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P02299 (H3_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone H3
Gene names
Name:His3
AND
Name:His3:CG31613
ORF Names:CG31613
AND
Name:His3:CG33803
ORF Names:CG33803
AND
Name:His3:CG33806
ORF Names:CG33806
AND
Name:His3:CG33809
ORF Names:CG33809
AND
Name:His3:CG33812
ORF Names:CG33812
AND
Name:His3:CG33815
ORF Names:CG33815
AND
Name:His3:CG33818
ORF Names:CG33818
AND
Name:His3:CG33821
ORF Names:CG33821
AND
Name:His3:CG33824
ORF Names:CG33824
AND
Name:His3:CG33827
ORF Names:CG33827
AND
Name:His3:CG33830
ORF Names:CG33830
AND
Name:His3:CG33833
ORF Names:CG33833
AND
Name:His3:CG33836
ORF Names:CG33836
AND
Name:His3:CG33839
ORF Names:CG33839
AND
Name:His3:CG33842
ORF Names:CG33842
AND
Name:His3:CG33845
ORF Names:CG33845
AND
Name:His3:CG33848
ORF Names:CG33848
AND
Name:His3:CG33851
ORF Names:CG33851
AND
Name:His3:CG33854
ORF Names:CG33854
AND
Name:His3:CG33857
ORF Names:CG33857
AND
Name:His3:CG33860
ORF Names:CG33860
AND
Name:His3:CG33863
ORF Names:CG33863
AND
Name:His3:CG33866
ORF Names:CG33866
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length136 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 By similarity. Chromosome By similarity.

Post-translational modification

Phosphorylation at Ser-11 by ial/aurora-B during mitosis and meiosis is crucial for chromosome condensation and cell-cycle progression. Phosphorylation at Ser-11 by JIL-1 during interphase is linked to gene activation and restricts the formation of heterochromatin at inappropriate sites. Phosphorylation at Ser-11 is enriched on male X chromosome compared to the autosome.

Acetylation is generally linked to gene activation. Acetylated on Lys-15 during prophase I of meiosis. Phosphorylation of H2A 'Thr-119' is a prerequisite for H3 Lys-15 acetylation. Acetylation on Lys-15 is enriched on male X chromosome compared to the autosome. Ref.6 Ref.7 Ref.11 Ref.13 Ref.14

Methylation at Lys-5 or Lys-80 is generally associated with active chromatin. Methylation at Lys-80 by gpp occurs at low levels in specific developmental stages and tissues undergoing active cell division, and at highest levels in epidermal cells undergoing differentiation. Ref.10 Ref.11 Ref.12

Sequence similarities

Belongs to the histone H3 family.

Ontologies

Keywords
   Cellular componentChromosome
Nucleosome core
Nucleus
   LigandDNA-binding
   PTMAcetylation
Methylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnucleosome assembly

Inferred from electronic annotation. Source: InterPro

   Cellular_componentnucleosome

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 10591219. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

KAT2BQ928312EBI-522090,EBI-477430From a different organism.
ScmQ9VHA04EBI-522090,EBI-89256

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 136135Histone H3
PRO_0000221300

Regions

Region6 – 116Su(var)205 chromodomain-binding

Amino acid modifications

Modified residue51N6,N6,N6-trimethyllysine; alternate Ref.10 Ref.11
Modified residue51N6,N6-dimethyllysine; alternate Ref.10 Ref.11
Modified residue51N6-methyllysine; alternate Ref.10 Ref.11
Modified residue101N6,N6-dimethyllysine; alternate Ref.11
Modified residue101N6-acetyllysine; alternate Ref.6 Ref.11 Ref.14
Modified residue101N6-methyllysine; alternate Ref.11
Modified residue111Phosphoserine Ref.6 Ref.7 Ref.8 Ref.9 Ref.10
Modified residue151N6,N6-dimethyllysine; alternate Ref.11
Modified residue151N6-acetyllysine; alternate Ref.6 Ref.7 Ref.11 Ref.13
Modified residue151N6-methyllysine; alternate Ref.11
Modified residue191N6-acetyllysine Ref.11
Modified residue241N6-acetyllysine Ref.11
Modified residue281N6,N6,N6-trimethyllysine; alternate Ref.11
Modified residue281N6,N6-dimethyllysine; alternate Ref.11
Modified residue281N6-methyllysine; alternate Ref.11
Modified residue371N6,N6-dimethyllysine; alternate Ref.11
Modified residue371N6-methyllysine; alternate Ref.11
Modified residue381N6,N6-dimethyllysine; alternate Ref.11
Modified residue381N6-methyllysine; alternate Ref.11
Modified residue801N6,N6-dimethyllysine; alternate Ref.10 Ref.11 Ref.12
Modified residue801N6-methyllysine; alternate Ref.10 Ref.11 Ref.12

Experimental info

Sequence conflict1181V → I Ref.1
Sequence conflict1181V → I Ref.2

Secondary structure

............. 136
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02299 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 6FD8508EA50A0EEC

FASTA13615,388
        10         20         30         40         50         60 
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE 

        70         80         90        100        110        120 
LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEASEAY LVGLFEDTNL CAIHAKRVTI 

       130 
MPKDIQLARR IRGERA 

« 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] (HIS3).
Strain: AK-194.
[2]Goldberg M.L.
Thesis (1979), University of Stanford, United States
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIS3).
[3]"Molecular evolution of the histone 3 multigene family in the Drosophila melanogaster species subgroup."
Matsuo Y.
Mol. Phylogenet. Evol. 16:339-343(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIS3).
Strain: Canton-S.
[4]"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] (HIS3:CG31613; HIS3:CG33803; HIS3:CG33806; HIS3:CG33809; HIS3:CG33812; HIS3:CG33815; HIS3:CG33818; HIS3:CG33821; HIS3:CG33824; HIS3:CG33827; HIS3:CG33830; HIS3:CG33833; HIS3:CG33836; HIS3:CG33839; HIS3:CG33842; HIS3:CG33845; HIS3:CG33848; HIS3:CG33851; HIS3:CG33854; HIS3:CG33857; HIS3:CG33860; HIS3:CG33863 AND HIS3:CG33866).
Strain: Berkeley.
[5]"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.
[6]"Phosphorylation of histone H3 correlates with transcriptionally active loci."
Nowak S.J., Corces V.G.
Genes Dev. 14:3003-3013(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-11, ACETYLATION AT LYS-10 AND LYS-15.
[7]"The JIL-1 tandem kinase mediates histone H3 phosphorylation and is required for maintenance of chromatin structure in Drosophila."
Wang Y., Zhang W., Jin Y., Johansen J., Johansen K.M.
Cell 105:433-443(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-11, ACETYLATION AT LYS-15.
[8]"Drosophila aurora B kinase is required for histone H3 phosphorylation and condensin recruitment during chromosome condensation and to organize the central spindle during cytokinesis."
Giet R., Glover D.M.
J. Cell Biol. 152:669-682(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-11.
[9]"Phosphorylation of histone H3 during transcriptional activation depends on promoter structure."
Labrador M., Corces V.G.
Genes Dev. 17:43-48(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-11.
[10]"The histone modification pattern of active genes revealed through genome-wide chromatin analysis of a higher eukaryote."
Schuebeler D., MacAlpine D.M., Scalzo D., Wirbelauer C., Kooperberg C., van Leeuwen F., Gottschling D.E., O'Neill L.P., Turner B.M., Delrow J., Bell S.P., Groudine M.
Genes Dev. 18:1263-1271(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-5 AND LYS-80, PHOSPHORYLATION AT SER-11.
[11]"Histone H3.3 is enriched in covalent modifications associated with active chromatin."
McKittrick E., Gafken P.R., Ahmad K., Henikoff S.
Proc. Natl. Acad. Sci. U.S.A. 101:1525-1530(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-5; LYS-10; LYS-15; LYS-28; LYS-37; LYS-38 AND LYS-80, ACETYLATION AT LYS-10; LYS-15; LYS-19 AND LYS-24, IDENTIFICATION BY MASS SPECTROMETRY.
[12]"Characterization of the grappa gene, the Drosophila histone H3 lysine 79 methyltransferase."
Shanower G.A., Mueller M., Blanton J.L., Honti V., Gyurkovics H., Schedl P.
Genetics 169:173-184(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-80.
[13]"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: ACETYLATION AT LYS-15.
[14]"Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail."
Jacobs S.A., Khorasanizadeh S.
Science 295:2080-2083(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-17, ACETYLATION AT LYS-10.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14215 Genomic DNA. Translation: CAA32434.1.
AB019400 Genomic DNA. Translation: BAA93621.1.
AE014134 Genomic DNA. Translation: AAN11127.1.
AE014134 Genomic DNA. Translation: AAZ66481.1.
AE014134 Genomic DNA. Translation: AAZ66485.1.
AE014134 Genomic DNA. Translation: AAZ66490.1.
AE014134 Genomic DNA. Translation: AAZ66494.1.
AE014134 Genomic DNA. Translation: AAZ66499.1.
AE014134 Genomic DNA. Translation: AAZ66504.1.
AE014134 Genomic DNA. Translation: AAZ66509.1.
AE014134 Genomic DNA. Translation: AAZ66514.1.
AE014134 Genomic DNA. Translation: AAZ66519.1.
AE014134 Genomic DNA. Translation: AAZ66524.1.
AE014134 Genomic DNA. Translation: AAZ66529.1.
AE014134 Genomic DNA. Translation: AAZ66534.1.
AE014134 Genomic DNA. Translation: AAZ66539.1.
AE014134 Genomic DNA. Translation: AAZ66544.1.
AE014134 Genomic DNA. Translation: AAZ66549.1.
AE014134 Genomic DNA. Translation: AAZ66554.1.
AE014134 Genomic DNA. Translation: AAZ66559.1.
AE014134 Genomic DNA. Translation: AAZ66564.1.
AE014134 Genomic DNA. Translation: AAZ66569.1.
AE014134 Genomic DNA. Translation: AAZ66574.1.
AE014134 Genomic DNA. Translation: AAZ66579.1.
AE014134 Genomic DNA. Translation: AAZ66583.1.
PIRA02630.
S10097.
RefSeqNP_001027285.1. NM_001032114.1.
NP_001027289.1. NM_001032118.1.
NP_001027294.1. NM_001032123.1.
NP_001027298.1. NM_001032127.1.
NP_001027303.1. NM_001032132.1.
NP_001027308.1. NM_001032137.1.
NP_001027313.1. NM_001032142.1.
NP_001027318.1. NM_001032147.1.
NP_001027323.1. NM_001032152.1.
NP_001027328.1. NM_001032157.1.
NP_001027333.1. NM_001032162.1.
NP_001027338.1. NM_001032167.1.
NP_001027343.1. NM_001032172.1.
NP_001027348.1. NM_001032177.1.
NP_001027353.1. NM_001032182.1.
NP_001027358.1. NM_001032187.1.
NP_001027363.1. NM_001032192.1.
NP_001027368.1. NM_001032197.1.
NP_001027373.1. NM_001032202.1.
NP_001027378.1. NM_001032207.1.
NP_001027383.1. NM_001032212.1.
NP_001027387.1. NM_001032216.1.
NP_724345.1. NM_165384.2.
UniGeneDm.29515.
Dm.34559.
Dm.34566.
Dm.34567.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KNAX-ray2.10P2-17[»]
1KNEX-ray2.40P2-17[»]
2NQBX-ray2.30A/E2-136[»]
2PYOX-ray2.43A/E2-136[»]
2YBAX-ray2.55C/D2-20[»]
4INMX-ray3.50A/E/K/O41-136[»]
ProteinModelPortalP02299.
SMRP02299. Positions 17-136.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid77140. 10 interactions.
DIPDIP-38722N.
IntActP02299. 15 interactions.
MINTMINT-271349.
STRING7227.FBpp0091051.

Proteomic databases

PaxDbP02299.
PRIDEP02299.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0085894; FBpp0085250; FBgn0051613.
FBtr0091807; FBpp0091051; FBgn0053803.
FBtr0091810; FBpp0091053; FBgn0053806.
FBtr0091813; FBpp0091056; FBgn0053809.
FBtr0091816; FBpp0091058; FBgn0053812.
FBtr0091819; FBpp0091061; FBgn0053815.
FBtr0091822; FBpp0091064; FBgn0053818.
FBtr0091825; FBpp0091067; FBgn0053821.
FBtr0091828; FBpp0091070; FBgn0053824.
FBtr0091831; FBpp0091073; FBgn0053827.
FBtr0091834; FBpp0091076; FBgn0053830.
FBtr0091837; FBpp0091079; FBgn0053833.
FBtr0091840; FBpp0091082; FBgn0053836.
FBtr0091843; FBpp0091085; FBgn0053839.
FBtr0091846; FBpp0091088; FBgn0053842.
FBtr0091849; FBpp0091091; FBgn0053845.
FBtr0091852; FBpp0091094; FBgn0053848.
FBtr0091855; FBpp0091097; FBgn0053851.
FBtr0091858; FBpp0091100; FBgn0053854.
FBtr0091861; FBpp0091103; FBgn0053857.
FBtr0091864; FBpp0091106; FBgn0053860.
FBtr0091867; FBpp0091109; FBgn0053863.
FBtr0091870; FBpp0091112; FBgn0053866.
GeneID318847.
3771723.
3771729.
3771771.
3771792.
3771959.
3772032.
3772149.
3772163.
3772173.
3772189.
3772191.
3772198.
3772231.
3772370.
3772374.
3772421.
3772489.
3772517.
3772518.
3772552.
3772607.
3772619.
KEGGdme:Dmel_CG31613.
dme:Dmel_CG33803.
dme:Dmel_CG33806.
dme:Dmel_CG33809.
dme:Dmel_CG33812.
dme:Dmel_CG33815.
dme:Dmel_CG33818.
dme:Dmel_CG33821.
dme:Dmel_CG33824.
dme:Dmel_CG33827.
dme:Dmel_CG33830.
dme:Dmel_CG33833.
dme:Dmel_CG33836.
dme:Dmel_CG33839.
dme:Dmel_CG33842.
dme:Dmel_CG33845.
dme:Dmel_CG33848.
dme:Dmel_CG33851.
dme:Dmel_CG33854.
dme:Dmel_CG33857.
dme:Dmel_CG33860.
dme:Dmel_CG33863.
dme:Dmel_CG33866.

Organism-specific databases

CTD318847.
3771723.
3771729.
3771771.
3771792.
3771959.
3772032.
3772149.
3772163.
3772173.
3772189.
3772191.
3772198.
3772231.
3772370.
3772374.
3772421.
3772489.
3772517.
3772518.
3772552.
3772607.
3772619.
FlyBaseFBgn0001199. His3.
FBgn0051613. His3:CG31613.
FBgn0053803. His3:CG33803.
FBgn0053806. His3:CG33806.
FBgn0053809. His3:CG33809.
FBgn0053812. His3:CG33812.
FBgn0053815. His3:CG33815.
FBgn0053818. His3:CG33818.
FBgn0053821. His3:CG33821.
FBgn0053824. His3:CG33824.
FBgn0053827. His3:CG33827.
FBgn0053830. His3:CG33830.
FBgn0053833. His3:CG33833.
FBgn0053836. His3:CG33836.
FBgn0053839. His3:CG33839.
FBgn0053842. His3:CG33842.
FBgn0053845. His3:CG33845.
FBgn0053848. His3:CG33848.
FBgn0053851. His3:CG33851.
FBgn0053854. His3:CG33854.
FBgn0053857. His3:CG33857.
FBgn0053860. His3:CG33860.
FBgn0053863. His3:CG33863.
FBgn0053866. His3:CG33866.

Phylogenomic databases

eggNOGCOG2036.
GeneTreeENSGT00750000117468.
InParanoidP02299.
KOK11253.
OMARISKMAR.
OrthoDBEOG7HB5C2.
PhylomeDBP02299.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000164. Histone_H3.
[Graphical view]
PANTHERPTHR11426. PTHR11426. 1 hit.
PfamPF00125. Histone. 1 hit.
[Graphical view]
PRINTSPR00622. HISTONEH3.
SMARTSM00428. H3. 1 hit.
[Graphical view]
SUPFAMSSF47113. SSF47113. 1 hit.
PROSITEPS00322. HISTONE_H3_1. 1 hit.
PS00959. HISTONE_H3_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP02299.
NextBio846322.

Entry information

Entry nameH3_DROME
AccessionPrimary (citable) accession number: P02299
Secondary accession number(s): Q4ABE4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 144 of the entry and version 4 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