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P84051

- H2A_DROME

UniProt

P84051 - H2A_DROME

Protein

Histone H2A

Gene

His2A

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

    GO - Biological processi

    1. centrosome duplication Source: FlyBase
    2. nucleosome assembly Source: UniProtKB

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone H2A
    Gene namesi
    Name:His2A
    Synonyms:H2a
    AND
    Name:His2A:CG31618
    ORF Names:CG31618
    AND
    Name:His2A:CG33808
    ORF Names:CG33808
    AND
    Name:His2A:CG33814
    ORF Names:CG33814
    AND
    Name:His2A:CG33817
    ORF Names:CG33817
    AND
    Name:His2A:CG33820
    ORF Names:CG33820
    AND
    Name:His2A:CG33823
    ORF Names:CG33823
    AND
    Name:His2A:CG33826
    ORF Names:CG33826
    AND
    Name:His2A:CG33829
    ORF Names:CG33829
    AND
    Name:His2A:CG33832
    ORF Names:CG33832
    AND
    Name:His2A:CG33835
    ORF Names:CG33835
    AND
    Name:His2A:CG33838
    ORF Names:CG33838
    AND
    Name:His2A:CG33841
    ORF Names:CG33841
    AND
    Name:His2A:CG33844
    ORF Names:CG33844
    AND
    Name:His2A:CG33847
    ORF Names:CG33847
    AND
    Name:His2A:CG33850
    ORF Names:CG33850
    AND
    Name:His2A:CG33862
    ORF Names:CG33862
    AND
    Name:His2A:CG33865
    ORF Names:CG33865
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2L

    Organism-specific databases

    FlyBaseiFBgn0001196. His2A.
    FBgn0051618. His2A:CG31618.
    FBgn0053808. His2A:CG33808.
    FBgn0053814. His2A:CG33814.
    FBgn0053817. His2A:CG33817.
    FBgn0053820. His2A:CG33820.
    FBgn0053823. His2A:CG33823.
    FBgn0053826. His2A:CG33826.
    FBgn0053829. His2A:CG33829.
    FBgn0053832. His2A:CG33832.
    FBgn0053835. His2A:CG33835.
    FBgn0053838. His2A:CG33838.
    FBgn0053841. His2A:CG33841.
    FBgn0053844. His2A:CG33844.
    FBgn0053847. His2A:CG33847.
    FBgn0053850. His2A:CG33850.
    FBgn0053862. His2A:CG33862.
    FBgn0053865. His2A:CG33865.

    Subcellular locationi

    GO - Cellular componenti

    1. lipid particle Source: FlyBase
    2. nucleosome Source: UniProtKB
    3. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chromosome, Nucleosome core, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 124123Histone H2APRO_0000055222Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei2 – 21Phosphoserine1 Publication
    Modified residuei104 – 1041N5-methylglutamineBy similarity
    Cross-linki119 – 119Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei120 – 1201Phosphothreonine2 Publications

    Post-translational modificationi

    The chromatin-associated form, but not the free cytoplasmic form, is phosphorylated on Thr-120 by NHK-1 during mitosis, and dephosphorylated during S-phase. Also phosphorylated on Thr-120 by NHK-1 during prophase I of meiosis; which is required for acetylation of H3 'Lys-14' and H4 'Lys-5', diassembly of the synaptonemal complex, and karyosome formation.3 Publications
    Monoubiquitination of Lys-119 by sce/dRING gives a specific tag for epigenetic transcriptional repression.
    Phosphorylation on Ser-2 is enhanced during mitosis. Phosphorylation on Ser-2 directly represses transcription By similarity.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP84051.

    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

    BioGridi534102. 2 interactions.
    77146. 7 interactions.
    DIPiDIP-17375N.
    DIP-29504N.
    IntActiP84051. 7 interactions.
    MINTiMINT-742075.
    STRINGi7227.FBpp0091111.

    Structurei

    Secondary structure

    1
    124
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi17 – 215
    Helixi27 – 3610
    Beta strandi41 – 433
    Helixi46 – 7227
    Beta strandi76 – 783
    Helixi80 – 889
    Helixi91 – 966
    Turni97 – 993
    Beta strandi100 – 1023
    Helixi113 – 1153

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2NQBX-ray2.30C/G2-124[»]
    2PYOX-ray2.43C/G2-121[»]
    4INMX-ray3.50C/G/M/Q16-117[»]
    ProteinModelPortaliP84051.
    SMRiP84051. Positions 14-119.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP84051.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histone H2A family.Curated

    Phylogenomic databases

    eggNOGiCOG5262.
    GeneTreeiENSGT00740000115227.
    InParanoidiP84051.
    KOiK11251.
    OMAiNIHTELL.
    OrthoDBiEOG7M0NTR.
    PhylomeDBiP84051.

    Family and domain databases

    Gene3Di1.10.20.10. 1 hit.
    InterProiIPR009072. Histone-fold.
    IPR007125. Histone_core_D.
    IPR002119. Histone_H2A.
    [Graphical view]
    PfamiPF00125. Histone. 1 hit.
    [Graphical view]
    PRINTSiPR00620. HISTONEH2A.
    SMARTiSM00414. H2A. 1 hit.
    [Graphical view]
    SUPFAMiSSF47113. SSF47113. 1 hit.
    PROSITEiPS00046. HISTONE_H2A. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P84051-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGRGKGGKV KGKAKSRSNR AGLQFPVGRI HRLLRKGNYA ERVGAGAPVY    50
    LAAVMEYLAA EVLELAGNAA RDNKKTRIIP RHLQLAIRND EELNKLLSGV 100
    TIAQGGVLPN IQAVLLPKKT EKKA 124
    Length:124
    Mass (Da):13,363
    Last modified:January 23, 2007 - v2
    Checksum:i725BA63C393155F6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14215 Genomic DNA. Translation: CAA32431.1.
    X14215 Genomic DNA. Translation: CAA32436.1.
    AE014134 Genomic DNA. Translation: AAN11125.1.
    AE014134 Genomic DNA. Translation: AAZ66488.1.
    AE014134 Genomic DNA. Translation: AAZ66497.1.
    AE014134 Genomic DNA. Translation: AAZ66502.1.
    AE014134 Genomic DNA. Translation: AAZ66507.1.
    AE014134 Genomic DNA. Translation: AAZ66512.1.
    AE014134 Genomic DNA. Translation: AAZ66517.1.
    AE014134 Genomic DNA. Translation: AAZ66522.1.
    AE014134 Genomic DNA. Translation: AAZ66527.1.
    AE014134 Genomic DNA. Translation: AAZ66532.1.
    AE014134 Genomic DNA. Translation: AAZ66537.1.
    AE014134 Genomic DNA. Translation: AAZ66542.1.
    AE014134 Genomic DNA. Translation: AAZ66547.1.
    AE014134 Genomic DNA. Translation: AAZ66552.1.
    AE014134 Genomic DNA. Translation: AAZ66557.1.
    AE014134 Genomic DNA. Translation: AAZ66577.1.
    AE014134 Genomic DNA. Translation: AAZ66582.1.
    PIRiS10094. HSFF2.
    RefSeqiNP_001027292.1. NM_001032121.1.
    NP_001027301.1. NM_001032130.1.
    NP_001027306.1. NM_001032135.1.
    NP_001027311.1. NM_001032140.1.
    NP_001027316.1. NM_001032145.1.
    NP_001027321.1. NM_001032150.1.
    NP_001027326.1. NM_001032155.1.
    NP_001027331.1. NM_001032160.1.
    NP_001027336.1. NM_001032165.1.
    NP_001027341.1. NM_001032170.1.
    NP_001027346.1. NM_001032175.1.
    NP_001027351.1. NM_001032180.1.
    NP_001027356.1. NM_001032185.1.
    NP_001027361.1. NM_001032190.1.
    NP_001027381.1. NM_001032210.1.
    NP_001027386.1. NM_001032215.1.
    NP_724343.1. NM_165382.2.
    UniGeneiDm.20811.
    Dm.33693.
    Dm.33771.
    Dm.33813.

    Genome annotation databases

    EnsemblMetazoaiFBtr0085893; FBpp0085249; FBgn0051618.
    FBtr0091812; FBpp0091055; FBgn0053808.
    FBtr0091818; FBpp0091060; FBgn0053814.
    FBtr0091821; FBpp0091063; FBgn0053817.
    FBtr0091824; FBpp0091066; FBgn0053820.
    FBtr0091827; FBpp0091069; FBgn0053823.
    FBtr0091830; FBpp0091072; FBgn0053826.
    FBtr0091833; FBpp0091075; FBgn0053829.
    FBtr0091836; FBpp0091078; FBgn0053832.
    FBtr0091839; FBpp0091081; FBgn0053835.
    FBtr0091842; FBpp0091084; FBgn0053838.
    FBtr0091845; FBpp0091087; FBgn0053841.
    FBtr0091848; FBpp0091090; FBgn0053844.
    FBtr0091851; FBpp0091093; FBgn0053847.
    FBtr0091854; FBpp0091096; FBgn0053850.
    FBtr0091866; FBpp0091108; FBgn0053862.
    FBtr0091869; FBpp0091111; FBgn0053865.
    GeneIDi318855.
    3771774.
    3771783.
    3771785.
    3772148.
    3772278.
    3772282.
    3772345.
    3772351.
    3772360.
    3772447.
    3772448.
    3772505.
    3772541.
    3772565.
    3772618.
    3772632.
    KEGGidme:Dmel_CG31618.
    dme:Dmel_CG33808.
    dme:Dmel_CG33814.
    dme:Dmel_CG33817.
    dme:Dmel_CG33820.
    dme:Dmel_CG33823.
    dme:Dmel_CG33826.
    dme:Dmel_CG33829.
    dme:Dmel_CG33832.
    dme:Dmel_CG33835.
    dme:Dmel_CG33838.
    dme:Dmel_CG33841.
    dme:Dmel_CG33844.
    dme:Dmel_CG33847.
    dme:Dmel_CG33850.
    dme:Dmel_CG33862.
    dme:Dmel_CG33865.
    UCSCiCG31618-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14215 Genomic DNA. Translation: CAA32431.1 .
    X14215 Genomic DNA. Translation: CAA32436.1 .
    AE014134 Genomic DNA. Translation: AAN11125.1 .
    AE014134 Genomic DNA. Translation: AAZ66488.1 .
    AE014134 Genomic DNA. Translation: AAZ66497.1 .
    AE014134 Genomic DNA. Translation: AAZ66502.1 .
    AE014134 Genomic DNA. Translation: AAZ66507.1 .
    AE014134 Genomic DNA. Translation: AAZ66512.1 .
    AE014134 Genomic DNA. Translation: AAZ66517.1 .
    AE014134 Genomic DNA. Translation: AAZ66522.1 .
    AE014134 Genomic DNA. Translation: AAZ66527.1 .
    AE014134 Genomic DNA. Translation: AAZ66532.1 .
    AE014134 Genomic DNA. Translation: AAZ66537.1 .
    AE014134 Genomic DNA. Translation: AAZ66542.1 .
    AE014134 Genomic DNA. Translation: AAZ66547.1 .
    AE014134 Genomic DNA. Translation: AAZ66552.1 .
    AE014134 Genomic DNA. Translation: AAZ66557.1 .
    AE014134 Genomic DNA. Translation: AAZ66577.1 .
    AE014134 Genomic DNA. Translation: AAZ66582.1 .
    PIRi S10094. HSFF2.
    RefSeqi NP_001027292.1. NM_001032121.1.
    NP_001027301.1. NM_001032130.1.
    NP_001027306.1. NM_001032135.1.
    NP_001027311.1. NM_001032140.1.
    NP_001027316.1. NM_001032145.1.
    NP_001027321.1. NM_001032150.1.
    NP_001027326.1. NM_001032155.1.
    NP_001027331.1. NM_001032160.1.
    NP_001027336.1. NM_001032165.1.
    NP_001027341.1. NM_001032170.1.
    NP_001027346.1. NM_001032175.1.
    NP_001027351.1. NM_001032180.1.
    NP_001027356.1. NM_001032185.1.
    NP_001027361.1. NM_001032190.1.
    NP_001027381.1. NM_001032210.1.
    NP_001027386.1. NM_001032215.1.
    NP_724343.1. NM_165382.2.
    UniGenei Dm.20811.
    Dm.33693.
    Dm.33771.
    Dm.33813.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2NQB X-ray 2.30 C/G 2-124 [» ]
    2PYO X-ray 2.43 C/G 2-121 [» ]
    4INM X-ray 3.50 C/G/M/Q 16-117 [» ]
    ProteinModelPortali P84051.
    SMRi P84051. Positions 14-119.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 534102. 2 interactions.
    77146. 7 interactions.
    DIPi DIP-17375N.
    DIP-29504N.
    IntActi P84051. 7 interactions.
    MINTi MINT-742075.
    STRINGi 7227.FBpp0091111.

    Proteomic databases

    PaxDbi P84051.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0085893 ; FBpp0085249 ; FBgn0051618 .
    FBtr0091812 ; FBpp0091055 ; FBgn0053808 .
    FBtr0091818 ; FBpp0091060 ; FBgn0053814 .
    FBtr0091821 ; FBpp0091063 ; FBgn0053817 .
    FBtr0091824 ; FBpp0091066 ; FBgn0053820 .
    FBtr0091827 ; FBpp0091069 ; FBgn0053823 .
    FBtr0091830 ; FBpp0091072 ; FBgn0053826 .
    FBtr0091833 ; FBpp0091075 ; FBgn0053829 .
    FBtr0091836 ; FBpp0091078 ; FBgn0053832 .
    FBtr0091839 ; FBpp0091081 ; FBgn0053835 .
    FBtr0091842 ; FBpp0091084 ; FBgn0053838 .
    FBtr0091845 ; FBpp0091087 ; FBgn0053841 .
    FBtr0091848 ; FBpp0091090 ; FBgn0053844 .
    FBtr0091851 ; FBpp0091093 ; FBgn0053847 .
    FBtr0091854 ; FBpp0091096 ; FBgn0053850 .
    FBtr0091866 ; FBpp0091108 ; FBgn0053862 .
    FBtr0091869 ; FBpp0091111 ; FBgn0053865 .
    GeneIDi 318855.
    3771774.
    3771783.
    3771785.
    3772148.
    3772278.
    3772282.
    3772345.
    3772351.
    3772360.
    3772447.
    3772448.
    3772505.
    3772541.
    3772565.
    3772618.
    3772632.
    KEGGi dme:Dmel_CG31618.
    dme:Dmel_CG33808.
    dme:Dmel_CG33814.
    dme:Dmel_CG33817.
    dme:Dmel_CG33820.
    dme:Dmel_CG33823.
    dme:Dmel_CG33826.
    dme:Dmel_CG33829.
    dme:Dmel_CG33832.
    dme:Dmel_CG33835.
    dme:Dmel_CG33838.
    dme:Dmel_CG33841.
    dme:Dmel_CG33844.
    dme:Dmel_CG33847.
    dme:Dmel_CG33850.
    dme:Dmel_CG33862.
    dme:Dmel_CG33865.
    UCSCi CG31618-RA. d. melanogaster.

    Organism-specific databases

    CTDi 318855.
    3771774.
    3771783.
    3771785.
    3772148.
    3772278.
    3772282.
    3772345.
    3772351.
    3772360.
    3772447.
    3772448.
    3772505.
    3772541.
    3772565.
    3772618.
    3772632.
    FlyBasei FBgn0001196. His2A.
    FBgn0051618. His2A:CG31618.
    FBgn0053808. His2A:CG33808.
    FBgn0053814. His2A:CG33814.
    FBgn0053817. His2A:CG33817.
    FBgn0053820. His2A:CG33820.
    FBgn0053823. His2A:CG33823.
    FBgn0053826. His2A:CG33826.
    FBgn0053829. His2A:CG33829.
    FBgn0053832. His2A:CG33832.
    FBgn0053835. His2A:CG33835.
    FBgn0053838. His2A:CG33838.
    FBgn0053841. His2A:CG33841.
    FBgn0053844. His2A:CG33844.
    FBgn0053847. His2A:CG33847.
    FBgn0053850. His2A:CG33850.
    FBgn0053862. His2A:CG33862.
    FBgn0053865. His2A:CG33865.

    Phylogenomic databases

    eggNOGi COG5262.
    GeneTreei ENSGT00740000115227.
    InParanoidi P84051.
    KOi K11251.
    OMAi NIHTELL.
    OrthoDBi EOG7M0NTR.
    PhylomeDBi P84051.

    Miscellaneous databases

    EvolutionaryTracei P84051.
    NextBioi 846332.

    Family and domain databases

    Gene3Di 1.10.20.10. 1 hit.
    InterProi IPR009072. Histone-fold.
    IPR007125. Histone_core_D.
    IPR002119. Histone_H2A.
    [Graphical view ]
    Pfami PF00125. Histone. 1 hit.
    [Graphical view ]
    PRINTSi PR00620. HISTONEH2A.
    SMARTi SM00414. H2A. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47113. SSF47113. 1 hit.
    PROSITEi PS00046. HISTONE_H2A. 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] (HIS2A).
      Strain: AK-194.
    2. "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] (HIS2A:CG31618; HIS2A:CG33808; HIS2A:CG33814; HIS2A:CG33817; HIS2A:CG33820; HIS2A:CG33823; HIS2A:CG33826; HIS2A:CG33829; HIS2A:CG33832; HIS2A:CG33835; HIS2A:CG33838; HIS2A:CG33841; HIS2A:CG33844; HIS2A:CG33847; HIS2A:CG33850; HIS2A:CG33862 AND HIS2A:CG33865).
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. "Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during mitosis in the early Drosophila embryo."
      Aihara H., Nakagawa T., Yasui K., Ohta T., Hirose S., Dhomae N., Takio K., Kaneko M., Takeshima Y., Muramatsu M., Ito T.
      Genes Dev. 18:877-888(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 96-122, PHOSPHORYLATION AT THR-120.
      Strain: Berkeley.
      Tissue: Embryo.
    5. Goldberg M.L.
      Thesis (1979), University of Stanford, United States
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-122 (HIS2A).
    6. "The enhancement of histone H4 and H2A serine 1 phosphorylation during mitosis and S-phase is evolutionarily conserved."
      Barber C.M., Turner F.B., Wang Y., Hagstrom K., Taverna S.D., Mollah S., Ueberheide B., Meyer B.J., Hunt D.F., Cheung P., Allis C.D.
      Chromosoma 112:360-371(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-2.
    7. "Role of histone H2A ubiquitination in Polycomb silencing."
      Wang H., Wang L., Erdjument-Bromage H., Vidal M., Tempst P., Jones R.S., Zhang Y.
      Nature 431:873-878(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    8. "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: PHOSPHORYLATION AT THR-120.

    Entry informationi

    Entry nameiH2A_DROME
    AccessioniPrimary (citable) accession number: P84051
    Secondary accession number(s): P02267, Q4ABC7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 94 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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