ID   H2B_TETPY               Reviewed;         121 AA.
AC   Q7M400;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Histone H2B;
OS   Tetrahymena pyriformis.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC   Tetrahymena.
OX   NCBI_TaxID=5908;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-121, AND ACETYLATION AT LYS-5.
RX   PubMed=6804458; DOI=10.1093/oxfordjournals.jbchem.a133778;
RA   Nomoto M., Hayashi H., Iwai K.;
RT   "Tetrahymena histone H2B. Complete amino acid sequence.";
RL   J. Biochem. 91:897-904(1982).
RN   [2]
RP   METHYLATION AT ALA-2, AND ACETYLATION AT LYS-5.
RX   PubMed=6818230; DOI=10.1093/oxfordjournals.jbchem.a134096;
RA   Nomoto M., Kyogoku Y., Iwai K.;
RT   "N-trimethylalanine, a novel blocked N-terminal residue of Tetrahymena
RT   histone H2B.";
RL   J. Biochem. 92:1675-1678(1982).
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-115 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: Acetylation occurs almost exclusively in the MAC. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
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DR   PIR; A61301; A61301.
DR   AlphaFoldDB; Q7M400; -.
DR   SMR; Q7M400; -.
DR   iPTMnet; Q7M400; -.
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; Methylation; Nucleosome core; Nucleus; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:6804458"
FT   CHAIN           2..121
FT                   /note="Histone H2B"
FT                   /id="PRO_0000071904"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N,N,N-trimethylalanine"
FT                   /evidence="ECO:0000269|PubMed:6818230"
FT   MOD_RES         5
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:6804458,
FT                   ECO:0000269|PubMed:6818230"
FT   MOD_RES         41
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        115
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   121 AA;  13518 MW;  1971A939600499A0 CRC64;
     MAPKKAPAAA EKKVKKAPTT EKKNKKKRSE TFAIYIFKVL KQVHPDVGIS KKAMNIMNSF
     INDSFERIAL ESSKLVRFNK RRTLSSREVQ TAVKLLLPGE LARHAISEGT KAVTKFSSST
     N