H33L2_CAEEL
ID H33L2_CAEEL Reviewed; 136 AA.
AC Q27532;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Histone H3.3-like type 2;
GN Name=his-74; ORFNames=W05B10.1;
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 IDENTIFICATION.
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: Putative variant histone H3 which may replace conventional H3
CC in a subset of nucleosomes. Nucleosomes wrap and compact DNA into
CC chromatin, limiting DNA accessibility to the cellular machineries which
CC require DNA as a template. Histones thereby play a central role in
CC transcription regulation, DNA repair, DNA replication and chromosomal
CC stability. DNA accessibility is regulated via a complex set of post-
CC translational modifications of histones, also called histone code, and
CC nucleosome remodeling (By similarity). {ECO:0000250}.
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 DNA
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
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; Z74476; CAA98963.1; -; Genomic_DNA.
DR PIR; T26178; T26178.
DR RefSeq; NP_506164.1; NM_073763.4.
DR AlphaFoldDB; Q27532; -.
DR SMR; Q27532; -.
DR BioGRID; 44754; 4.
DR DIP; DIP-24615N; -.
DR STRING; 6239.W05B10.1; -.
DR EPD; Q27532; -.
DR PaxDb; Q27532; -.
DR PeptideAtlas; Q27532; -.
DR PRIDE; Q27532; -.
DR EnsemblMetazoa; W05B10.1.1; W05B10.1.1; WBGene00012276.
DR GeneID; 179734; -.
DR KEGG; cel:CELE_W05B10.1; -.
DR UCSC; W05B10.1; c. elegans.
DR CTD; 179734; -.
DR WormBase; W05B10.1; CE06544; WBGene00012276; his-74.
DR eggNOG; KOG1745; Eukaryota.
DR GeneTree; ENSGT01050000244918; -.
DR HOGENOM; CLU_078295_4_0_1; -.
DR InParanoid; Q27532; -.
DR OMA; THIRITR; -.
DR OrthoDB; 1564596at2759; -.
DR PhylomeDB; Q27532; -.
DR PRO; PR:Q27532; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00012276; Expressed in adult organism and 4 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; PS00959; HISTONE_H3_2; 1.
PE 3: Inferred from homology;
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-like type 2"
FT /id="PRO_0000268634"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 5
FT /note="N6-methylated lysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 10
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 10
FT /note="N6-methylated lysine; 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-methylated lysine"
FT /evidence="ECO:0000250"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 37
FT /note="N6-methylated lysine"
FT /evidence="ECO:0000250"
FT MOD_RES 80
FT /note="N6-methylated lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 136 AA; 15349 MW; D93AECF349E14D2D CRC64;
MARTKQTARK STGGKAPRKA LATKAARKSA IVTGSVKKVH RFRPGTVALR EIRRYQKSTE
LLLRKLPFQR LVREIAQDFK TDLRFQSAAI GALQEASEAY LVGLFEDTNL CAIHAKRVTI
MPKDMQLARR IRGERS
