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P08985

- H2AV_DROME

UniProt

P08985 - H2AV_DROME

Protein

Histone H2A.v

Gene

His2Av

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

    Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. 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. Acts as a Polycomb group (PcG) protein required to maintain the transcriptionally repressive state of homeotic genes of the animal throughout development. Required for histone H3 'Lys-9' methylation and histone H4 'Lys-12' acetylation, two modifications that are essential for heterochromatin formation. Also involved in DNA double strand break (DSB) repair. Essential for early development.4 Publications

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: FlyBase
    2. DNA repair Source: UniProtKB-KW
    3. multicellular organismal development Source: UniProtKB-KW
    4. nucleosome assembly Source: InterPro
    5. protein localization to chromatin Source: FlyBase

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone H2A.v
    Alternative name(s):
    H2A.F/Z
    Short name:
    H2A.Z
    Gene namesi
    Name:His2Av
    Synonyms:H2AvD, His2AvD
    ORF Names:CG5499
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0001197. His2Av.

    Subcellular locationi

    Nucleus 1 Publication. Chromosome 1 Publication
    Note: Widely distributed in the genome, irrespective of the transcriptional status or coding capacity of the sequence.

    GO - Cellular componenti

    1. chromosome Source: FlyBase
    2. lipid particle Source: FlyBase
    3. nucleosome Source: FlyBase
    4. nucleus Source: FlyBase
    5. polytene chromosome Source: FlyBase
    6. polytene chromosome chromocenter Source: FlyBase

    Keywords - Cellular componenti

    Chromosome, Nucleosome core, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 141140Histone H2A.vPRO_0000055309Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei5 – 51N6-acetyllysine1 Publication
    Cross-linki121 – 121Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei138 – 1381Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated. Phosphorylation of Ser-138 occurs in response to DNA double strand breaks (DSBs) generated by exogenous genotoxic agents. Phosphorylation is dependent on the DNA damage checkpoint kinases ATR and ATM, spreads on either side of a detected DSB site and may mark the surrounding chromatin for recruitment of proteins required for DNA damage signaling and repair.1 Publication
    Acetylated on Lys-5 by Tip60. Acetylation is enhanced by Ser-138 phosphorylation and promotes the exchange of the phosphorylated form with the unmodified form of H2AV.2 Publications
    Monoubiquitination of Lys-121 by sce/dRING gives a specific tag for epigenetic transcriptional repression.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP08985.
    PRIDEiP08985.

    Expressioni

    Developmental stagei

    Expressed both maternally and zygotically. Expressed in embryos and adults (females only).1 Publication

    Gene expression databases

    BgeeiP08985.

    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. H2A or its variant His2Av forms a heterodimer with H2B.

    Protein-protein interaction databases

    BioGridi68120. 8 interactions.
    DIPiDIP-23205N.
    IntActiP08985. 2 interactions.
    MINTiMINT-1547881.

    Structurei

    3D structure databases

    ProteinModelPortaliP08985.
    SMRiP08985. Positions 17-122.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni93 – 10311Essential for function in developmentAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi138 – 1392[ST]-Q motif

    Domaini

    The [ST]-Q motif constitutes a recognition sequence for kinases from the PI3/PI4-kinase family.

    Sequence similaritiesi

    Belongs to the histone H2A family.Curated

    Phylogenomic databases

    eggNOGiCOG5262.
    GeneTreeiENSGT00710000106735.
    InParanoidiP08985.
    KOiK11251.
    OMAiDPQRKGN.
    OrthoDBiEOG7M0NTR.
    PhylomeDBiP08985.

    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.

    P08985-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGGKAGKDS GKAKAKAVSR SARAGLQFPV GRIHRHLKSR TTSHGRVGAT    50
    AAVYSAAILE YLTAEVLELA GNASKDLKVK RITPRHLQLA IRGDEELDSL 100
    IKATIAGGGV IPHIHKSLIG KKEETVQDPQ RKGNVILSQA Y 141
    Length:141
    Mass (Da):14,981
    Last modified:January 23, 2007 - v2
    Checksum:i0DA41C01F831A5B6
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti25 – 251G → D in strain: ZBMEL377.
    Natural varianti90 – 901A → T in strain: ZBMEL131.
    Natural varianti95 – 951E → K in strain: MEL16 and ZBMEL84. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07485 mRNA. Translation: CAA30370.1.
    X15549 Genomic DNA. Translation: CAA33555.1.
    AM294365 Genomic DNA. Translation: CAL26295.1.
    AM294366 Genomic DNA. Translation: CAL26296.1.
    AM294367 Genomic DNA. Translation: CAL26297.1.
    AM294368 Genomic DNA. Translation: CAL26298.1.
    AM294369 Genomic DNA. Translation: CAL26299.1.
    AM294370 Genomic DNA. Translation: CAL26300.1.
    AM294371 Genomic DNA. Translation: CAL26301.1.
    AM294372 Genomic DNA. Translation: CAL26302.1.
    FM245434 Genomic DNA. Translation: CAR93360.1.
    FM245435 Genomic DNA. Translation: CAR93361.1.
    FM245436 Genomic DNA. Translation: CAR93362.1.
    FM245437 Genomic DNA. Translation: CAR93363.1.
    FM245438 Genomic DNA. Translation: CAR93364.1.
    FM245439 Genomic DNA. Translation: CAR93365.1.
    FM245440 Genomic DNA. Translation: CAR93366.1.
    FM245441 Genomic DNA. Translation: CAR93367.1.
    FM245442 Genomic DNA. Translation: CAR93368.1.
    FM245443 Genomic DNA. Translation: CAR93369.1.
    FM245444 Genomic DNA. Translation: CAR93370.1.
    FM245445 Genomic DNA. Translation: CAR93371.1.
    AE014297 Genomic DNA. Translation: AAF56631.1.
    AY118910 mRNA. Translation: AAM50770.1.
    S42733 Genomic DNA. Translation: AAB22897.1.
    PIRiS08118.
    RefSeqiNP_001262997.1. NM_001276068.1.
    NP_524519.1. NM_079795.3.
    UniGeneiDm.2346.

    Genome annotation databases

    EnsemblMetazoaiFBtr0085062; FBpp0084434; FBgn0001197.
    GeneIDi43229.
    KEGGidme:Dmel_CG5499.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07485 mRNA. Translation: CAA30370.1 .
    X15549 Genomic DNA. Translation: CAA33555.1 .
    AM294365 Genomic DNA. Translation: CAL26295.1 .
    AM294366 Genomic DNA. Translation: CAL26296.1 .
    AM294367 Genomic DNA. Translation: CAL26297.1 .
    AM294368 Genomic DNA. Translation: CAL26298.1 .
    AM294369 Genomic DNA. Translation: CAL26299.1 .
    AM294370 Genomic DNA. Translation: CAL26300.1 .
    AM294371 Genomic DNA. Translation: CAL26301.1 .
    AM294372 Genomic DNA. Translation: CAL26302.1 .
    FM245434 Genomic DNA. Translation: CAR93360.1 .
    FM245435 Genomic DNA. Translation: CAR93361.1 .
    FM245436 Genomic DNA. Translation: CAR93362.1 .
    FM245437 Genomic DNA. Translation: CAR93363.1 .
    FM245438 Genomic DNA. Translation: CAR93364.1 .
    FM245439 Genomic DNA. Translation: CAR93365.1 .
    FM245440 Genomic DNA. Translation: CAR93366.1 .
    FM245441 Genomic DNA. Translation: CAR93367.1 .
    FM245442 Genomic DNA. Translation: CAR93368.1 .
    FM245443 Genomic DNA. Translation: CAR93369.1 .
    FM245444 Genomic DNA. Translation: CAR93370.1 .
    FM245445 Genomic DNA. Translation: CAR93371.1 .
    AE014297 Genomic DNA. Translation: AAF56631.1 .
    AY118910 mRNA. Translation: AAM50770.1 .
    S42733 Genomic DNA. Translation: AAB22897.1 .
    PIRi S08118.
    RefSeqi NP_001262997.1. NM_001276068.1.
    NP_524519.1. NM_079795.3.
    UniGenei Dm.2346.

    3D structure databases

    ProteinModelPortali P08985.
    SMRi P08985. Positions 17-122.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 68120. 8 interactions.
    DIPi DIP-23205N.
    IntActi P08985. 2 interactions.
    MINTi MINT-1547881.

    Proteomic databases

    PaxDbi P08985.
    PRIDEi P08985.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0085062 ; FBpp0084434 ; FBgn0001197 .
    GeneIDi 43229.
    KEGGi dme:Dmel_CG5499.

    Organism-specific databases

    CTDi 43229.
    FlyBasei FBgn0001197. His2Av.

    Phylogenomic databases

    eggNOGi COG5262.
    GeneTreei ENSGT00710000106735.
    InParanoidi P08985.
    KOi K11251.
    OMAi DPQRKGN.
    OrthoDBi EOG7M0NTR.
    PhylomeDBi P08985.

    Miscellaneous databases

    ChiTaRSi His2Av. drosophila.
    GenomeRNAii 43229.
    NextBioi 832825.

    Gene expression databases

    Bgeei P08985.

    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. "Drosophila has a single copy of the gene encoding a highly conserved histone H2A variant of the H2A.F/Z type."
      van Daal A., White E.M., Gorovsky M.A., Elgin S.C.R.
      Nucleic Acids Res. 16:7487-7497(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Embryo.
    2. "Conservation of intron position indicates separation of major and variant H2As is an early event in the evolution of eukaryotes."
      van Daal A., White E.M., Elgin S.C.R., Gorovsky M.A.
      J. Mol. Evol. 30:449-455(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Canton-S.
    3. "Widespread adaptive evolution of Drosophila genes with sex-biased expression."
      Proeschel M., Zhang Z., Parsch J.
      Genetics 174:893-900(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ZBMEL131, ZBMEL186, ZBMEL191, ZBMEL377, ZBMEL384, ZBMEL82, ZBMEL84 and ZBMEL95.
    4. "The influence of demography and weak selection on the McDonald-Kreitman test: an empirical study in Drosophila."
      Parsch J., Zhang Z., Baines J.F.
      Mol. Biol. Evol. 26:691-698(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-95.
      Strain: MEL01, MEL02, MEL11, MEL12, MEL13, MEL14, MEL15, MEL16, MEL17, MEL18, MEL19 and MEL20.
    5. "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].
      Strain: Berkeley.
    6. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.
    8. "A histone variant, H2AvD, is essential in Drosophila melanogaster."
      Van Daal A., Elgin S.C.R.
      Mol. Biol. Cell 3:593-602(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-53, FUNCTION, DEVELOPMENTAL STAGE.
    9. "Regions of variant histone His2AvD required for Drosophila development."
      Clarkson M.J., Wells J.R.E., Gibson F., Saint R., Tremethick D.J.
      Nature 399:694-697(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Histone H2A.Z is widely but nonrandomly distributed in chromosomes of Drosophila melanogaster."
      Leach T.J., Mazzeo M., Chotkowski H.L., Madigan J.P., Wotring M.G., Glaser R.L.
      J. Biol. Chem. 275:23267-23272(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    11. "DNA double-strand break-induced phosphorylation of Drosophila histone variant H2Av helps prevent radiation-induced apoptosis."
      Madigan J.P., Chotkowski H.L., Glaser R.L.
      Nucleic Acids Res. 30:3698-3705(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-138.
    12. "Acetylation by Tip60 is required for selective histone variant exchange at DNA lesions."
      Kusch T., Florens L., Macdonald W.H., Swanson S.K., Glaser R.L., Yates J.R. III, Abmayr S.M., Washburn M.P., Workman J.L.
      Science 306:2084-2087(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-5.
    13. "The role of histone H2Av variant replacement and histone H4 acetylation in the establishment of Drosophila heterochromatin."
      Swaminathan J., Baxter E.M., Corces V.G.
      Genes Dev. 19:65-76(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiH2AV_DROME
    AccessioniPrimary (citable) accession number: P08985
    Secondary accession number(s): A0ANX7
    , A0ANX8, A0ANY0, A0ANY3, C0MJB2, C0MJB9, Q26252, Q540X2, Q9VBB1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 136 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    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