ID   H2B_AGABI               Reviewed;         143 AA.
AC   P78567;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Histone H2B;
GN   Name=htbA;
OS   Agaricus bisporus (White button mushroom).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricaceae; Agaricus.
OX   NCBI_TaxID=5341;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Horst U1;
RX   PubMed=8953726; DOI=10.1128/aem.62.12.4542-4547.1996;
RA   Sonnenberg A.S.M., de Groot P.W.J., Schaap P.J., Baars J.J.P., Visser J.,
RA   van Griensven L.J.L.D.;
RT   "Isolation of expressed sequence tags of Agaricus bisporus and their
RT   assignment to chromosomes.";
RL   Appl. Environ. Microbiol. 62:4542-4547(1996).
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: Monoubiquitinated to form H2BK123ub1. H2BK123ub1 gives a specific
CC       tag for epigenetic transcriptional activation and is also prerequisite
CC       for H3K4me and H3K79me formation. H2BK123ub1 also modulates the
CC       formation of double-strand breaks during meiosis and is a prerequisite
CC       for DNA-damage checkpoint activation (By similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylated to form H2BS10ph during progression through meiotic
CC       prophase. May be correlated with chromosome condensation (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: Acetylation of N-terminal lysines and particularly formation of
CC       H2BK11ac has a positive effect on transcription. {ECO:0000250}.
CC   -!- PTM: Sumoylation to form H2BK6su occurs preferentially near the
CC       telomeres and represses gene transcription. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
CC   -!- CAUTION: To ensure consistency between histone entries, we follow the
CC       'Brno' nomenclature for histone modifications, with positions referring
CC       to those used in the literature for the 'closest' model organism. Due
CC       to slight variations in histone sequences between organisms and to the
CC       presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the
CC       actual positions of modified amino acids in the sequence generally
CC       differ. In this entry the following conventions are used: H2BK6ac =
CC       acetylated Lys-11; H2BK6su = sumoylated Lys-11; H2BS10ph =
CC       phosphorylated Ser-15; H2BK11ac = acetylated Lys-19; H2BK123ub1 =
CC       monoubiquitinated Lys-137. {ECO:0000305}.
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DR   EMBL; X94188; CAA63898.1; -; mRNA.
DR   AlphaFoldDB; P78567; -.
DR   SMR; P78567; -.
DR   PRIDE; P78567; -.
DR   OMA; AQLCQTT; -.
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   2: Evidence at transcript level;
KW   Acetylation; Chromosome; DNA-binding; Isopeptide bond; Nucleosome core;
KW   Nucleus; Phosphoprotein; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..143
FT                   /note="Histone H2B"
FT                   /id="PRO_0000071926"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         11
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         15
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         19
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        11
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO); alternate"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        137
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   143 AA;  15165 MW;  69640102E31F4B56 CRC64;
     MAPKPASTAG KAPASTASKA PVKSDAAKTA SKSKVSSGAD GEKKKRKKTR KETYSSYIYK
     VLKQVHPDTG ISNKAMAILN SFVNDIFERI ATEASKLASY SKKSTISSRE IQTSVRLILP
     GELAKHAISE GTKSVTKFSS GGK