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Protein

Histone H3

Gene

His3

more
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: 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-KW
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_285740. PKMTs methylate histone lysines.
REACT_287092. Factors involved in megakaryocyte development and platelet production.
REACT_305574. RMTs methylate histone arginines.
REACT_307216. HATs acetylate histones.
REACT_319512. HDMs demethylate histones.
REACT_344008. PRC2 methylates histones and DNA.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H3
Gene namesi
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
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0001199. 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.

Subcellular locationi

  1. Nucleus By similarity
  2. Chromosome By similarity

GO - Cellular componenti

  1. nucleosome Source: UniProtKB-KW
  2. 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
Chaini2 – 136135Histone H3PRO_0000221300Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51N6,N6,N6-trimethyllysine; alternate2 Publications
Modified residuei5 – 51N6,N6-dimethyllysine; alternate2 Publications
Modified residuei5 – 51N6-methyllysine; alternate2 Publications
Modified residuei10 – 101N6,N6-dimethyllysine; alternate1 Publication
Modified residuei10 – 101N6-acetyllysine; alternate3 Publications
Modified residuei10 – 101N6-methyllysine; alternate1 Publication
Modified residuei11 – 111Phosphoserine5 Publications
Modified residuei15 – 151N6,N6-dimethyllysine; alternate1 Publication
Modified residuei15 – 151N6-acetyllysine; alternate4 Publications
Modified residuei15 – 151N6-methyllysine; alternate1 Publication
Modified residuei19 – 191N6-acetyllysine1 Publication
Modified residuei24 – 241N6-acetyllysine1 Publication
Modified residuei28 – 281N6,N6,N6-trimethyllysine; alternate1 Publication
Modified residuei28 – 281N6,N6-dimethyllysine; alternate1 Publication
Modified residuei28 – 281N6-methyllysine; alternate1 Publication
Modified residuei37 – 371N6,N6-dimethyllysine; alternate1 Publication
Modified residuei37 – 371N6-methyllysine; alternate1 Publication
Modified residuei38 – 381N6,N6-dimethyllysine; alternate1 Publication
Modified residuei38 – 381N6-methyllysine; alternate1 Publication
Modified residuei80 – 801N6,N6-dimethyllysine; alternate3 Publications
Modified residuei80 – 801N6-methyllysine; alternate3 Publications

Post-translational modificationi

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.5 Publications
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.5 Publications
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.3 Publications

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PaxDbiP02299.
PRIDEiP02299.

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
KAT2BQ928312EBI-522090,EBI-477430From a different organism.
ScmQ9VHA04EBI-522090,EBI-89256

Protein-protein interaction databases

BioGridi77140. 10 interactions.
DIPiDIP-38722N.
IntActiP02299. 15 interactions.
MINTiMINT-271349.
STRINGi7227.FBpp0091051.

Structurei

Secondary structure

1
136
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi46 – 5712Combined sources
Helixi65 – 7713Combined sources
Beta strandi80 – 823Combined sources
Helixi87 – 11428Combined sources
Beta strandi118 – 1203Combined sources
Helixi122 – 13110Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4UUZX-ray2.90A1-136[»]
4X23X-ray3.50A/E/K/O41-133[»]
ProteinModelPortaliP02299.
SMRiP02299. Positions 17-136.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02299.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni6 – 116Su(var)205 chromodomain-binding

Sequence similaritiesi

Belongs to the histone H3 family.Curated

Phylogenomic databases

eggNOGiCOG2036.
GeneTreeiENSGT00760000118967.
InParanoidiP02299.
KOiK11253.
OMAiRISKMAR.
OrthoDBiEOG7HB5C2.
PhylomeDBiP02299.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000164. Histone_H3/CENP-A.
[Graphical view]
PANTHERiPTHR11426. PTHR11426. 1 hit.
PfamiPF00125. Histone. 1 hit.
[Graphical view]
PRINTSiPR00622. HISTONEH3.
SMARTiSM00428. H3. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00322. HISTONE_H3_1. 1 hit.
PS00959. HISTONE_H3_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02299-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR
60 70 80 90 100
EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEASEAY
110 120 130
LVGLFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA
Length:136
Mass (Da):15,388
Last modified:January 23, 2007 - v4
Checksum:i6FD8508EA50A0EEC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti118 – 1181V → I (PubMed:2536150).Curated
Sequence conflicti118 – 1181V → I (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA02630.
S10097.
RefSeqiNP_001027285.1. NM_001032114.2.
NP_001027289.1. NM_001032118.2.
NP_001027294.1. NM_001032123.2.
NP_001027298.1. NM_001032127.2.
NP_001027303.1. NM_001032132.2.
NP_001027308.1. NM_001032137.2.
NP_001027313.1. NM_001032142.2.
NP_001027318.1. NM_001032147.2.
NP_001027323.1. NM_001032152.2.
NP_001027328.1. NM_001032157.2.
NP_001027333.1. NM_001032162.2.
NP_001027338.1. NM_001032167.2.
NP_001027343.1. NM_001032172.2.
NP_001027348.1. NM_001032177.2.
NP_001027353.1. NM_001032182.2.
NP_001027358.1. NM_001032187.2.
NP_001027363.1. NM_001032192.2.
NP_001027368.1. NM_001032197.2.
NP_001027373.1. NM_001032202.2.
NP_001027378.1. NM_001032207.2.
NP_001027383.1. NM_001032212.2.
NP_001027387.1. NM_001032216.2.
NP_724345.1. NM_165384.3.

Genome annotation databases

EnsemblMetazoaiFBtr0085894; 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.
GeneIDi318847.
3771723.
3771729.
3771771.
3771792.
3771959.
3772032.
3772149.
3772163.
3772173.
3772189.
3772191.
3772198.
3772231.
3772370.
3772374.
3772421.
3772489.
3772517.
3772518.
3772552.
3772607.
3772619.
KEGGidme: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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA02630.
S10097.
RefSeqiNP_001027285.1. NM_001032114.2.
NP_001027289.1. NM_001032118.2.
NP_001027294.1. NM_001032123.2.
NP_001027298.1. NM_001032127.2.
NP_001027303.1. NM_001032132.2.
NP_001027308.1. NM_001032137.2.
NP_001027313.1. NM_001032142.2.
NP_001027318.1. NM_001032147.2.
NP_001027323.1. NM_001032152.2.
NP_001027328.1. NM_001032157.2.
NP_001027333.1. NM_001032162.2.
NP_001027338.1. NM_001032167.2.
NP_001027343.1. NM_001032172.2.
NP_001027348.1. NM_001032177.2.
NP_001027353.1. NM_001032182.2.
NP_001027358.1. NM_001032187.2.
NP_001027363.1. NM_001032192.2.
NP_001027368.1. NM_001032197.2.
NP_001027373.1. NM_001032202.2.
NP_001027378.1. NM_001032207.2.
NP_001027383.1. NM_001032212.2.
NP_001027387.1. NM_001032216.2.
NP_724345.1. NM_165384.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4UUZX-ray2.90A1-136[»]
4X23X-ray3.50A/E/K/O41-133[»]
ProteinModelPortaliP02299.
SMRiP02299. Positions 17-136.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi77140. 10 interactions.
DIPiDIP-38722N.
IntActiP02299. 15 interactions.
MINTiMINT-271349.
STRINGi7227.FBpp0091051.

Proteomic databases

PaxDbiP02299.
PRIDEiP02299.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0085894; 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.
GeneIDi318847.
3771723.
3771729.
3771771.
3771792.
3771959.
3772032.
3772149.
3772163.
3772173.
3772189.
3772191.
3772198.
3772231.
3772370.
3772374.
3772421.
3772489.
3772517.
3772518.
3772552.
3772607.
3772619.
KEGGidme: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

CTDi318847.
3771723.
3771729.
3771771.
3771792.
3771959.
3772032.
3772149.
3772163.
3772173.
3772189.
3772191.
3772198.
3772231.
3772370.
3772374.
3772421.
3772489.
3772517.
3772518.
3772552.
3772607.
3772619.
FlyBaseiFBgn0001199. 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

eggNOGiCOG2036.
GeneTreeiENSGT00760000118967.
InParanoidiP02299.
KOiK11253.
OMAiRISKMAR.
OrthoDBiEOG7HB5C2.
PhylomeDBiP02299.

Enzyme and pathway databases

ReactomeiREACT_285740. PKMTs methylate histone lysines.
REACT_287092. Factors involved in megakaryocyte development and platelet production.
REACT_305574. RMTs methylate histone arginines.
REACT_307216. HATs acetylate histones.
REACT_319512. HDMs demethylate histones.
REACT_344008. PRC2 methylates histones and DNA.

Miscellaneous databases

EvolutionaryTraceiP02299.
NextBioi846322.
PROiP02299.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000164. Histone_H3/CENP-A.
[Graphical view]
PANTHERiPTHR11426. PTHR11426. 1 hit.
PfamiPF00125. Histone. 1 hit.
[Graphical view]
PRINTSiPR00622. HISTONEH3.
SMARTiSM00428. H3. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00322. HISTONE_H3_1. 1 hit.
PS00959. HISTONE_H3_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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] (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.
    , 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. 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.

Entry informationi

Entry nameiH3_DROME
AccessioniPrimary (citable) accession number: P02299
Secondary accession number(s): Q4ABE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 153 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.