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P40963

- SAS2_YEAST

UniProt

P40963 - SAS2_YEAST

Protein

Histone acetyltransferase SAS2

Gene

SAS2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Histone acetyltransferase (HAT) subunit of the SAS complex, a multiprotein complex that acetylates 'Lys-16' of histone H4 and 'Lys-14' of histone H3. The SAS complex is however unable to acetylate nucleosomal histones. The complex is involved in transcriptional silencing at telomeres and at HML locus. Also involved in rDNA silencing and G0 control.1 Publication

    Catalytic activityi

    Acetyl-CoA + [histone] = CoA + acetyl-[histone].

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei168 – 1681By similarity
    Active sitei208 – 2081NucleophileBy similarity
    Binding sitei246 – 2461Acetyl-CoABy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri101 – 12323C2HC-typeAdd
    BLAST

    GO - Molecular functioni

    1. acetyltransferase activity Source: SGD
    2. histone acetyltransferase activity Source: SGD
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: IntAct

    GO - Biological processi

    1. chromatin silencing at telomere Source: SGD
    2. histone acetylation Source: SGD
    3. histone exchange Source: SGD
    4. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Acyltransferase, Chromatin regulator, Repressor, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32820-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone acetyltransferase SAS2 (EC:2.3.1.48)
    Alternative name(s):
    Something about silencing protein 2
    Gene namesi
    Name:SAS2
    Synonyms:ESO1
    Ordered Locus Names:YMR127C
    ORF Names:YM9553.03C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIII

    Organism-specific databases

    CYGDiYMR127c.
    SGDiS000004734. SAS2.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nuclear chromatin Source: SGD
    3. nuclear chromosome, telomeric region Source: SGD
    4. SAS acetyltransferase complex Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi106 – 1061C → L: Loss of function. 2 Publications
    Mutagenesisi213 – 2142PP → AV: Loss of function. 1 Publication
    Mutagenesisi216 – 2172QR → AA: Abolishes silencing activity. 1 Publication
    Mutagenesisi219 – 2213GLG → AAA: Does not affect silencing activity. 1 Publication
    Mutagenesisi224 – 2252LI → AA: Does not affect silencing activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 338338Histone acetyltransferase SAS2PRO_0000051578Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei168 – 1681N6-acetyllysine; by autocatalysisBy similarity

    Post-translational modificationi

    Autoacetylation at Lys-168 is required for proper function.By similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP40963.

    Expressioni

    Gene expression databases

    GenevestigatoriP40963.

    Interactioni

    Subunit structurei

    Interacts with CAC1. Component of the SAS complex, at least composed of SAS2, SAS4 and SAS5. These three proteins constitute the core of the complex and are sufficient to acetylate histones. SAS4 is essential for HAT activity of the complex, while SAS5 is required for maxiaml HAT activity.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ASF1P324474EBI-16476,EBI-3003
    RLF2Q124954EBI-16476,EBI-3913
    SAS4Q040037EBI-16476,EBI-38500

    Protein-protein interaction databases

    BioGridi35304. 85 interactions.
    DIPiDIP-4601N.
    IntActiP40963. 6 interactions.
    MINTiMINT-497812.
    STRINGi4932.YMR127C.

    Structurei

    3D structure databases

    ProteinModelPortaliP40963.
    SMRiP40963. Positions 100-302.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini45 – 338294MYST-type HATAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni216 – 2227Acetyl-CoA bindingBy similarity

    Sequence similaritiesi

    Belongs to the MYST (SAS/MOZ) family.Curated
    Contains 1 C2HC-type zinc finger.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri101 – 12323C2HC-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5027.
    GeneTreeiENSGT00730000114398.
    HOGENOMiHOG000066050.
    KOiK11401.
    OMAiNDNNLAC.
    OrthoDBiEOG74TX7K.

    Family and domain databases

    Gene3Di3.40.630.30. 1 hit.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR002717. MOZ_SAS.
    [Graphical view]
    PfamiPF01853. MOZ_SAS. 1 hit.
    [Graphical view]
    SUPFAMiSSF55729. SSF55729. 1 hit.
    PROSITEiPS51726. MYST_HAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P40963-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARSLSQSLT ATTQKLKGKK NGGKGKNKPS AKIKKTQKEM LYGILNERNI    50
    RQIQFGLNKK FSTWYGSAVY FDPETKRLGC SETKGQLSSV SNSQYWLDTL 100
    FVCEYCFKYT DDQTRFVGHV ASCPFQYRVP GKIKYKSPEY TIRRVKGSKY 150
    QLFCQCLCLF TKLYLDNKSM YFKVDHYEFY IVYETGSTKP MGFFSKDLVS 200
    YQQNNLACIL IFPPYQRRGL GLLLIEFSYK LSQLEGVISG PEVPLSPFGL 250
    IGYLKYWSQI LCWHLIEGDL AHYDKVTLED LSIVTGMRVN DVILTLKHLN 300
    CIGENNQIYL QSLNSWLKLH GTKRNWFKLK DEYLLIDD 338
    Length:338
    Mass (Da):39,206
    Last modified:February 1, 1995 - v1
    Checksum:i22CBDC0D1B62A947
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U14548 Genomic DNA. Translation: AAA21555.1.
    Z48622 Genomic DNA. Translation: CAA88552.1.
    BK006946 Genomic DNA. Translation: DAA10024.1.
    PIRiS48299.
    RefSeqiNP_013846.1. NM_001182628.1.

    Genome annotation databases

    EnsemblFungiiYMR127C; YMR127C; YMR127C.
    GeneIDi855157.
    KEGGisce:YMR127C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U14548 Genomic DNA. Translation: AAA21555.1 .
    Z48622 Genomic DNA. Translation: CAA88552.1 .
    BK006946 Genomic DNA. Translation: DAA10024.1 .
    PIRi S48299.
    RefSeqi NP_013846.1. NM_001182628.1.

    3D structure databases

    ProteinModelPortali P40963.
    SMRi P40963. Positions 100-302.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35304. 85 interactions.
    DIPi DIP-4601N.
    IntActi P40963. 6 interactions.
    MINTi MINT-497812.
    STRINGi 4932.YMR127C.

    Proteomic databases

    PaxDbi P40963.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YMR127C ; YMR127C ; YMR127C .
    GeneIDi 855157.
    KEGGi sce:YMR127C.

    Organism-specific databases

    CYGDi YMR127c.
    SGDi S000004734. SAS2.

    Phylogenomic databases

    eggNOGi COG5027.
    GeneTreei ENSGT00730000114398.
    HOGENOMi HOG000066050.
    KOi K11401.
    OMAi NDNNLAC.
    OrthoDBi EOG74TX7K.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32820-MONOMER.

    Miscellaneous databases

    NextBioi 978572.

    Gene expression databases

    Genevestigatori P40963.

    Family and domain databases

    Gene3Di 3.40.630.30. 1 hit.
    InterProi IPR016181. Acyl_CoA_acyltransferase.
    IPR002717. MOZ_SAS.
    [Graphical view ]
    Pfami PF01853. MOZ_SAS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55729. SSF55729. 1 hit.
    PROSITEi PS51726. MYST_HAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The role of Sas2, an acetyltransferase homologue of Saccharomyces cerevisiae, in silencing and ORC function."
      Ehrenhofer-Murray A.E., Rivier D.H., Rine J.
      Genetics 145:923-934(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "Yeast SAS silencing genes and human genes associated with AML and HIV-1 Tat interactions are homologous with acetyltransferases."
      Reifsnyder C., Lowell J., Clarke A., Pillus L.
      Nat. Genet. 14:42-49(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    5. Erratum
      Reifsnyder C., Lowell J., Clarke A., Pillus L.
      Nat. Genet. 16:109-109(1997) [PubMed] [Europe PMC] [Abstract]
    6. "The yeast SAS (something about silencing) protein complex contains a MYST-type putative acetyltransferase and functions with chromatin assembly factor ASF1."
      Osada S., Sutton A., Muster N., Brown C.E., Yates J.R. III, Sternglanz R., Workman J.L.
      Genes Dev. 15:3155-3168(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, COMPONENT OF THE SAS COMPLEX WITH SAS2 AND SAS5, MUTAGENESIS OF 216-GLN-ARG-217; 219-GLY--GLY-221 AND 224-LEU-ILE-225.
    7. "The silencing complex SAS-I links histone acetylation to the assembly of repressed chromatin by CAF-I and Asf1 in Saccharomyces cerevisiae."
      Meijsing S.H., Ehrenhofer-Murray A.E.
      Genes Dev. 15:3169-3182(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: COMPONENT OF THE SAS COMPLEX WITH SAS2 AND SAS5, INTERACTION WITH CAC1, MUTAGENESIS OF CYS-106 AND 213-PRO-PRO-214.
    8. "Sas4 and Sas5 are required for the histone acetyltransferase activity of Sas2 in the SAS complex."
      Sutton A., Shia W.-J., Band D., Kaufman P.D., Osada S., Workman J.L., Sternglanz R.
      J. Biol. Chem. 278:16887-16892(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE SAS COMPLEX.
    9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSAS2_YEAST
    AccessioniPrimary (citable) accession number: P40963
    Secondary accession number(s): D6VZV0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 127 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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 XIII
      Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

    External Data

    Dasty 3