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Protein

NAD-dependent protein deacetylase HST1

Gene

HST1

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 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.2 Publications

Catalytic activityi

NAD+ + an acetylprotein = nicotinamide + O-acetyl-ADP-ribose + a protein.PROSITE-ProRule annotation2 Publications

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Kineticsi

  1. KM=94.2 µM for NAD+1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei310 – 3101Proton acceptorPROSITE-ProRule annotation
    Metal bindingi318 – 3181ZincPROSITE-ProRule annotation
    Metal bindingi321 – 3211ZincPROSITE-ProRule annotation
    Metal bindingi342 – 3421ZincPROSITE-ProRule annotation
    Metal bindingi345 – 3451ZincPROSITE-ProRule annotation
    Binding sitei454 – 4541NAD; via amide nitrogenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi208 – 22720NADBy similarityAdd
    BLAST
    Nucleotide bindingi290 – 2934NADBy similarity
    Nucleotide bindingi412 – 4143NADBy similarity
    Nucleotide bindingi437 – 4393NADBy similarity

    GO - Molecular functioni

    • NAD+ binding Source: InterPro
    • NAD-dependent histone deacetylase activity Source: SGD
    • NAD-independent histone deacetylase activity Source: SGD
    • zinc ion binding Source: InterPro

    GO - Biological processi

    • chromatin silencing at silent mating-type cassette Source: SGD
    • histone deacetylation Source: SGD
    • negative regulation of mitotic recombination Source: SGD
    • regulation of thiamine biosynthetic process Source: CACAO
    • sporulation resulting in formation of a cellular spore Source: UniProtKB-KW
    • transcription, DNA-templated Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Molecular functioni

    Chromatin regulator, Hydrolase, Repressor

    Keywords - Biological processi

    Sporulation, Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, NAD, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33473-MONOMER.
    ReactomeiR-SCE-3371453. Regulation of HSF1-mediated heat shock response.
    R-SCE-427359. SIRT1 negatively regulates rRNA Expression.
    SABIO-RKP53685.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NAD-dependent protein deacetylase HST1 (EC:3.5.1.-)
    Alternative name(s):
    Homologous to SIR2 protein 1
    Regulatory protein SIR2 homolog 1
    Gene namesi
    Name:HST1
    Ordered Locus Names:YOL068C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome XV

    Organism-specific databases

    EuPathDBiFungiDB:YOL068C.
    SGDiS000005429. HST1.

    Subcellular locationi

    GO - Cellular componenti

    • Set3 complex Source: SGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 503503NAD-dependent protein deacetylase HST1PRO_0000110281Add
    BLAST

    Proteomic databases

    MaxQBiP53685.
    PeptideAtlasiP53685.

    Interactioni

    Subunit structurei

    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 RFM1.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SIF2P382622EBI-8691,EBI-17136

    Protein-protein interaction databases

    BioGridi34333. 75 interactions.
    DIPiDIP-6757N.
    IntActiP53685. 5 interactions.
    MINTiMINT-639447.

    Structurei

    3D structure databases

    ProteinModelPortaliP53685.
    SMRiP53685. Positions 65-494.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini191 – 470280Deacetylase 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

    GeneTreeiENSGT00740000115330.
    HOGENOMiHOG000191845.
    InParanoidiP53685.
    KOiK11121.
    OrthoDBiEOG7MWH64.

    Family and domain databases

    Gene3Di3.30.1600.10. 2 hits.
    3.40.50.1220. 3 hits.
    InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
    IPR007654. NAD-dep_histone_deAcase_SIR2_N.
    IPR003000. Sirtuin.
    IPR026591. Sirtuin_cat_small_dom.
    IPR026590. Ssirtuin_cat_dom.
    [Graphical view]
    PANTHERiPTHR11085. PTHR11085. 2 hits.
    PfamiPF04574. DUF592. 1 hit.
    PF02146. SIR2. 1 hit.
    [Graphical view]
    SUPFAMiSSF52467. SSF52467. 2 hits.
    PROSITEiPS50305. SIRTUIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P53685-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MNILLMQRIV SFILVVSQGR YFHVGELTMT MLKRPQEEES DNNATKKLKT
    60 70 80 90 100
    RLTYPCILGK DKVTGKFIFP AITKDDVMNA RLFLKDNDLK TFLEYFLPVE
    110 120 130 140 150
    VNSIYIYFMI KLLGFDVKDK ELFMALNSNI TSNKERSSAE LSSIHAKAED
    160 170 180 190 200
    EDELTDPLEK KHAVKLIKDL QKAINKVLST RLRLPNFNTI DHFTATLRNA
    210 220 230 240 250
    KKILVLTGAG VSTSLGIPDF RSSEGFYSKI RHLGLEDPQD VFNLDIFLQD
    260 270 280 290 300
    PSVFYNIAHM VLPPENMYSP LHSFIKMLQD KGKLLRNYTQ NIDNLESYAG
    310 320 330 340 350
    IDPDKLVQCH GSFATASCVT CHWQIPGEKI FENIRNLELP LCPYCYQKRK
    360 370 380 390 400
    QYFPMSNGNN TVQTNINFNS PILKSYGVLK PDMTFFGEAL PSRFHKTIRK
    410 420 430 440 450
    DILECDLLIC IGTSLKVAPV SEIVNMVPSH VPQILINRDM VTHAEFDLNL
    460 470 480 490 500
    LGFCDDVASL VAKKCHWDIP HKKWQDLKKI DYNCTEIDKG TYKIKKQPRK

    KQQ
    Length:503
    Mass (Da):57,702
    Last modified:October 1, 1996 - v1
    Checksum:i4CDF2799E4135ABB
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U39041 Genomic DNA. Translation: AAA81033.1.
    L47120 Genomic DNA. Translation: AAB38430.1.
    Z74810 Genomic DNA. Translation: CAA99078.1.
    BK006948 Genomic DNA. Translation: DAA10715.1.
    PIRiS59698.
    RefSeqiNP_014573.1. NM_001183323.1.

    Genome annotation databases

    EnsemblFungiiYOL068C; YOL068C; YOL068C.
    GeneIDi854086.
    KEGGisce:YOL068C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U39041 Genomic DNA. Translation: AAA81033.1.
    L47120 Genomic DNA. Translation: AAB38430.1.
    Z74810 Genomic DNA. Translation: CAA99078.1.
    BK006948 Genomic DNA. Translation: DAA10715.1.
    PIRiS59698.
    RefSeqiNP_014573.1. NM_001183323.1.

    3D structure databases

    ProteinModelPortaliP53685.
    SMRiP53685. Positions 65-494.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi34333. 75 interactions.
    DIPiDIP-6757N.
    IntActiP53685. 5 interactions.
    MINTiMINT-639447.

    Proteomic databases

    MaxQBiP53685.
    PeptideAtlasiP53685.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYOL068C; YOL068C; YOL068C.
    GeneIDi854086.
    KEGGisce:YOL068C.

    Organism-specific databases

    EuPathDBiFungiDB:YOL068C.
    SGDiS000005429. HST1.

    Phylogenomic databases

    GeneTreeiENSGT00740000115330.
    HOGENOMiHOG000191845.
    InParanoidiP53685.
    KOiK11121.
    OrthoDBiEOG7MWH64.

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33473-MONOMER.
    ReactomeiR-SCE-3371453. Regulation of HSF1-mediated heat shock response.
    R-SCE-427359. SIRT1 negatively regulates rRNA Expression.
    SABIO-RKP53685.

    Miscellaneous databases

    PROiP53685.

    Family and domain databases

    Gene3Di3.30.1600.10. 2 hits.
    3.40.50.1220. 3 hits.
    InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
    IPR007654. NAD-dep_histone_deAcase_SIR2_N.
    IPR003000. Sirtuin.
    IPR026591. Sirtuin_cat_small_dom.
    IPR026590. Ssirtuin_cat_dom.
    [Graphical view]
    PANTHERiPTHR11085. PTHR11085. 2 hits.
    PfamiPF04574. DUF592. 1 hit.
    PF02146. SIR2. 1 hit.
    [Graphical view]
    SUPFAMiSSF52467. SSF52467. 2 hits.
    PROSITEiPS50305. SIRTUIN. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    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. "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] [Europe PMC] [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] [Europe PMC] [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.
      , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
      Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. 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] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. Cited for: ENZYME ACTIVITY.
    8. "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] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH HOS2; SIF2; SNT1; CPR1; YIL112W AND SET3.
    9. "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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RFM1.
    10. "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] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiHST1_YEAST
    AccessioniPrimary (citable) accession number: P53685
    Secondary accession number(s): D6W1Z9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: June 8, 2016
    This is version 151 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 1440 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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