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P08985

- H2AV_DROME

UniProt

P08985 - H2AV_DROME

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Protein
Histone H2A.v
Gene
His2Av, H2AvD, His2AvD, CG5499
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

GO - Biological processi

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

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

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
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 141140Histone H2A.v
PRO_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.1 Publication
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.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni93 – 10311Essential for function in development
Add
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.

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...

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 135 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

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