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P08985 (H2AV_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone H2A.v
Alternative name(s):
H2A.F/Z
Short name=H2A.Z
Gene names
Name:His2Av
Synonyms:H2AvD, His2AvD
ORF Names:CG5499
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length141 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.9 Ref.11 Ref.13

Subunit structure

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.

Subcellular location

Nucleus. Chromosome. Note: Widely distributed in the genome, irrespective of the transcriptional status or coding capacity of the sequence. Ref.10

Developmental stage

Expressed both maternally and zygotically. Expressed in embryos and adults (females only). Ref.8

Domain

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

Post-translational modification

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. Ref.11

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. Ref.11

Monoubiquitination of Lys-121 by sce/dRING gives a specific tag for epigenetic transcriptional repression By similarity.

Sequence similarities

Belongs to the histone H2A family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 141140Histone H2A.v
PRO_0000055309

Regions

Region93 – 10311Essential for function in development
Motif138 – 1392[ST]-Q motif

Amino acid modifications

Modified residue51N6-acetyllysine Ref.12
Modified residue1381Phosphoserine Ref.11
Cross-link121Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Natural variant251G → D in strain: ZBMEL377.
Natural variant901A → T in strain: ZBMEL131.
Natural variant951E → K in strain: MEL16 and ZBMEL84. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P08985 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 0DA41C01F831A5B6

FASTA14114,981
        10         20         30         40         50         60 
MAGGKAGKDS GKAKAKAVSR SARAGLQFPV GRIHRHLKSR TTSHGRVGAT AAVYSAAILE 

        70         80         90        100        110        120 
YLTAEVLELA GNASKDLKVK RITPRHLQLA IRGDEELDSL IKATIAGGGV IPHIHKSLIG 

       130        140 
KKEETVQDPQ RKGNVILSQA Y 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[7]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS08118.
RefSeqNP_001262997.1. NM_001276068.1.
NP_524519.1. NM_079795.3.
UniGeneDm.2346.

3D structure databases

ProteinModelPortalP08985.
SMRP08985. Positions 17-122.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid68120. 8 interactions.
DIPDIP-23205N.
IntActP08985. 2 interactions.
MINTMINT-1547881.

Proteomic databases

PaxDbP08985.
PRIDEP08985.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0085062; FBpp0084434; FBgn0001197.
GeneID43229.
KEGGdme:Dmel_CG5499.

Organism-specific databases

CTD43229.
FlyBaseFBgn0001197. His2Av.

Phylogenomic databases

eggNOGCOG5262.
GeneTreeENSGT00710000106735.
InParanoidP08985.
KOK11251.
OMAIHRYLMN.
OrthoDBEOG7M0NTR.
PhylomeDBP08985.

Gene expression databases

BgeeP08985.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR002119. Histone_H2A.
[Graphical view]
PfamPF00125. Histone. 1 hit.
[Graphical view]
PRINTSPR00620. HISTONEH2A.
SMARTSM00414. H2A. 1 hit.
[Graphical view]
SUPFAMSSF47113. SSF47113. 1 hit.
PROSITEPS00046. HISTONE_H2A. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHis2Av. drosophila.
GenomeRNAi43229.
NextBio832825.

Entry information

Entry nameH2AV_DROME
AccessionPrimary (citable) accession number: P08985
Secondary accession number(s): A0ANX7 expand/collapse secondary AC list , A0ANX8, A0ANY0, A0ANY3, C0MJB2, C0MJB9, Q26252, Q540X2, Q9VBB1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase