Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P84249

- H33_DROME

UniProt

P84249 - H33_DROME

Protein

Histone H3.3

Gene

His3.3A

more
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes and is specifically enriched in modifications associated with active chromatin. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. 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.1 Publication

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB

    GO - Biological processi

    1. cell adhesion Source: FlyBase
    2. male meiosis Source: FlyBase
    3. nucleosome assembly Source: UniProtKB
    4. regulation of cell shape Source: FlyBase

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_180258. Factors involved in megakaryocyte development and platelet production.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone H3.3
    Alternative name(s):
    H3.3Q
    H3.A/B
    Gene namesi
    Name:His3.3A
    ORF Names:CG5825
    AND
    Name:His3.3B
    ORF Names:CG8989
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2L, UP000000803: Chromosome X

    Organism-specific databases

    FlyBaseiFBgn0014857. His3.3A.
    FBgn0004828. His3.3B.

    Subcellular locationi

    Nucleus By similarity. Chromosome By similarity

    GO - Cellular componenti

    1. nucleosome Source: UniProtKB
    2. nucleus Source: UniProtKB-SubCell
    3. polytene chromosome Source: FlyBase

    Keywords - Cellular componenti

    Chromosome, Nucleosome core, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 136135Histone H3.3PRO_0000221302Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei5 – 51N6,N6,N6-trimethyllysine; alternate1 Publication
    Modified residuei5 – 51N6,N6-dimethyllysine; alternate1 Publication
    Modified residuei5 – 51N6-methyllysine; alternate1 Publication
    Modified residuei10 – 101N6,N6-dimethyllysine; alternate1 Publication
    Modified residuei10 – 101N6-acetyllysine; alternate2 Publications
    Modified residuei10 – 101N6-methyllysine; alternate1 Publication
    Modified residuei11 – 111PhosphoserineBy similarity
    Modified residuei15 – 151N6,N6-dimethyllysine; alternate1 Publication
    Modified residuei15 – 151N6-acetyllysine; alternate3 Publications
    Modified residuei15 – 151N6-methyllysine; alternate1 Publication
    Modified residuei19 – 191N6-acetyllysine1 Publication
    Modified residuei24 – 241N6-acetyllysine1 Publication
    Modified residuei28 – 281N6,N6,N6-trimethyllysine; alternate1 Publication
    Modified residuei28 – 281N6,N6-dimethyllysine; alternate1 Publication
    Modified residuei28 – 281N6-methyllysine; alternate1 Publication
    Modified residuei37 – 371N6,N6-dimethyllysine; alternate1 Publication
    Modified residuei37 – 371N6-methyllysine; alternate1 Publication
    Modified residuei38 – 381N6,N6-dimethyllysine; alternate1 Publication
    Modified residuei38 – 381N6-methyllysine; alternate1 Publication
    Modified residuei80 – 801N6,N6-dimethyllysine; alternate2 Publications
    Modified residuei80 – 801N6-methyllysine; alternate2 Publications

    Post-translational modificationi

    Phosphorylation at Ser-11 by ial/aurora-B during mitosis and meiosis is crucial for chromosome condensation and cell-cycle progression. Phosphorylation at Ser-11 by JIL-1 during interphase is linked to gene activation and restricts the formation of heterochromatin at inappropriate sites. Phosphorylation at Ser-11 is enriched on male X chromosome compared to the autosome.4 Publications
    Acetylation is generally linked to gene activation. Acetylated on Lys-15 during prophase I of meiosis. Phosphorylation of H2A 'Thr-119' is a prerequisite for H3 Lys-15 acetylation. Acetylation on Lys-15 is enriched on male X chromosome compared to the autosome.3 Publications
    Methylation at Lys-5 or Lys-80 is generally associated with active chromatin. Methylation at Lys-80 by gpp occurs at low levels in specific developmental stages and tissues undergoing active cell division, and at highest levels in epidermal cells undergoing differentiation.2 Publications

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    PaxDbiP84249.
    PRIDEiP84249.

    Expressioni

    Gene expression databases

    BgeeiP84249.

    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.

    Protein-protein interaction databases

    BioGridi58303. 8 interactions.
    59912. 17 interactions.
    IntActiP84249. 7 interactions.
    MINTiMINT-840146.

    Structurei

    3D structure databases

    ProteinModelPortaliP84249.
    SMRiP84249. Positions 17-136.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histone H3 family.Curated

    Phylogenomic databases

    eggNOGiCOG2036.
    GeneTreeiENSGT00750000117538.
    InParanoidiP84249.
    KOiK11253.
    OMAiHIVMART.
    OrthoDBiEOG7HB5C2.
    PhylomeDBiP84249.

    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.

    P84249-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARTKQTARK STGGKAPRKQ LATKAARKSA PSTGGVKKPH RYRPGTVALR    50
    EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSAAI GALQEASEAY 100
    LVGLFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA 136
    Length:136
    Mass (Da):15,328
    Last modified:January 23, 2007 - v2
    Checksum:i5158ED279E6F9E1C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53822 mRNA. Translation: CAA37819.1.
    X82257 mRNA. Translation: CAA57712.1.
    X81205 Genomic DNA. Translation: CAA57077.1.
    X81207 Genomic DNA. Translation: CAA57080.1.
    AE014298 Genomic DNA. Translation: AAF46452.1.
    AE014134 Genomic DNA. Translation: AAF52213.1.
    AE014298 Genomic DNA. Translation: AAN09245.1.
    AE014298 Genomic DNA. Translation: AAO41645.1.
    AY071057 mRNA. Translation: AAL48679.1.
    AY118325 mRNA. Translation: AAM48354.1.
    AY119629 mRNA. Translation: AAM50283.1.
    PIRiS61220.
    RefSeqiNP_001259374.1. NM_001272445.1.
    NP_001260082.1. NM_001273153.1.
    NP_511095.1. NM_078540.4.
    NP_523479.1. NM_078755.3.
    NP_723056.2. NM_164624.3.
    NP_727314.1. NM_167180.4.
    NP_788892.1. NM_176719.1.
    UniGeneiDm.2931.
    Dm.35099.
    Dm.7418.

    Genome annotation databases

    EnsemblMetazoaiFBtr0071345; FBpp0071280; FBgn0004828.
    FBtr0071346; FBpp0071281; FBgn0004828.
    FBtr0071347; FBpp0071282; FBgn0004828.
    FBtr0079010; FBpp0078649; FBgn0014857.
    FBtr0333476; FBpp0305663; FBgn0004828.
    FBtr0333536; FBpp0305716; FBgn0014857.
    FBtr0333537; FBpp0305717; FBgn0014857.
    GeneIDi31848.
    33736.
    KEGGidme:Dmel_CG5825.
    dme:Dmel_CG8989.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53822 mRNA. Translation: CAA37819.1 .
    X82257 mRNA. Translation: CAA57712.1 .
    X81205 Genomic DNA. Translation: CAA57077.1 .
    X81207 Genomic DNA. Translation: CAA57080.1 .
    AE014298 Genomic DNA. Translation: AAF46452.1 .
    AE014134 Genomic DNA. Translation: AAF52213.1 .
    AE014298 Genomic DNA. Translation: AAN09245.1 .
    AE014298 Genomic DNA. Translation: AAO41645.1 .
    AY071057 mRNA. Translation: AAL48679.1 .
    AY118325 mRNA. Translation: AAM48354.1 .
    AY119629 mRNA. Translation: AAM50283.1 .
    PIRi S61220.
    RefSeqi NP_001259374.1. NM_001272445.1.
    NP_001260082.1. NM_001273153.1.
    NP_511095.1. NM_078540.4.
    NP_523479.1. NM_078755.3.
    NP_723056.2. NM_164624.3.
    NP_727314.1. NM_167180.4.
    NP_788892.1. NM_176719.1.
    UniGenei Dm.2931.
    Dm.35099.
    Dm.7418.

    3D structure databases

    ProteinModelPortali P84249.
    SMRi P84249. Positions 17-136.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 58303. 8 interactions.
    59912. 17 interactions.
    IntActi P84249. 7 interactions.
    MINTi MINT-840146.

    Proteomic databases

    PaxDbi P84249.
    PRIDEi P84249.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0071345 ; FBpp0071280 ; FBgn0004828 .
    FBtr0071346 ; FBpp0071281 ; FBgn0004828 .
    FBtr0071347 ; FBpp0071282 ; FBgn0004828 .
    FBtr0079010 ; FBpp0078649 ; FBgn0014857 .
    FBtr0333476 ; FBpp0305663 ; FBgn0004828 .
    FBtr0333536 ; FBpp0305716 ; FBgn0014857 .
    FBtr0333537 ; FBpp0305717 ; FBgn0014857 .
    GeneIDi 31848.
    33736.
    KEGGi dme:Dmel_CG5825.
    dme:Dmel_CG8989.

    Organism-specific databases

    CTDi 31848.
    33736.
    FlyBasei FBgn0014857. His3.3A.
    FBgn0004828. His3.3B.

    Phylogenomic databases

    eggNOGi COG2036.
    GeneTreei ENSGT00750000117538.
    InParanoidi P84249.
    KOi K11253.
    OMAi HIVMART.
    OrthoDBi EOG7HB5C2.
    PhylomeDBi P84249.

    Enzyme and pathway databases

    Reactomei REACT_180258. Factors involved in megakaryocyte development and platelet production.

    Miscellaneous databases

    NextBioi 775637.
    PROi P84249.

    Gene expression databases

    Bgeei P84249.

    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. "A Drosophila melanogaster H3.3 cDNA encodes a histone variant identical with the vertebrate H3.3."
      Fretzin S., Allan B.D., van Daal A., Elgin S.C.R.
      Gene 107:341-342(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (HIS3.3B).
    2. "Structure and expression of histone H3.3 genes in Drosophila melanogaster and Drosophila hydei."
      Akhmanova A.S., Bindels P.S.T., Xu J., Miedema K., Kremer H., Hennig W.
      Genome 38:586-600(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (HIS3.3A AND HIS3.3B).
      Strain: Canton-S.
    3. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HIS3.3A AND HIS3.3B).
      Strain: Berkeley.
    4. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (HIS3.3A AND HIS3.3B).
      Strain: Berkeley.
      Tissue: Embryo.
    6. "Phosphorylation of histone H3 correlates with transcriptionally active loci."
      Nowak S.J., Corces V.G.
      Genes Dev. 14:3003-3013(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-11, ACETYLATION AT LYS-10 AND LYS-15.
    7. "The JIL-1 tandem kinase mediates histone H3 phosphorylation and is required for maintenance of chromatin structure in Drosophila."
      Wang Y., Zhang W., Jin Y., Johansen J., Johansen K.M.
      Cell 105:433-443(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-11, ACETYLATION AT LYS-15.
    8. "Drosophila aurora B kinase is required for histone H3 phosphorylation and condensin recruitment during chromosome condensation and to organize the central spindle during cytokinesis."
      Giet R., Glover D.M.
      J. Cell Biol. 152:669-682(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-11.
    9. "Phosphorylation of histone H3 during transcriptional activation depends on promoter structure."
      Labrador M., Corces V.G.
      Genes Dev. 17:43-48(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-11.
    10. "Histone H3.3 is enriched in covalent modifications associated with active chromatin."
      McKittrick E., Gafken P.R., Ahmad K., Henikoff S.
      Proc. Natl. Acad. Sci. U.S.A. 101:1525-1530(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, METHYLATION AT LYS-5; LYS-10; LYS-15; LYS-28; LYS-37; LYS-38 AND LYS-80, ACETYLATION AT LYS-10; LYS-15; LYS-19 AND LYS-24, IDENTIFICATION BY MASS SPECTROMETRY.
    11. "Characterization of the grappa gene, the Drosophila histone H3 lysine 79 methyltransferase."
      Shanower G.A., Mueller M., Blanton J.L., Honti V., Gyurkovics H., Schedl P.
      Genetics 169:173-184(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-80.

    Entry informationi

    Entry nameiH33_DROME
    AccessioniPrimary (citable) accession number: P84249
    Secondary accession number(s): A4V466
    , P06351, P33155, Q9V3W4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 95 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Miscellaneous

    This histone is the predominant form in non-dividing cells.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3