H33L1_CAEEL
ID H33L1_CAEEL Reviewed; 134 AA.
AC Q27490;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Histone H3.3-like type 1;
GN Name=his-70; ORFNames=E03A3.4;
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; Z38112; CAA86229.2; -; Genomic_DNA.
DR PIR; T20427; T20427.
DR RefSeq; NP_497812.2; NM_065411.2.
DR AlphaFoldDB; Q27490; -.
DR SMR; Q27490; -.
DR STRING; 6239.E03A3.4; -.
DR EPD; Q27490; -.
DR PaxDb; Q27490; -.
DR PeptideAtlas; Q27490; -.
DR EnsemblMetazoa; E03A3.4.1; E03A3.4.1; WBGene00001944.
DR GeneID; 184006; -.
DR KEGG; cel:CELE_E03A3.4; -.
DR UCSC; E03A3.4; c. elegans.
DR CTD; 184006; -.
DR WormBase; E03A3.4; CE44880; WBGene00001944; his-70.
DR eggNOG; KOG1745; Eukaryota.
DR GeneTree; ENSGT01050000244889; -.
DR HOGENOM; CLU_078295_4_0_1; -.
DR InParanoid; Q27490; -.
DR OMA; DSNICAI; -.
DR OrthoDB; 1564596at2759; -.
DR PhylomeDB; Q27490; -.
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-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-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:Q27490; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001944; Expressed in larva and 1 other tissue.
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..134
FT /note="Histone H3.3-like type 1"
FT /id="PRO_0000268633"
FT REGION 1..25
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 37
FT /note="N6-methylated lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 134 AA; 15286 MW; 28819741B20BF017 CRC64;
MARTKHTARK SFGGKAPRKS LATKAARKVF PVDGQVKKRY RPSSNALKEI RKYQKSTELL
VRKLPFQRLV REVAQEIMPN VRFQSAAIQA LHEAAEAYLI GLFEDTNLCA IHAKRVTIMP
KDMQLARRIR GERG
