.10, 2 hits
    InterProiView protein in InterPro
    IPR029035 DHS-like_NAD/FAD-binding_dom
    IPR003000 Sirtuin
    IPR026591 Sirtuin_cat_small_dom_sf
    IPR017328 Sirtuin_class_I
    IPR026590 Ssirtuin_cat_dom
    PfamiView protein in Pfam
    PF02146 SIR2, 1 hit
    PIRSFiPIRSF037938 SIR2_euk, 1 hit
    SUPFAMiSSF52467 SSF52467, 1 hit
    PROSITEiView protein in PROSITE
    PS50305 SIRTUIN, 1 hit
    ProtoNetiSearch...

    Entry informationi

    Entry nameiHST2_YEAST
    AccessioniPrimary (citable) accession number: P53686
    Secondary accession number(s): D6W3Z7
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: September 12, 2018
    This is version 163 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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