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Protein

Histone H3.3

Gene

His3.3A

more
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes and is specifically enriched in modifications associated with active chromatin. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. 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.1 Publication

GO - Molecular functioni

  • DNA binding Source: UniProtKB
  • nucleosomal DNA binding Source: GO_Central

GO - Biological processi

  • cell adhesion Source: FlyBase
  • male meiosis Source: FlyBase
  • nucleosome assembly Source: UniProtKB
  • regulation of cell shape Source: FlyBase
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-DME-212300. PRC2 methylates histones and DNA.
R-DME-2559580. Oxidative Stress Induced Senescence.
R-DME-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-DME-427359. SIRT1 negatively regulates rRNA Expression.
R-DME-427413. NoRC negatively regulates rRNA expression.
R-DME-5578749. Transcriptional regulation by small RNAs.
R-DME-73777. RNA Polymerase I Chain Elongation.
R-DME-983231. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H3.3
Alternative name(s):
H3.3Q
H3.A/B
Gene namesi
Name:His3.3A
ORF Names:CG5825
AND
Name:His3.3B
ORF Names:CG8989
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componentsi: Chromosome 2L, Chromosome X

Organism-specific databases

FlyBaseiFBgn0014857. His3.3A.
FBgn0004828. His3.3B.

Subcellular locationi

GO - Cellular componenti

  • nucleosome Source: UniProtKB
  • nucleus Source: GO_Central
  • polytene chromosome Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002213022 – 136Histone H3.3Add BLAST135

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei5N6,N6,N6-trimethyllysine; alternate1 Publication1
Modified residuei5N6,N6-dimethyllysine; alternate1 Publication1
Modified residuei5N6-methyllysine; alternate1 Publication1
Modified residuei10N6,N6-dimethyllysine; alternate1 Publication1
Modified residuei10N6-acetyllysine; alternate2 Publications1
Modified residuei10N6-methyllysine; alternate1 Publication1
Modified residuei11PhosphoserineBy similarity1
Modified residuei15N6,N6-dimethyllysine; alternate1 Publication1
Modified residuei15N6-acetyllysine; alternate3 Publications1
Modified residuei15N6-methyllysine; alternate1 Publication1
Modified residuei19N6-acetyllysine1 Publication1
Modified residuei24N6-acetyllysine1 Publication1
Modified residuei28N6,N6,N6-trimethyllysine; alternate1 Publication1
Modified residuei28N6,N6-dimethyllysine; alternate1 Publication1
Modified residuei28N6-methyllysine; alternate1 Publication1
Modified residuei37N6,N6-dimethyllysine; alternate1 Publication1
Modified residuei37N6-methyllysine; alternate1 Publication1
Modified residuei38N6,N6-dimethyllysine; alternate1 Publication1
Modified residuei38N6-methyllysine; alternate1 Publication1
Modified residuei80N6,N6-dimethyllysine; alternate2 Publications1
Modified residuei80N6-methyllysine; alternate2 Publications1

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.4 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.3 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.2 Publications

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PaxDbiP84249.
PRIDEiP84249.

Expressioni

Gene expression databases

BgeeiFBgn0004828.
ExpressionAtlasiP84249. baseline.
GenevisibleiP84249. DM.

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

BioGridi58303. 8 interactors.
59912. 19 interactors.
IntActiP84249. 7 interactors.
MINTiMINT-840146.
STRINGi7227.FBpp0305663.

Structurei

3D structure databases

ProteinModelPortaliP84249.
SMRiP84249.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H3 family.Curated

Phylogenomic databases

eggNOGiKOG1745. Eukaryota.
COG2036. LUCA.
GeneTreeiENSGT00760000118967.
InParanoidiP84249.
KOiK11253.
OMAiCHASMAR.
OrthoDBiEOG091G0XGD.
PhylomeDBiP84249.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_H2A/H2B/H3.
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.

P84249-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARTKQTARK STGGKAPRKQ LATKAARKSA PSTGGVKKPH RYRPGTVALR
60 70 80 90 100
EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSAAI GALQEASEAY
110 120 130
LVGLFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA
Length:136
Mass (Da):15,328
Last modified:January 23, 2007 - v2
Checksum:i5158ED279E6F9E1C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53822 mRNA. Translation: CAA37819.1.
X82257 mRNA. Translation: CAA57712.1.
X81205 Genomic DNA. Translation: CAA57077.1.
X81207 Genomic DNA. Translation: CAA57080.1.
AE014298 Genomic DNA. Translation: AAF46452.1.
AE014134 Genomic DNA. Translation: AAF52213.1.
AE014298 Genomic DNA. Translation: AAN09245.1.
AE014298 Genomic DNA. Translation: AAO41645.1.
AY071057 mRNA. Translation: AAL48679.1.
AY118325 mRNA. Translation: AAM48354.1.
AY119629 mRNA. Translation: AAM50283.1.
PIRiS61220.
RefSeqiNP_001259374.1. NM_001272445.2.
NP_001260082.1. NM_001273153.1.
NP_511095.1. NM_078540.5.
NP_523479.1. NM_078755.3.
NP_723056.2. NM_164624.3.
NP_727314.1. NM_167180.4.
NP_788892.1. NM_176719.1.
UniGeneiDm.2931.
Dm.35099.
Dm.7418.

Genome annotation databases

EnsemblMetazoaiFBtr0071345; FBpp0071280; FBgn0004828.
FBtr0071346; FBpp0071281; FBgn0004828.
FBtr0071347; FBpp0071282; FBgn0004828.
FBtr0079010; FBpp0078649; FBgn0014857.
FBtr0333536; FBpp0305716; FBgn0014857.
FBtr0333537; FBpp0305717; FBgn0014857.
FBtr0340343; FBpp0309302; FBgn0004828.
GeneIDi31848.
33736.
KEGGidme:Dmel_CG5825.
dme:Dmel_CG8989.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53822 mRNA. Translation: CAA37819.1.
X82257 mRNA. Translation: CAA57712.1.
X81205 Genomic DNA. Translation: CAA57077.1.
X81207 Genomic DNA. Translation: CAA57080.1.
AE014298 Genomic DNA. Translation: AAF46452.1.
AE014134 Genomic DNA. Translation: AAF52213.1.
AE014298 Genomic DNA. Translation: AAN09245.1.
AE014298 Genomic DNA. Translation: AAO41645.1.
AY071057 mRNA. Translation: AAL48679.1.
AY118325 mRNA. Translation: AAM48354.1.
AY119629 mRNA. Translation: AAM50283.1.
PIRiS61220.
RefSeqiNP_001259374.1. NM_001272445.2.
NP_001260082.1. NM_001273153.1.
NP_511095.1. NM_078540.5.
NP_523479.1. NM_078755.3.
NP_723056.2. NM_164624.3.
NP_727314.1. NM_167180.4.
NP_788892.1. NM_176719.1.
UniGeneiDm.2931.
Dm.35099.
Dm.7418.

3D structure databases

ProteinModelPortaliP84249.
SMRiP84249.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi58303. 8 interactors.
59912. 19 interactors.
IntActiP84249. 7 interactors.
MINTiMINT-840146.
STRINGi7227.FBpp0305663.

Proteomic databases

PaxDbiP84249.
PRIDEiP84249.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0071345; FBpp0071280; FBgn0004828.
FBtr0071346; FBpp0071281; FBgn0004828.
FBtr0071347; FBpp0071282; FBgn0004828.
FBtr0079010; FBpp0078649; FBgn0014857.
FBtr0333536; FBpp0305716; FBgn0014857.
FBtr0333537; FBpp0305717; FBgn0014857.
FBtr0340343; FBpp0309302; FBgn0004828.
GeneIDi31848.
33736.
KEGGidme:Dmel_CG5825.
dme:Dmel_CG8989.

Organism-specific databases

CTDi31848.
33736.
FlyBaseiFBgn0014857. His3.3A.
FBgn0004828. His3.3B.

Phylogenomic databases

eggNOGiKOG1745. Eukaryota.
COG2036. LUCA.
GeneTreeiENSGT00760000118967.
InParanoidiP84249.
KOiK11253.
OMAiCHASMAR.
OrthoDBiEOG091G0XGD.
PhylomeDBiP84249.

Enzyme and pathway databases

ReactomeiR-DME-212300. PRC2 methylates histones and DNA.
R-DME-2559580. Oxidative Stress Induced Senescence.
R-DME-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-DME-427359. SIRT1 negatively regulates rRNA Expression.
R-DME-427413. NoRC negatively regulates rRNA expression.
R-DME-5578749. Transcriptional regulation by small RNAs.
R-DME-73777. RNA Polymerase I Chain Elongation.
R-DME-983231. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

PROiP84249.

Gene expression databases

BgeeiFBgn0004828.
ExpressionAtlasiP84249. baseline.
GenevisibleiP84249. DM.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_H2A/H2B/H3.
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...

Entry informationi

Entry nameiH33_DROME
AccessioniPrimary (citable) accession number: P84249
Secondary accession number(s): A4V466
, P06351, P33155, Q9V3W4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

This histone is the predominant form in non-dividing cells.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.