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P02299

- H3_DROME

UniProt

P02299 - H3_DROME

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Protein

Histone H3

Gene

His3

more
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-KW
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_180258. Factors involved in megakaryocyte development and platelet production.

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: 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

Nucleus By similarity. Chromosome By similarity

GO - Cellular componenti

  1. nucleosome Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
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 – 5712
Helixi65 – 7713
Beta strandi80 – 823
Helixi87 – 11428
Beta strandi118 – 1203
Helixi122 – 13110

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
4INMX-ray3.50A/E/K/O41-136[»]
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 → I1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi A02630.
S10097.
RefSeqi NP_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:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KNA X-ray 2.10 P 2-17 [» ]
1KNE X-ray 2.40 P 2-17 [» ]
2NQB X-ray 2.30 A/E 2-136 [» ]
2PYO X-ray 2.43 A/E 2-136 [» ]
2YBA X-ray 2.55 C/D 2-20 [» ]
4INM X-ray 3.50 A/E/K/O 41-136 [» ]
ProteinModelPortali P02299.
SMRi P02299. Positions 17-136.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 77140. 10 interactions.
DIPi DIP-38722N.
IntActi P02299. 15 interactions.
MINTi MINT-271349.
STRINGi 7227.FBpp0091051.

Proteomic databases

PaxDbi P02299.
PRIDEi P02299.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0085894 ; 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 .
GeneIDi 318847.
3771723.
3771729.
3771771.
3771792.
3771959.
3772032.
3772149.
3772163.
3772173.
3772189.
3772191.
3772198.
3772231.
3772370.
3772374.
3772421.
3772489.
3772517.
3772518.
3772552.
3772607.
3772619.
KEGGi dme: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

CTDi 318847.
3771723.
3771729.
3771771.
3771792.
3771959.
3772032.
3772149.
3772163.
3772173.
3772189.
3772191.
3772198.
3772231.
3772370.
3772374.
3772421.
3772489.
3772517.
3772518.
3772552.
3772607.
3772619.
FlyBasei FBgn0001199. 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

eggNOGi COG2036.
GeneTreei ENSGT00760000118967.
InParanoidi P02299.
KOi K11253.
OMAi RISKMAR.
OrthoDBi EOG7HB5C2.
PhylomeDBi P02299.

Enzyme and pathway databases

Reactomei REACT_180258. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

EvolutionaryTracei P02299.
NextBioi 846322.

Family and domain databases

Gene3Di 1.10.20.10. 1 hit.
InterProi IPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000164. Histone_H3/CENP-A.
[Graphical view ]
PANTHERi PTHR11426. PTHR11426. 1 hit.
Pfami PF00125. Histone. 1 hit.
[Graphical view ]
PRINTSi PR00622. HISTONEH3.
SMARTi SM00428. H3. 1 hit.
[Graphical view ]
SUPFAMi SSF47113. SSF47113. 1 hit.
PROSITEi PS00322. HISTONE_H3_1. 1 hit.
PS00959. HISTONE_H3_2. 1 hit.
[Graphical view ]
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Publicationsi

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  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: October 29, 2014
This is version 147 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

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