H2B_OLILU
ID H2B_OLILU Reviewed; 114 AA.
AC P82887;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Histone H2B;
OS Olisthodiscus luteus (Marine phytoflagellate).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Olisthodiscophyceae;
OC Olisthodiscaceae; Olisthodiscus.
OX NCBI_TaxID=83000;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-114, AND ACETYLATION AT LYS-3.
RA Rodrigues J.A., Spit A., Brandt W.F.;
RL Submitted (DEC-2000) to UniProtKB.
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-110 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P82887; -.
DR SMR; P82887; -.
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 1: Evidence at protein level;
KW Acetylation; Chromosome; Direct protein sequencing; DNA-binding;
KW Isopeptide bond; Nucleosome core; Nucleus; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.1"
FT CHAIN 2..114
FT /note="Histone H2B"
FT /id="PRO_0000071871"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 3
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|Ref.1"
FT CROSSLNK 110
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 114 AA; 12662 MW; C85728D45B37C4D3 CRC64;
MAKTPSKKAA KAPKKAGSKR NKRVETYSSY IYKVLKQVHP DTGISKRGMS IMNSFINDIF
ERLAGEASRL ARYNKRSTLS SREIQTAVRL MLPGELAKHA VSEGTKAVTK FTSN