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P84051 (H2A_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Gene names
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
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length124 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

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.

Subcellular location

Nucleus. Chromosome.

Post-translational modification

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. Ref.4 Ref.6 Ref.8

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.

Sequence similarities

Belongs to the histone H2A family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 124123Histone H2A
PRO_0000055222

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue21Phosphoserine Probable
Modified residue1041N5-methylglutamine By similarity
Modified residue1201Phosphothreonine Ref.4 Ref.8
Cross-link119Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Probable

Secondary structure

................... 124
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P84051 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 725BA63C393155F6

FASTA12413,363
        10         20         30         40         50         60 
MSGRGKGGKV KGKAKSRSNR AGLQFPVGRI HRLLRKGNYA ERVGAGAPVY LAAVMEYLAA 

        70         80         90        100        110        120 
EVLELAGNAA RDNKKTRIIP RHLQLAIRND EELNKLLSGV TIAQGGVLPN IQAVLLPKKT 


EKKA 

« Hide

References

« Hide 'large scale' references
[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. 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] (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]"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.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRHSFF2. S10094.
RefSeqNP_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.
UniGeneDm.20811.
Dm.33693.
Dm.33771.
Dm.33813.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2NQBX-ray2.30C/G2-124[»]
2PYOX-ray2.43C/G2-121[»]
4INMX-ray3.50C/G/M/Q16-117[»]
ProteinModelPortalP84051.
SMRP84051. Positions 14-119.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid534102. 2 interactions.
77146. 7 interactions.
DIPDIP-17375N.
DIP-29504N.
IntActP84051. 7 interactions.
MINTMINT-742075.
STRING7227.FBpp0091111.

Proteomic databases

PaxDbP84051.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0085893; 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.
GeneID318855.
3771774.
3771783.
3771785.
3772148.
3772278.
3772282.
3772345.
3772351.
3772360.
3772447.
3772448.
3772505.
3772541.
3772565.
3772618.
3772632.
KEGGdme: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.
UCSCCG31618-RA. d. melanogaster.

Organism-specific databases

CTD318855.
3771774.
3771783.
3771785.
3772148.
3772278.
3772282.
3772345.
3772351.
3772360.
3772447.
3772448.
3772505.
3772541.
3772565.
3772618.
3772632.
FlyBaseFBgn0001196. 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

eggNOGCOG5262.
GeneTreeENSGT00740000115227.
InParanoidP84051.
KOK11251.
OMANIHTELL.
OrthoDBEOG7M0NTR.
PhylomeDBP84051.

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

EvolutionaryTraceP84051.
NextBio846332.

Entry information

Entry nameH2A_DROME
AccessionPrimary (citable) accession number: P84051
Secondary accession number(s): P02267, Q4ABC7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 93 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Drosophila

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