ID   H2B_DROMA               Reviewed;         123 AA.
AC   Q76FE5;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Histone H2B;
GN   Name=His2B;
OS   Drosophila mauritiana (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=14676429; DOI=10.1266/ggs.78.383;
RA   Kakita M., Shimizu T., Emoto M., Nagai M., Takeguchi M., Hosono Y.,
RA   Kume N., Ozawa T., Ueda M., Bhuiyan M.S., Matsuo Y.;
RT   "Divergence and heterogeneity of the histone gene repeating units in the
RT   Drosophila melanogaster species subgroup.";
RL   Genes Genet. Syst. 78:383-389(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
RX   PubMed=10555282; DOI=10.1093/oxfordjournals.molbev.a026063;
RA   Baldo A.M., Les D.H., Strausbaugh L.D.;
RT   "Potentials and limitations of histone repeat sequences for phylogenetic
RT   reconstruction of Sophophora.";
RL   Mol. Biol. Evol. 16:1511-1520(1999).
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: Monoubiquitination of Lys-118 by Bre1 gives a specific tag for
CC       epigenetic transcriptional activation and is also prerequisite for
CC       histone H3 'Lys-4' and 'Lys-79' methylation. {ECO:0000250}.
CC   -!- PTM: GlcNAcylation at Ser-110 promotes monoubiquitination of Lys-118.
CC       It fluctuates in response to extracellular glucose, and associates with
CC       transcribed genes (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
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DR   EMBL; AB105182; BAD02434.1; -; Genomic_DNA.
DR   EMBL; AJ224806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; Q76FE5; -.
DR   SMR; Q76FE5; -.
DR   FlyBase; FBgn0028807; Dmau\His2B.
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:0044877; F:protein-containing complex binding; ISS:UniProtKB.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
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   3: Inferred from homology;
KW   Chromosome; DNA-binding; Glycoprotein; Isopeptide bond; Methylation;
KW   Nucleosome core; Nucleus; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..123
FT                   /note="Histone H2B"
FT                   /id="PRO_0000071860"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-methylproline"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        110
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        118
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   123 AA;  13696 MW;  0774D25F34003062 CRC64;
     MPPKTSGKAA KKAGKAQKNI TKTDKKKKRK RKESYAIYIY KVLKQVHPDT GISSKAMSIM
     NSFVNDIFER IAAEASRLAH YNKRSTITSR EIQTAVRLLL PGELAKHAVS EGTKAVTKYT
     SSK