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Histone H3

 H3_DROME                Reviewed;         136 AA.
P02299; Q4ABE4;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
18-JUL-2018, entry version 183.
RecName: Full=Histone H3;
Name=His3;
and
Name=His3:CG31613; ORFNames=CG31613;
and
Name=His3:CG33803; ORFNames=CG33803;
and
Name=His3:CG33806; ORFNames=CG33806;
and
Name=His3:CG33809; ORFNames=CG33809;
and
Name=His3:CG33812; ORFNames=CG33812;
and
Name=His3:CG33815; ORFNames=CG33815;
and
Name=His3:CG33818; ORFNames=CG33818;
and
Name=His3:CG33821; ORFNames=CG33821;
and
Name=His3:CG33824; ORFNames=CG33824;
and
Name=His3:CG33827; ORFNames=CG33827;
and
Name=His3:CG33830; ORFNames=CG33830;
and
Name=His3:CG33833; ORFNames=CG33833;
and
Name=His3:CG33836; ORFNames=CG33836;
and
Name=His3:CG33839; ORFNames=CG33839;
and
Name=His3:CG33842; ORFNames=CG33842;
and
Name=His3:CG33845; ORFNames=CG33845;
and
Name=His3:CG33848; ORFNames=CG33848;
and
Name=His3:CG33851; ORFNames=CG33851;
and
Name=His3:CG33854; ORFNames=CG33854;
and
Name=His3:CG33857; ORFNames=CG33857;
and
Name=His3:CG33860; ORFNames=CG33860;
and
Name=His3:CG33863; ORFNames=CG33863;
and
Name=His3:CG33866; ORFNames=CG33866;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIS3).
STRAIN=AK-194;
PubMed=2536150; DOI=10.1093/nar/17.1.225;
Matsuo Y., Yamazaki T.;
"tRNA derived insertion element in histone gene repeating unit of
Drosophila melanogaster.";
Nucleic Acids Res. 17:225-238(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIS3).
Goldberg M.L.;
Thesis (1979), University of Stanford, United States.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIS3).
STRAIN=Canton-S;
PubMed=10991787; DOI=10.1006/mpev.2000.0810;
Matsuo Y.;
"Molecular evolution of the histone 3 multigene family in the
Drosophila melanogaster species subgroup.";
Mol. Phylogenet. Evol. 16:339-343(2000).
[4]
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;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[5]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
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.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[6]
PHOSPHORYLATION AT SER-11, AND ACETYLATION AT LYS-10 AND LYS-15.
PubMed=11114889; DOI=10.1101/gad.848800;
Nowak S.J., Corces V.G.;
"Phosphorylation of histone H3 correlates with transcriptionally
active loci.";
Genes Dev. 14:3003-3013(2000).
[7]
PHOSPHORYLATION AT SER-11, AND ACETYLATION AT LYS-15.
PubMed=11371341; DOI=10.1016/S0092-8674(01)00325-7;
Wang Y., Zhang W., Jin Y., Johansen J., Johansen K.M.;
"The JIL-1 tandem kinase mediates histone H3 phosphorylation and is
required for maintenance of chromatin structure in Drosophila.";
Cell 105:433-443(2001).
[8]
PHOSPHORYLATION AT SER-11.
PubMed=11266459; DOI=10.1083/jcb.152.4.669;
Giet R., Glover D.M.;
"Drosophila aurora B kinase is required for histone H3 phosphorylation
and condensin recruitment during chromosome condensation and to
organize the central spindle during cytokinesis.";
J. Cell Biol. 152:669-682(2001).
[9]
PHOSPHORYLATION AT SER-11.
PubMed=12514098; DOI=10.1101/gad.1021403;
Labrador M., Corces V.G.;
"Phosphorylation of histone H3 during transcriptional activation
depends on promoter structure.";
Genes Dev. 17:43-48(2003).
[10]
METHYLATION AT LYS-5 AND LYS-80, AND PHOSPHORYLATION AT SER-11.
PubMed=15175259; DOI=10.1101/gad.1198204;
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.;
"The histone modification pattern of active genes revealed through
genome-wide chromatin analysis of a higher eukaryote.";
Genes Dev. 18:1263-1271(2004).
[11]
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, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=14732680; DOI=10.1073/pnas.0308092100;
McKittrick E., Gafken P.R., Ahmad K., Henikoff S.;
"Histone H3.3 is enriched in covalent modifications associated with
active chromatin.";
Proc. Natl. Acad. Sci. U.S.A. 101:1525-1530(2004).
[12]
METHYLATION AT LYS-80.
PubMed=15371351; DOI=10.1534/genetics.104.033191;
Shanower G.A., Mueller M., Blanton J.L., Honti V., Gyurkovics H.,
Schedl P.;
"Characterization of the grappa gene, the Drosophila histone H3 lysine
79 methyltransferase.";
Genetics 169:173-184(2005).
[13]
ACETYLATION AT LYS-15.
PubMed=16230526; DOI=10.1101/gad.1348905;
Ivanovska I., Khandan T., Ito T., Orr-Weaver T.L.;
"A histone code in meiosis: the histone kinase, NHK-1, is required for
proper chromosomal architecture in Drosophila oocytes.";
Genes Dev. 19:2571-2582(2005).
[14]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-17, AND ACETYLATION AT
LYS-10.
PubMed=11859155; DOI=10.1126/science.1069473;
Jacobs S.A., Khorasanizadeh S.;
"Structure of HP1 chromodomain bound to a lysine 9-methylated histone
H3 tail.";
Science 295:2080-2083(2002).
[15]
SUCCINYLATION AT LYS-57 AND LYS-80.
PubMed=22389435; DOI=10.1074/mcp.M111.015875;
Xie Z., Dai J., Dai L., Tan M., Cheng Z., Wu Y., Boeke J.D., Zhao Y.;
"Lysine succinylation and lysine malonylation in histones.";
Mol. Cell. Proteomics 11:100-107(2012).
-!- 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: 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.
-!- INTERACTION:
P42124:E(z); NbExp=5; IntAct=EBI-522090, EBI-112315;
Q92831:KAT2B (xeno); NbExp=2; IntAct=EBI-522090, EBI-477430;
P26017:Pc; NbExp=6; IntAct=EBI-522090, EBI-177152;
Q7JXA8:rhi; NbExp=4; IntAct=EBI-522090, EBI-149916;
Q9VHA0:Scm; NbExp=4; IntAct=EBI-522090, EBI-89256;
O94267:spt16 (xeno); NbExp=4; IntAct=EBI-522090, EBI-7414132;
P05205:Su(var)205; NbExp=8; IntAct=EBI-522090, EBI-155532;
P20659:trx; NbExp=6; IntAct=EBI-522090, EBI-591327;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome
{ECO:0000250}.
-!- PTM: 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.
{ECO:0000269|PubMed:11114889, ECO:0000269|PubMed:11266459,
ECO:0000269|PubMed:11371341, ECO:0000269|PubMed:12514098,
ECO:0000269|PubMed:15175259}.
-!- PTM: 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. {ECO:0000269|PubMed:11114889,
ECO:0000269|PubMed:11371341, ECO:0000269|PubMed:11859155,
ECO:0000269|PubMed:14732680, ECO:0000269|PubMed:16230526}.
-!- PTM: 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. {ECO:0000269|PubMed:14732680,
ECO:0000269|PubMed:15175259, ECO:0000269|PubMed:15371351}.
-!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
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EMBL; X14215; CAA32434.1; -; Genomic_DNA.
EMBL; AB019400; BAA93621.1; -; Genomic_DNA.
EMBL; AE014134; AAN11127.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66481.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66485.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66490.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66494.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66499.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66504.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66509.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66514.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66519.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66524.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66529.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66534.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66539.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66544.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66549.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66554.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66559.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66564.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66569.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66574.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66579.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66583.1; -; Genomic_DNA.
PIR; A02630; A02630.
PIR; S10097; S10097.
RefSeq; NP_001027285.1; NM_001032114.2.
RefSeq; NP_001027289.1; NM_001032118.2.
RefSeq; NP_001027294.1; NM_001032123.2.
RefSeq; NP_001027298.1; NM_001032127.2.
RefSeq; NP_001027303.1; NM_001032132.2.
RefSeq; NP_001027308.1; NM_001032137.2.
RefSeq; NP_001027313.1; NM_001032142.2.
RefSeq; NP_001027318.1; NM_001032147.2.
RefSeq; NP_001027323.1; NM_001032152.2.
RefSeq; NP_001027328.1; NM_001032157.2.
RefSeq; NP_001027333.1; NM_001032162.2.
RefSeq; NP_001027338.1; NM_001032167.2.
RefSeq; NP_001027343.1; NM_001032172.2.
RefSeq; NP_001027348.1; NM_001032177.2.
RefSeq; NP_001027353.1; NM_001032182.2.
RefSeq; NP_001027358.1; NM_001032187.2.
RefSeq; NP_001027363.1; NM_001032192.2.
RefSeq; NP_001027368.1; NM_001032197.2.
RefSeq; NP_001027373.1; NM_001032202.2.
RefSeq; NP_001027378.1; NM_001032207.2.
RefSeq; NP_001027383.1; NM_001032212.2.
RefSeq; NP_001027387.1; NM_001032216.2.
RefSeq; NP_724345.1; NM_165384.3.
PDB; 1KNA; X-ray; 2.10 A; P=2-17.
PDB; 1KNE; X-ray; 2.40 A; P=2-17.
PDB; 2NQB; X-ray; 2.30 A; A/E=2-136.
PDB; 2PYO; X-ray; 2.43 A; A/E=2-136.
PDB; 2YBA; X-ray; 2.55 A; C/D=2-20.
PDB; 4QLC; X-ray; 3.50 A; A/E=2-136.
PDB; 4UUZ; X-ray; 2.90 A; A=1-136.
PDB; 4X23; X-ray; 3.50 A; A/E/K/O=41-133.
PDB; 5KOG; X-ray; 1.52 A; P=6-11.
PDB; 6ASZ; X-ray; 1.52 A; P=6-11.
PDB; 6AT0; X-ray; 1.28 A; P=6-11.
PDBsum; 1KNA; -.
PDBsum; 1KNE; -.
PDBsum; 2NQB; -.
PDBsum; 2PYO; -.
PDBsum; 2YBA; -.
PDBsum; 4QLC; -.
PDBsum; 4UUZ; -.
PDBsum; 4X23; -.
PDBsum; 5KOG; -.
PDBsum; 6ASZ; -.
PDBsum; 6AT0; -.
ProteinModelPortal; P02299; -.
SMR; P02299; -.
BioGrid; 534149; 3.
BioGrid; 77140; 52.
DIP; DIP-38722N; -.
IntAct; P02299; 28.
MINT; P02299; -.
STRING; 7227.FBpp0091112; -.
iPTMnet; P02299; -.
PaxDb; P02299; -.
PRIDE; P02299; -.
EnsemblMetazoa; FBtr0085894; FBpp0085250; FBgn0051613.
EnsemblMetazoa; FBtr0091807; FBpp0091051; FBgn0053803.
EnsemblMetazoa; FBtr0091810; FBpp0091053; FBgn0053806.
EnsemblMetazoa; FBtr0091813; FBpp0091056; FBgn0053809.
EnsemblMetazoa; FBtr0091816; FBpp0091058; FBgn0053812.
EnsemblMetazoa; FBtr0091819; FBpp0091061; FBgn0053815.
EnsemblMetazoa; FBtr0091822; FBpp0091064; FBgn0053818.
EnsemblMetazoa; FBtr0091825; FBpp0091067; FBgn0053821.
EnsemblMetazoa; FBtr0091828; FBpp0091070; FBgn0053824.
EnsemblMetazoa; FBtr0091831; FBpp0091073; FBgn0053827.
EnsemblMetazoa; FBtr0091834; FBpp0091076; FBgn0053830.
EnsemblMetazoa; FBtr0091837; FBpp0091079; FBgn0053833.
EnsemblMetazoa; FBtr0091840; FBpp0091082; FBgn0053836.
EnsemblMetazoa; FBtr0091843; FBpp0091085; FBgn0053839.
EnsemblMetazoa; FBtr0091846; FBpp0091088; FBgn0053842.
EnsemblMetazoa; FBtr0091849; FBpp0091091; FBgn0053845.
EnsemblMetazoa; FBtr0091852; FBpp0091094; FBgn0053848.
EnsemblMetazoa; FBtr0091855; FBpp0091097; FBgn0053851.
EnsemblMetazoa; FBtr0091858; FBpp0091100; FBgn0053854.
EnsemblMetazoa; FBtr0091861; FBpp0091103; FBgn0053857.
EnsemblMetazoa; FBtr0091864; FBpp0091106; FBgn0053860.
EnsemblMetazoa; FBtr0091867; FBpp0091109; FBgn0053863.
EnsemblMetazoa; FBtr0091870; FBpp0091112; FBgn0053866.
GeneID; 318847; -.
GeneID; 3771723; -.
GeneID; 3771729; -.
GeneID; 3771771; -.
GeneID; 3771792; -.
GeneID; 3771959; -.
GeneID; 3772032; -.
GeneID; 3772149; -.
GeneID; 3772163; -.
GeneID; 3772173; -.
GeneID; 3772189; -.
GeneID; 3772191; -.
GeneID; 3772198; -.
GeneID; 3772231; -.
GeneID; 3772370; -.
GeneID; 3772374; -.
GeneID; 3772421; -.
GeneID; 3772489; -.
GeneID; 3772517; -.
GeneID; 3772518; -.
GeneID; 3772552; -.
GeneID; 3772607; -.
GeneID; 3772619; -.
KEGG; dme:Dmel_CG31613; -.
KEGG; dme:Dmel_CG33803; -.
KEGG; dme:Dmel_CG33806; -.
KEGG; dme:Dmel_CG33809; -.
KEGG; dme:Dmel_CG33812; -.
KEGG; dme:Dmel_CG33815; -.
KEGG; dme:Dmel_CG33818; -.
KEGG; dme:Dmel_CG33821; -.
KEGG; dme:Dmel_CG33824; -.
KEGG; dme:Dmel_CG33827; -.
KEGG; dme:Dmel_CG33830; -.
KEGG; dme:Dmel_CG33833; -.
KEGG; dme:Dmel_CG33836; -.
KEGG; dme:Dmel_CG33839; -.
KEGG; dme:Dmel_CG33842; -.
KEGG; dme:Dmel_CG33845; -.
KEGG; dme:Dmel_CG33848; -.
KEGG; dme:Dmel_CG33851; -.
KEGG; dme:Dmel_CG33854; -.
KEGG; dme:Dmel_CG33857; -.
KEGG; dme:Dmel_CG33860; -.
KEGG; dme:Dmel_CG33863; -.
KEGG; dme:Dmel_CG33866; -.
CTD; 318847; -.
CTD; 3771723; -.
CTD; 3771729; -.
CTD; 3771771; -.
CTD; 3771792; -.
CTD; 3771959; -.
CTD; 3772032; -.
CTD; 3772149; -.
CTD; 3772163; -.
CTD; 3772173; -.
CTD; 3772189; -.
CTD; 3772191; -.
CTD; 3772198; -.
CTD; 3772231; -.
CTD; 3772370; -.
CTD; 3772374; -.
CTD; 3772421; -.
CTD; 3772489; -.
CTD; 3772517; -.
CTD; 3772518; -.
CTD; 3772552; -.
CTD; 3772607; -.
CTD; 3772619; -.
FlyBase; FBgn0001199; His3.
FlyBase; FBgn0051613; His3:CG31613.
FlyBase; FBgn0053803; His3:CG33803.
FlyBase; FBgn0053806; His3:CG33806.
FlyBase; FBgn0053809; His3:CG33809.
FlyBase; FBgn0053812; His3:CG33812.
FlyBase; FBgn0053815; His3:CG33815.
FlyBase; FBgn0053818; His3:CG33818.
FlyBase; FBgn0053821; His3:CG33821.
FlyBase; FBgn0053824; His3:CG33824.
FlyBase; FBgn0053827; His3:CG33827.
FlyBase; FBgn0053830; His3:CG33830.
FlyBase; FBgn0053833; His3:CG33833.
FlyBase; FBgn0053836; His3:CG33836.
FlyBase; FBgn0053839; His3:CG33839.
FlyBase; FBgn0053842; His3:CG33842.
FlyBase; FBgn0053845; His3:CG33845.
FlyBase; FBgn0053848; His3:CG33848.
FlyBase; FBgn0053851; His3:CG33851.
FlyBase; FBgn0053854; His3:CG33854.
FlyBase; FBgn0053857; His3:CG33857.
FlyBase; FBgn0053860; His3:CG33860.
FlyBase; FBgn0053863; His3:CG33863.
FlyBase; FBgn0053866; His3:CG33866.
eggNOG; KOG1745; Eukaryota.
eggNOG; COG2036; LUCA.
GeneTree; ENSGT00760000118967; -.
InParanoid; P02299; -.
KO; K11253; -.
OMA; ANLCTIH; -.
OrthoDB; EOG091G0XGD; -.
PhylomeDB; P02299; -.
Reactome; R-DME-1266695; Interleukin-7 signaling.
Reactome; R-DME-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-DME-212300; PRC2 methylates histones and DNA.
Reactome; R-DME-2299718; Condensation of Prophase Chromosomes.
Reactome; R-DME-2559580; Oxidative Stress Induced Senescence.
Reactome; R-DME-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-DME-3214815; HDACs deacetylate histones.
Reactome; R-DME-3214841; PKMTs methylate histone lysines.
Reactome; R-DME-3214842; HDMs demethylate histones.
Reactome; R-DME-3214847; HATs acetylate histones.
Reactome; R-DME-3214858; RMTs methylate histone arginines.
Reactome; R-DME-3247509; Chromatin modifying enzymes.
Reactome; R-DME-427359; SIRT1 negatively regulates rRNA expression.
Reactome; R-DME-427413; NoRC negatively regulates rRNA expression.
Reactome; R-DME-5578749; Transcriptional regulation by small RNAs.
Reactome; R-DME-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
Reactome; R-DME-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-DME-5693571; Nonhomologous End-Joining (NHEJ).
Reactome; R-DME-73777; RNA Polymerase I Chain Elongation.
Reactome; R-DME-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-DME-9018519; Estrogen-dependent gene expression.
Reactome; R-DME-983231; Factors involved in megakaryocyte development and platelet production.
EvolutionaryTrace; P02299; -.
PRO; PR:P02299; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0051613; -.
Genevisible; P02299; DM.
GO; GO:0000788; C:nuclear nucleosome; ISS:FlyBase.
GO; GO:0000786; C:nucleosome; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
GO; GO:0035059; C:RCAF complex; IDA:FlyBase.
GO; GO:0031492; F:nucleosomal DNA binding; ISS:FlyBase.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
GO; GO:0006334; P:nucleosome assembly; ISS:FlyBase.
Gene3D; 1.10.20.10; -; 1.
InterPro; IPR009072; Histone-fold.
InterPro; IPR007125; Histone_H2A/H2B/H3.
InterPro; IPR000164; Histone_H3/CENP-A.
PANTHER; PTHR11426; PTHR11426; 1.
Pfam; PF00125; Histone; 1.
PRINTS; PR00622; HISTONEH3.
SMART; SM00428; H3; 1.
SUPFAM; SSF47113; SSF47113; 1.
PROSITE; PS00322; HISTONE_H3_1; 1.
PROSITE; PS00959; HISTONE_H3_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Chromosome; Complete proteome; DNA-binding;
Methylation; Nucleosome core; Nucleus; Phosphoprotein;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000305}.
CHAIN 2 136 Histone H3.
/FTId=PRO_0000221300.
REGION 6 11 Su(var)205 chromodomain-binding.
MOD_RES 5 5 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:14732680,
ECO:0000269|PubMed:15175259}.
MOD_RES 5 5 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:14732680,
ECO:0000269|PubMed:15175259}.
MOD_RES 5 5 N6-methyllysine; alternate.
{ECO:0000269|PubMed:14732680,
ECO:0000269|PubMed:15175259}.
MOD_RES 10 10 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:14732680}.
MOD_RES 10 10 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:11114889,
ECO:0000269|PubMed:11859155,
ECO:0000269|PubMed:14732680}.
MOD_RES 10 10 N6-methyllysine; alternate.
{ECO:0000269|PubMed:14732680}.
MOD_RES 11 11 Phosphoserine.
{ECO:0000269|PubMed:11114889,
ECO:0000269|PubMed:11266459,
ECO:0000269|PubMed:11371341,
ECO:0000269|PubMed:12514098,
ECO:0000269|PubMed:15175259}.
MOD_RES 15 15 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:14732680}.
MOD_RES 15 15 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:11114889,
ECO:0000269|PubMed:11371341,
ECO:0000269|PubMed:14732680,
ECO:0000269|PubMed:16230526}.
MOD_RES 15 15 N6-methyllysine; alternate.
{ECO:0000269|PubMed:14732680}.
MOD_RES 19 19 N6-acetyllysine.
{ECO:0000269|PubMed:14732680}.
MOD_RES 24 24 N6-acetyllysine.
{ECO:0000269|PubMed:14732680}.
MOD_RES 28 28 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:14732680}.
MOD_RES 28 28 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:14732680}.
MOD_RES 28 28 N6-methyllysine; alternate.
{ECO:0000269|PubMed:14732680}.
MOD_RES 37 37 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:14732680}.
MOD_RES 37 37 N6-methyllysine; alternate.
{ECO:0000269|PubMed:14732680}.
MOD_RES 38 38 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:14732680}.
MOD_RES 38 38 N6-methyllysine; alternate.
{ECO:0000269|PubMed:14732680}.
MOD_RES 57 57 N6-succinyllysine.
{ECO:0000269|PubMed:22389435}.
MOD_RES 80 80 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:14732680,
ECO:0000269|PubMed:15175259,
ECO:0000269|PubMed:15371351}.
MOD_RES 80 80 N6-methyllysine; alternate.
{ECO:0000269|PubMed:14732680,
ECO:0000269|PubMed:15175259,
ECO:0000269|PubMed:15371351}.
MOD_RES 80 80 N6-succinyllysine; alternate.
{ECO:0000269|PubMed:22389435}.
CONFLICT 118 118 V -> I (in Ref. 1 and 2). {ECO:0000305}.
STRAND 7 9 {ECO:0000244|PDB:6AT0}.
HELIX 46 57 {ECO:0000244|PDB:2NQB}.
HELIX 65 77 {ECO:0000244|PDB:2NQB}.
STRAND 80 82 {ECO:0000244|PDB:2NQB}.
HELIX 87 114 {ECO:0000244|PDB:2NQB}.
STRAND 118 120 {ECO:0000244|PDB:2NQB}.
HELIX 122 131 {ECO:0000244|PDB:2NQB}.
SEQUENCE 136 AA; 15388 MW; 6FD8508EA50A0EEC CRC64;
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE
LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEASEAY LVGLFEDTNL CAIHAKRVTI
MPKDIQLARR IRGERA


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