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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: 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.PROSITE-ProRule annotation1 Publication

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)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

    • NAD+ binding Source: InterPro
    • NAD-dependent histone deacetylase activity Source: SGD
    • NAD-dependent histone deacetylase activity (H4-K16 specific) Source: UniProtKB
    • zinc ion binding Source: InterPro

    GO - Biological processi

    • chromatin silencing at rDNA Source: SGD
    • chronological cell aging Source: SGD
    • histone H4 deacetylation Source: UniProtKB
    • negative regulation of chromatin silencing at telomere Source: SGD
    • negative regulation of mitotic recombination Source: SGD
    • 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
    Proteomesi
    • UP000002311 Componenti: Chromosome XVI

    Organism-specific databases

    EuPathDBiFungiDB:YPL015C.
    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

    • cytoplasm Source: SGD
    • nucleus Source: SGD
    Complete GO annotation...

    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.
    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. 41 interactors.
    IntActiP53686. 3 interactors.
    MINTiMINT-4504340.

    Chemistry databases

    BindingDBiP53686.

    Structurei

    Secondary structure

    1357
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi3 – 6Combined sources4
    Helixi9 – 21Combined sources13
    Beta strandi27 – 31Combined sources5
    Helixi33 – 39Combined sources7
    Beta strandi44 – 46Combined sources3
    Turni47 – 49Combined sources3
    Helixi51 – 53Combined sources3
    Helixi56 – 58Combined sources3
    Helixi63 – 67Combined sources5
    Helixi69 – 74Combined sources6
    Helixi77 – 86Combined sources10
    Beta strandi88 – 90Combined sources3
    Helixi95 – 105Combined sources11
    Beta strandi109 – 114Combined sources6
    Helixi120 – 123Combined sources4
    Helixi128 – 130Combined sources3
    Beta strandi131 – 133Combined sources3
    Beta strandi136 – 143Combined sources8
    Turni144 – 146Combined sources3
    Helixi153 – 159Combined sources7
    Beta strandi161 – 163Combined sources3
    Turni171 – 173Combined sources3
    Beta strandi176 – 181Combined sources6
    Helixi191 – 208Combined sources18
    Beta strandi218 – 223Combined sources6
    Turni230 – 232Combined sources3
    Helixi233 – 237Combined sources5
    Beta strandi242 – 250Combined sources9
    Helixi254 – 257Combined sources4
    Beta strandi264 – 266Combined sources3
    Helixi270 – 281Combined sources12
    Helixi284 – 291Combined sources8
    Helixi304 – 313Combined sources10

    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...

    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
    Contains 1 deacetylase sirtuin-type domain.PROSITE-ProRule annotation

    Phylogenomic databases

    GeneTreeiENSGT00850000132288.
    HOGENOMiHOG000085952.
    InParanoidiP53686.
    KOiK11121.
    OMAiKVIFMVG.
    OrthoDBiEOG092C1NXT.

    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.
    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. 41 interactors.
    IntActiP53686. 3 interactors.
    MINTiMINT-4504340.

    Chemistry databases

    BindingDBiP53686.
    ChEMBLiCHEMBL5933.

    PTM databases

    iPTMnetiP53686.

    Proteomic databases

    MaxQBiP53686.
    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

    GeneTreeiENSGT00850000132288.
    HOGENOMiHOG000085952.
    InParanoidiP53686.
    KOiK11121.
    OMAiKVIFMVG.
    OrthoDBiEOG092C1NXT.

    Enzyme and pathway databases

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

    Miscellaneous databases

    EvolutionaryTraceiP53686.
    PROiP53686.

    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]
    ProtoNetiSearch...

    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 2, 2016
    This is version 149 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.