ID   H2B_ONCMY               Reviewed;         124 AA.
AC   P69069; P02282;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Histone H2B;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2997457; DOI=10.1007/bf02105800;
RA   Winkfein R.J., Connor W., Mezquita J., Dixon G.H.;
RT   "Histone H4 and H2B genes in rainbow trout (Salmo gairdnerii).";
RL   J. Mol. Evol. 22:1-19(1985).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-23, AND ACETYLATION AT LYS-6; LYS-11; LYS-14 AND
RP   LYS-19.
RX   PubMed=4506069; DOI=10.1073/pnas.69.8.2015;
RA   Candido E.P.M., Dixon G.H.;
RT   "Amino-terminal sequences and sites of in vivo acetylation of trout-testis
RT   histones 3 and IIb 2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 69:2015-2019(1972).
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-119 by BRE1 gives a specific tag for
CC       epigenetic transcriptional activation and is also prerequisite for
CC       histone H3 'Lys-4' and 'Lys-79' methylation.
CC       {ECO:0000250|UniProtKB:P33778}.
CC   -!- PTM: Phosphorylated during apoptosis; which facilitates apoptotic
CC       chromatin condensation. {ECO:0000250|UniProtKB:P06900}.
CC   -!- PTM: GlcNAcylation at Ser-111 promotes monoubiquitination of Lys-119.
CC       It fluctuates in response to extracellular glucose, and associates with
CC       transcribed genes (By similarity). {ECO:0000250|UniProtKB:P62807}.
CC   -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
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DR   EMBL; X02916; CAA26673.1; -; Genomic_DNA.
DR   PIR; A92961; HSTR2B.
DR   AlphaFoldDB; P69069; -.
DR   SMR; P69069; -.
DR   iPTMnet; P69069; -.
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   Glycoprotein; Isopeptide bond; Nucleosome core; Nucleus; Phosphoprotein;
KW   Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4506069"
FT   CHAIN           2..124
FT                   /note="Histone H2B"
FT                   /id="PRO_0000071851"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..33
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         6
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:4506069"
FT   MOD_RES         11
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:4506069"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P06900"
FT   MOD_RES         14
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:4506069"
FT   MOD_RES         19
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:4506069"
FT   CARBOHYD        111
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250|UniProtKB:P62807"
FT   CROSSLNK        119
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1H4"
FT   CONFLICT        29..30
FT                   /note="KR -> RK (in Ref. 1; CAA26673)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   124 AA;  13596 MW;  30097D5582BE0B84 CRC64;
     MPEPAKSAPK KGSKKAVTKT AGKGGKKRKR SRKESYAIYV YKVLKQVHPD TGISSKAMGI
     MNSFVNDIFE RIAGESSRLA HYNKRSTITS REIQTAVRLL LPGELAKHAV SEGTKAVTKY
     TSSK