H331_CAEEL
ID H331_CAEEL Reviewed; 136 AA.
AC Q10453;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Histone H3.3 type 1;
GN Name=his-71; ORFNames=F45E1.6;
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 [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 [2]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=16846252; DOI=10.1371/journal.pgen.0020097;
RA Ooi S.L., Priess J.R., Henikoff S.;
RT "Histone H3.3 variant dynamics in the germline of Caenorhabditis elegans.";
RL PLoS Genet. 2:883-895(2006).
CC -!- FUNCTION: Variant histone H3 which replaces conventional H3 in a wide
CC range of nucleosomes in active genes. Constitutes the predominant form
CC of histone H3 in non-dividing cells and is incorporated into chromatin
CC independently of DNA synthesis. Deposited at sites of nucleosomal
CC displacement throughout transcribed genes, suggesting that it
CC represents an epigenetic imprint of transcriptionally active chromatin.
CC Nucleosomes wrap and compact DNA into chromatin, limiting DNA
CC accessibility to the cellular machineries which require DNA as a
CC template. Histones thereby play a central role in transcription
CC regulation, DNA repair, DNA replication and chromosomal stability. DNA
CC accessibility is regulated via a complex set of post-translational
CC modifications of histones, also called histone code, and nucleosome
CC remodeling. {ECO:0000269|PubMed:16846252}.
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 -!- TISSUE SPECIFICITY: Highly expressed in all adult nuclei.
CC {ECO:0000269|PubMed:16846252}.
CC -!- PTM: Acetylation is generally linked to gene activation. {ECO:0000250}.
CC -!- PTM: Methylation at Lys-5 is linked to gene activation. Methylation at
CC Lys-10 is linked to gene repression (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
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DR EMBL; FO080773; CCD66641.1; -; Genomic_DNA.
DR PIR; T16361; T16361.
DR RefSeq; NP_509344.1; NM_076943.4.
DR PDB; 4ZBJ; X-ray; 2.25 A; B=62-136.
DR PDBsum; 4ZBJ; -.
DR AlphaFoldDB; Q10453; -.
DR SMR; Q10453; -.
DR BioGRID; 45980; 3.
DR DIP; DIP-26634N; -.
DR STRING; 6239.F45E1.6; -.
DR EPD; Q10453; -.
DR PaxDb; Q10453; -.
DR PeptideAtlas; Q10453; -.
DR PRIDE; Q10453; -.
DR EnsemblMetazoa; F45E1.6.1; F45E1.6.1; WBGene00001945.
DR GeneID; 181057; -.
DR KEGG; cel:CELE_F45E1.6; -.
DR UCSC; F45E1.6.2; c. elegans.
DR CTD; 181057; -.
DR WormBase; F45E1.6; CE01943; WBGene00001945; his-71.
DR eggNOG; KOG1745; Eukaryota.
DR GeneTree; ENSGT01050000244918; -.
DR HOGENOM; CLU_078295_4_0_1; -.
DR InParanoid; Q10453; -.
DR OMA; HIVMART; -.
DR OrthoDB; 1564596at2759; -.
DR PhylomeDB; Q10453; -.
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-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-CEL-427359; SIRT1 negatively regulates rRNA expression.
DR Reactome; R-CEL-427413; NoRC negatively regulates rRNA expression.
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-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 Reactome; R-CEL-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:Q10453; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00001945; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
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 3D-structure; Acetylation; Chromosome; DNA-binding; Methylation;
KW Nucleosome core; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..136
FT /note="Histone H3.3 type 1"
FT /id="PRO_0000221298"
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:0000250"
FT MOD_RES 5
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 5
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 5
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 10
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 10
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 10
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 15
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 24
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 28
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 28
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 28
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 37
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 37
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 80
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 136 AA; 15342 MW; 57E8809145022E77 CRC64;
MARTKQTARK STGGKAPRKQ LATKAARKSA PTTGGVKKPH RYRPGTVALR EIRRYQKSTE
LLIRKLPFQR LVREIAQDFK TDLRFQSAAI GALQEASEAY LVGLFEDTNL CAIHAKRVTI
MPKDIQLARR IRGERA
