ID   H2B2_MAIZE              Reviewed;         150 AA.
AC   P30756;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Histone H2B.2;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Wisconsin 22;
RX   PubMed=1450375; DOI=10.1007/bf00046443;
RA   Joanin P., Gigot C., Phillipps G.;
RT   "Nucleotide sequence and expression of two cDNA coding for two histone H2B
RT   variants of maize.";
RL   Plant Mol. Biol. 20:581-588(1992).
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   -!- 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-34; H2BK143ub1 =
CC       monoubiquitinated Lys-146. {ECO:0000305}.
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DR   EMBL; X57313; CAA40565.1; -; mRNA.
DR   PIR; S28049; S28049.
DR   RefSeq; NP_001131654.1; NM_001138182.1.
DR   AlphaFoldDB; P30756; -.
DR   SMR; P30756; -.
DR   STRING; 4577.GRMZM2G119071_P01; -.
DR   PaxDb; P30756; -.
DR   PRIDE; P30756; -.
DR   EnsemblPlants; Zm00001eb177270_T001; Zm00001eb177270_P001; Zm00001eb177270.
DR   GeneID; 100193014; -.
DR   Gramene; Zm00001eb177270_T001; Zm00001eb177270_P001; Zm00001eb177270.
DR   KEGG; zma:100193014; -.
DR   MaizeGDB; 65109; -.
DR   eggNOG; KOG1744; Eukaryota.
DR   HOGENOM; CLU_075666_1_0_1; -.
DR   OMA; ANIACNS; -.
DR   OrthoDB; 1536672at2759; -.
DR   Proteomes; UP000007305; Chromosome 4.
DR   ExpressionAtlas; P30756; baseline and differential.
DR   Genevisible; P30756; ZM.
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   2: Evidence at transcript 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..150
FT                   /note="Histone H2B.2"
FT                   /id="PRO_0000071916"
FT   REGION          1..57
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         34
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;  16174 MW;  917A627B9B426949 CRC64;
     MAPKAEKKPA AKKPAEEEPA AEKAPAGKKP KAEKRVPAGK SAGKEGGEGK RGRKKGKKSV
     ETYKIYIFKV LKQVHPDIGI SSKAMSIMNS FINDIFEKLA AEAAKLARYN KKPTITSREI
     QTSVRLVLPG ELAKHAVSEG TKAVTKFTSS