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P84249

- H33_DROME

UniProt

P84249 - H33_DROME

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Protein

Histone H3.3

Gene

His3.3A

more
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - 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

  1. DNA binding Source: UniProtKB

GO - Biological processi

  1. cell adhesion Source: FlyBase
  2. male meiosis Source: FlyBase
  3. nucleosome assembly Source: UniProtKB
  4. regulation of cell shape Source: FlyBase
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_180258. Factors involved in megakaryocyte development and platelet production.
REACT_271477. PRC2 methylates histones and DNA.

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
ProteomesiUP000000803: Chromosome 2L, UP000000803: Chromosome X

Organism-specific databases

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

Subcellular locationi

Nucleus By similarity. Chromosome By similarity

GO - Cellular componenti

  1. nucleosome Source: UniProtKB
  2. nucleus Source: UniProtKB-KW
  3. polytene chromosome Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 136135Histone H3.3PRO_0000221302Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51N6,N6,N6-trimethyllysine; alternate1 Publication
Modified residuei5 – 51N6,N6-dimethyllysine; alternate1 Publication
Modified residuei5 – 51N6-methyllysine; alternate1 Publication
Modified residuei10 – 101N6,N6-dimethyllysine; alternate1 Publication
Modified residuei10 – 101N6-acetyllysine; alternate2 Publications
Modified residuei10 – 101N6-methyllysine; alternate1 Publication
Modified residuei11 – 111PhosphoserineBy similarity
Modified residuei15 – 151N6,N6-dimethyllysine; alternate1 Publication
Modified residuei15 – 151N6-acetyllysine; alternate3 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; alternate2 Publications
Modified residuei80 – 801N6-methyllysine; alternate2 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.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

BgeeiP84249.
ExpressionAtlasiP84249. differential.

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 interactions.
59912. 18 interactions.
IntActiP84249. 7 interactions.
MINTiMINT-840146.

Structurei

3D structure databases

ProteinModelPortaliP84249.
SMRiP84249. Positions 17-136.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H3 family.Curated

Phylogenomic databases

eggNOGiCOG2036.
GeneTreeiENSGT00760000118967.
InParanoidiP84249.
KOiK11253.
OMAiHIVMART.
OrthoDBiEOG7HB5C2.
PhylomeDBiP84249.

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.

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.
FBtr0333476; FBpp0305663; FBgn0004828.
FBtr0333536; FBpp0305716; FBgn0014857.
FBtr0333537; FBpp0305717; FBgn0014857.
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 .
PIRi S61220.
RefSeqi NP_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.
UniGenei Dm.2931.
Dm.35099.
Dm.7418.

3D structure databases

ProteinModelPortali P84249.
SMRi P84249. Positions 17-136.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 58303. 8 interactions.
59912. 18 interactions.
IntActi P84249. 7 interactions.
MINTi MINT-840146.

Proteomic databases

PaxDbi P84249.
PRIDEi P84249.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0071345 ; FBpp0071280 ; FBgn0004828 .
FBtr0071346 ; FBpp0071281 ; FBgn0004828 .
FBtr0071347 ; FBpp0071282 ; FBgn0004828 .
FBtr0079010 ; FBpp0078649 ; FBgn0014857 .
FBtr0333476 ; FBpp0305663 ; FBgn0004828 .
FBtr0333536 ; FBpp0305716 ; FBgn0014857 .
FBtr0333537 ; FBpp0305717 ; FBgn0014857 .
GeneIDi 31848.
33736.
KEGGi dme:Dmel_CG5825.
dme:Dmel_CG8989.

Organism-specific databases

CTDi 31848.
33736.
FlyBasei FBgn0014857. His3.3A.
FBgn0004828. His3.3B.

Phylogenomic databases

eggNOGi COG2036.
GeneTreei ENSGT00760000118967.
InParanoidi P84249.
KOi K11253.
OMAi HIVMART.
OrthoDBi EOG7HB5C2.
PhylomeDBi P84249.

Enzyme and pathway databases

Reactomei REACT_180258. Factors involved in megakaryocyte development and platelet production.
REACT_271477. PRC2 methylates histones and DNA.

Miscellaneous databases

NextBioi 775637.
PROi P84249.

Gene expression databases

Bgeei P84249.
ExpressionAtlasi P84249. differential.

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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A Drosophila melanogaster H3.3 cDNA encodes a histone variant identical with the vertebrate H3.3."
    Fretzin S., Allan B.D., van Daal A., Elgin S.C.R.
    Gene 107:341-342(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (HIS3.3B).
  2. "Structure and expression of histone H3.3 genes in Drosophila melanogaster and Drosophila hydei."
    Akhmanova A.S., Bindels P.S.T., Xu J., Miedema K., Kremer H., Hennig W.
    Genome 38:586-600(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (HIS3.3A AND HIS3.3B).
    Strain: Canton-S.
  3. "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] (HIS3.3A AND HIS3.3B).
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (HIS3.3A AND HIS3.3B).
    Strain: Berkeley.
    Tissue: Embryo.
  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. "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: FUNCTION, 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.
  11. "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.

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 26, 2014
This is version 97 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

External Data

Dasty 3