ID   H2B_CYPCA               Reviewed;          29 AA.
AC   P83837;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Histone H2B;
DE   Flags: Fragment;
OS   Cyprinus carpio (Common carp).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Cyprinus.
OX   NCBI_TaxID=7962 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 2-29.
RC   TISSUE=Gill;
RA   Schuurmans Stekhoven F.M.A.H., Wendelaar Bonga S.E., Flik G.;
RT   "Extranuclear histones in teleost gills: an evolutionary study.";
RL   Fish Physiol. Biochem. 30:201-211(2004).
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 at the C-terminal Lys 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   -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
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DR   AlphaFoldDB; P83837; -.
DR   Proteomes; UP000694384; Unplaced.
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.
PE   1: Evidence at protein level;
KW   Acetylation; Chromosome; Direct protein sequencing; DNA-binding;
KW   Nucleosome core; Nucleus; Phosphoprotein; Reference proteome;
KW   Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.1"
FT   CHAIN           2..>29
FT                   /note="Histone H2B"
FT                   /id="PRO_0000071848"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         6
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1H4"
FT   MOD_RES         11
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1H4"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P06900"
FT   NON_TER         29
SQ   SEQUENCE   29 AA;  3139 MW;  FEE7F55539D9B3E5 CRC64;
     MPEPAKSAPK KGSTRTAAKG GKKRRKSRK