H3_DROME
ID H3_DROME Reviewed; 136 AA.
AC P02299; Q4ABE4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Histone H3;
GN Name=His3;
GN and
GN Name=His3:CG31613; ORFNames=CG31613;
GN and
GN Name=His3:CG33803; ORFNames=CG33803;
GN and
GN Name=His3:CG33806; ORFNames=CG33806;
GN and
GN Name=His3:CG33809; ORFNames=CG33809;
GN and
GN Name=His3:CG33812; ORFNames=CG33812;
GN and
GN Name=His3:CG33815; ORFNames=CG33815;
GN and
GN Name=His3:CG33818; ORFNames=CG33818;
GN and
GN Name=His3:CG33821; ORFNames=CG33821;
GN and
GN Name=His3:CG33824; ORFNames=CG33824;
GN and
GN Name=His3:CG33827; ORFNames=CG33827;
GN and
GN Name=His3:CG33830; ORFNames=CG33830;
GN and
GN Name=His3:CG33833; ORFNames=CG33833;
GN and
GN Name=His3:CG33836; ORFNames=CG33836;
GN and
GN Name=His3:CG33839; ORFNames=CG33839;
GN and
GN Name=His3:CG33842; ORFNames=CG33842;
GN and
GN Name=His3:CG33845; ORFNames=CG33845;
GN and
GN Name=His3:CG33848; ORFNames=CG33848;
GN and
GN Name=His3:CG33851; ORFNames=CG33851;
GN and
GN Name=His3:CG33854; ORFNames=CG33854;
GN and
GN Name=His3:CG33857; ORFNames=CG33857;
GN and
GN Name=His3:CG33860; ORFNames=CG33860;
GN and
GN Name=His3:CG33863; ORFNames=CG33863;
GN and
GN Name=His3:CG33866; ORFNames=CG33866;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIS3).
RC STRAIN=AK-194;
RX PubMed=2536150; DOI=10.1093/nar/17.1.225;
RA Matsuo Y., Yamazaki T.;
RT "tRNA derived insertion element in histone gene repeating unit of
RT Drosophila melanogaster.";
RL Nucleic Acids Res. 17:225-238(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIS3).
RA Goldberg M.L.;
RL Thesis (1979), University of Stanford, United States.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIS3).
RC STRAIN=Canton-S;
RX PubMed=10991787; DOI=10.1006/mpev.2000.0810;
RA Matsuo Y.;
RT "Molecular evolution of the histone 3 multigene family in the Drosophila
RT melanogaster species subgroup.";
RL Mol. Phylogenet. Evol. 16:339-343(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HIS3:CG31613; HIS3:CG33803;
RP HIS3:CG33806; HIS3:CG33809; HIS3:CG33812; HIS3:CG33815; HIS3:CG33818;
RP HIS3:CG33821; HIS3:CG33824; HIS3:CG33827; HIS3:CG33830; HIS3:CG33833;
RP HIS3:CG33836; HIS3:CG33839; HIS3:CG33842; HIS3:CG33845; HIS3:CG33848;
RP HIS3:CG33851; HIS3:CG33854; HIS3:CG33857; HIS3:CG33860; HIS3:CG33863 AND
RP HIS3:CG33866).
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP PHOSPHORYLATION AT SER-11, AND ACETYLATION AT LYS-10 AND LYS-15.
RX PubMed=11114889; DOI=10.1101/gad.848800;
RA Nowak S.J., Corces V.G.;
RT "Phosphorylation of histone H3 correlates with transcriptionally active
RT loci.";
RL Genes Dev. 14:3003-3013(2000).
RN [7]
RP PHOSPHORYLATION AT SER-11, AND ACETYLATION AT LYS-15.
RX PubMed=11371341; DOI=10.1016/s0092-8674(01)00325-7;
RA Wang Y., Zhang W., Jin Y., Johansen J., Johansen K.M.;
RT "The JIL-1 tandem kinase mediates histone H3 phosphorylation and is
RT required for maintenance of chromatin structure in Drosophila.";
RL Cell 105:433-443(2001).
RN [8]
RP PHOSPHORYLATION AT SER-11.
RX PubMed=11266459; DOI=10.1083/jcb.152.4.669;
RA Giet R., Glover D.M.;
RT "Drosophila aurora B kinase is required for histone H3 phosphorylation and
RT condensin recruitment during chromosome condensation and to organize the
RT central spindle during cytokinesis.";
RL J. Cell Biol. 152:669-682(2001).
RN [9]
RP PHOSPHORYLATION AT SER-11.
RX PubMed=12514098; DOI=10.1101/gad.1021403;
RA Labrador M., Corces V.G.;
RT "Phosphorylation of histone H3 during transcriptional activation depends on
RT promoter structure.";
RL Genes Dev. 17:43-48(2003).
RN [10]
RP METHYLATION AT LYS-5 AND LYS-80, AND PHOSPHORYLATION AT SER-11.
RX PubMed=15175259; DOI=10.1101/gad.1198204;
RA Schuebeler D., MacAlpine D.M., Scalzo D., Wirbelauer C., Kooperberg C.,
RA van Leeuwen F., Gottschling D.E., O'Neill L.P., Turner B.M., Delrow J.,
RA Bell S.P., Groudine M.;
RT "The histone modification pattern of active genes revealed through genome-
RT wide chromatin analysis of a higher eukaryote.";
RL Genes Dev. 18:1263-1271(2004).
RN [11]
RP METHYLATION AT LYS-5; LYS-10; LYS-15; LYS-28; LYS-37; LYS-38 AND LYS-80,
RP ACETYLATION AT LYS-10; LYS-15; LYS-19 AND LYS-24, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=14732680; DOI=10.1073/pnas.0308092100;
RA McKittrick E., Gafken P.R., Ahmad K., Henikoff S.;
RT "Histone H3.3 is enriched in covalent modifications associated with active
RT chromatin.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:1525-1530(2004).
RN [12]
RP METHYLATION AT LYS-80.
RX PubMed=15371351; DOI=10.1534/genetics.104.033191;
RA Shanower G.A., Mueller M., Blanton J.L., Honti V., Gyurkovics H.,
RA Schedl P.;
RT "Characterization of the grappa gene, the Drosophila histone H3 lysine 79
RT methyltransferase.";
RL Genetics 169:173-184(2005).
RN [13]
RP ACETYLATION AT LYS-15.
RX PubMed=16230526; DOI=10.1101/gad.1348905;
RA Ivanovska I., Khandan T., Ito T., Orr-Weaver T.L.;
RT "A histone code in meiosis: the histone kinase, NHK-1, is required for
RT proper chromosomal architecture in Drosophila oocytes.";
RL Genes Dev. 19:2571-2582(2005).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-17, AND ACETYLATION AT LYS-10.
RX PubMed=11859155; DOI=10.1126/science.1069473;
RA Jacobs S.A., Khorasanizadeh S.;
RT "Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3
RT tail.";
RL Science 295:2080-2083(2002).
RN [15]
RP SUCCINYLATION AT LYS-57 AND LYS-80.
RX PubMed=22389435; DOI=10.1074/mcp.m111.015875;
RA Xie Z., Dai J., Dai L., Tan M., Cheng Z., Wu Y., Boeke J.D., Zhao Y.;
RT "Lysine succinylation and lysine malonylation in histones.";
RL Mol. Cell. Proteomics 11:100-107(2012).
RN [16]
RP PHOSPHORYLATION AT THR-4.
RX PubMed=32750047; DOI=10.1371/journal.pgen.1008962;
RA Fresan U., Rodriguez-Sanchez M.A., Reina O., Corces V.G., Espinas M.L.;
RT "Haspin kinase modulates nuclear architecture and Polycomb-dependent gene
RT silencing.";
RL PLoS Genet. 16:e1008962-e1008962(2020).
CC -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact
CC DNA into chromatin, limiting DNA accessibility to the cellular
CC machineries which require DNA as a template. Histones thereby play a
CC central role in transcription regulation, DNA repair, DNA replication
CC and chromosomal stability. DNA accessibility is regulated via a complex
CC set of post-translational modifications of histones, also called
CC histone code, and nucleosome remodeling.
CC -!- SUBUNIT: The nucleosome is a histone octamer containing two molecules
CC each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and
CC two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of
CC DNA.
CC -!- INTERACTION:
CC P02299; Q7JXA8: rhi; NbExp=4; IntAct=EBI-522090, EBI-149916;
CC P02299; Q9VHA0: Scm; NbExp=4; IntAct=EBI-522090, EBI-89256;
CC P02299; P05205: Su(var)205; NbExp=3; IntAct=EBI-522090, EBI-155532;
CC P02299; Q92831: KAT2B; Xeno; NbExp=2; IntAct=EBI-522090, EBI-477430;
CC P02299; O94267: spt16; Xeno; NbExp=4; IntAct=EBI-522090, EBI-7414132;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- PTM: Phosphorylated at Thr-4 (H3T3ph) by Haspin during mitosis and
CC interphase (PubMed:32750047). Phosphorylation at Ser-11 by aurB/ial
CC during mitosis and meiosis is crucial for chromosome condensation and
CC cell-cycle progression (PubMed:11114889, PubMed:11266459,
CC PubMed:11371341, PubMed:12514098, PubMed:15175259). Phosphorylation at
CC Ser-11 by JIL-1 during interphase is linked to gene activation and
CC restricts the formation of heterochromatin at inappropriate sites.
CC Phosphorylation at Ser-11 is enriched on male X chromosome compared to
CC the autosome (PubMed:11114889, PubMed:11266459, PubMed:11371341,
CC PubMed:12514098, PubMed:15175259). {ECO:0000269|PubMed:11114889,
CC ECO:0000269|PubMed:11266459, ECO:0000269|PubMed:11371341,
CC ECO:0000269|PubMed:12514098, ECO:0000269|PubMed:15175259,
CC ECO:0000269|PubMed:32750047}.
CC -!- PTM: Acetylation is generally linked to gene activation. Acetylated on
CC Lys-15 during prophase I of meiosis. Phosphorylation of H2A 'Thr-119'
CC is a prerequisite for H3 Lys-15 acetylation. Acetylation on Lys-15 is
CC enriched on male X chromosome compared to the autosome.
CC {ECO:0000269|PubMed:11114889, ECO:0000269|PubMed:11371341,
CC ECO:0000269|PubMed:11859155, ECO:0000269|PubMed:14732680,
CC ECO:0000269|PubMed:16230526}.
CC -!- PTM: Methylation at Lys-5 or Lys-80 is generally associated with active
CC chromatin. Methylation at Lys-80 by gpp occurs at low levels in
CC specific developmental stages and tissues undergoing active cell
CC division, and at highest levels in epidermal cells undergoing
CC differentiation. {ECO:0000269|PubMed:14732680,
CC ECO:0000269|PubMed:15175259, ECO:0000269|PubMed:15371351}.
CC -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
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DR EMBL; X14215; CAA32434.1; -; Genomic_DNA.
DR EMBL; AB019400; BAA93621.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN11127.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66481.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66485.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66490.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66494.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66499.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66504.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66509.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66514.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66519.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66524.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66529.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66534.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66539.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66544.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66549.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66554.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66559.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66564.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66569.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66574.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66579.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66583.1; -; Genomic_DNA.
DR PIR; A02630; A02630.
DR PIR; S10097; S10097.
DR RefSeq; NP_001027285.1; NM_001032114.2.
DR RefSeq; NP_001027289.1; NM_001032118.2.
DR RefSeq; NP_001027294.1; NM_001032123.2.
DR RefSeq; NP_001027298.1; NM_001032127.2.
DR RefSeq; NP_001027303.1; NM_001032132.2.
DR RefSeq; NP_001027308.1; NM_001032137.2.
DR RefSeq; NP_001027313.1; NM_001032142.2.
DR RefSeq; NP_001027318.1; NM_001032147.2.
DR RefSeq; NP_001027323.1; NM_001032152.2.
DR RefSeq; NP_001027328.1; NM_001032157.2.
DR RefSeq; NP_001027333.1; NM_001032162.2.
DR RefSeq; NP_001027338.1; NM_001032167.2.
DR RefSeq; NP_001027343.1; NM_001032172.2.
DR RefSeq; NP_001027348.1; NM_001032177.2.
DR RefSeq; NP_001027353.1; NM_001032182.2.
DR RefSeq; NP_001027358.1; NM_001032187.2.
DR RefSeq; NP_001027363.1; NM_001032192.2.
DR RefSeq; NP_001027368.1; NM_001032197.2.
DR RefSeq; NP_001027373.1; NM_001032202.2.
DR RefSeq; NP_001027378.1; NM_001032207.2.
DR RefSeq; NP_001027383.1; NM_001032212.2.
DR RefSeq; NP_001027387.1; NM_001032216.2.
DR RefSeq; NP_724345.1; NM_165384.3.
DR PDB; 1KNA; X-ray; 2.10 A; P=2-17.
DR PDB; 1KNE; X-ray; 2.40 A; P=2-17.
DR PDB; 2NQB; X-ray; 2.30 A; A/E=2-136.
DR PDB; 2PYO; X-ray; 2.43 A; A/E=2-136.
DR PDB; 2YBA; X-ray; 2.55 A; C/D=2-20.
DR PDB; 4QLC; X-ray; 3.50 A; A/E=2-136.
DR PDB; 4UUZ; X-ray; 2.90 A; A=1-136.
DR PDB; 4X23; X-ray; 3.50 A; A/E/K/O=41-133.
DR PDB; 5WCU; X-ray; 5.53 A; A/E/K/O=39-136.
DR PDB; 6ASZ; X-ray; 1.52 A; P=6-11.
DR PDB; 6AT0; X-ray; 1.28 A; P=6-11.
DR PDB; 6DZT; EM; 2.99 A; A/E=1-136.
DR PDB; 6MHA; X-ray; 1.50 A; B=6-11.
DR PDB; 6PWE; EM; 3.95 A; A/E=1-136.
DR PDB; 6PWF; EM; 4.07 A; A/E=1-136.
DR PDBsum; 1KNA; -.
DR PDBsum; 1KNE; -.
DR PDBsum; 2NQB; -.
DR PDBsum; 2PYO; -.
DR PDBsum; 2YBA; -.
DR PDBsum; 4QLC; -.
DR PDBsum; 4UUZ; -.
DR PDBsum; 4X23; -.
DR PDBsum; 5WCU; -.
DR PDBsum; 6ASZ; -.
DR PDBsum; 6AT0; -.
DR PDBsum; 6DZT; -.
DR PDBsum; 6MHA; -.
DR PDBsum; 6PWE; -.
DR PDBsum; 6PWF; -.
DR AlphaFoldDB; P02299; -.
DR BMRB; P02299; -.
DR SMR; P02299; -.
DR BioGRID; 534149; 3.
DR BioGRID; 77140; 78.
DR DIP; DIP-38722N; -.
DR IntAct; P02299; 19.
DR MINT; P02299; -.
DR STRING; 7227.FBpp0085250; -.
DR iPTMnet; P02299; -.
DR PaxDb; P02299; -.
DR PRIDE; P02299; -.
DR EnsemblMetazoa; FBtr0085894; FBpp0085250; FBgn0051613.
DR EnsemblMetazoa; FBtr0091807; FBpp0091051; FBgn0053803.
DR EnsemblMetazoa; FBtr0091810; FBpp0091053; FBgn0053806.
DR EnsemblMetazoa; FBtr0091813; FBpp0091056; FBgn0053809.
DR EnsemblMetazoa; FBtr0091816; FBpp0091058; FBgn0053812.
DR EnsemblMetazoa; FBtr0091819; FBpp0091061; FBgn0053815.
DR EnsemblMetazoa; FBtr0091822; FBpp0091064; FBgn0053818.
DR EnsemblMetazoa; FBtr0091825; FBpp0091067; FBgn0053821.
DR EnsemblMetazoa; FBtr0091828; FBpp0091070; FBgn0053824.
DR EnsemblMetazoa; FBtr0091831; FBpp0091073; FBgn0053827.
DR EnsemblMetazoa; FBtr0091834; FBpp0091076; FBgn0053830.
DR EnsemblMetazoa; FBtr0091837; FBpp0091079; FBgn0053833.
DR EnsemblMetazoa; FBtr0091840; FBpp0091082; FBgn0053836.
DR EnsemblMetazoa; FBtr0091843; FBpp0091085; FBgn0053839.
DR EnsemblMetazoa; FBtr0091846; FBpp0091088; FBgn0053842.
DR EnsemblMetazoa; FBtr0091849; FBpp0091091; FBgn0053845.
DR EnsemblMetazoa; FBtr0091852; FBpp0091094; FBgn0053848.
DR EnsemblMetazoa; FBtr0091855; FBpp0091097; FBgn0053851.
DR EnsemblMetazoa; FBtr0091858; FBpp0091100; FBgn0053854.
DR EnsemblMetazoa; FBtr0091861; FBpp0091103; FBgn0053857.
DR EnsemblMetazoa; FBtr0091864; FBpp0091106; FBgn0053860.
DR EnsemblMetazoa; FBtr0091867; FBpp0091109; FBgn0053863.
DR EnsemblMetazoa; FBtr0091870; FBpp0091112; FBgn0053866.
DR GeneID; 318847; -.
DR GeneID; 3771723; -.
DR GeneID; 3771729; -.
DR GeneID; 3771771; -.
DR GeneID; 3771792; -.
DR GeneID; 3771959; -.
DR GeneID; 3772032; -.
DR GeneID; 3772149; -.
DR GeneID; 3772163; -.
DR GeneID; 3772173; -.
DR GeneID; 3772189; -.
DR GeneID; 3772191; -.
DR GeneID; 3772198; -.
DR GeneID; 3772231; -.
DR GeneID; 3772370; -.
DR GeneID; 3772374; -.
DR GeneID; 3772421; -.
DR GeneID; 3772489; -.
DR GeneID; 3772517; -.
DR GeneID; 3772518; -.
DR GeneID; 3772552; -.
DR GeneID; 3772607; -.
DR GeneID; 3772619; -.
DR KEGG; dme:Dmel_CG31613; -.
DR KEGG; dme:Dmel_CG33803; -.
DR KEGG; dme:Dmel_CG33806; -.
DR KEGG; dme:Dmel_CG33809; -.
DR KEGG; dme:Dmel_CG33812; -.
DR KEGG; dme:Dmel_CG33815; -.
DR KEGG; dme:Dmel_CG33818; -.
DR KEGG; dme:Dmel_CG33821; -.
DR KEGG; dme:Dmel_CG33824; -.
DR KEGG; dme:Dmel_CG33827; -.
DR KEGG; dme:Dmel_CG33830; -.
DR KEGG; dme:Dmel_CG33833; -.
DR KEGG; dme:Dmel_CG33836; -.
DR KEGG; dme:Dmel_CG33839; -.
DR KEGG; dme:Dmel_CG33842; -.
DR KEGG; dme:Dmel_CG33845; -.
DR KEGG; dme:Dmel_CG33848; -.
DR KEGG; dme:Dmel_CG33851; -.
DR KEGG; dme:Dmel_CG33854; -.
DR KEGG; dme:Dmel_CG33857; -.
DR KEGG; dme:Dmel_CG33860; -.
DR KEGG; dme:Dmel_CG33863; -.
DR KEGG; dme:Dmel_CG33866; -.
DR CTD; 318847; -.
DR CTD; 3771723; -.
DR CTD; 3771729; -.
DR CTD; 3771771; -.
DR CTD; 3771792; -.
DR CTD; 3771959; -.
DR CTD; 3772032; -.
DR CTD; 3772149; -.
DR CTD; 3772163; -.
DR CTD; 3772173; -.
DR CTD; 3772189; -.
DR CTD; 3772191; -.
DR CTD; 3772198; -.
DR CTD; 3772231; -.
DR CTD; 3772370; -.
DR CTD; 3772374; -.
DR CTD; 3772421; -.
DR CTD; 3772489; -.
DR CTD; 3772517; -.
DR CTD; 3772518; -.
DR CTD; 3772552; -.
DR CTD; 3772607; -.
DR CTD; 3772619; -.
DR FlyBase; FBgn0001199; His3.
DR FlyBase; FBgn0051613; His3:CG31613.
DR FlyBase; FBgn0053803; His3:CG33803.
DR FlyBase; FBgn0053806; His3:CG33806.
DR FlyBase; FBgn0053809; His3:CG33809.
DR FlyBase; FBgn0053812; His3:CG33812.
DR FlyBase; FBgn0053815; His3:CG33815.
DR FlyBase; FBgn0053818; His3:CG33818.
DR FlyBase; FBgn0053821; His3:CG33821.
DR FlyBase; FBgn0053824; His3:CG33824.
DR FlyBase; FBgn0053827; His3:CG33827.
DR FlyBase; FBgn0053830; His3:CG33830.
DR FlyBase; FBgn0053833; His3:CG33833.
DR FlyBase; FBgn0053836; His3:CG33836.
DR FlyBase; FBgn0053839; His3:CG33839.
DR FlyBase; FBgn0053842; His3:CG33842.
DR FlyBase; FBgn0053845; His3:CG33845.
DR FlyBase; FBgn0053848; His3:CG33848.
DR FlyBase; FBgn0053851; His3:CG33851.
DR FlyBase; FBgn0053854; His3:CG33854.
DR FlyBase; FBgn0053857; His3:CG33857.
DR FlyBase; FBgn0053860; His3:CG33860.
DR FlyBase; FBgn0053863; His3:CG33863.
DR FlyBase; FBgn0053866; His3:CG33866.
DR VEuPathDB; VectorBase:FBgn0051613; -.
DR VEuPathDB; VectorBase:FBgn0053803; -.
DR VEuPathDB; VectorBase:FBgn0053806; -.
DR VEuPathDB; VectorBase:FBgn0053809; -.
DR VEuPathDB; VectorBase:FBgn0053812; -.
DR VEuPathDB; VectorBase:FBgn0053815; -.
DR VEuPathDB; VectorBase:FBgn0053818; -.
DR VEuPathDB; VectorBase:FBgn0053821; -.
DR VEuPathDB; VectorBase:FBgn0053824; -.
DR VEuPathDB; VectorBase:FBgn0053827; -.
DR VEuPathDB; VectorBase:FBgn0053830; -.
DR VEuPathDB; VectorBase:FBgn0053833; -.
DR VEuPathDB; VectorBase:FBgn0053836; -.
DR VEuPathDB; VectorBase:FBgn0053839; -.
DR VEuPathDB; VectorBase:FBgn0053842; -.
DR VEuPathDB; VectorBase:FBgn0053845; -.
DR VEuPathDB; VectorBase:FBgn0053848; -.
DR VEuPathDB; VectorBase:FBgn0053851; -.
DR VEuPathDB; VectorBase:FBgn0053854; -.
DR VEuPathDB; VectorBase:FBgn0053857; -.
DR VEuPathDB; VectorBase:FBgn0053860; -.
DR VEuPathDB; VectorBase:FBgn0053863; -.
DR VEuPathDB; VectorBase:FBgn0053866; -.
DR eggNOG; KOG1745; Eukaryota.
DR GeneTree; ENSGT01050000244889; -.
DR HOGENOM; CLU_078295_4_0_1; -.
DR InParanoid; P02299; -.
DR OrthoDB; 1564596at2759; -.
DR PhylomeDB; P02299; -.
DR Reactome; R-DME-1266695; Interleukin-7 signaling.
DR Reactome; R-DME-212300; PRC2 methylates histones and DNA.
DR Reactome; R-DME-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-DME-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-DME-3214847; HATs acetylate histones.
DR Reactome; R-DME-3247509; Chromatin modifying enzymes.
DR Reactome; R-DME-427359; SIRT1 negatively regulates rRNA expression.
DR Reactome; R-DME-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-DME-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-DME-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-DME-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-DME-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-DME-9018519; Estrogen-dependent gene expression.
DR Reactome; R-DME-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; P02299; -.
DR EvolutionaryTrace; P02299; -.
DR PRO; PR:P02299; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0051613; Expressed in ovary and 12 other tissues.
DR Genevisible; P02299; DM.
DR GO; GO:0000785; C:chromatin; IDA:FlyBase.
DR GO; GO:0000786; C:nucleosome; ISS:FlyBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0035059; C:RCAF complex; IDA:FlyBase.
DR GO; GO:0031492; F:nucleosomal DNA binding; ISS:FlyBase.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006334; P:nucleosome assembly; ISS:FlyBase.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR000164; Histone_H3/CENP-A.
DR PANTHER; PTHR11426; PTHR11426; 1.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00622; HISTONEH3.
DR SMART; SM00428; H3; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00322; HISTONE_H3_1; 1.
DR PROSITE; PS00959; HISTONE_H3_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromosome; DNA-binding; Methylation;
KW Nucleosome core; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..136
FT /note="Histone H3"
FT /id="PRO_0000221300"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 6..11
FT /note="Su(var)205 chromodomain-binding"
FT MOD_RES 4
FT /note="Phosphothreonine; by Haspin"
FT /evidence="ECO:0000269|PubMed:32750047"
FT MOD_RES 5
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:14732680,
FT ECO:0000269|PubMed:15175259"
FT MOD_RES 5
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:14732680,
FT ECO:0000269|PubMed:15175259"
FT MOD_RES 5
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:14732680,
FT ECO:0000269|PubMed:15175259"
FT MOD_RES 10
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:14732680"
FT MOD_RES 10
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:11114889,
FT ECO:0000269|PubMed:11859155, ECO:0000269|PubMed:14732680"
FT MOD_RES 10
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:14732680"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11114889,
FT ECO:0000269|PubMed:11266459, ECO:0000269|PubMed:11371341,
FT ECO:0000269|PubMed:12514098, ECO:0000269|PubMed:15175259"
FT MOD_RES 15
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:14732680"
FT MOD_RES 15
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:11114889,
FT ECO:0000269|PubMed:11371341, ECO:0000269|PubMed:14732680,
FT ECO:0000269|PubMed:16230526"
FT MOD_RES 15
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:14732680"
FT MOD_RES 19
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:14732680"
FT MOD_RES 24
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:14732680"
FT MOD_RES 28
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:14732680"
FT MOD_RES 28
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:14732680"
FT MOD_RES 28
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:14732680"
FT MOD_RES 37
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:14732680"
FT MOD_RES 37
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:14732680"
FT MOD_RES 38
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:14732680"
FT MOD_RES 38
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:14732680"
FT MOD_RES 57
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000269|PubMed:22389435"
FT MOD_RES 80
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:14732680,
FT ECO:0000269|PubMed:15175259, ECO:0000269|PubMed:15371351"
FT MOD_RES 80
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:14732680,
FT ECO:0000269|PubMed:15175259, ECO:0000269|PubMed:15371351"
FT MOD_RES 80
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:22389435"
FT CONFLICT 118
FT /note="V -> I (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:6AT0"
FT HELIX 46..57
FT /evidence="ECO:0007829|PDB:2NQB"
FT HELIX 65..77
FT /evidence="ECO:0007829|PDB:2NQB"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:2NQB"
FT HELIX 87..114
FT /evidence="ECO:0007829|PDB:2NQB"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:2NQB"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:2NQB"
SQ SEQUENCE 136 AA; 15388 MW; 6FD8508EA50A0EEC CRC64;
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE
LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEASEAY LVGLFEDTNL CAIHAKRVTI
MPKDIQLARR IRGERA
