ID   H2B3_WHEAT              Reviewed;         138 AA.
AC   Q43217;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Histone H2B.3;
DE   AltName: Full=wcH2B-8;
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   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7787180; DOI=10.1007/bf00042047;
RA   Yang P., Taoka K., Nakayma T., Iwabuchi M.;
RT   "Structural and functional characterization of two wheat histone H2B
RT   promoters.";
RL   Plant Mol. Biol. 28:155-172(1995).
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 {ECO:0000250}. Chromosome {ECO:0000250}.
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-7; H2BK33ac = acetylated Lys-27; H2BK143ub1 =
CC       monoubiquitinated Lys-134. {ECO:0000305}.
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DR   EMBL; D37943; BAA07157.1; -; mRNA.
DR   PIR; S56685; S56685.
DR   AlphaFoldDB; Q43217; -.
DR   SMR; Q43217; -.
DR   STRING; 4565.Traes_7DL_1FC95654F.1; -.
DR   PRIDE; Q43217; -.
DR   eggNOG; KOG1744; Eukaryota.
DR   Proteomes; UP000019116; Unplaced.
DR   ExpressionAtlas; Q43217; baseline.
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; DNA-binding; Isopeptide bond; Nucleosome core;
KW   Nucleus; Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..138
FT                   /note="Histone H2B.3"
FT                   /id="PRO_0000239423"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         7
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         27
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        134
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   138 AA;  15105 MW;  18B285CC1DB5613E CRC64;
     MAPKAEKKPV AEKAEKTTAA KKTKAEKRPP ASKEGGDKKG KKKSKKSVET YKIYIFKVLK
     QVHPDIGISS KAMSIMNSFI NDIFEKLAGE SAKLARYNKK PTITSREIQT SVRLVLPGEL
     AKHAVSEGTK AVTKFTSA