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)

P02299

- H3_DROME

UniProt

P02299 - H3_DROME

Protein

Histone H3

Gene

His3

more
Organism
Drosophila melanogaster (Fruit fly)
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.

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. nucleosome assembly Source: InterPro

    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
    Gene namesi
    Name:His3
    AND
    Name:His3:CG31613
    ORF Names:CG31613
    AND
    Name:His3:CG33803
    ORF Names:CG33803
    AND
    Name:His3:CG33806
    ORF Names:CG33806
    AND
    Name:His3:CG33809
    ORF Names:CG33809
    AND
    Name:His3:CG33812
    ORF Names:CG33812
    AND
    Name:His3:CG33815
    ORF Names:CG33815
    AND
    Name:His3:CG33818
    ORF Names:CG33818
    AND
    Name:His3:CG33821
    ORF Names:CG33821
    AND
    Name:His3:CG33824
    ORF Names:CG33824
    AND
    Name:His3:CG33827
    ORF Names:CG33827
    AND
    Name:His3:CG33830
    ORF Names:CG33830
    AND
    Name:His3:CG33833
    ORF Names:CG33833
    AND
    Name:His3:CG33836
    ORF Names:CG33836
    AND
    Name:His3:CG33839
    ORF Names:CG33839
    AND
    Name:His3:CG33842
    ORF Names:CG33842
    AND
    Name:His3:CG33845
    ORF Names:CG33845
    AND
    Name:His3:CG33848
    ORF Names:CG33848
    AND
    Name:His3:CG33851
    ORF Names:CG33851
    AND
    Name:His3:CG33854
    ORF Names:CG33854
    AND
    Name:His3:CG33857
    ORF Names:CG33857
    AND
    Name:His3:CG33860
    ORF Names:CG33860
    AND
    Name:His3:CG33863
    ORF Names:CG33863
    AND
    Name:His3:CG33866
    ORF Names:CG33866
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2L

    Organism-specific databases

    FlyBaseiFBgn0001199. His3.
    FBgn0051613. His3:CG31613.
    FBgn0053803. His3:CG33803.
    FBgn0053806. His3:CG33806.
    FBgn0053809. His3:CG33809.
    FBgn0053812. His3:CG33812.
    FBgn0053815. His3:CG33815.
    FBgn0053818. His3:CG33818.
    FBgn0053821. His3:CG33821.
    FBgn0053824. His3:CG33824.
    FBgn0053827. His3:CG33827.
    FBgn0053830. His3:CG33830.
    FBgn0053833. His3:CG33833.
    FBgn0053836. His3:CG33836.
    FBgn0053839. His3:CG33839.
    FBgn0053842. His3:CG33842.
    FBgn0053845. His3:CG33845.
    FBgn0053848. His3:CG33848.
    FBgn0053851. His3:CG33851.
    FBgn0053854. His3:CG33854.
    FBgn0053857. His3:CG33857.
    FBgn0053860. His3:CG33860.
    FBgn0053863. His3:CG33863.
    FBgn0053866. His3:CG33866.

    Subcellular locationi

    Nucleus By similarity. Chromosome By similarity

    GO - Cellular componenti

    1. nucleosome Source: UniProtKB-KW
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chromosome, Nucleosome core, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 136135Histone H3PRO_0000221300Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei5 – 51N6,N6,N6-trimethyllysine; alternate2 Publications
    Modified residuei5 – 51N6,N6-dimethyllysine; alternate2 Publications
    Modified residuei5 – 51N6-methyllysine; alternate2 Publications
    Modified residuei10 – 101N6,N6-dimethyllysine; alternate1 Publication
    Modified residuei10 – 101N6-acetyllysine; alternate3 Publications
    Modified residuei10 – 101N6-methyllysine; alternate1 Publication
    Modified residuei11 – 111Phosphoserine5 Publications
    Modified residuei15 – 151N6,N6-dimethyllysine; alternate1 Publication
    Modified residuei15 – 151N6-acetyllysine; alternate4 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; alternate3 Publications
    Modified residuei80 – 801N6-methyllysine; alternate3 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.5 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.5 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.3 Publications

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    PaxDbiP02299.
    PRIDEiP02299.

    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.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    KAT2BQ928312EBI-522090,EBI-477430From a different organism.
    ScmQ9VHA04EBI-522090,EBI-89256

    Protein-protein interaction databases

    BioGridi77140. 10 interactions.
    DIPiDIP-38722N.
    IntActiP02299. 15 interactions.
    MINTiMINT-271349.
    STRINGi7227.FBpp0091051.

    Structurei

    Secondary structure

    1
    136
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi46 – 5712
    Helixi65 – 7713
    Beta strandi80 – 823
    Helixi87 – 11428
    Beta strandi118 – 1203
    Helixi122 – 13110

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KNAX-ray2.10P2-17[»]
    1KNEX-ray2.40P2-17[»]
    2NQBX-ray2.30A/E2-136[»]
    2PYOX-ray2.43A/E2-136[»]
    2YBAX-ray2.55C/D2-20[»]
    4INMX-ray3.50A/E/K/O41-136[»]
    ProteinModelPortaliP02299.
    SMRiP02299. Positions 17-136.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02299.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni6 – 116Su(var)205 chromodomain-binding

    Sequence similaritiesi

    Belongs to the histone H3 family.Curated

    Phylogenomic databases

    eggNOGiCOG2036.
    GeneTreeiENSGT00750000117468.
    InParanoidiP02299.
    KOiK11253.
    OMAiRISKMAR.
    OrthoDBiEOG7HB5C2.
    PhylomeDBiP02299.

    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.

    P02299-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR    50
    EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEASEAY 100
    LVGLFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA 136
    Length:136
    Mass (Da):15,388
    Last modified:January 23, 2007 - v4
    Checksum:i6FD8508EA50A0EEC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti118 – 1181V → I(PubMed:2536150)Curated
    Sequence conflicti118 – 1181V → I1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14215 Genomic DNA. Translation: CAA32434.1.
    AB019400 Genomic DNA. Translation: BAA93621.1.
    AE014134 Genomic DNA. Translation: AAN11127.1.
    AE014134 Genomic DNA. Translation: AAZ66481.1.
    AE014134 Genomic DNA. Translation: AAZ66485.1.
    AE014134 Genomic DNA. Translation: AAZ66490.1.
    AE014134 Genomic DNA. Translation: AAZ66494.1.
    AE014134 Genomic DNA. Translation: AAZ66499.1.
    AE014134 Genomic DNA. Translation: AAZ66504.1.
    AE014134 Genomic DNA. Translation: AAZ66509.1.
    AE014134 Genomic DNA. Translation: AAZ66514.1.
    AE014134 Genomic DNA. Translation: AAZ66519.1.
    AE014134 Genomic DNA. Translation: AAZ66524.1.
    AE014134 Genomic DNA. Translation: AAZ66529.1.
    AE014134 Genomic DNA. Translation: AAZ66534.1.
    AE014134 Genomic DNA. Translation: AAZ66539.1.
    AE014134 Genomic DNA. Translation: AAZ66544.1.
    AE014134 Genomic DNA. Translation: AAZ66549.1.
    AE014134 Genomic DNA. Translation: AAZ66554.1.
    AE014134 Genomic DNA. Translation: AAZ66559.1.
    AE014134 Genomic DNA. Translation: AAZ66564.1.
    AE014134 Genomic DNA. Translation: AAZ66569.1.
    AE014134 Genomic DNA. Translation: AAZ66574.1.
    AE014134 Genomic DNA. Translation: AAZ66579.1.
    AE014134 Genomic DNA. Translation: AAZ66583.1.
    PIRiA02630.
    S10097.
    RefSeqiNP_001027285.1. NM_001032114.1.
    NP_001027289.1. NM_001032118.1.
    NP_001027294.1. NM_001032123.1.
    NP_001027298.1. NM_001032127.1.
    NP_001027303.1. NM_001032132.1.
    NP_001027308.1. NM_001032137.1.
    NP_001027313.1. NM_001032142.1.
    NP_001027318.1. NM_001032147.1.
    NP_001027323.1. NM_001032152.1.
    NP_001027328.1. NM_001032157.1.
    NP_001027333.1. NM_001032162.1.
    NP_001027338.1. NM_001032167.1.
    NP_001027343.1. NM_001032172.1.
    NP_001027348.1. NM_001032177.1.
    NP_001027353.1. NM_001032182.1.
    NP_001027358.1. NM_001032187.1.
    NP_001027363.1. NM_001032192.1.
    NP_001027368.1. NM_001032197.1.
    NP_001027373.1. NM_001032202.1.
    NP_001027378.1. NM_001032207.1.
    NP_001027383.1. NM_001032212.1.
    NP_001027387.1. NM_001032216.1.
    NP_724345.1. NM_165384.2.
    UniGeneiDm.29515.
    Dm.34559.
    Dm.34566.
    Dm.34567.

    Genome annotation databases

    EnsemblMetazoaiFBtr0085894; FBpp0085250; FBgn0051613.
    FBtr0091807; FBpp0091051; FBgn0053803.
    FBtr0091810; FBpp0091053; FBgn0053806.
    FBtr0091813; FBpp0091056; FBgn0053809.
    FBtr0091816; FBpp0091058; FBgn0053812.
    FBtr0091819; FBpp0091061; FBgn0053815.
    FBtr0091822; FBpp0091064; FBgn0053818.
    FBtr0091825; FBpp0091067; FBgn0053821.
    FBtr0091828; FBpp0091070; FBgn0053824.
    FBtr0091831; FBpp0091073; FBgn0053827.
    FBtr0091834; FBpp0091076; FBgn0053830.
    FBtr0091837; FBpp0091079; FBgn0053833.
    FBtr0091840; FBpp0091082; FBgn0053836.
    FBtr0091843; FBpp0091085; FBgn0053839.
    FBtr0091846; FBpp0091088; FBgn0053842.
    FBtr0091849; FBpp0091091; FBgn0053845.
    FBtr0091852; FBpp0091094; FBgn0053848.
    FBtr0091855; FBpp0091097; FBgn0053851.
    FBtr0091858; FBpp0091100; FBgn0053854.
    FBtr0091861; FBpp0091103; FBgn0053857.
    FBtr0091864; FBpp0091106; FBgn0053860.
    FBtr0091867; FBpp0091109; FBgn0053863.
    FBtr0091870; FBpp0091112; FBgn0053866.
    GeneIDi318847.
    3771723.
    3771729.
    3771771.
    3771792.
    3771959.
    3772032.
    3772149.
    3772163.
    3772173.
    3772189.
    3772191.
    3772198.
    3772231.
    3772370.
    3772374.
    3772421.
    3772489.
    3772517.
    3772518.
    3772552.
    3772607.
    3772619.
    KEGGidme:Dmel_CG31613.
    dme:Dmel_CG33803.
    dme:Dmel_CG33806.
    dme:Dmel_CG33809.
    dme:Dmel_CG33812.
    dme:Dmel_CG33815.
    dme:Dmel_CG33818.
    dme:Dmel_CG33821.
    dme:Dmel_CG33824.
    dme:Dmel_CG33827.
    dme:Dmel_CG33830.
    dme:Dmel_CG33833.
    dme:Dmel_CG33836.
    dme:Dmel_CG33839.
    dme:Dmel_CG33842.
    dme:Dmel_CG33845.
    dme:Dmel_CG33848.
    dme:Dmel_CG33851.
    dme:Dmel_CG33854.
    dme:Dmel_CG33857.
    dme:Dmel_CG33860.
    dme:Dmel_CG33863.
    dme:Dmel_CG33866.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14215 Genomic DNA. Translation: CAA32434.1 .
    AB019400 Genomic DNA. Translation: BAA93621.1 .
    AE014134 Genomic DNA. Translation: AAN11127.1 .
    AE014134 Genomic DNA. Translation: AAZ66481.1 .
    AE014134 Genomic DNA. Translation: AAZ66485.1 .
    AE014134 Genomic DNA. Translation: AAZ66490.1 .
    AE014134 Genomic DNA. Translation: AAZ66494.1 .
    AE014134 Genomic DNA. Translation: AAZ66499.1 .
    AE014134 Genomic DNA. Translation: AAZ66504.1 .
    AE014134 Genomic DNA. Translation: AAZ66509.1 .
    AE014134 Genomic DNA. Translation: AAZ66514.1 .
    AE014134 Genomic DNA. Translation: AAZ66519.1 .
    AE014134 Genomic DNA. Translation: AAZ66524.1 .
    AE014134 Genomic DNA. Translation: AAZ66529.1 .
    AE014134 Genomic DNA. Translation: AAZ66534.1 .
    AE014134 Genomic DNA. Translation: AAZ66539.1 .
    AE014134 Genomic DNA. Translation: AAZ66544.1 .
    AE014134 Genomic DNA. Translation: AAZ66549.1 .
    AE014134 Genomic DNA. Translation: AAZ66554.1 .
    AE014134 Genomic DNA. Translation: AAZ66559.1 .
    AE014134 Genomic DNA. Translation: AAZ66564.1 .
    AE014134 Genomic DNA. Translation: AAZ66569.1 .
    AE014134 Genomic DNA. Translation: AAZ66574.1 .
    AE014134 Genomic DNA. Translation: AAZ66579.1 .
    AE014134 Genomic DNA. Translation: AAZ66583.1 .
    PIRi A02630.
    S10097.
    RefSeqi NP_001027285.1. NM_001032114.1.
    NP_001027289.1. NM_001032118.1.
    NP_001027294.1. NM_001032123.1.
    NP_001027298.1. NM_001032127.1.
    NP_001027303.1. NM_001032132.1.
    NP_001027308.1. NM_001032137.1.
    NP_001027313.1. NM_001032142.1.
    NP_001027318.1. NM_001032147.1.
    NP_001027323.1. NM_001032152.1.
    NP_001027328.1. NM_001032157.1.
    NP_001027333.1. NM_001032162.1.
    NP_001027338.1. NM_001032167.1.
    NP_001027343.1. NM_001032172.1.
    NP_001027348.1. NM_001032177.1.
    NP_001027353.1. NM_001032182.1.
    NP_001027358.1. NM_001032187.1.
    NP_001027363.1. NM_001032192.1.
    NP_001027368.1. NM_001032197.1.
    NP_001027373.1. NM_001032202.1.
    NP_001027378.1. NM_001032207.1.
    NP_001027383.1. NM_001032212.1.
    NP_001027387.1. NM_001032216.1.
    NP_724345.1. NM_165384.2.
    UniGenei Dm.29515.
    Dm.34559.
    Dm.34566.
    Dm.34567.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KNA X-ray 2.10 P 2-17 [» ]
    1KNE X-ray 2.40 P 2-17 [» ]
    2NQB X-ray 2.30 A/E 2-136 [» ]
    2PYO X-ray 2.43 A/E 2-136 [» ]
    2YBA X-ray 2.55 C/D 2-20 [» ]
    4INM X-ray 3.50 A/E/K/O 41-136 [» ]
    ProteinModelPortali P02299.
    SMRi P02299. Positions 17-136.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 77140. 10 interactions.
    DIPi DIP-38722N.
    IntActi P02299. 15 interactions.
    MINTi MINT-271349.
    STRINGi 7227.FBpp0091051.

    Proteomic databases

    PaxDbi P02299.
    PRIDEi P02299.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0085894 ; FBpp0085250 ; FBgn0051613 .
    FBtr0091807 ; FBpp0091051 ; FBgn0053803 .
    FBtr0091810 ; FBpp0091053 ; FBgn0053806 .
    FBtr0091813 ; FBpp0091056 ; FBgn0053809 .
    FBtr0091816 ; FBpp0091058 ; FBgn0053812 .
    FBtr0091819 ; FBpp0091061 ; FBgn0053815 .
    FBtr0091822 ; FBpp0091064 ; FBgn0053818 .
    FBtr0091825 ; FBpp0091067 ; FBgn0053821 .
    FBtr0091828 ; FBpp0091070 ; FBgn0053824 .
    FBtr0091831 ; FBpp0091073 ; FBgn0053827 .
    FBtr0091834 ; FBpp0091076 ; FBgn0053830 .
    FBtr0091837 ; FBpp0091079 ; FBgn0053833 .
    FBtr0091840 ; FBpp0091082 ; FBgn0053836 .
    FBtr0091843 ; FBpp0091085 ; FBgn0053839 .
    FBtr0091846 ; FBpp0091088 ; FBgn0053842 .
    FBtr0091849 ; FBpp0091091 ; FBgn0053845 .
    FBtr0091852 ; FBpp0091094 ; FBgn0053848 .
    FBtr0091855 ; FBpp0091097 ; FBgn0053851 .
    FBtr0091858 ; FBpp0091100 ; FBgn0053854 .
    FBtr0091861 ; FBpp0091103 ; FBgn0053857 .
    FBtr0091864 ; FBpp0091106 ; FBgn0053860 .
    FBtr0091867 ; FBpp0091109 ; FBgn0053863 .
    FBtr0091870 ; FBpp0091112 ; FBgn0053866 .
    GeneIDi 318847.
    3771723.
    3771729.
    3771771.
    3771792.
    3771959.
    3772032.
    3772149.
    3772163.
    3772173.
    3772189.
    3772191.
    3772198.
    3772231.
    3772370.
    3772374.
    3772421.
    3772489.
    3772517.
    3772518.
    3772552.
    3772607.
    3772619.
    KEGGi dme:Dmel_CG31613.
    dme:Dmel_CG33803.
    dme:Dmel_CG33806.
    dme:Dmel_CG33809.
    dme:Dmel_CG33812.
    dme:Dmel_CG33815.
    dme:Dmel_CG33818.
    dme:Dmel_CG33821.
    dme:Dmel_CG33824.
    dme:Dmel_CG33827.
    dme:Dmel_CG33830.
    dme:Dmel_CG33833.
    dme:Dmel_CG33836.
    dme:Dmel_CG33839.
    dme:Dmel_CG33842.
    dme:Dmel_CG33845.
    dme:Dmel_CG33848.
    dme:Dmel_CG33851.
    dme:Dmel_CG33854.
    dme:Dmel_CG33857.
    dme:Dmel_CG33860.
    dme:Dmel_CG33863.
    dme:Dmel_CG33866.

    Organism-specific databases

    CTDi 318847.
    3771723.
    3771729.
    3771771.
    3771792.
    3771959.
    3772032.
    3772149.
    3772163.
    3772173.
    3772189.
    3772191.
    3772198.
    3772231.
    3772370.
    3772374.
    3772421.
    3772489.
    3772517.
    3772518.
    3772552.
    3772607.
    3772619.
    FlyBasei FBgn0001199. His3.
    FBgn0051613. His3:CG31613.
    FBgn0053803. His3:CG33803.
    FBgn0053806. His3:CG33806.
    FBgn0053809. His3:CG33809.
    FBgn0053812. His3:CG33812.
    FBgn0053815. His3:CG33815.
    FBgn0053818. His3:CG33818.
    FBgn0053821. His3:CG33821.
    FBgn0053824. His3:CG33824.
    FBgn0053827. His3:CG33827.
    FBgn0053830. His3:CG33830.
    FBgn0053833. His3:CG33833.
    FBgn0053836. His3:CG33836.
    FBgn0053839. His3:CG33839.
    FBgn0053842. His3:CG33842.
    FBgn0053845. His3:CG33845.
    FBgn0053848. His3:CG33848.
    FBgn0053851. His3:CG33851.
    FBgn0053854. His3:CG33854.
    FBgn0053857. His3:CG33857.
    FBgn0053860. His3:CG33860.
    FBgn0053863. His3:CG33863.
    FBgn0053866. His3:CG33866.

    Phylogenomic databases

    eggNOGi COG2036.
    GeneTreei ENSGT00750000117468.
    InParanoidi P02299.
    KOi K11253.
    OMAi RISKMAR.
    OrthoDBi EOG7HB5C2.
    PhylomeDBi P02299.

    Enzyme and pathway databases

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

    Miscellaneous databases

    EvolutionaryTracei P02299.
    NextBioi 846322.

    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. "tRNA derived insertion element in histone gene repeating unit of Drosophila melanogaster."
      Matsuo Y., Yamazaki T.
      Nucleic Acids Res. 17:225-238(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIS3).
      Strain: AK-194.
    2. Goldberg M.L.
      Thesis (1979), University of Stanford, United States
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIS3).
    3. "Molecular evolution of the histone 3 multigene family in the Drosophila melanogaster species subgroup."
      Matsuo Y.
      Mol. Phylogenet. Evol. 16:339-343(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIS3).
      Strain: Canton-S.
    4. "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:CG31613; HIS3:CG33803; HIS3:CG33806; HIS3:CG33809; HIS3:CG33812; HIS3:CG33815; HIS3:CG33818; HIS3:CG33821; HIS3:CG33824; HIS3:CG33827; HIS3:CG33830; HIS3:CG33833; HIS3:CG33836; HIS3:CG33839; HIS3:CG33842; HIS3:CG33845; HIS3:CG33848; HIS3:CG33851; HIS3:CG33854; HIS3:CG33857; HIS3:CG33860; HIS3:CG33863 AND HIS3:CG33866).
      Strain: Berkeley.
    5. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    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. "The histone modification pattern of active genes revealed through genome-wide chromatin analysis of a higher eukaryote."
      Schuebeler D., MacAlpine D.M., Scalzo D., Wirbelauer C., Kooperberg C., van Leeuwen F., Gottschling D.E., O'Neill L.P., Turner B.M., Delrow J., Bell S.P., Groudine M.
      Genes Dev. 18:1263-1271(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-5 AND LYS-80, PHOSPHORYLATION AT SER-11.
    11. "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: 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.
    12. "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.
    13. "A histone code in meiosis: the histone kinase, NHK-1, is required for proper chromosomal architecture in Drosophila oocytes."
      Ivanovska I., Khandan T., Ito T., Orr-Weaver T.L.
      Genes Dev. 19:2571-2582(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-15.
    14. "Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail."
      Jacobs S.A., Khorasanizadeh S.
      Science 295:2080-2083(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-17, ACETYLATION AT LYS-10.

    Entry informationi

    Entry nameiH3_DROME
    AccessioniPrimary (citable) accession number: P02299
    Secondary accession number(s): Q4ABE4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 146 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3