ID   H2BE_STRPU              Reviewed;         124 AA.
AC   P02289;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Histone H2B, embryonic;
OS   Strongylocentrotus purpuratus (Purple sea urchin).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC   Strongylocentrotus.
OX   NCBI_TaxID=7668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=728984; DOI=10.1016/0092-8674(78)90287-8;
RA   Sures I., Lowry J., Kedes L.H.;
RT   "The DNA sequence of sea urchin (S. purpuratus) H2A, H2B and H3 histone
RT   coding and spacer regions.";
RL   Cell 15:1033-1044(1978).
RN   [2]
RP   UBIQUITINATION.
RX   PubMed=7796537; DOI=10.1002/dvg.1020160308;
RA   Jasinskiene N., Jasinskas A., Langmore J.P.;
RT   "Embryonic regulation of histone ubiquitination in the sea urchin.";
RL   Dev. Genet. 16:278-290(1995).
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-119 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-111 promotes monoubiquitination of Lys-119.
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; V01356; CAA24646.2; ALT_SEQ; Genomic_DNA.
DR   PIR; A02617; HSUR2S.
DR   RefSeq; NP_999710.2; NM_214545.1.
DR   iPTMnet; P02289; -.
DR   GeneID; 373336; -.
DR   CTD; 373336; -.
DR   eggNOG; KOG1744; Eukaryota.
DR   HOGENOM; CLU_075666_2_1_1; -.
DR   OrthoDB; 1536672at2759; -.
DR   Proteomes; UP000007110; Unassembled WGS sequence.
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   Chromosome; DNA-binding; Glycoprotein; Isopeptide bond; Nucleosome core;
KW   Nucleus; Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..124
FT                   /note="Histone H2B, embryonic"
FT                   /id="PRO_0000071895"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..30
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        111
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        119
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000305|PubMed:7796537"
SQ   SEQUENCE   124 AA;  13628 MW;  F3190858888D435E CRC64;
     MAPTAQVAKK GSKKAVKGTK TAXGGKKRNR KRKESYGIYI YKVLKQVHPD TGISSRAMVI
     MNSFVNDIFE RIAGESSRLA QYNKKSTISS REIQTAVRLI LPGELAKHAV SEGTKAVTKY
     TTSK