H33B_DROME
ID H33B_DROME Reviewed; 136 AA.
AC C0HL67; A4V466; E2QCP0; P06351; P33155; P84249; Q9V3W4;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Histone H3.3B {ECO:0000303|PubMed:7557364};
DE AltName: Full=H3.B {ECO:0000312|FlyBase:FBgn0004828};
GN Name=His3.3B {ECO:0000303|PubMed:7557364, ECO:0000312|FlyBase:FBgn0004828};
GN ORFNames=CG8989 {ECO:0000312|FlyBase:FBgn0004828};
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 [MRNA].
RX PubMed=1748304; DOI=10.1016/0378-1119(91)90337-b;
RA Fretzin S., Allan B.D., van Daal A., Elgin S.C.R.;
RT "A Drosophila melanogaster H3.3 cDNA encodes a histone variant identical
RT with the vertebrate H3.3.";
RL Gene 107:341-342(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Canton-S;
RX PubMed=7557364; DOI=10.1139/g95-075;
RA Akhmanova A.S., Bindels P.S.T., Xu J., Miedema K., Kremer H., Hennig W.;
RT "Structure and expression of histone H3.3 genes in Drosophila melanogaster
RT and Drosophila hydei.";
RL Genome 38:586-600(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6] {ECO:0000312|EMBL:ANY27398.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:ANY27398.1};
RA Wan K., Booth B., Spirohn K., Hao T., Hu Y., Calderwood M., Hill D.,
RA Mohr S., Vidal M., Celniker S., Perrimon N.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
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 [9]
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 [10]
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 [11]
RP FUNCTION, METHYLATION AT LYS-5; LYS-10; LYS-15; LYS-28; LYS-37; LYS-38 AND
RP LYS-80, ACETYLATION AT LYS-10; LYS-15; LYS-19 AND LYS-24, AND
RP IDENTIFICATION BY 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 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 [14]
RP INTERACTION WITH DAXX.
RX PubMed=28320872; DOI=10.1128/mcb.00597-16;
RA Fromental-Ramain C., Ramain P., Hamiche A.;
RT "The Drosophila DAXX-Like Protein (DLP) Cooperates with ASF1 for H3.3
RT Deposition and Heterochromatin Formation.";
RL Mol. Cell. Biol. 37:0-0(2017).
CC -!- FUNCTION: Variant histone H3 which replaces conventional H3 in a wide
CC range of nucleosomes in active genes and is specifically enriched in
CC modifications associated with active chromatin. Constitutes the
CC predominant form of histone H3 in non-dividing cells and is
CC incorporated into chromatin independently of DNA synthesis. Deposited
CC at sites of nucleosomal displacement throughout transcribed genes,
CC suggesting that it represents an epigenetic imprint of
CC transcriptionally active chromatin. Nucleosomes wrap and compact DNA
CC into chromatin, limiting DNA accessibility to the cellular machineries
CC which require DNA as a template. Histones thereby play a central role
CC in transcription regulation, DNA repair, DNA replication and
CC chromosomal stability. DNA accessibility is regulated via a complex set
CC of post-translational modifications of histones, also called histone
CC code, and nucleosome remodeling. {ECO:0000269|PubMed:14732680}.
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. Interacts with Daxx (via C-terminus) (PubMed:28320872).
CC {ECO:0000269|PubMed:28320872}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Low levels of expression in ovaries and moderate
CC levels of expression in the testes. Highest levels of expression in
CC embryos. {ECO:0000269|PubMed:7557364}.
CC -!- PTM: Phosphorylation at Ser-11 by aurB/ial during mitosis and meiosis
CC is crucial for chromosome condensation and cell-cycle progression.
CC Phosphorylation at Ser-11 by JIL-1 during interphase is linked to gene
CC activation and restricts the formation of heterochromatin at
CC inappropriate sites. Phosphorylation at Ser-11 is enriched on male X
CC chromosome compared to the autosome. {ECO:0000269|PubMed:11114889,
CC ECO:0000269|PubMed:11266459, ECO:0000269|PubMed:11371341,
CC ECO:0000269|PubMed:12514098}.
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:14732680}.
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:15371351}.
CC -!- MISCELLANEOUS: This histone is the predominant form in non-dividing
CC cells.
CC -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
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DR EMBL; X53822; CAA37819.1; -; mRNA.
DR EMBL; X81205; CAA57077.1; -; Genomic_DNA.
DR EMBL; X81207; CAA57080.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF46452.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09245.1; -; Genomic_DNA.
DR EMBL; AE014298; AAO41645.1; -; Genomic_DNA.
DR EMBL; AE014298; AGB95217.1; -; Genomic_DNA.
DR EMBL; AY118325; AAM48354.1; -; mRNA.
DR EMBL; KX531588; ANY27398.1; -; mRNA.
DR PIR; S61220; S61220.
DR RefSeq; NP_001259374.1; NM_001272445.2.
DR RefSeq; NP_001260082.1; NM_001273153.1.
DR RefSeq; NP_511095.1; NM_078540.5.
DR RefSeq; NP_523479.1; NM_078755.3.
DR RefSeq; NP_723056.2; NM_164624.3.
DR RefSeq; NP_727314.1; NM_167180.4.
DR RefSeq; NP_788892.1; NM_176719.1.
DR AlphaFoldDB; C0HL67; -.
DR SMR; C0HL67; -.
DR iPTMnet; C0HL67; -.
DR DNASU; 33736; -.
DR EnsemblMetazoa; FBtr0071345; FBpp0071280; FBgn0004828.
DR EnsemblMetazoa; FBtr0071346; FBpp0071281; FBgn0004828.
DR EnsemblMetazoa; FBtr0071347; FBpp0071282; FBgn0004828.
DR EnsemblMetazoa; FBtr0079010; FBpp0078649; FBgn0014857.
DR EnsemblMetazoa; FBtr0333536; FBpp0305716; FBgn0014857.
DR EnsemblMetazoa; FBtr0333537; FBpp0305717; FBgn0014857.
DR EnsemblMetazoa; FBtr0340343; FBpp0309302; FBgn0004828.
DR GeneID; 31848; -.
DR GeneID; 33736; -.
DR KEGG; dme:Dmel_CG5825; -.
DR KEGG; dme:Dmel_CG8989; -.
DR CTD; 31848; -.
DR CTD; 33736; -.
DR FlyBase; FBgn0004828; His3.3B.
DR VEuPathDB; VectorBase:FBgn0004828; -.
DR VEuPathDB; VectorBase:FBgn0014857; -.
DR OMA; SDCERRK; -.
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-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 PRO; PR:C0HL67; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0004828; Expressed in brain and 27 other tissues.
DR ExpressionAtlas; C0HL67; baseline and differential.
DR Genevisible; P84249; DM.
DR GO; GO:0000786; C:nucleosome; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IGI:FlyBase.
DR GO; GO:0006334; P:nucleosome assembly; NAS:UniProtKB.
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 Acetylation; Chromosome; DNA-binding; Methylation; Nucleosome core;
KW Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..136
FT /note="Histone H3.3B"
FT /id="PRO_0000443324"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:14732680"
FT MOD_RES 5
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:14732680"
FT MOD_RES 5
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:14732680"
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: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:0000250"
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 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:15371351"
FT MOD_RES 80
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:14732680,
FT ECO:0000269|PubMed:15371351"
FT MOD_RES 80
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:22389435"
SQ SEQUENCE 136 AA; 15328 MW; 5158ED279E6F9E1C CRC64;
MARTKQTARK STGGKAPRKQ LATKAARKSA PSTGGVKKPH RYRPGTVALR EIRRYQKSTE
LLIRKLPFQR LVREIAQDFK TDLRFQSAAI GALQEASEAY LVGLFEDTNL CAIHAKRVTI
MPKDIQLARR IRGERA
