ID   H2B_CRONI               Reviewed;          93 AA.
AC   P02280;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Histone H2B;
DE   Flags: Fragment;
OS   Crocodylus niloticus (Nile crocodile) (African crocodile).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Longirostres; Crocodylidae;
OC   Crocodylus.
OX   NCBI_TaxID=8501;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-93.
RC   TISSUE=Erythrocyte;
RX   PubMed=638193; DOI=10.1016/0005-2795(78)90572-x;
RA   van Helden P., Strickland W.N., Brandt W.F., von Holt C.;
RT   "Histone H2B variants from the erythrocytes of an amphibian, a reptile and
RT   a bird.";
RL   Biochim. Biophys. Acta 533:278-281(1978).
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 on Ser-15 during apoptosis; which facilitates
CC       apoptotic chromatin condensation. {ECO:0000250|UniProtKB:P06900}.
CC   -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
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DR   PIR; A02607; HSAK22.
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   SUPFAM; SSF47113; SSF47113; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chromosome; Direct protein sequencing; DNA-binding;
KW   Nucleosome core; Nucleus; Phosphoprotein; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:638193"
FT   CHAIN           2..>93
FT                   /note="Histone H2B"
FT                   /id="PRO_0000071847"
FT   REGION          1..52
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         13
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1H4"
FT   MOD_RES         15
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P06900"
FT   MOD_RES         16
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1H4"
FT   MOD_RES         21
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1H4"
FT   NON_TER         93
SQ   SEQUENCE   93 AA;  10351 MW;  413D37C83FE30D2E CRC64;
     MPEPAKSAPA PKKGSKKAVT KTQKKGDKKR XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
     XXMNSFVNDI FERIAGEASR LAHYNKRSTI TSR