H332_CAEEL
ID H332_CAEEL Reviewed; 136 AA.
AC Q9U281;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Histone H3.3 type 2;
GN Name=his-72; ORFNames=Y49E10.6;
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 FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR
RP LOCATION.
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:0000269|PubMed:16846252}. Chromosome
CC {ECO:0000269|PubMed:16846252}. Note=Depleted from the meiotically
CC silenced X chromosome.
CC -!- TISSUE SPECIFICITY: Highly expressed in nearly all larval and adult
CC nuclei. Expressed only at low levels in intestine. Expressed throughout
CC all stages of gametogenesis. {ECO:0000269|PubMed:16846252}.
CC -!- DEVELOPMENTAL STAGE: Present at all embryonic stages (at protein
CC level). {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; Z98866; CAB11546.1; -; Genomic_DNA.
DR PIR; T27037; T27037.
DR RefSeq; NP_001255163.1; NM_001268234.1.
DR AlphaFoldDB; Q9U281; -.
DR SMR; Q9U281; -.
DR BioGRID; 41839; 3.
DR DIP; DIP-26716N; -.
DR IntAct; Q9U281; 1.
DR EPD; Q9U281; -.
DR PeptideAtlas; Q9U281; -.
DR PRIDE; Q9U281; -.
DR EnsemblMetazoa; Y49E10.6a.1; Y49E10.6a.1; WBGene00001946.
DR GeneID; 176660; -.
DR UCSC; Y49E10.6.2; c. elegans.
DR CTD; 176660; -.
DR WormBase; Y49E10.6a; CE22223; WBGene00001946; his-72.
DR HOGENOM; CLU_078295_4_0_1; -.
DR InParanoid; Q9U281; -.
DR PhylomeDB; Q9U281; -.
DR PRO; PR:Q9U281; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001946; Expressed in embryo and 4 other tissues.
DR ExpressionAtlas; Q9U281; baseline and differential.
DR GO; GO:0000786; C:nucleosome; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
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 Acetylation; Chromosome; DNA-binding; Methylation; Nucleosome core;
KW 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 2"
FT /id="PRO_0000268632"
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; 15360 MW; 57E8809451022E77 CRC64;
MARTKQTARK STGGKAPRKQ LATKAARKSA PTTGGVKKPH RYRPGTVALR EIRRYQKSTE
LLIRKLPFQR LVREIAQDFK TDLRFQSAAI GALQEASEAY LVGLFEDTNL CAIHAKRVTI
MPKDMQLARR IRGERA
