ID   H2B2_WHEAT              Reviewed;         150 AA.
AC   P05621;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Histone H2B.2;
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-150.
RC   TISSUE=Germ;
RX   PubMed=3131141; DOI=10.1111/j.1432-1033.1988.tb14033.x;
RA   Brandt W.F., de Andrade Rodrigues J., von Holt C.;
RT   "The amino acid sequence of wheat histone H2B(2). A core histone with a
RT   novel repetitive N-terminal extension.";
RL   Eur. J. Biochem. 173:547-554(1988).
RN   [2]
RP   LACK OF PHOSPHORYLATION.
RX   PubMed=16667585; DOI=10.1104/pp.93.3.1241;
RA   Green G.R., Gustavsen L.C., Poccia D.L.;
RT   "Phosphorylation of plant H2A histones.";
RL   Plant Physiol. 93:1241-1245(1990).
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 and H2BK33ac. {ECO:0000250}.
CC   -!- PTM: Monoubiquitinated to form H2BK143ub1; may give a specific tag for
CC       epigenetic transcriptional activation. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Phosphorylation of H2B was not detected.
CC   -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
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-4; H2BK33ac = acetylated Lys-29; H2BK143ub1 =
CC       monoubiquitinated Lys-146. {ECO:0000305}.
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DR   PIR; S00622; HSWT2B.
DR   STRING; 4565.Traes_1AL_3EC96C539.2; -.
DR   PRIDE; P05621; -.
DR   eggNOG; KOG1744; Eukaryota.
DR   Proteomes; UP000019116; Unplaced.
DR   ExpressionAtlas; P05621; baseline and differential.
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; IBA:GO_Central.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
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; Nucleosome core; Nucleus; Reference proteome;
KW   Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:3131141"
FT   CHAIN           2..150
FT                   /note="Histone H2B.2"
FT                   /id="PRO_0000071925"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="Blocked amino end (Pro)"
FT                   /evidence="ECO:0000269|PubMed:3131141"
FT   MOD_RES         4
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         29
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        146
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   150 AA;  16226 MW;  4B892A9074408FA2 CRC64;
     MPBKKPAAEN KVEKAAEKTP AGKKPKAEKR LPAGKTASKE AGGEGKTRGR KKGSKAKKGV
     ETYKIYIFKV LKQVHPDIGI SSKAMSIMNS FINDIFEKLA GESAKLARYN KKPTITSREI
     QTSVRLVLPG ELAKHAVSEG TKAVTKFTSS