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P84249 (H33_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone H3.3
Alternative name(s):
H3.3Q
H3.A/B
Gene names
Name:His3.3A
ORF Names:CG5825
AND
Name:His3.3B
ORF Names:CG8989
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

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. Ref.10

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.10

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

Miscellaneous

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

Sequence similarities

Belongs to the histone H3 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 136135Histone H3.3
PRO_0000221302

Amino acid modifications

Modified residue51N6,N6,N6-trimethyllysine; alternate Ref.10
Modified residue51N6,N6-dimethyllysine; alternate Ref.10
Modified residue51N6-methyllysine; alternate Ref.10
Modified residue101N6,N6-dimethyllysine; alternate Ref.10
Modified residue101N6-acetyllysine; alternate Ref.6 Ref.10
Modified residue101N6-methyllysine; alternate Ref.10
Modified residue111Phosphoserine By similarity
Modified residue151N6,N6-dimethyllysine; alternate Ref.10
Modified residue151N6-acetyllysine; alternate Ref.6 Ref.7 Ref.10
Modified residue151N6-methyllysine; alternate Ref.10
Modified residue191N6-acetyllysine Ref.10
Modified residue241N6-acetyllysine Ref.10
Modified residue281N6,N6,N6-trimethyllysine; alternate Ref.10
Modified residue281N6,N6-dimethyllysine; alternate Ref.10
Modified residue281N6-methyllysine; alternate Ref.10
Modified residue371N6,N6-dimethyllysine; alternate Ref.10
Modified residue371N6-methyllysine; alternate Ref.10
Modified residue381N6,N6-dimethyllysine; alternate Ref.10
Modified residue381N6-methyllysine; alternate Ref.10
Modified residue801N6,N6-dimethyllysine; alternate Ref.10 Ref.11
Modified residue801N6-methyllysine; alternate Ref.10 Ref.11

Sequences

Sequence LengthMass (Da)Tools
P84249 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 5158ED279E6F9E1C

FASTA13615,328
        10         20         30         40         50         60 
MARTKQTARK STGGKAPRKQ LATKAARKSA PSTGGVKKPH RYRPGTVALR EIRRYQKSTE 

        70         80         90        100        110        120 
LLIRKLPFQR LVREIAQDFK TDLRFQSAAI GALQEASEAY LVGLFEDTNL CAIHAKRVTI 

       130 
MPKDIQLARR IRGERA 

« Hide

References

« Hide 'large scale' references
[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. 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] (HIS3.3A AND HIS3.3B).
Strain: Berkeley.
[4]"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.
[5]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS61220.
RefSeqNP_001259374.1. NM_001272445.1.
NP_001260082.1. NM_001273153.1.
NP_511095.1. NM_078540.4.
NP_523479.1. NM_078755.3.
NP_723056.2. NM_164624.3.
NP_727314.1. NM_167180.4.
NP_788892.1. NM_176719.1.
UniGeneDm.2931.
Dm.35099.
Dm.7418.

3D structure databases

ProteinModelPortalP84249.
SMRP84249. Positions 17-136.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid58303. 8 interactions.
59912. 17 interactions.
IntActP84249. 7 interactions.
MINTMINT-840146.

Proteomic databases

PaxDbP84249.
PRIDEP84249.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0071345; FBpp0071280; FBgn0004828.
FBtr0071346; FBpp0071281; FBgn0004828.
FBtr0071347; FBpp0071282; FBgn0004828.
FBtr0079010; FBpp0078649; FBgn0014857.
FBtr0333476; FBpp0305663; FBgn0004828.
FBtr0333536; FBpp0305716; FBgn0014857.
FBtr0333537; FBpp0305717; FBgn0014857.
GeneID31848.
33736.
KEGGdme:Dmel_CG5825.
dme:Dmel_CG8989.

Organism-specific databases

CTD31848.
33736.
FlyBaseFBgn0014857. His3.3A.
FBgn0004828. His3.3B.

Phylogenomic databases

eggNOGCOG2036.
GeneTreeENSGT00750000117538.
InParanoidP84249.
KOK11253.
OMAHIVMART.
OrthoDBEOG7HB5C2.
PhylomeDBP84249.

Gene expression databases

BgeeP84249.

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

NextBio775637.
PROP84249.

Entry information

Entry nameH33_DROME
AccessionPrimary (citable) accession number: P84249
Secondary accession number(s): A4V466 expand/collapse secondary AC list , P06351, P33155, Q9V3W4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase