H2B4_CAEEL
ID H2B4_CAEEL Reviewed; 123 AA.
AC Q27876;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Probable histone H2B 4;
GN Name=his-48; ORFNames=B0035.8;
GN and
GN Name=his-58; ORFNames=F54E12.4;
GN and
GN Name=his-62; ORFNames=F55G1.3;
GN and
GN Name=his-66; ORFNames=H02I12.6;
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).
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 -!- PTM: Monoubiquitination of Lys-118 gives a specific tag for epigenetic
CC transcriptional activation and is also prerequisite for histone H3
CC 'Lys-4' and 'Lys-79' methylation. {ECO:0000250}.
CC -!- PTM: GlcNAcylation at Ser-110 promotes monoubiquitination of Lys-118.
CC It fluctuates in response to extracellular glucose, and associates with
CC transcribed genes (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
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DR EMBL; Z82271; CAB05211.1; -; Genomic_DNA.
DR EMBL; FO081135; CCD69391.1; -; Genomic_DNA.
DR EMBL; Z73102; CAA97413.1; -; Genomic_DNA.
DR EMBL; Z92789; CAB07220.1; -; Genomic_DNA.
DR PIR; F88730; F88730.
DR RefSeq; NP_501202.1; NM_068801.1.
DR RefSeq; NP_502132.1; NM_069731.4.
DR RefSeq; NP_502140.1; NM_069739.5.
DR RefSeq; NP_502149.1; NM_069748.1.
DR AlphaFoldDB; Q27876; -.
DR SMR; Q27876; -.
DR BioGRID; 43148; 3.
DR BioGRID; 51070; 1.
DR BioGRID; 51393; 5.
DR STRING; 6239.B0035.8; -.
DR EPD; Q27876; -.
DR PaxDb; Q27876; -.
DR PeptideAtlas; Q27876; -.
DR PRIDE; Q27876; -.
DR EnsemblMetazoa; B0035.8.1; B0035.8.1; WBGene00001922.
DR EnsemblMetazoa; F54E12.4.1; F54E12.4.1; WBGene00001932.
DR EnsemblMetazoa; F55G1.3.1; F55G1.3.1; WBGene00001936.
DR EnsemblMetazoa; H02I12.6.1; H02I12.6.1; WBGene00001940.
DR GeneID; 178049; -.
DR GeneID; 186251; -.
DR GeneID; 186326; -.
DR GeneID; 186670; -.
DR KEGG; cel:CELE_B0035.8; -.
DR KEGG; cel:CELE_F54E12.4; -.
DR KEGG; cel:CELE_F55G1.3; -.
DR KEGG; cel:CELE_H02I12.6; -.
DR UCSC; F55G1.3; c. elegans.
DR CTD; 178049; -.
DR CTD; 186251; -.
DR CTD; 186326; -.
DR CTD; 186670; -.
DR WormBase; B0035.8; CE05165; WBGene00001922; his-48.
DR WormBase; F54E12.4; CE05165; WBGene00001932; his-58.
DR WormBase; F55G1.3; CE05165; WBGene00001936; his-62.
DR WormBase; H02I12.6; CE05165; WBGene00001940; his-66.
DR eggNOG; KOG1744; Eukaryota.
DR GeneTree; ENSGT01050000244943; -.
DR HOGENOM; CLU_075666_2_1_1; -.
DR InParanoid; Q27876; -.
DR OMA; YLQIAFX; -.
DR OrthoDB; 1536672at2759; -.
DR PhylomeDB; Q27876; -.
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-3214847; HATs acetylate histones.
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-5689880; Ub-specific processing proteases.
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:Q27876; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001922; 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:0044877; F:protein-containing complex binding; ISS:UniProtKB.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR000558; Histone_H2B.
DR PANTHER; PTHR23428; PTHR23428; 1.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00621; HISTONEH2B.
DR SMART; SM00427; H2B; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00357; HISTONE_H2B; 1.
PE 3: Inferred from homology;
KW Chromosome; DNA-binding; Glycoprotein; Isopeptide bond; Nucleosome core;
KW Nucleus; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..123
FT /note="Probable histone H2B 4"
FT /id="PRO_0000071870"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 110
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CROSSLNK 118
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 123 AA; 13586 MW; 9300DE62E1CD517D CRC64;
MPPKPSAKGA KKAAKTVVAK PKDGKKRRHA RKESYSVYIY RVLKQVHPDT GVSSKAMSIM
NSFVNDVFER IASEASRLAH YNKRSTISSR EIQTAVRLIL PGELAKHAVS EGTKAVTKYT
SSK
