H4_CAEEL
ID H4_CAEEL Reviewed; 103 AA.
AC P62784; O02619; P02306; P18678; Q7JNV2;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Histone H4;
GN Name=his-1; ORFNames=T10C6.14;
GN and
GN Name=his-5; ORFNames=F45F2.3;
GN and
GN Name=his-10; ORFNames=ZK131.4;
GN and
GN Name=his-14; ORFNames=ZK131.8;
GN and
GN Name=his-18; ORFNames=K06C4.10;
GN and
GN Name=his-26; ORFNames=ZK131.1;
GN and
GN Name=his-28; ORFNames=K06C4.2;
GN and
GN Name=his-31; ORFNames=F17E9.12;
GN and
GN Name=his-37; ORFNames=C50F4.7;
GN and
GN Name=his-38; ORFNames=K03A1.6;
GN and
GN Name=his-46; ORFNames=B0035.9;
GN and
GN Name=his-50; ORFNames=F07B7.9;
GN and
GN Name=his-56; ORFNames=F54E12.3;
GN and
GN Name=his-60; ORFNames=F55G1.11;
GN and
GN Name=his-64; ORFNames=F22B3.1;
GN and
GN Name=his-67; ORFNames=T23D8.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2544730; DOI=10.1016/0022-2836(89)90566-4;
RA Roberts S.B., Emmons S.W., Childs G.;
RT "Nucleotide sequences of Caenorhabditis elegans core histone genes. Genes
RT for different histone classes share common flanking sequence elements.";
RL J. Mol. Biol. 206:567-577(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP PROTEIN SEQUENCE OF 2-103, ACETYLATION AT SER-2, AND METHYLATION AT LYS-21.
RX PubMed=3665432; DOI=10.1016/0305-0491(87)90400-7;
RA Vanfleteren J.R., van Bun S.M., van Beeumen J.J.;
RT "The primary structure of histone H4 from the nematode Caenorhabditis
RT elegans.";
RL Comp. Biochem. Physiol. 87B:847-849(1987).
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. Chromosome.
CC -!- SIMILARITY: Belongs to the histone H4 family. {ECO:0000305}.
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DR EMBL; X15634; CAA33643.1; -; Genomic_DNA.
DR EMBL; FO081018; CCD68533.1; -; Genomic_DNA.
DR EMBL; FO081059; CCD68871.1; -; Genomic_DNA.
DR EMBL; FO081135; CCD69398.1; -; Genomic_DNA.
DR EMBL; FO081223; CCD70020.1; -; Genomic_DNA.
DR EMBL; FO081551; CCD72360.1; -; Genomic_DNA.
DR EMBL; FO081551; CCD72370.1; -; Genomic_DNA.
DR EMBL; FO081579; CCD72542.1; -; Genomic_DNA.
DR EMBL; Z68336; CAA92734.1; -; Genomic_DNA.
DR EMBL; Z70750; CAA94742.1; -; Genomic_DNA.
DR EMBL; Z73102; CAA97407.1; -; Genomic_DNA.
DR EMBL; Z81128; CAB03396.1; -; Genomic_DNA.
DR EMBL; Z82271; CAB05210.1; -; Genomic_DNA.
DR EMBL; Z83245; CAB05835.4; -; Genomic_DNA.
DR EMBL; Z83245; CAB05837.1; -; Genomic_DNA.
DR EMBL; Z83245; CAB05839.1; -; Genomic_DNA.
DR EMBL; Z93388; CAB07657.1; -; Genomic_DNA.
DR PIR; JS0314; JS0314.
DR PIR; S04240; S04240.
DR PIR; T27741; T27741.
DR PIR; T29230; T29230.
DR RefSeq; NP_492641.1; NM_060240.4.
DR RefSeq; NP_496889.1; NM_064488.1.
DR RefSeq; NP_496893.1; NM_064492.1.
DR RefSeq; NP_496896.1; NM_064495.1.
DR RefSeq; NP_501203.2; NM_068802.5.
DR RefSeq; NP_501406.1; NM_069005.1.
DR RefSeq; NP_502133.1; NM_069732.1.
DR RefSeq; NP_502139.1; NM_069738.1.
DR RefSeq; NP_502154.1; NM_069753.3.
DR RefSeq; NP_505200.1; NM_072799.3.
DR RefSeq; NP_505275.1; NM_072874.1.
DR RefSeq; NP_505291.1; NM_072890.1.
DR RefSeq; NP_505298.1; NM_072897.4.
DR RefSeq; NP_505466.1; NM_073065.6.
DR RefSeq; NP_507034.1; NM_074633.1.
DR RefSeq; NP_509231.1; NM_076830.1.
DR AlphaFoldDB; P62784; -.
DR SMR; P62784; -.
DR BioGRID; 43149; 2.
DR BioGRID; 44273; 1.
DR BioGRID; 44379; 2.
DR BioGRID; 53446; 48.
DR BioGRID; 56168; 3.
DR BioGRID; 56177; 1.
DR IntAct; P62784; 2.
DR STRING; 6239.B0035.9; -.
DR iPTMnet; P62784; -.
DR EPD; P62784; -.
DR PaxDb; P62784; -.
DR PeptideAtlas; P62784; -.
DR PRIDE; P62784; -.
DR ABCD; P62784; 1 sequenced antibody.
DR EnsemblMetazoa; B0035.9.1; B0035.9.1; WBGene00001920.
DR EnsemblMetazoa; C50F4.7.1; C50F4.7.1; WBGene00001911.
DR EnsemblMetazoa; F07B7.9.1; F07B7.9.1; WBGene00001924.
DR EnsemblMetazoa; F17E9.12.1; F17E9.12.1; WBGene00001905.
DR EnsemblMetazoa; F22B3.1.1; F22B3.1.1; WBGene00001938.
DR EnsemblMetazoa; F45F2.3.1; F45F2.3.1; WBGene00001879.
DR EnsemblMetazoa; F54E12.3.1; F54E12.3.1; WBGene00001930.
DR EnsemblMetazoa; F55G1.11.1; F55G1.11.1; WBGene00001934.
DR EnsemblMetazoa; K03A1.6.1; K03A1.6.1; WBGene00001912.
DR EnsemblMetazoa; K06C4.10.1; K06C4.10.1; WBGene00001892.
DR EnsemblMetazoa; K06C4.2.1; K06C4.2.1; WBGene00001902.
DR EnsemblMetazoa; T10C6.14.1; T10C6.14.1; WBGene00001875.
DR EnsemblMetazoa; T23D8.5.1; T23D8.5.1; WBGene00001941.
DR EnsemblMetazoa; ZK131.1.1; ZK131.1.1; WBGene00001900.
DR EnsemblMetazoa; ZK131.4.1; ZK131.4.1; WBGene00001884.
DR EnsemblMetazoa; ZK131.8.1; ZK131.8.1; WBGene00001888.
DR GeneID; 175027; -.
DR GeneID; 175032; -.
DR GeneID; 177522; -.
DR GeneID; 178050; -.
DR GeneID; 178055; -.
DR GeneID; 178066; -.
DR GeneID; 179233; -.
DR GeneID; 179260; -.
DR GeneID; 179264; -.
DR GeneID; 179267; -.
DR GeneID; 179341; -.
DR GeneID; 188792; -.
DR GeneID; 191667; -.
DR GeneID; 191671; -.
DR GeneID; 191677; -.
DR GeneID; 191680; -.
DR KEGG; cel:CELE_B0035.9; -.
DR KEGG; cel:CELE_C50F4.7; -.
DR KEGG; cel:CELE_F07B7.9; -.
DR KEGG; cel:CELE_F17E9.12; -.
DR KEGG; cel:CELE_F22B3.1; -.
DR KEGG; cel:CELE_F45F2.3; -.
DR KEGG; cel:CELE_F54E12.3; -.
DR KEGG; cel:CELE_F55G1.11; -.
DR KEGG; cel:CELE_K03A1.6; -.
DR KEGG; cel:CELE_K06C4.10; -.
DR KEGG; cel:CELE_K06C4.2; -.
DR KEGG; cel:CELE_T10C6.14; -.
DR KEGG; cel:CELE_T23D8.5; -.
DR KEGG; cel:CELE_ZK131.1; -.
DR KEGG; cel:CELE_ZK131.4; -.
DR KEGG; cel:CELE_ZK131.8; -.
DR UCSC; T23D8.5; c. elegans.
DR CTD; 175027; -.
DR CTD; 175032; -.
DR CTD; 177522; -.
DR CTD; 178050; -.
DR CTD; 178055; -.
DR CTD; 178066; -.
DR CTD; 179233; -.
DR CTD; 179260; -.
DR CTD; 179264; -.
DR CTD; 179267; -.
DR CTD; 179341; -.
DR CTD; 188792; -.
DR CTD; 191667; -.
DR CTD; 191671; -.
DR CTD; 191677; -.
DR CTD; 191680; -.
DR WormBase; B0035.9; CE03252; WBGene00001920; his-46.
DR WormBase; C50F4.7; CE03252; WBGene00001911; his-37.
DR WormBase; F07B7.9; CE03252; WBGene00001924; his-50.
DR WormBase; F17E9.12; CE03252; WBGene00001905; his-31.
DR WormBase; F22B3.1; CE03252; WBGene00001938; his-64.
DR WormBase; F45F2.3; CE03252; WBGene00001879; his-5.
DR WormBase; F54E12.3; CE03252; WBGene00001930; his-56.
DR WormBase; F55G1.11; CE03252; WBGene00001934; his-60.
DR WormBase; K03A1.6; CE03252; WBGene00001912; his-38.
DR WormBase; K06C4.10; CE03252; WBGene00001892; his-18.
DR WormBase; K06C4.2; CE03252; WBGene00001902; his-28.
DR WormBase; T10C6.14; CE03252; WBGene00001875; his-1.
DR WormBase; T23D8.5; CE03252; WBGene00001941; his-67.
DR WormBase; ZK131.1; CE03252; WBGene00001900; his-26.
DR WormBase; ZK131.4; CE03252; WBGene00001884; his-10.
DR WormBase; ZK131.8; CE03252; WBGene00001888; his-14.
DR eggNOG; KOG3467; Eukaryota.
DR GeneTree; ENSGT01050000244867; -.
DR HOGENOM; CLU_109117_2_3_1; -.
DR InParanoid; P62784; -.
DR OMA; XLARRGG; -.
DR OrthoDB; 1564596at2759; -.
DR PhylomeDB; P62784; -.
DR Reactome; R-CEL-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-CEL-212300; PRC2 methylates histones and DNA.
DR Reactome; R-CEL-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-CEL-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-CEL-3214815; HDACs deacetylate histones.
DR Reactome; R-CEL-3214841; PKMTs methylate histone lysines.
DR Reactome; R-CEL-3214842; HDMs demethylate histones.
DR Reactome; R-CEL-3214847; HATs acetylate histones.
DR Reactome; R-CEL-3214858; RMTs methylate histone arginines.
DR Reactome; R-CEL-427359; SIRT1 negatively regulates rRNA expression.
DR Reactome; R-CEL-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-CEL-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-CEL-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-CEL-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-CEL-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-CEL-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-CEL-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-CEL-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-CEL-9018519; Estrogen-dependent gene expression.
DR PRO; PR:P62784; -.
DR Proteomes; UP000001940; Chromosome I.
DR Proteomes; UP000001940; Chromosome II.
DR Proteomes; UP000001940; Chromosome IV.
DR Proteomes; UP000001940; Chromosome V.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00001875; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
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; IBA:GO_Central.
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 Pfam; PF15511; CENP-T_C; 1.
DR PRINTS; PR00623; HISTONEH4.
DR SMART; SM00417; H4; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00047; HISTONE_H4; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromosome; Direct protein sequencing; DNA-binding;
KW Methylation; Nucleosome core; Nucleus; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3665432"
FT CHAIN 2..103
FT /note="Histone H4"
FT /id="PRO_0000158290"
FT DNA_BIND 17..21
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:3665432"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 21
FT /note="N6-methyllysine"
FT /evidence="ECO:0000269|PubMed:3665432"
FT CONFLICT 3
FT /note="G -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 103 AA; 11369 MW; A9E5DFD3F8AF04FF CRC64;
MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK
VFLENVIRDA VTYCEHAKRK TVTAMDVVYA LKRQGRTLYG FGG