ID   H2B_EUPCR               Reviewed;         113 AA.
AC   O97484;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Histone H2B;
GN   Name=H2B1;
GN   and
GN   Name=H2B2;
OS   Euplotes crassus.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Hypotrichia; Euplotida; Euplotidae; Moneuplotes.
OX   NCBI_TaxID=5936;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9332355; DOI=10.1016/s0378-1119(97)00248-5;
RA   Tebeau C.M., Jahn C.L.;
RT   "Sequence and transcript analysis of macronuclear histone H2B genes from
RT   Euplotes crassus.";
RL   Gene 197:109-113(1997).
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 {ECO:0000250}. Chromosome {ECO:0000250}.
CC   -!- PTM: Monoubiquitination of Lys-109 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   -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
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DR   EMBL; U93852; AAC47753.1; -; Genomic_DNA.
DR   EMBL; U93853; AAC47754.1; -; Genomic_DNA.
DR   AlphaFoldDB; O97484; -.
DR   SMR; O97484; -.
DR   PRIDE; O97484; -.
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; 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; 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; Isopeptide bond; Nucleosome core; Nucleus;
KW   Ubl conjugation.
FT   CHAIN           1..113
FT                   /note="Histone H2B"
FT                   /id="PRO_0000071902"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        109
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   113 AA;  12896 MW;  09E383379DF385A9 CRC64;
     MPATPAKRAK RVQQEKRHHK KRTETFSVYI YRVLKQVHPE TGVSKKSMSI MNSFINDIFE
     KIALEASKLV RYNKKHTLSS REVQTAVRLL LPGELAKHAV SEGTKAVTKY TSS