ID   H2B_PATGR               Reviewed;         122 AA.
AC   P02284;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Histone H2B, gonadal;
OS   Patella granatina (Sandpaper limpet).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Patellogastropoda; Patelloidea; Patellidae; Cymbula.
OX   NCBI_TaxID=87972;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-122.
RX   PubMed=436833; DOI=10.1111/j.1432-1033.1979.tb12796.x;
RA   van Helden P., Strickland W.N., Brandt W.F., von Holt C.;
RT   "The complete amino-acid sequence of histone H2B from the mollusc Patella
RT   granatina.";
RL   Eur. J. Biochem. 93:71-78(1979).
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-117 gives a specific tag for epigenetic
CC       transcriptional activation and is also prerequisite for histone H3
CC       'Lys-4' and 'Lys-79' methylation. {ECO:0000250}.
CC   -!- PTM: GlcNAcylation at Ser-109 promotes monoubiquitination of Lys-117.
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   PIR; A02611; HSKP22.
DR   AlphaFoldDB; P02284; -.
DR   SMR; P02284; -.
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   1: Evidence at protein level;
KW   Chromosome; Direct protein sequencing; DNA-binding; Glycoprotein;
KW   Isopeptide bond; Nucleosome core; Nucleus; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:436833"
FT   CHAIN           2..122
FT                   /note="Histone H2B, gonadal"
FT                   /id="PRO_0000071877"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..31
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        109
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        117
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   122 AA;  13525 MW;  DA00007E2D2937B8 CRC64;
     MPPKVSSKGA KKAGKAKAAR SGDKKRKRRR KESYSIYIYK VLKQVHPDTG VSSKAMSIMN
     SFVNDIFERI AAEASRLAHY NKRSTITSRE IQTAVRLLLP GELAKHAVSE GTKAVTKYTS
     SK