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P61830

- H3_YEAST

UniProt

P61830 - H3_YEAST

Protein

Histone H3

Gene

HHT1

more
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Component of the UAF (upstream activation factor) complex which interacts with the upstream element of the RNA polymerase I promoter and forms a stable preinitiation complex. Together with SPT15/TBP, UAF seems to stimulate basal transcription to a fully activated level.

    GO - Molecular functioni

    1. DNA binding Source: SGD
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. chromatin assembly or disassembly Source: SGD
    2. global genome nucleotide-excision repair Source: SGD
    3. mitotic spindle assembly checkpoint Source: SGD
    4. nucleosome assembly Source: InterPro
    5. rRNA transcription Source: SGD
    6. sexual sporulation resulting in formation of a cellular spore Source: SGD

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-28997-MONOMER.
    YEAST:G3O-33068-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone H3
    Gene namesi
    Name:HHT1
    Ordered Locus Names:YBR010W
    ORF Names:YBR0201
    AND
    Name:HHT2
    Synonyms:SIN2
    Ordered Locus Names:YNL031C
    ORF Names:N2749
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II, UP000002311: Chromosome XIV

    Organism-specific databases

    SGDiS000000214. HHT1.
    S000004976. HHT2.

    Subcellular locationi

    GO - Cellular componenti

    1. CENP-A containing nucleosome Source: SGD
    2. nuclear nucleosome Source: SGD
    3. replication fork protection complex Source: SGD

    Keywords - Cellular componenti

    Chromosome, Nucleosome core, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi11 – 111S → A: Impairs histone H3 phosphorylation and reduces transcription of some GCN5 regulated genes. 2 Publications
    Mutagenesisi53 – 531R → A, K or Q: Lethal. 1 Publication
    Mutagenesisi57 – 571K → A, Q or R: Increases sensitivity to genotoxic agents inducing DNA breaks during replication. 3 Publications
    Mutagenesisi80 – 801K → A, P or Q: Compromises telomeric silencing. 2 Publications
    Mutagenesisi119 – 1191T → A or E: Lethal. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 136135Histone H3PRO_0000221370Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei5 – 51N6,N6,N6-trimethyllysine; alternate11 Publications
    Modified residuei5 – 51N6,N6-dimethyllysine; alternate11 Publications
    Modified residuei5 – 51N6-methyllysine; alternate11 Publications
    Modified residuei10 – 101N6-acetyllysine; alternate5 Publications
    Modified residuei10 – 101N6-methyllysine; alternate1 Publication
    Modified residuei11 – 111Phosphoserine3 Publications
    Modified residuei15 – 151N6,N6-dimethyllysine; alternate1 Publication
    Modified residuei15 – 151N6-acetyllysine; alternate8 Publications
    Modified residuei19 – 191N6-acetyllysine; alternate5 Publications
    Modified residuei19 – 191N6-methyllysine; alternate1 Publication
    Modified residuei24 – 241N6-acetyllysine; alternate3 Publications
    Modified residuei24 – 241N6-methyllysine; alternate1 Publication
    Modified residuei28 – 281N6,N6,N6-trimethyllysine; alternate1 Publication
    Modified residuei28 – 281N6,N6-dimethyllysine; alternate1 Publication
    Modified residuei28 – 281N6-acetyllysine; alternate3 Publications
    Modified residuei28 – 281N6-methyllysine; alternate1 Publication
    Modified residuei37 – 371N6,N6,N6-trimethyllysine; alternate7 Publications
    Modified residuei37 – 371N6,N6-dimethyllysine; alternate7 Publications
    Modified residuei37 – 371N6-acetyllysine; alternate3 Publications
    Modified residuei37 – 371N6-methyllysine; alternate7 Publications
    Modified residuei57 – 571N6-acetyllysine6 Publications
    Modified residuei65 – 651N6-acetyllysine2 Publications
    Modified residuei80 – 801N6,N6,N6-trimethyllysine; alternate6 Publications
    Modified residuei80 – 801N6,N6-dimethyllysine; alternate6 Publications
    Modified residuei80 – 801N6-methyllysine; alternate6 Publications

    Post-translational modificationi

    Phosphorylated by IPL1 to form H3S10ph in a cell cycle-dependent manner during mitosis and meiosis. H3S10ph is also formed by SNF1, promotes subsequent H3K14ac formation by GCN5, and is required for transcriptional activation through TBP recruitment to the promoters. Dephosphorylation is performed by GLC7.3 Publications
    Mono-, di- and trimethylated by the COMPASS complex to form H3K4me1/2/3. H3K4me activates gene expression by regulating transcription elongation and plays a role in telomere length maintenance. H3K4me enrichment correlates with transcription levels, and occurs in a 5' to 3' gradient with H3K4me3 enrichment at the 5'-end of genes, shifting to H3K4me2 and then H3K4me1. Methylated by SET2 to form H3K36me. H3K36me represses gene expression. Methylated by DOT1 to form H3K79me. H3K79me is required for association of SIR proteins with telomeric regions and for telomeric silencing. The COMPASS-mediated formation of H3K4me2/3 and the DOT1-mediated formation of H3K79me require H2BK123ub1.20 Publications
    Acetylation of histone H3 leads to transcriptional activation. H3K14ac formation by GCN5, a component of the SAGA complex, is promoted by H3S10ph. Further acetylated by GCN5 to form H3K9ac, H3K18ac, H3K23ac, H3K27ac and H3K36ac. H3K14ac can also be formed by ESA1, a component of the NuA4 histone acetyltransferase (HAT) complex. H3K56ac formation occurs predominantly in newly synthesized H3 molecules during G1, S and G2/M of the cell cycle and may be involved in DNA repair.13 Publications

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP61830.
    PaxDbiP61830.

    Expressioni

    Gene expression databases

    GenevestigatoriP61830.

    Interactioni

    Subunit structurei

    The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. Histone H3 is a component of the UAF (upstream activation factor) complex, which consists of UAF30, RRN5, RRN9, RRN10, and histones H3 and H4.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ASF1P324474EBI-8098,EBI-3003
    BDF1P358172EBI-8098,EBI-3493
    FPR4Q062055EBI-8098,EBI-6956
    HHF2P023097EBI-8098,EBI-8113
    HOS2P530962EBI-8098,EBI-8475
    SET3P361242EBI-8098,EBI-16993
    STH1P325974EBI-8098,EBI-18410
    YNG1Q084655EBI-8098,EBI-31890

    Protein-protein interaction databases

    BioGridi32711. 720 interactions.
    35796. 651 interactions.
    DIPiDIP-417N.
    IntActiP61830. 144 interactions.
    MINTiMINT-702778.

    Structurei

    Secondary structure

    1
    136
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 83
    Beta strandi11 – 133
    Helixi46 – 5510
    Helixi66 – 7712
    Helixi87 – 11428
    Beta strandi118 – 1203
    Helixi124 – 1318

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ID3X-ray3.10A/E2-136[»]
    1M1DX-ray2.20B/D2-21[»]
    1PU9X-ray2.30B6-24[»]
    1PUAX-ray2.30B6-24[»]
    1QSNX-ray2.20B10-20[»]
    2CNXX-ray2.10P2-6[»]
    2H2GX-ray1.63B114-124[»]
    2IDCX-ray2.20A119-135[»]
    2JMJNMR-P2-10[»]
    2RNWNMR-B2-16[»]
    2RNXNMR-B32-43[»]
    2RSNNMR-B2-18[»]
    3MP1X-ray2.60P2-6[»]
    3MP6X-ray1.48P2-5[»]
    3Q33X-ray2.80D2-15[»]
    4JJNX-ray3.09A/E2-136[»]
    4KUDX-ray3.20A/E1-136[»]
    ProteinModelPortaliP61830.
    SMRiP61830. Positions 2-136.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP61830.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histone H3 family.Curated

    Phylogenomic databases

    eggNOGiCOG2036.
    GeneTreeiENSGT00750000117538.
    KOiK11253.
    OMAiQKEMART.
    OrthoDBiEOG7T4MZ6.

    Family and domain databases

    Gene3Di1.10.20.10. 1 hit.
    InterProiIPR009072. Histone-fold.
    IPR007125. Histone_core_D.
    IPR000164. Histone_H3.
    [Graphical view]
    PANTHERiPTHR11426. PTHR11426. 1 hit.
    PfamiPF00125. Histone. 1 hit.
    [Graphical view]
    PRINTSiPR00622. HISTONEH3.
    SMARTiSM00428. H3. 1 hit.
    [Graphical view]
    SUPFAMiSSF47113. SSF47113. 1 hit.
    PROSITEiPS00322. HISTONE_H3_1. 1 hit.
    PS00959. HISTONE_H3_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P61830-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARTKQTARK STGGKAPRKQ LASKAARKSA PSTGGVKKPH RYKPGTVALR    50
    EIRRFQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSAI GALQESVEAY 100
    LVSLFEDTNL AAIHAKRVTI QKKDIKLARR LRGERS 136
    Length:136
    Mass (Da):15,356
    Last modified:January 23, 2007 - v2
    Checksum:iA6115FEB480AC67A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti124 – 1241D → E AA sequence (PubMed:7035169)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X00724 Genomic DNA. Translation: CAA25310.1.
    X00725 Genomic DNA. Translation: CAA25312.1.
    Z35879 Genomic DNA. Translation: CAA84948.1.
    Z71306 Genomic DNA. Translation: CAA95893.1.
    Z71307 Genomic DNA. Translation: CAA95894.1.
    AY558343 Genomic DNA. Translation: AAS56669.1.
    AY692987 Genomic DNA. Translation: AAT93006.1.
    AY554000 Genomic DNA. Translation: AAS64341.1.
    AY554001 Genomic DNA. Translation: AAS64342.1.
    AY554002 Genomic DNA. Translation: AAS64343.1.
    AY554003 Genomic DNA. Translation: AAS64344.1.
    AY554004 Genomic DNA. Translation: AAS64345.1.
    AY554005 Genomic DNA. Translation: AAS64346.1.
    AY554006 Genomic DNA. Translation: AAS64347.1.
    AY554007 Genomic DNA. Translation: AAS64348.1.
    AY554008 Genomic DNA. Translation: AAS64349.1.
    BK006936 Genomic DNA. Translation: DAA07131.1.
    BK006947 Genomic DNA. Translation: DAA10514.1.
    PIRiS45265. HSBY3.
    RefSeqiNP_009564.1. NM_001178358.1.
    NP_014367.1. NM_001182870.1.

    Genome annotation databases

    EnsemblFungiiYBR010W; YBR010W; YBR010W.
    YNL031C; YNL031C; YNL031C.
    GeneIDi852295.
    855700.
    KEGGisce:YBR010W.
    sce:YNL031C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X00724 Genomic DNA. Translation: CAA25310.1 .
    X00725 Genomic DNA. Translation: CAA25312.1 .
    Z35879 Genomic DNA. Translation: CAA84948.1 .
    Z71306 Genomic DNA. Translation: CAA95893.1 .
    Z71307 Genomic DNA. Translation: CAA95894.1 .
    AY558343 Genomic DNA. Translation: AAS56669.1 .
    AY692987 Genomic DNA. Translation: AAT93006.1 .
    AY554000 Genomic DNA. Translation: AAS64341.1 .
    AY554001 Genomic DNA. Translation: AAS64342.1 .
    AY554002 Genomic DNA. Translation: AAS64343.1 .
    AY554003 Genomic DNA. Translation: AAS64344.1 .
    AY554004 Genomic DNA. Translation: AAS64345.1 .
    AY554005 Genomic DNA. Translation: AAS64346.1 .
    AY554006 Genomic DNA. Translation: AAS64347.1 .
    AY554007 Genomic DNA. Translation: AAS64348.1 .
    AY554008 Genomic DNA. Translation: AAS64349.1 .
    BK006936 Genomic DNA. Translation: DAA07131.1 .
    BK006947 Genomic DNA. Translation: DAA10514.1 .
    PIRi S45265. HSBY3.
    RefSeqi NP_009564.1. NM_001178358.1.
    NP_014367.1. NM_001182870.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ID3 X-ray 3.10 A/E 2-136 [» ]
    1M1D X-ray 2.20 B/D 2-21 [» ]
    1PU9 X-ray 2.30 B 6-24 [» ]
    1PUA X-ray 2.30 B 6-24 [» ]
    1QSN X-ray 2.20 B 10-20 [» ]
    2CNX X-ray 2.10 P 2-6 [» ]
    2H2G X-ray 1.63 B 114-124 [» ]
    2IDC X-ray 2.20 A 119-135 [» ]
    2JMJ NMR - P 2-10 [» ]
    2RNW NMR - B 2-16 [» ]
    2RNX NMR - B 32-43 [» ]
    2RSN NMR - B 2-18 [» ]
    3MP1 X-ray 2.60 P 2-6 [» ]
    3MP6 X-ray 1.48 P 2-5 [» ]
    3Q33 X-ray 2.80 D 2-15 [» ]
    4JJN X-ray 3.09 A/E 2-136 [» ]
    4KUD X-ray 3.20 A/E 1-136 [» ]
    ProteinModelPortali P61830.
    SMRi P61830. Positions 2-136.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32711. 720 interactions.
    35796. 651 interactions.
    DIPi DIP-417N.
    IntActi P61830. 144 interactions.
    MINTi MINT-702778.

    Proteomic databases

    MaxQBi P61830.
    PaxDbi P61830.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBR010W ; YBR010W ; YBR010W .
    YNL031C ; YNL031C ; YNL031C .
    GeneIDi 852295.
    855700.
    KEGGi sce:YBR010W.
    sce:YNL031C.

    Organism-specific databases

    SGDi S000000214. HHT1.
    S000004976. HHT2.

    Phylogenomic databases

    eggNOGi COG2036.
    GeneTreei ENSGT00750000117538.
    KOi K11253.
    OMAi QKEMART.
    OrthoDBi EOG7T4MZ6.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-28997-MONOMER.
    YEAST:G3O-33068-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P61830.
    NextBioi 970949.

    Gene expression databases

    Genevestigatori P61830.

    Family and domain databases

    Gene3Di 1.10.20.10. 1 hit.
    InterProi IPR009072. Histone-fold.
    IPR007125. Histone_core_D.
    IPR000164. Histone_H3.
    [Graphical view ]
    PANTHERi PTHR11426. PTHR11426. 1 hit.
    Pfami PF00125. Histone. 1 hit.
    [Graphical view ]
    PRINTSi PR00622. HISTONEH3.
    SMARTi SM00428. H3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47113. SSF47113. 1 hit.
    PROSITEi PS00322. HISTONE_H3_1. 1 hit.
    PS00959. HISTONE_H3_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "DNA sequences of yeast H3 and H4 histone genes from two non-allelic gene sets encode identical H3 and H4 proteins."
      Smith M.M., Andresson O.S.
      J. Mol. Biol. 169:663-690(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Complete DNA sequence of yeast chromosome II."
      Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
      , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
      EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HHT1).
      Strain: ATCC 204508 / S288c.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
      Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
      , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
      Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HHT2).
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION (HHT1 AND HHT2).
      Strain: ATCC 204508 / S288c.
    5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HHT1 AND HHT2).
      Strain: ATCC 204508 / S288c.
    6. "The primary structure of yeast histone H3."
      Brandt W.F., von Holt C.
      Eur. J. Biochem. 121:501-510(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-136.
    7. "Population genetic variation in gene expression is associated with phenotypic variation in Saccharomyces cerevisiae."
      Fay J.C., McCullough H.L., Sniegowski P.D., Eisen M.B.
      Genome Biol. 5:R26.1-R26.14(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-134.
      Strain: ATCC 204508 / S288c, M13, M14, M22, M32, M34, M5, M8 and YPS163.
    8. "The occurrence of histone H3 and H4 in yeast."
      Brandt W.F., von Holt C.
      FEBS Lett. 65:386-390(1976) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-16.
    9. "Identification of histone H3 lysine 36 acetylation as a highly conserved histone modification."
      Morris S.A., Rao B., Garcia B.A., Hake S.B., Diaz R.L., Shabanowitz J., Hunt D.F., Allis C.D., Lieb J.D., Strahl B.D.
      J. Biol. Chem. 282:7632-7640(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 28-41, ACETYLATION AT LYS-37.
    10. "Insights into the role of histone H3 and histone H4 core modifiable residues in Saccharomyces cerevisiae."
      Hyland E.M., Cosgrove M.S., Molina H., Wang D., Pandey A., Cottee R.J., Boeke J.D.
      Mol. Cell. Biol. 25:10060-10070(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 55-64, ACETYLATION AT LYS-57, MUTAGENESIS OF ARG-53; LYS-57; LYS-80 AND THR-119.
    11. "Histones H3 and H4 are components of upstream activation factor required for the high-level transcription of yeast rDNA by RNA polymerase I."
      Keener J., Dodd J.A., Lalo D., Nomura M.
      Proc. Natl. Acad. Sci. U.S.A. 94:13458-13462(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE UAF COMPLEX.
    12. "Essential and redundant functions of histone acetylation revealed by mutation of target lysines and loss of the Gcn5p acetyltransferase."
      Zhang W., Bone J.R., Edmondson D.G., Turner B.M., Roth S.Y.
      EMBO J. 17:3155-3167(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-10; LYS-15 AND LYS-19.
    13. "Esa1p is an essential histone acetyltransferase required for cell cycle progression."
      Clarke A.S., Lowell J.E., Jacobson S.J., Pillus L.
      Mol. Cell. Biol. 19:2515-2526(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-15.
    14. "Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes."
      Hsu J.-Y., Sun Z.-W., Li X., Reuben M., Tatchell K., Bishop D.K., Grushcow J.M., Brame C.J., Caldwell J.A., Hunt D.F., Lin R., Smith M.M., Allis C.D.
      Cell 102:279-291(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-11 BY IPL1, DEPHOSPHORYLATION BY GLC7, MUTAGENESIS OF SER-11.
    15. "Steady-state levels of histone acetylation in Saccharomyces cerevisiae."
      Waterborg J.H.
      J. Biol. Chem. 275:13007-13011(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION.
    16. "Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine 14."
      Lo W.-S., Trievel R.C., Rojas J.R., Duggan L., Hsu J.-Y., Allis C.D., Marmorstein R., Berger S.L.
      Mol. Cell 5:917-926(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-11, ACETYLATION AT LYS-15, MUTAGENESIS OF SER-11.
    17. "The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4."
      Roguev A., Schaft D., Shevchenko A., Pijnappel W.W.M.P., Wilm M., Aasland R., Stewart A.F.
      EMBO J. 20:7137-7148(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-5.
    18. "Histone H3 lysine 4 methylation is mediated by Set1 and required for cell growth and rDNA silencing in Saccharomyces cerevisiae."
      Briggs S.D., Bryk M., Strahl B.D., Cheung W.L., Davie J.K., Dent S.Y.R., Winston F., Allis C.D.
      Genes Dev. 15:3286-3295(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-5.
    19. "Highly specific antibodies determine histone acetylation site usage in yeast heterochromatin and euchromatin."
      Suka N., Suka Y., Carmen A.A., Wu J., Grunstein M.
      Mol. Cell 8:473-479(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-10; LYS-15; LYS-19; LYS-24 AND LYS-28.
    20. "Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association."
      Ng H.H., Feng Q., Wang H., Erdjument-Bromage H., Tempst P., Zhang Y., Struhl K.
      Genes Dev. 16:1518-1527(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-80, MUTAGENESIS OF LYS-80.
    21. "Disruptor of telomeric silencing-1 is a chromatin-specific histone H3 methyltransferase."
      Lacoste N., Utley R.T., Hunter J.M., Poirier G.G., Cote J.
      J. Biol. Chem. 277:30421-30424(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-80.
    22. "Set2 is a nucleosomal histone H3-selective methyltransferase that mediates transcriptional repression."
      Strahl B.D., Grant P.A., Briggs S.D., Sun Z.-W., Bone J.R., Caldwell J.A., Mollah S., Cook R.G., Shabanowitz J., Hunt D.F., Allis C.D.
      Mol. Cell. Biol. 22:1298-1306(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-37.
    23. Cited for: METHYLATION AT LYS-5; LYS-37 AND LYS-80.
    24. Cited for: METHYLATION AT LYS-5.
    25. "A trithorax-group complex purified from Saccharomyces cerevisiae is required for methylation of histone H3."
      Nagy P.L., Griesenbeck J., Kornberg R.D., Cleary M.L.
      Proc. Natl. Acad. Sci. U.S.A. 99:90-94(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-5.
    26. "Phosphorylation of RNA polymerase II CTD regulates H3 methylation in yeast."
      Xiao T., Hall H., Kizer K.O., Shibata Y., Hall M.C., Borchers C.H., Strahl B.D.
      Genes Dev. 17:654-663(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-37.
    27. "Methylation of histone H3 by Set2 in Saccharomyces cerevisiae is linked to transcriptional elongation by RNA polymerase II."
      Krogan N.J., Kim M., Tong A., Golshani A., Cagney G., Canadien V., Richards D.P., Beattie B.K., Emili A., Boone C., Shilatifard A., Buratowski S., Greenblatt J.
      Mol. Cell. Biol. 23:4207-4218(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-37.
    28. "Set2-catalyzed methylation of histone H3 represses basal expression of GAL4 in Saccharomyces cerevisiae."
      Landry J., Sutton A., Hesman T., Min J., Xu R.-M., Johnston M., Sternglanz R.
      Mol. Cell. Biol. 23:5972-5978(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-37.
    29. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    30. "Lysine-79 of histone H3 is hypomethylated at silenced loci in yeast and mammalian cells: a potential mechanism for position-effect variegation."
      Ng H.H., Ciccone D.N., Morshead K.B., Oettinger M.A., Struhl K.
      Proc. Natl. Acad. Sci. U.S.A. 100:1820-1825(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-80.
    31. "Saccharomyces cerevisiae Set1p is a methyltransferase specific for lysine 4 of histone H3 and is required for efficient gene expression."
      Boa S., Coert C., Patterton H.-G.
      Yeast 20:827-835(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-5, IDENTIFICATION BY MASS SPECTROMETRY.
    32. "Histone H3 phosphorylation can promote TBP recruitment through distinct promoter-specific mechanisms."
      Lo W.-S., Gamache E.R., Henry K.W., Yang D., Pillus L., Berger S.L.
      EMBO J. 24:997-1008(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-11, ACETYLATION AT LYS-15.
    33. "The DNA damage checkpoint response requires histone H2B ubiquitination by Rad6-Bre1 and H3 methylation by Dot1."
      Giannattasio M., Lazzaro F., Plevani P., Muzi-Falconi M.
      J. Biol. Chem. 280:9879-9886(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-80.
    34. "Characterization of lysine 56 of histone H3 as an acetylation site in Saccharomyces cerevisiae."
      Ozdemir A., Spicuglia S., Lasonder E., Vermeulen M., Campsteijn C., Stunnenberg H.G., Logie C.
      J. Biol. Chem. 280:25949-25952(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-57, MUTAGENESIS OF LYS-57.
    35. "Histone H3 lysine 4 mono-methylation does not require ubiquitination of histone H2B."
      Dehe P.-M., Pamblanco M., Luciano P., Lebrun R., Moinier D., Sendra R., Verreault A., Tordera V., Geli V.
      J. Mol. Biol. 353:477-484(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-5.
    36. "Dynamic lysine methylation on histone H3 defines the regulatory phase of gene transcription."
      Morillon A., Karabetsou N., Nair A., Mellor J.
      Mol. Cell 18:723-734(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-5.
    37. "Molecular regulation of histone H3 trimethylation by COMPASS and the regulation of gene expression."
      Schneider J., Wood A., Lee J.-S., Schuster R., Dueker J., Maguire C., Swanson S.K., Florens L., Washburn M.P., Shilatifard A.
      Mol. Cell 19:849-856(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-5.
    38. "A novel domain in Set2 mediates RNA polymerase II interaction and couples histone H3 K36 methylation with transcript elongation."
      Kizer K.O., Phatnani H.P., Shibata Y., Hall H., Greenleaf A.L., Strahl B.D.
      Mol. Cell. Biol. 25:3305-3316(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-37.
    39. "A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response."
      Masumoto H., Hawke D., Kobayashi R., Verreault A.
      Nature 436:294-298(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-57, MUTAGENESIS OF LYS-57, IDENTIFICATION BY MASS SPECTROMETRY.
    40. "Single-nucleosome mapping of histone modifications in S. cerevisiae."
      Liu C.L., Kaplan T., Kim M., Buratowski S., Schreiber S.L., Friedman N., Rando O.J.
      PLoS Biol. 3:1-17(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-5, ACETYLATION AT LYS-10; LYS-15 AND LYS-19.
    41. "Organismal differences in post-translational modifications in histones H3 and H4."
      Garcia B.A., Hake S.B., Diaz R.L., Kauer M., Morris S.A., Recht J., Shabanowitz J., Mishra N., Strahl B.D., Allis C.D., Hunt D.F.
      J. Biol. Chem. 282:7641-7655(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-10; LYS-15; LYS-19; LYS-24; LYS-28; LYS-37; LYS-57 AND LYS-65, METHYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24; LYS-28; LYS-37 AND LYS-80, IDENTIFICATION BY MASS SPECTROMETRY.
    42. "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: ACETYLATION AT LYS-57, IDENTIFICATION BY MASS SPECTROMETRY.
    43. "Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions."
      White C.L., Suto R.K., Luger K.
      EMBO J. 20:5207-5218(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF H3 IN NUCLEOSOME COMPLEX.

    Entry informationi

    Entry nameiH3_YEAST
    AccessioniPrimary (citable) accession number: P61830
    Secondary accession number(s): D6VQ11
    , E9PAG1, P02303, P13996, Q6B1U3, Q6Q7G9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 121 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 213000 molecules/cell in log phase SD medium.1 Publication

    Caution

    To ensure consistency between histone entries, we follow the 'Brno' nomenclature for histone modifications, with positions referring to those used in the literature for the 'closest' model organism. Due to slight variations in histone sequences between organisms and to the presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the actual positions of modified amino acids in the sequence generally differ. In this entry the following conventions are used: H3K4me1/2/3 = mono-, di- and trimethylated Lys-5; H3K9ac = acetylated Lys-10; H3K9me1 = monomethylated Lys-10; H3S10ph = phosphorylated Ser-11; H3K14ac = acetylated Lys-15; H3K14me2 = dimethylated Lys-15; H3K18ac = acetylated Lys-19; H3K18me1 = monomethylated Lys-19; H3K23ac = acetylated Lys-24; H3K23me1 = monomethylated Lys-24; H3K27ac = acetylated Lys-28; H3K27me1/2/3 = mono-, di- and trimethylated Lys-28; H3K36ac = acetylated Lys-37; H3K36me1/2/3 = mono-, di- and trimethylated Lys-37; H3K56ac = acetylated Lys-57; H3K64ac = acetylated Lys-65; H3K79me1/2/3 = mono-, di- and trimethylated Lys-80.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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 XIV
      Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names
    5. Yeast chromosome II
      Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

    External Data

    Dasty 3