H2B1_WHEAT
ID H2B1_WHEAT Reviewed; 152 AA.
AC P27807;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Histone H2B.1;
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].
RC STRAIN=cv. Horoshirikomugi; TISSUE=Seedling;
RX PubMed=1923777; DOI=10.1093/nar/19.18.5077;
RA Yang P., Katsura M., Nakayama T., Mikami K., Iwabuchi M.;
RT "Molecular cloning and nucleotide sequences of cDNAs for histone H1 and H2B
RT variants from wheat.";
RL Nucleic Acids Res. 19:5077-5077(1991).
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-7; H2BK33ac = acetylated Lys-37; H2BK143ub1 =
CC monoubiquitinated Lys-148. {ECO:0000305}.
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DR EMBL; X59873; CAA42530.1; -; mRNA.
DR PIR; S22323; S22323.
DR AlphaFoldDB; P27807; -.
DR SMR; P27807; -.
DR STRING; 4565.Traes_4AL_948151631.1; -.
DR PRIDE; P27807; -.
DR EnsemblPlants; TraesCAD_scaffold_029575_01G000400.1; TraesCAD_scaffold_029575_01G000400.1; TraesCAD_scaffold_029575_01G000400.
DR EnsemblPlants; TraesCAD_scaffold_075776_01G000500.1; TraesCAD_scaffold_075776_01G000500.1; TraesCAD_scaffold_075776_01G000500.
DR EnsemblPlants; TraesCLE_scaffold_051194_01G000500.1; TraesCLE_scaffold_051194_01G000500.1; TraesCLE_scaffold_051194_01G000500.
DR EnsemblPlants; TraesCLE_scaffold_057438_01G000200.1; TraesCLE_scaffold_057438_01G000200.1; TraesCLE_scaffold_057438_01G000200.
DR EnsemblPlants; TraesCS4A02G260400.1; TraesCS4A02G260400.1.cds1; TraesCS4A02G260400.
DR EnsemblPlants; TraesCS4D02G054200.1; TraesCS4D02G054200.1.cds1; TraesCS4D02G054200.
DR EnsemblPlants; TraesPAR_scaffold_025250_01G000400.1; TraesPAR_scaffold_025250_01G000400.1; TraesPAR_scaffold_025250_01G000400.
DR EnsemblPlants; TraesPAR_scaffold_072635_01G000100.1; TraesPAR_scaffold_072635_01G000100.1; TraesPAR_scaffold_072635_01G000100.
DR EnsemblPlants; TraesROB_scaffold_057369_01G000300.1; TraesROB_scaffold_057369_01G000300.1; TraesROB_scaffold_057369_01G000300.
DR EnsemblPlants; TraesROB_scaffold_063112_01G000500.1; TraesROB_scaffold_063112_01G000500.1; TraesROB_scaffold_063112_01G000500.
DR EnsemblPlants; TraesWEE_scaffold_026722_01G000500.1; TraesWEE_scaffold_026722_01G000500.1; TraesWEE_scaffold_026722_01G000500.
DR EnsemblPlants; TraesWEE_scaffold_058384_01G000500.1; TraesWEE_scaffold_058384_01G000500.1; TraesWEE_scaffold_058384_01G000500.
DR Gramene; TraesCAD_scaffold_029575_01G000400.1; TraesCAD_scaffold_029575_01G000400.1; TraesCAD_scaffold_029575_01G000400.
DR Gramene; TraesCAD_scaffold_075776_01G000500.1; TraesCAD_scaffold_075776_01G000500.1; TraesCAD_scaffold_075776_01G000500.
DR Gramene; TraesCLE_scaffold_051194_01G000500.1; TraesCLE_scaffold_051194_01G000500.1; TraesCLE_scaffold_051194_01G000500.
DR Gramene; TraesCLE_scaffold_057438_01G000200.1; TraesCLE_scaffold_057438_01G000200.1; TraesCLE_scaffold_057438_01G000200.
DR Gramene; TraesCS4A02G260400.1; TraesCS4A02G260400.1.cds1; TraesCS4A02G260400.
DR Gramene; TraesCS4D02G054200.1; TraesCS4D02G054200.1.cds1; TraesCS4D02G054200.
DR Gramene; TraesPAR_scaffold_025250_01G000400.1; TraesPAR_scaffold_025250_01G000400.1; TraesPAR_scaffold_025250_01G000400.
DR Gramene; TraesPAR_scaffold_072635_01G000100.1; TraesPAR_scaffold_072635_01G000100.1; TraesPAR_scaffold_072635_01G000100.
DR Gramene; TraesROB_scaffold_057369_01G000300.1; TraesROB_scaffold_057369_01G000300.1; TraesROB_scaffold_057369_01G000300.
DR Gramene; TraesROB_scaffold_063112_01G000500.1; TraesROB_scaffold_063112_01G000500.1; TraesROB_scaffold_063112_01G000500.
DR Gramene; TraesWEE_scaffold_026722_01G000500.1; TraesWEE_scaffold_026722_01G000500.1; TraesWEE_scaffold_026722_01G000500.
DR Gramene; TraesWEE_scaffold_058384_01G000500.1; TraesWEE_scaffold_058384_01G000500.1; TraesWEE_scaffold_058384_01G000500.
DR eggNOG; KOG1744; Eukaryota.
DR HOGENOM; CLU_075666_1_0_1; -.
DR OMA; KRCCKET; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; P27807; 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; 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..152
FT /note="Histone H2B.1"
FT /id="PRO_0000071924"
FT REGION 1..60
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 37
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT CROSSLNK 148
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 152 AA; 16433 MW; BE864018C99A1FDA CRC64;
MAPKAEKKPA AKKPAEEEPA AEKAEKTPAG KKPKAEKRLP AGKSAAKEGG DKKGKKKAKK
SVETYKIYIF KVLKQVHPDI GISSKAMSIM NSFINDIFEK LAGEAAKLAR YNKKPTITSR
EIQTSVRLVL PGELAKHAVS EGTKAVTKFT SS
