ID   H2B_DROHY               Reviewed;         123 AA.
AC   P17271;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Histone H2B;
GN   Name=His2B;
OS   Drosophila hydei (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7224;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2109309; DOI=10.1093/nar/18.6.1573;
RA   Kremer H., Hennig W.;
RT   "Isolation and characterization of a Drosophila hydei histone DNA repeat
RT   unit.";
RL   Nucleic Acids Res. 18:1573-1580(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8487638; DOI=10.1093/oxfordjournals.molbev.a040011;
RA   Fitch D.H., Strausbaugh L.D.;
RT   "Low codon bias and high rates of synonymous substitution in Drosophila
RT   hydei and D. melanogaster histone genes.";
RL   Mol. Biol. Evol. 10:397-413(1993).
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; X17072; CAA34922.1; -; Genomic_DNA.
DR   EMBL; X52576; CAA36808.1; -; Genomic_DNA.
DR   PIR; S21939; S21939.
DR   AlphaFoldDB; P17271; -.
DR   SMR; P17271; -.
DR   IntAct; P17271; 1.
DR   FlyBase; FBgn0012376; Dhyd\His2B.
DR   OMA; ELAKHAX; -.
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_0000071859"
FT   REGION          1..31
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"
FT   CONFLICT        23
FT                   /note="N -> T (in Ref. 2; CAA36808)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        34
FT                   /note="S -> T (in Ref. 2; CAA36808)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   123 AA;  13709 MW;  64BBF38D20ABC4DD CRC64;
     MPPKTSGKAA KKAGKAQKNI TKNDKKKKRK RKESYAIYIY KVLKQVHPDT GISSKAMSIM
     NSFVNDIFER IAAEASRLAH YNKRSTITSR EIQTAVRLLL PGELAKHAVS EGTKAVTKYT
     SSK