P84249 (H33_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	136 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. 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.

Ontologies

Keywords
Cellular component	Chromosome Nucleosome core Nucleus
Ligand	DNA-binding
PTM	Acetylation Methylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Inferred from mutant phenotype PubMed 14527345. Source: FlyBase male meiosis Inferred from genetic interaction PubMed 19781938. Source: FlyBase nucleosome assembly Non-traceable author statement Ref.1Ref.2. Source: UniProtKB regulation of cell shape Inferred from mutant phenotype PubMed 14527345. Source: FlyBase
Cellular_component	nucleosome Non-traceable author statement Ref.1Ref.2. Source: UniProtKB nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell polytene chromosome Inferred from direct assay PubMed 19781938. Source: FlyBase
Molecular_function	DNA binding Non-traceable author statement Ref.1Ref.2. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 136	135	Histone H3.3		PRO_0000221302
Amino acid modifications
	Modified residue	5	1	N6,N6,N6-trimethyllysine; alternate Ref.10
	Modified residue	5	1	N6,N6-dimethyllysine; alternate Ref.10
	Modified residue	5	1	N6-methyllysine; alternate Ref.10
	Modified residue	10	1	N6,N6-dimethyllysine; alternate Ref.10
	Modified residue	10	1	N6-acetyllysine; alternate Ref.6 Ref.10
	Modified residue	10	1	N6-methyllysine; alternate Ref.10
	Modified residue	11	1	Phosphoserine By similarity
	Modified residue	15	1	N6,N6-dimethyllysine; alternate Ref.10
	Modified residue	15	1	N6-acetyllysine; alternate Ref.6 Ref.7 Ref.10
	Modified residue	15	1	N6-methyllysine; alternate Ref.10
	Modified residue	19	1	N6-acetyllysine Ref.10
	Modified residue	24	1	N6-acetyllysine Ref.10
	Modified residue	28	1	N6,N6,N6-trimethyllysine; alternate Ref.10
	Modified residue	28	1	N6,N6-dimethyllysine; alternate Ref.10
	Modified residue	28	1	N6-methyllysine; alternate Ref.10
	Modified residue	37	1	N6,N6-dimethyllysine; alternate Ref.10
	Modified residue	37	1	N6-methyllysine; alternate Ref.10
	Modified residue	38	1	N6,N6-dimethyllysine; alternate Ref.10
	Modified residue	38	1	N6-methyllysine; alternate Ref.10
	Modified residue	80	1	N6,N6-dimethyllysine; alternate Ref.10 Ref.11
	Modified residue	80	1	N6-methyllysine; alternate Ref.10 Ref.11

Sequences

	Sequence		Length	Mass (Da)
	P84249 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 5158ED279E6F9E1C	FASTA	136	15,328
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, 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.
PIR	S61220.
RefSeq	NP_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.
UniGene	Dm.2931. Dm.35099. Dm.7418.
3D structure databases
ProteinModelPortal	P84249.
ModBase	Search...
Protein-protein interaction databases
IntAct	P84249. 6 interactions.
MINT	MINT-840146.
Proteomic databases
PaxDb	P84249.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0071345; FBpp0071280; FBgn0004828. FBtr0071346; FBpp0071281; FBgn0004828. FBtr0071347; FBpp0071282; FBgn0004828. FBtr0079010; FBpp0078649; FBgn0014857. FBtr0333476; FBpp0305663; FBgn0004828. FBtr0333536; FBpp0305716; FBgn0014857. FBtr0333537; FBpp0305717; FBgn0014857.
GeneID	31848. 33736.
KEGG	dme:Dmel_CG5825. dme:Dmel_CG8989.
Organism-specific databases
CTD	31848. 33736.
FlyBase	FBgn0014857. His3.3A. FBgn0004828. His3.3B.
Phylogenomic databases
eggNOG	COG2036.
GeneTree	ENSGT00670000097754.
InParanoid	P84249.
KO	K11253.
OMA	CCIRGER.
OrthoDB	EOG4M37RZ.
PhylomeDB	P84249.
Gene expression databases
Bgee	P84249.
GermOnline	CG5825. Drosophila melanogaster. CG8989. Drosophila melanogaster.
Family and domain databases
Gene3D	1.10.20.10. 1 hit.
InterPro	IPR009072. Histone-fold. IPR007125. Histone_core_D. IPR000164. Histone_H3. [Graphical view]
PANTHER	PTHR11426. PTHR11426. 1 hit.
Pfam	PF00125. Histone. 1 hit. [Graphical view]
PRINTS	PR00622. HISTONEH3.
SMART	SM00428. H3. 1 hit. [Graphical view]
SUPFAM	SSF47113. Histone-fold. 1 hit.
PROSITE	PS00322. HISTONE_H3_1. 1 hit. PS00959. HISTONE_H3_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	775637.

Entry information

Entry name

H33_DROME

Accession

Primary (citable) accession number: P84249
Secondary accession number(s): A4V466 , P06351, P33155, Q9V3W4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project