H4_DROME
ID H4_DROME Reviewed; 103 AA.
AC P84040; A4V2W8; P02307; Q4AB71; Q4ABE0; Q6AWN1; Q9VFH7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Histone H4;
GN Name=His4; Synonyms=H4;
GN and
GN Name=His4r; Synonyms=H4r; ORFNames=CG3379;
GN and
GN Name=His4:CG31611; ORFNames=CG31611;
GN and
GN Name=His4:CG33869; ORFNames=CG33869;
GN and
GN Name=His4:CG33871; ORFNames=CG33871;
GN and
GN Name=His4:CG33873; ORFNames=CG33873;
GN and
GN Name=His4:CG33875; ORFNames=CG33875;
GN and
GN Name=His4:CG33877; ORFNames=CG33877;
GN and
GN Name=His4:CG33879; ORFNames=CG33879;
GN and
GN Name=His4:CG33881; ORFNames=CG33881;
GN and
GN Name=His4:CG33883; ORFNames=CG33883;
GN and
GN Name=His4:CG33885; ORFNames=CG33885;
GN and
GN Name=His4:CG33887; ORFNames=CG33887;
GN and
GN Name=His4:CG33889; ORFNames=CG33889;
GN and
GN Name=His4:CG33891; ORFNames=CG33891;
GN and
GN Name=His4:CG33893; ORFNames=CG33893;
GN and
GN Name=His4:CG33895; ORFNames=CG33895;
GN and
GN Name=His4:CG33897; ORFNames=CG33897;
GN and
GN Name=His4:CG33899; ORFNames=CG33899;
GN and
GN Name=His4:CG33901; ORFNames=CG33901;
GN and
GN Name=His4:CG33903; ORFNames=CG33903;
GN and
GN Name=His4:CG33905; ORFNames=CG33905;
GN and
GN Name=His4:CG33907; ORFNames=CG33907;
GN and
GN Name=His4:CG33909; ORFNames=CG33909;
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] (HIS4).
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 / MRNA] (HIS4R).
RC STRAIN=Canton-S;
RX PubMed=8690091; DOI=10.1016/0014-5793(96)00551-0;
RA Akhmanova A., Miedema K., Hennig W.;
RT "Identification and characterization of the Drosophila histone H4
RT replacement gene.";
RL FEBS Lett. 388:219-222(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HIS4R; HIS4:CG31611;
RP HIS4:CG33869; HIS4:CG33871; HIS4:CG33873; HIS4:CG33875; HIS4:CG33877;
RP HIS4:CG33879; HIS4:CG33881; HIS4:CG33883; HIS4:CG33885; HIS4:CG33887;
RP HIS4:CG33889; HIS4:CG33891; HIS4:CG33893; HIS4:CG33895; HIS4:CG33897;
RP HIS4:CG33899; HIS4:CG33901; HIS4:CG33903; HIS4:CG33905; HIS4:CG33907 AND
RP HIS4:CG33909).
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=Head;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE OF 1-72 (HIS4).
RA Goldberg M.L.;
RL Thesis (1979), University of Stanford, United States.
RN [8]
RP ACETYLATION AT LYS-6 AND LYS-13.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-81 AND THR-83, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [10]
RP SUCCINYLATION AT LYS-32; LYS-78; LYS-80 AND LYS-92.
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).
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 P84040; Q92831: KAT2B; Xeno; NbExp=2; IntAct=EBI-185028, EBI-477430;
CC P84040; O94267: spt16; Xeno; NbExp=2; IntAct=EBI-185028, EBI-7414132;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- PTM: Acetylated on Lys-6 and Lys-13 during prophase I of meiosis.
CC Phosphorylation of H2A 'Thr-119' is a prerequisite for H4 Lys-6
CC acetylation but not for H4 Lys-13 acetylation.
CC {ECO:0000269|PubMed:16230526, ECO:0000269|PubMed:18327897}.
CC -!- SIMILARITY: Belongs to the histone H4 family. {ECO:0000305}.
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DR EMBL; X14215; CAA32435.1; -; Genomic_DNA.
DR EMBL; X97437; CAA66067.1; -; Genomic_DNA.
DR EMBL; X97438; CAA66068.1; -; mRNA.
DR EMBL; AE014297; AAF55080.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN11126.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13612.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13613.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66480.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66484.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66489.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66493.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66498.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66503.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66508.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66513.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66518.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66523.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66528.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66533.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66538.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66543.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66548.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66553.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66558.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66563.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66568.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66573.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66578.1; -; Genomic_DNA.
DR EMBL; BT001842; AAN71603.1; -; mRNA.
DR EMBL; BT015217; AAT94446.1; -; mRNA.
DR PIR; S10098; HSFF4.
DR RefSeq; NP_001027284.1; NM_001032113.2.
DR RefSeq; NP_001027288.1; NM_001032117.2.
DR RefSeq; NP_001027293.1; NM_001032122.2.
DR RefSeq; NP_001027297.1; NM_001032126.2.
DR RefSeq; NP_001027302.1; NM_001032131.2.
DR RefSeq; NP_001027307.1; NM_001032136.2.
DR RefSeq; NP_001027312.1; NM_001032141.2.
DR RefSeq; NP_001027317.1; NM_001032146.2.
DR RefSeq; NP_001027322.1; NM_001032151.2.
DR RefSeq; NP_001027327.1; NM_001032156.2.
DR RefSeq; NP_001027332.1; NM_001032161.2.
DR RefSeq; NP_001027337.1; NM_001032166.2.
DR RefSeq; NP_001027342.1; NM_001032171.2.
DR RefSeq; NP_001027347.1; NM_001032176.2.
DR RefSeq; NP_001027352.1; NM_001032181.2.
DR RefSeq; NP_001027357.1; NM_001032186.2.
DR RefSeq; NP_001027362.1; NM_001032191.2.
DR RefSeq; NP_001027367.1; NM_001032196.1.
DR RefSeq; NP_001027372.1; NM_001032201.1.
DR RefSeq; NP_001027377.1; NM_001032206.1.
DR RefSeq; NP_001027382.1; NM_001032211.1.
DR RefSeq; NP_001262576.1; NM_001275647.1.
DR RefSeq; NP_524352.1; NM_079628.4.
DR RefSeq; NP_724344.1; NM_165383.3.
DR RefSeq; NP_731927.1; NM_169592.3.
DR RefSeq; NP_731928.1; NM_169593.3.
DR PDB; 2NQB; X-ray; 2.30 A; B/F=2-103.
DR PDB; 2PYO; X-ray; 2.43 A; B/F=2-103.
DR PDB; 2XYI; X-ray; 1.75 A; B=27-46.
DR PDB; 3C9C; X-ray; 3.20 A; B=16-42.
DR PDB; 4QLC; X-ray; 3.50 A; B/F=2-103.
DR PDB; 4UUZ; X-ray; 2.90 A; B=1-103.
DR PDB; 4X23; X-ray; 3.50 A; B/F/L/P=25-103.
DR PDB; 5WCU; X-ray; 5.53 A; B/F/L/P=22-103.
DR PDB; 6DZT; EM; 2.99 A; B/F=2-103.
DR PDB; 6PWE; EM; 3.95 A; B/F=1-103.
DR PDB; 6PWF; EM; 4.07 A; B/F=1-103.
DR PDB; 6XWS; X-ray; 4.36 A; B=1-103.
DR PDB; 6XWT; X-ray; 3.47 A; B/D=1-103.
DR PDBsum; 2NQB; -.
DR PDBsum; 2PYO; -.
DR PDBsum; 2XYI; -.
DR PDBsum; 3C9C; -.
DR PDBsum; 4QLC; -.
DR PDBsum; 4UUZ; -.
DR PDBsum; 4X23; -.
DR PDBsum; 5WCU; -.
DR PDBsum; 6DZT; -.
DR PDBsum; 6PWE; -.
DR PDBsum; 6PWF; -.
DR PDBsum; 6XWS; -.
DR PDBsum; 6XWT; -.
DR AlphaFoldDB; P84040; -.
DR SMR; P84040; -.
DR BioGRID; 534263; 1.
DR BioGRID; 66847; 11.
DR BioGRID; 77139; 46.
DR DIP; DIP-29505N; -.
DR IntAct; P84040; 33.
DR MINT; P84040; -.
DR STRING; 7227.FBpp0082421; -.
DR iPTMnet; P84040; -.
DR PaxDb; P84040; -.
DR PRIDE; P84040; -.
DR DNASU; 3772708; -.
DR EnsemblMetazoa; FBtr0082962; FBpp0082421; FBgn0013981.
DR EnsemblMetazoa; FBtr0082963; FBpp0082422; FBgn0013981.
DR EnsemblMetazoa; FBtr0082964; FBpp0082423; FBgn0013981.
DR EnsemblMetazoa; FBtr0085926; FBpp0085280; FBgn0051611.
DR EnsemblMetazoa; FBtr0091875; FBpp0091116; FBgn0053871.
DR EnsemblMetazoa; FBtr0091877; FBpp0091118; FBgn0053873.
DR EnsemblMetazoa; FBtr0091879; FBpp0091120; FBgn0053875.
DR EnsemblMetazoa; FBtr0091887; FBpp0091128; FBgn0053883.
DR EnsemblMetazoa; FBtr0091889; FBpp0091130; FBgn0053885.
DR EnsemblMetazoa; FBtr0091891; FBpp0091132; FBgn0053887.
DR EnsemblMetazoa; FBtr0091893; FBpp0091134; FBgn0053889.
DR EnsemblMetazoa; FBtr0091895; FBpp0091136; FBgn0053891.
DR EnsemblMetazoa; FBtr0091897; FBpp0091138; FBgn0053893.
DR EnsemblMetazoa; FBtr0091899; FBpp0091140; FBgn0053895.
DR EnsemblMetazoa; FBtr0091901; FBpp0091142; FBgn0053897.
DR EnsemblMetazoa; FBtr0091903; FBpp0091144; FBgn0053899.
DR EnsemblMetazoa; FBtr0091905; FBpp0091146; FBgn0053901.
DR EnsemblMetazoa; FBtr0091907; FBpp0091148; FBgn0053903.
DR EnsemblMetazoa; FBtr0091909; FBpp0091150; FBgn0053905.
DR EnsemblMetazoa; FBtr0091911; FBpp0091152; FBgn0053907.
DR EnsemblMetazoa; FBtr0091913; FBpp0091154; FBgn0053909.
DR EnsemblMetazoa; FBtr0334029; FBpp0306146; FBgn0013981.
DR GeneID; 318846; -.
DR GeneID; 3771854; -.
DR GeneID; 3771893; -.
DR GeneID; 3771908; -.
DR GeneID; 3771935; -.
DR GeneID; 3771938; -.
DR GeneID; 3771941; -.
DR GeneID; 3771947; -.
DR GeneID; 3772096; -.
DR GeneID; 3772113; -.
DR GeneID; 3772129; -.
DR GeneID; 3772172; -.
DR GeneID; 3772211; -.
DR GeneID; 3772254; -.
DR GeneID; 3772314; -.
DR GeneID; 3772317; -.
DR GeneID; 3772319; -.
DR GeneID; 3772325; -.
DR GeneID; 3772509; -.
DR GeneID; 3772519; -.
DR GeneID; 3772666; -.
DR GeneID; 3772708; -.
DR GeneID; 41773; -.
DR KEGG; dme:Dmel_CG31611; -.
DR KEGG; dme:Dmel_CG3379; -.
DR KEGG; dme:Dmel_CG33869; -.
DR KEGG; dme:Dmel_CG33871; -.
DR KEGG; dme:Dmel_CG33873; -.
DR KEGG; dme:Dmel_CG33875; -.
DR KEGG; dme:Dmel_CG33877; -.
DR KEGG; dme:Dmel_CG33879; -.
DR KEGG; dme:Dmel_CG33881; -.
DR KEGG; dme:Dmel_CG33883; -.
DR KEGG; dme:Dmel_CG33885; -.
DR KEGG; dme:Dmel_CG33887; -.
DR KEGG; dme:Dmel_CG33889; -.
DR KEGG; dme:Dmel_CG33891; -.
DR KEGG; dme:Dmel_CG33893; -.
DR KEGG; dme:Dmel_CG33895; -.
DR KEGG; dme:Dmel_CG33897; -.
DR KEGG; dme:Dmel_CG33899; -.
DR KEGG; dme:Dmel_CG33901; -.
DR KEGG; dme:Dmel_CG33903; -.
DR KEGG; dme:Dmel_CG33905; -.
DR KEGG; dme:Dmel_CG33907; -.
DR KEGG; dme:Dmel_CG33909; -.
DR UCSC; CG31611-RA; d. melanogaster.
DR CTD; 318846; -.
DR CTD; 3771854; -.
DR CTD; 3771893; -.
DR CTD; 3771908; -.
DR CTD; 3771935; -.
DR CTD; 3771938; -.
DR CTD; 3771941; -.
DR CTD; 3771947; -.
DR CTD; 3772096; -.
DR CTD; 3772113; -.
DR CTD; 3772129; -.
DR CTD; 3772172; -.
DR CTD; 3772211; -.
DR CTD; 3772254; -.
DR CTD; 3772314; -.
DR CTD; 3772317; -.
DR CTD; 3772319; -.
DR CTD; 3772325; -.
DR CTD; 3772509; -.
DR CTD; 3772519; -.
DR CTD; 3772666; -.
DR CTD; 3772708; -.
DR CTD; 41773; -.
DR FlyBase; FBgn0001200; His4.
DR FlyBase; FBgn0051611; His4:CG31611.
DR FlyBase; FBgn0053869; His4:CG33869.
DR FlyBase; FBgn0053871; His4:CG33871.
DR FlyBase; FBgn0053873; His4:CG33873.
DR FlyBase; FBgn0053875; His4:CG33875.
DR FlyBase; FBgn0053877; His4:CG33877.
DR FlyBase; FBgn0053879; His4:CG33879.
DR FlyBase; FBgn0053881; His4:CG33881.
DR FlyBase; FBgn0053883; His4:CG33883.
DR FlyBase; FBgn0053885; His4:CG33885.
DR FlyBase; FBgn0053887; His4:CG33887.
DR FlyBase; FBgn0053889; His4:CG33889.
DR FlyBase; FBgn0053891; His4:CG33891.
DR FlyBase; FBgn0053893; His4:CG33893.
DR FlyBase; FBgn0053895; His4:CG33895.
DR FlyBase; FBgn0053897; His4:CG33897.
DR FlyBase; FBgn0053899; His4:CG33899.
DR FlyBase; FBgn0053901; His4:CG33901.
DR FlyBase; FBgn0053903; His4:CG33903.
DR FlyBase; FBgn0053905; His4:CG33905.
DR FlyBase; FBgn0053907; His4:CG33907.
DR FlyBase; FBgn0053909; His4:CG33909.
DR FlyBase; FBgn0013981; His4r.
DR VEuPathDB; VectorBase:FBgn0013981; -.
DR VEuPathDB; VectorBase:FBgn0051611; -.
DR VEuPathDB; VectorBase:FBgn0053871; -.
DR VEuPathDB; VectorBase:FBgn0053873; -.
DR VEuPathDB; VectorBase:FBgn0053875; -.
DR VEuPathDB; VectorBase:FBgn0053883; -.
DR VEuPathDB; VectorBase:FBgn0053885; -.
DR VEuPathDB; VectorBase:FBgn0053887; -.
DR VEuPathDB; VectorBase:FBgn0053889; -.
DR VEuPathDB; VectorBase:FBgn0053891; -.
DR VEuPathDB; VectorBase:FBgn0053893; -.
DR VEuPathDB; VectorBase:FBgn0053895; -.
DR VEuPathDB; VectorBase:FBgn0053897; -.
DR VEuPathDB; VectorBase:FBgn0053899; -.
DR VEuPathDB; VectorBase:FBgn0053901; -.
DR VEuPathDB; VectorBase:FBgn0053903; -.
DR VEuPathDB; VectorBase:FBgn0053905; -.
DR VEuPathDB; VectorBase:FBgn0053907; -.
DR VEuPathDB; VectorBase:FBgn0053909; -.
DR eggNOG; KOG3467; Eukaryota.
DR GeneTree; ENSGT00990000203553; -.
DR HOGENOM; CLU_109117_2_3_1; -.
DR InParanoid; P84040; -.
DR OrthoDB; 1594208at2759; -.
DR PhylomeDB; P84040; -.
DR SignaLink; P84040; -.
DR BioGRID-ORCS; 41773; 0 hits in 1 CRISPR screen.
DR ChiTaRS; His4r; fly.
DR EvolutionaryTrace; P84040; -.
DR PRO; PR:P84040; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0013981; Expressed in eye disc (Drosophila) and 24 other tissues.
DR ExpressionAtlas; P84040; baseline and differential.
DR Genevisible; P84040; DM.
DR GO; GO:0005694; C:chromosome; IDA:FlyBase.
DR GO; GO:0000228; C:nuclear chromosome; IDA:FlyBase.
DR GO; GO:0000786; C:nucleosome; IDA:UniProtKB.
DR GO; GO:0035059; C:RCAF complex; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB.
DR CDD; cd00076; H4; 1.
DR DisProt; DP01870; -.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR035425; CENP-T/H4_C.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR001951; Histone_H4.
DR InterPro; IPR019809; Histone_H4_CS.
DR InterPro; IPR004823; TAF_TATA-bd_Histone-like_dom.
DR Pfam; PF15511; CENP-T_C; 1.
DR PRINTS; PR00623; HISTONEH4.
DR SMART; SM00417; H4; 1.
DR SMART; SM00803; TAF; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00047; HISTONE_H4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromosome; DNA-binding; Nucleosome core;
KW Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..103
FT /note="Histone H4"
FT /id="PRO_0000158305"
FT DNA_BIND 17..21
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:16230526"
FT MOD_RES 13
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:16230526"
FT MOD_RES 32
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000269|PubMed:22389435"
FT MOD_RES 78
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000269|PubMed:22389435"
FT MOD_RES 80
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000269|PubMed:22389435"
FT MOD_RES 81
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 83
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 92
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000269|PubMed:22389435"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:2NQB"
FT HELIX 32..40
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:4UUZ"
FT HELIX 51..76
FT /evidence="ECO:0007829|PDB:2NQB"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:2NQB"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:2NQB"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:2NQB"
SQ SEQUENCE 103 AA; 11381 MW; DF3EB26393BD208C CRC64;
MTGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK
VFLENVIRDA VTYTEHAKRK TVTAMDVVYA LKRQGRTLYG FGG
