ID   H2B_PEA                 Reviewed;         120 AA.
AC   Q99285;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Histone H2B;
DE   Flags: Fragments;
GN   Name=HIS2B {ECO:0000250|UniProtKB:O49118};
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 2-120, AND VARIANTS ASP-29 AND ILE-106.
RX   PubMed=914793;
RA   Hayashi H., Iwai K., Johnson J.D., Bonner J.;
RT   "Pea histones H2A and H2B. Variable and conserved regions in the
RT   sequences.";
RL   J. Biochem. 82:503-510(1977).
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: Can be acetylated to form H2BK6ac, H2BK33ac and H2BK34ac.
CC       {ECO:0000250}.
CC   -!- PTM: Monoubiquitinated to form H2BK143ub1; may give a specific tag for
CC       epigenetic transcriptional activation. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000255}.
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-7; H2BK33ac = acetylated Lys-10; H2BK34ac = acetylated
CC       Lys-11; H2BK143ub1 = monoubiquitinated Lys-115. {ECO:0000305}.
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DR   AlphaFoldDB; Q99285; -.
DR   SMR; Q99285; -.
DR   PRIDE; Q99285; -.
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   GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
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.
PE   1: Evidence at protein level;
KW   Acetylation; Chromosome; Direct protein sequencing; DNA condensation;
KW   DNA-binding; Isopeptide bond; Nucleosome core; Nucleus; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:914793"
FT   CHAIN           2..120
FT                   /note="Histone H2B"
FT                   /id="PRO_0000071920"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="Blocked amino end (Ala)"
FT   MOD_RES         7
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         10
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         11
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"
FT   VARIANT         29
FT                   /note="S -> D"
FT                   /evidence="ECO:0000269|PubMed:914793"
FT   VARIANT         106
FT                   /note="V -> I"
FT                   /evidence="ECO:0000269|PubMed:914793"
FT   NON_CONS        6..7
FT                   /evidence="ECO:0000305"
FT   NON_CONS        10..11
FT                   /evidence="ECO:0000305"
FT   NON_CONS        14..15
FT                   /evidence="ECO:0000305"
FT   NON_CONS        17..18
FT                   /evidence="ECO:0000305"
FT   NON_CONS        20..21
FT                   /evidence="ECO:0000305"
FT   NON_CONS        22..23
FT                   /evidence="ECO:0000305"
FT   NON_CONS        24..25
FT                   /evidence="ECO:0000305"
FT   NON_CONS        26..27
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   120 AA;  13471 MW;  FAB7766B8B92AD03 CRC64;
     MAEPAKKKPK KLPKKDKGQK DIKRKKKESY TVKIYIFKVL KQVHPDIGIS SKAMGIMNSF
     INDIFEKLAS EASRLARYNK KSTITPREIQ TAVRLLLPGE VAKHKVSEAT KAVTKFTSGA