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Q07794

- RT109_YEAST

UniProt

Q07794 - RT109_YEAST

Protein

Histone acetyltransferase RTT109

Gene

RTT109

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 105 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Required for acetylation of 'Lys-56' of histone H3 (H3K56ac) which occurs in S phase and disappears during G2/M phase of the cell cycle and is involved in transcription DNA repair process. H3K56 acetylation weakens of the interaction between the histone core and the surrounding DNA in the nucleosomal particle and drives chromatin disassembly. Involved in regulation of Ty1 transposition.9 Publications

    Catalytic activityi

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

    GO - Molecular functioni

    1. H3 histone acetyltransferase activity Source: SGD

    GO - Biological processi

    1. double-strand break repair via nonhomologous end joining Source: SGD
    2. histone acetylation Source: SGD
    3. histone H3 acetylation Source: GOC
    4. maintenance of rDNA Source: SGD
    5. negative regulation of transposition, RNA-mediated Source: SGD
    6. regulation of transcription from RNA polymerase II promoter in response to stress Source: SGD
    7. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    DNA damage, Transcription, Transcription regulation

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32107-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone acetyltransferase RTT109 (EC:2.3.1.48)
    Alternative name(s):
    Regulator of Ty1 transposition protein 109
    Gene namesi
    Name:RTT109
    Synonyms:KIM2, REM50
    Ordered Locus Names:YLL002W
    ORF Names:L1377
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XII

    Organism-specific databases

    CYGDiYLL002w.
    SGDiS000003925. RTT109.

    Subcellular locationi

    Nucleus 2 Publications

    GO - Cellular componenti

    1. nucleus Source: SGD

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi89 – 891D → A or N: Losses histone acetylase activity. 1 Publication
    Mutagenesisi287 – 2882DD → AA or NN: Reduces histone acetylase activity.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 436436Histone acetyltransferase RTT109PRO_0000268738Add
    BLAST

    Proteomic databases

    PaxDbiQ07794.

    Expressioni

    Inductioni

    Expression peaks in cell cycle G1.1 Publication

    Gene expression databases

    GenevestigatoriQ07794.

    Interactioni

    Subunit structurei

    Interacts with ASF1 and VPS75.5 Publications

    Protein-protein interaction databases

    BioGridi31249. 356 interactions.
    DIPiDIP-8842N.
    IntActiQ07794. 1 interaction.
    MINTiMINT-2781350.
    STRINGi4932.YLL002W.

    Structurei

    Secondary structure

    1
    436
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 108
    Beta strandi16 – 238
    Beta strandi27 – 293
    Beta strandi37 – 404
    Beta strandi44 – 5714
    Beta strandi60 – 7718
    Beta strandi79 – 9012
    Helixi100 – 11213
    Helixi117 – 1204
    Beta strandi121 – 1244
    Helixi135 – 1373
    Helixi144 – 15815
    Beta strandi159 – 1613
    Helixi164 – 1674
    Helixi169 – 1746
    Beta strandi175 – 1773
    Helixi182 – 1843
    Beta strandi186 – 1938
    Helixi195 – 1973
    Beta strandi199 – 2013
    Helixi204 – 2063
    Beta strandi207 – 2093
    Helixi215 – 23319
    Beta strandi239 – 2435
    Helixi249 – 2568
    Beta strandi259 – 2624
    Beta strandi264 – 2674
    Helixi273 – 2764
    Helixi278 – 2803
    Helixi289 – 29911
    Turni303 – 3053
    Helixi308 – 31811
    Helixi320 – 3234
    Turni324 – 3263
    Beta strandi328 – 3347
    Beta strandi336 – 3383
    Turni346 – 3483
    Helixi355 – 36612
    Helixi373 – 39119
    Beta strandi396 – 3994
    Helixi411 – 42313

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2RIMX-ray2.20A1-436[»]
    2ZFNX-ray1.90A1-436[»]
    3CZ7X-ray2.00A1-127[»]
    A171-403[»]
    3Q33X-ray2.80A1-436[»]
    3Q35X-ray3.30A1-436[»]
    3Q66X-ray2.70C1-436[»]
    3Q68X-ray2.70C1-436[»]
    3QM0X-ray3.10A1-436[»]
    ProteinModelPortaliQ07794.
    SMRiQ07794. Positions 1-426.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ07794.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RTT109 family.Curated

    Phylogenomic databases

    eggNOGiCOG5087.
    HOGENOMiHOG000001105.
    KOiK11309.
    OMAiFTSKENS.
    OrthoDBiEOG79PJZ1.

    Family and domain databases

    InterProiIPR013178. Histone_H3-K56_AcTrfase_RTT109.
    IPR016849. Histone_H3-K56_AcTrfase_yeast.
    [Graphical view]
    PfamiPF08214. KAT11. 1 hit.
    [Graphical view]
    PIRSFiPIRSF027124. Histone_acetylase_Rtt109. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q07794-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSLNDFLSSV LPVSEQFEYL SLQSIPLETH AVVTPNKDDK RVPKSTIKTQ    50
    HFFSLFHQGK VFFSLEVYVY VTLWDEADAE RLIFVSKADT NGYCNTRVSV 100
    RDITKIILEF ILSIDPNYYL QKVKPAIRSY KKISPELISA ASTPARTLRI 150
    LARRLKQSGS TVLKEIESPR FQQDLYLSFT CPREILTKIC LFTRPASQYL 200
    FPDSSKNSKK HILNGEELMK WWGFILDRLL IECFQNDTQA KLRIPGEDPA 250
    RVRSYLRGMK YPLWQVGDIF TSKENSLAVY NIPLFPDDPK ARFIHQLAEE 300
    DRLLKVSLSS FWIELQERQE FKLSVTSSVM GISGYSLATP SLFPSSADVI 350
    VPKSRKQFRA IKKYITGEEY DTEEGAIEAF TNIRDFLLLR MATNLQSLTG 400
    KREHRERNQP VPASNINTLA ITMLKPRKKA KALPKT 436
    Length:436
    Mass (Da):50,096
    Last modified:November 1, 1996 - v1
    Checksum:i17825D6EF97C4BB5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91488 Genomic DNA. Translation: CAA62768.1.
    Z73107 Genomic DNA. Translation: CAA97445.1.
    BK006945 Genomic DNA. Translation: DAA09317.1.
    PIRiS64744.
    RefSeqiNP_013099.1. NM_001181822.1.

    Genome annotation databases

    EnsemblFungiiYLL002W; YLL002W; YLL002W.
    GeneIDi850658.
    KEGGisce:YLL002W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91488 Genomic DNA. Translation: CAA62768.1 .
    Z73107 Genomic DNA. Translation: CAA97445.1 .
    BK006945 Genomic DNA. Translation: DAA09317.1 .
    PIRi S64744.
    RefSeqi NP_013099.1. NM_001181822.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2RIM X-ray 2.20 A 1-436 [» ]
    2ZFN X-ray 1.90 A 1-436 [» ]
    3CZ7 X-ray 2.00 A 1-127 [» ]
    A 171-403 [» ]
    3Q33 X-ray 2.80 A 1-436 [» ]
    3Q35 X-ray 3.30 A 1-436 [» ]
    3Q66 X-ray 2.70 C 1-436 [» ]
    3Q68 X-ray 2.70 C 1-436 [» ]
    3QM0 X-ray 3.10 A 1-436 [» ]
    ProteinModelPortali Q07794.
    SMRi Q07794. Positions 1-426.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31249. 356 interactions.
    DIPi DIP-8842N.
    IntActi Q07794. 1 interaction.
    MINTi MINT-2781350.
    STRINGi 4932.YLL002W.

    Proteomic databases

    PaxDbi Q07794.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YLL002W ; YLL002W ; YLL002W .
    GeneIDi 850658.
    KEGGi sce:YLL002W.

    Organism-specific databases

    CYGDi YLL002w.
    SGDi S000003925. RTT109.

    Phylogenomic databases

    eggNOGi COG5087.
    HOGENOMi HOG000001105.
    KOi K11309.
    OMAi FTSKENS.
    OrthoDBi EOG79PJZ1.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32107-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q07794.
    NextBioi 966623.

    Gene expression databases

    Genevestigatori Q07794.

    Family and domain databases

    InterProi IPR013178. Histone_H3-K56_AcTrfase_RTT109.
    IPR016849. Histone_H3-K56_AcTrfase_yeast.
    [Graphical view ]
    Pfami PF08214. KAT11. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF027124. Histone_acetylase_Rtt109. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Sequence analysis of the CEN12 region of Saccharomyces cerevisiae on a 43.7 kb fragment of chromosome XII including an open reading frame homologous to the human cystic fibrosis transmembrane conductance regulator protein CFTR."
      Miosga T., Zimmermann F.K.
      Yeast 12:693-708(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204511 / S288c / AB972.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
      Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
      , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
      Nature 387:87-90(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. "Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have conserved roles in genome maintenance."
      Scholes D.T., Banerjee M., Bowen B., Curcio M.J.
      Genetics 159:1449-1465(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    7. "Localization of proteins that are coordinately expressed with Cln2 during the cell cycle."
      Sundin B.A., Chiu C.-H., Riffle M., Davis T.N., Muller E.G.D.
      Yeast 21:793-800(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, SUBCELLULAR LOCATION.
    8. "Rtt109 is required for proper H3K56 acetylation: a chromatin mark associated with the elongating RNA polymerase II."
      Schneider J., Bajwa P., Johnson F.C., Bhaumik S.R., Shilatifard A.
      J. Biol. Chem. 281:37270-37274(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "The Rtt109-Vps75 histone acetyltransferase complex acetylates non-nucleosomal histone H3."
      Han J., Zhou H., Li Z., Xu R.-M., Zhang Z.
      J. Biol. Chem. 282:14158-14164(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH VPS75.
    10. "Acetylation of lysine 56 of histone H3 catalyzed by RTT109 and regulated by ASF1 is required for replisome integrity."
      Han J., Zhou H., Li Z., Xu R.-M., Zhang Z.
      J. Biol. Chem. 282:28587-28596(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ASF1 AND VPS75.
    11. "Histone H3-K56 acetylation is catalyzed by histone chaperone-dependent complexes."
      Tsubota T., Berndsen C.E., Erkmann J.A., Smith C.L., Yang L., Freitas M.A., Denu J.M., Kaufman P.D.
      Mol. Cell 25:703-712(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ASF1 AND VPS75.
    12. "Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56."
      Driscoll R., Hudson A., Jackson S.P.
      Science 315:649-652(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication."
      Han J., Zhou H., Horazdovsky B., Zhang K., Xu R.-M., Zhang Z.
      Science 315:653-655(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ASP-89 AND 287-ASP-ASP-288, INTERACTION WITH VPS75.
    14. "Acetylation in the globular core of histone H3 on lysine-56 promotes chromatin disassembly during transcriptional activation."
      Williams S.K., Truong D., Tyler J.K.
      Proc. Natl. Acad. Sci. U.S.A. 105:9000-9005(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "Structure of Vps75 and implications for histone chaperone function."
      Tang Y., Meeth K., Jiang E., Luo C., Marmorstein R.
      Proc. Natl. Acad. Sci. U.S.A. 105:12206-12211(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH VPS75.

    Entry informationi

    Entry nameiRT109_YEAST
    AccessioniPrimary (citable) accession number: Q07794
    Secondary accession number(s): D6VY01
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 12, 2006
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 105 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 1140 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 XII
      Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

    External Data

    Dasty 3