SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P84051

- H2A_DROME

UniProt

P84051 - H2A_DROME

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Histone H2A
Gene
His2A, H2a
His2A:CG31618, CG31618
His2A:CG33808, CG33808
His2A:CG33814, CG33814
His2A:CG33817, CG33817
His2A:CG33820, CG33820
more..
His2A:CG33823, CG33823
His2A:CG33826, CG33826
His2A:CG33829, CG33829
His2A:CG33832, CG33832
His2A:CG33835, CG33835
His2A:CG33838, CG33838
His2A:CG33841, CG33841
His2A:CG33844, CG33844
His2A:CG33847, CG33847
His2A:CG33850, CG33850
His2A:CG33862, CG33862
His2A:CG33865, CG33865 less..
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

GO - Biological processi

  1. centrosome duplication Source: FlyBase
  2. nucleosome assembly Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Organism-specific databases

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
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
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 – 124123Histone H2A
PRO_0000055222Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine By similarity
Modified residuei2 – 21Phosphoserine Inferred
Modified residuei104 – 1041N5-methylglutamine By similarity
Cross-linki119 – 119Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Inferred
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.

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

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.

Miscellaneous databases

EvolutionaryTraceiP84051.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2A family.

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...

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 93 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

Similar proteinsi