H4_DROSI
ID H4_DROSI Reviewed; 103 AA.
AC P84043; B4NV77; P02307; Q9VFH7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Histone H4;
GN Name=His4; Synonyms=H4;
GN and
GN ORFNames=GD12574;
GN and
GN ORFNames=GD18968;
OS Drosophila simulans (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7240;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIS4).
RX PubMed=11922104; DOI=10.1266/ggs.76.355;
RA Tsunemoto K., Matsuo Y.;
RT "Molecular evolutionary analysis of a histone gene repeating unit from
RT Drosophila simulans.";
RL Genes Genet. Syst. 76:355-361(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (GD12574 AND GD18968).
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone H4 family. {ECO:0000305}.
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DR EMBL; AB055959; BAC54547.1; -; Genomic_DNA.
DR EMBL; CH986436; EDX15953.1; -; Genomic_DNA.
DR EMBL; CH986794; EDX15974.1; -; Genomic_DNA.
DR EMBL; CH987252; EDX16002.1; -; Genomic_DNA.
DR EMBL; CH987286; EDX16007.1; -; Genomic_DNA.
DR EMBL; CH988002; EDX16053.1; -; Genomic_DNA.
DR EMBL; CH988652; EDX16098.1; -; Genomic_DNA.
DR EMBL; CH988719; EDX16106.1; -; Genomic_DNA.
DR EMBL; CH989288; EDX16152.1; -; Genomic_DNA.
DR EMBL; CH989298; EDX16154.1; -; Genomic_DNA.
DR EMBL; CH990027; EDX16208.1; -; Genomic_DNA.
DR EMBL; CH991103; EDX16251.1; -; Genomic_DNA.
DR EMBL; CM000364; EDX12930.1; -; Genomic_DNA.
DR RefSeq; XP_002077371.1; XM_002077335.2.
DR RefSeq; XP_016034694.1; XM_016175314.1.
DR RefSeq; XP_016034695.1; XM_016175315.1.
DR AlphaFoldDB; P84043; -.
DR SMR; P84043; -.
DR STRING; 7240.P84043; -.
DR EnsemblMetazoa; FBtr0212484; FBpp0210976; FBgn0184301.
DR EnsemblMetazoa; FBtr0218878; FBpp0217370; FBgn0190477.
DR EnsemblMetazoa; FBtr0356260; FBpp0320456; FBgn0190477.
DR GeneID; 6728075; -.
DR GeneID; 6740547; -.
DR HOGENOM; CLU_109117_2_3_1; -.
DR OMA; QKEHING; -.
DR PhylomeDB; P84043; -.
DR Proteomes; UP000000304; Chromosome 3r.
DR Proteomes; UP000000304; Unassembled WGS sequence.
DR Bgee; FBgn0184301; Expressed in embryo and 3 other tissues.
DR GO; GO:0000786; C:nucleosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; ISS: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; ISS:UniProtKB.
DR CDD; cd00076; H4; 1.
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 3: Inferred from homology;
KW Acetylation; Chromosome; DNA-binding; Nucleosome core; Nucleus;
KW 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_0000158308"
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:0000250|UniProtKB:P84040"
FT MOD_RES 13
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P84040"
FT MOD_RES 32
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P84040"
FT MOD_RES 78
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P84040"
FT MOD_RES 80
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P84040"
FT MOD_RES 81
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P84040"
FT MOD_RES 83
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P84040"
FT MOD_RES 92
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P84040"
SQ SEQUENCE 103 AA; 11381 MW; DF3EB26393BD208C CRC64;
MTGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK
VFLENVIRDA VTYTEHAKRK TVTAMDVVYA LKRQGRTLYG FGG
