H4_DROER
ID H4_DROER Reviewed; 103 AA.
AC P84041; B3NLS1; 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=GG16866;
GN and
GN ORFNames=GG21497;
GN and
GN ORFNames=GG21499;
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
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] (GG16866; GG21497 AND
RP GG21499).
RC STRAIN=Tucson 14021-0224.01;
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; AB073634; BAC54551.1; -; Genomic_DNA.
DR EMBL; CH954179; EDV54409.1; -; Genomic_DNA.
DR EMBL; CH954179; EDV54414.1; -; Genomic_DNA.
DR EMBL; CH954181; EDV48906.1; -; Genomic_DNA.
DR RefSeq; XP_001974009.1; XM_001973973.2.
DR RefSeq; XP_001974014.1; XM_001973978.2.
DR RefSeq; XP_001979948.1; XM_001979912.2.
DR RefSeq; XP_001982909.2; XM_001982873.2.
DR RefSeq; XP_015008608.1; XM_015153122.1.
DR AlphaFoldDB; P84041; -.
DR SMR; P84041; -.
DR EnsemblMetazoa; FBtr0136920; FBpp0135412; FBgn0109094.
DR EnsemblMetazoa; FBtr0141551; FBpp0140043; FBgn0113676.
DR EnsemblMetazoa; FBtr0141553; FBpp0140045; FBgn0113678.
DR GeneID; 6548695; -.
DR GeneID; 6552863; -.
DR GeneID; 6556039; -.
DR GeneID; 6556049; -.
DR KEGG; der:6548695; -.
DR KEGG; der:6552863; -.
DR KEGG; der:6556039; -.
DR KEGG; der:6556049; -.
DR FlyBase; FBgn0064617; Dere\His4.
DR eggNOG; KOG3467; Eukaryota.
DR HOGENOM; CLU_109117_2_3_1; -.
DR OMA; RRNRNMS; -.
DR OrthoDB; 1594208at2759; -.
DR PhylomeDB; P84041; -.
DR Proteomes; UP000008711; Unassembled WGS sequence.
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.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..103
FT /note="Histone H4"
FT /id="PRO_0000158302"
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
