Reviewed, UniProtKB/Swiss-Prot P02299 (H3_DROME)

Names and origin

Protein names

Recommended name:
    Histone H3

Gene names

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

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

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	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.
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	NucleusBy 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.
Sequence similarities	Belongs to the histone H3 family.

Ontologies

Keywords
Cellular component	Chromosomal protein Nucleosome core Nucleus
Ligand	DNA-binding
PTM	Acetylation Methylation Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	nucleosome assembly Inferred from electronic annotation. Source: InterPro
Cellular component	RCAF complex Inferred from direct assay. Source: FlyBase nucleosome Inferred from electronic annotation. Source: InterPro polytene chromosome Inferred from direct assay. Source: FlyBase
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EP300	Q09472	1	EBI-522090,EBI-447295	From a different organism.
GATAD2A	Q86YP4	1	EBI-522090,EBI-726224	From a different organism.
GATAD2B	Q8WXI9	1	EBI-522090,EBI-923440	From a different organism.
PCAF	Q92831	1	EBI-522090,EBI-477430	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 136

135

Histone H3

PRO_0000221300

Regions

Region

6 – 11

6

Su(var)205 chromodomain-binding

Amino acid modifications

Modified residue

5

1

N6,N6,N6-trimethyllysine; alternate

Modified residue

5

1

N6,N6-dimethyllysine; alternate

Modified residue

5

1

N6-methyllysine; alternate

Modified residue

10

1

N6,N6-dimethyllysine; alternate

Modified residue

10

1

N6-methyllysine; alternate

Modified residue

11

1

Phosphoserine

Modified residue

15

1

N6,N6-dimethyllysine; alternate

Modified residue

15

1

N6-acetyllysine; alternate

Modified residue

15

1

N6-methyllysine; alternate

Modified residue

19

1

N6-acetyllysine

Modified residue

24

1

N6-acetyllysine

Modified residue

28

1

N6,N6,N6-trimethyllysine; alternate

Modified residue

28

1

N6,N6-dimethyllysine; alternate

Modified residue

28

1

N6-methyllysine; alternate

Modified residue

37

1

N6,N6-dimethyllysine; alternate

Modified residue

37

1

N6-methyllysine; alternate

Modified residue

38

1

N6,N6-dimethyllysine; alternate

Modified residue

38

1

N6-methyllysine; alternate

Modified residue

80

1

N6,N6-dimethyllysine; alternate

Modified residue

80

1

N6-methyllysine; alternate

Experimental info

Sequence conflict

118

1

V → I Ref.1 Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

136

Helix Strand Turn

Details...

Helix

46 – 57

12

Helix

65 – 77

13

Beta strand

80 – 82

3

Helix

87 – 114

28

Beta strand

118 – 120

3

Helix

122 – 131

10

Sequences

	Sequence		Length	Mass (Da)
	P02299-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 6FD8508EA50A0EEC	FASTA	136	15,388
	10 20 30 40 50 60 MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE 70 80 90 100 110 120 LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEASEAY LVGLFEDTNL CAIHAKRVTI 130 MPKDIQLARR IRGERA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2536150] [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: 10991787] [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: 10731132] [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]	"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: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[6]	"Phosphorylation of histone H3 correlates with transcriptionally active loci." Nowak S.J., Corces V.G. Genes Dev. 14:3003-3013(2000) [PubMed: 11114889] [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: 11371341] [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: 11266459] [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: 12514098] [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: 15175259] [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: 14732680] [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, 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: 15371351] [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: 16230526] [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: 11859155] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-17, ACETYLATION AT LYS-10.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

PIR

A02630.
S10097.

RefSeq

NP_001027285.1.
NP_001027289.1.
NP_001027294.1.
NP_001027298.1.
NP_001027303.1.
NP_001027308.1.
NP_001027313.1.
NP_001027318.1.
NP_001027323.1.
NP_001027328.1.
NP_001027333.1.
NP_001027338.1.
NP_001027343.1.
NP_001027348.1.
NP_001027353.1.
NP_001027358.1.
NP_001027363.1.
NP_001027368.1.
NP_001027373.1.
NP_001027378.1.
NP_001027383.1.
NP_001027387.1.
NP_724345.1.

UniGene

Dm.29515
Dm.34559
Dm.34566
Dm.34567

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KNA	X-ray	2.10	P	1-16	[»]
1KNE	X-ray	2.40	P	1-16	[»]
2NQB	X-ray	2.30	A/E	2-136	[»]
2PYO	X-ray	2.43	A/E	2-136	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P02299.

Genome annotation databases

Ensembl

CG31613. Drosophila melanogaster. [Contig view]
CG33803. Drosophila melanogaster. [Contig view]
CG33806. Drosophila melanogaster. [Contig view]
CG33809. Drosophila melanogaster. [Contig view]
CG33812. Drosophila melanogaster. [Contig view]
CG33815. Drosophila melanogaster. [Contig view]
CG33818. Drosophila melanogaster. [Contig view]
CG33821. Drosophila melanogaster. [Contig view]
CG33824. Drosophila melanogaster. [Contig view]
CG33827. Drosophila melanogaster. [Contig view]
CG33830. Drosophila melanogaster. [Contig view]
CG33833. Drosophila melanogaster. [Contig view]
CG33836. Drosophila melanogaster. [Contig view]
CG33839. Drosophila melanogaster. [Contig view]
CG33842. Drosophila melanogaster. [Contig view]
CG33845. Drosophila melanogaster. [Contig view]
CG33848. Drosophila melanogaster. [Contig view]
CG33851. Drosophila melanogaster. [Contig view]
CG33854. Drosophila melanogaster. [Contig view]
CG33857. Drosophila melanogaster. [Contig view]
CG33860. Drosophila melanogaster. [Contig view]
CG33863. Drosophila melanogaster. [Contig view]
CG33866. Drosophila melanogaster. [Contig view]

GeneID

318847.
3771723.
3771729.
3771771.
3771792.
3771959.
3772032.
3772149.
3772163.
3772173.
3772189.
3772191.
3772198.