ID   H2BL1_STRPU             Reviewed;         123 AA.
AC   P16888;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Late histone H2B.L1;
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=3697096; DOI=10.1093/nar/15.24.10569;
RA   Maxson R., Mohun T., Gormezano G., Kedes L.;
RT   "Evolution of late H2A, H2B, and H4 histone genes of the sea urchin,
RT   Strongylocentrotus purpuratus.";
RL   Nucleic Acids Res. 15:10569-10582(1987).
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-118 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-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; X06640; CAA29848.1; -; Genomic_DNA.
DR   PIR; S01619; S01619.
DR   RefSeq; NP_999717.1; NM_214552.1.
DR   AlphaFoldDB; P16888; -.
DR   SMR; P16888; -.
DR   STRING; 7668.SPU_024343-tr; -.
DR   iPTMnet; P16888; -.
DR   EnsemblMetazoa; NM_214552; NP_999717; LOC373347.
DR   GeneID; 373347; -.
DR   KEGG; spu:373347; -.
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..123
FT                   /note="Late histone H2B.L1"
FT                   /id="PRO_0000071898"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..33
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000305|PubMed:7796537"
SQ   SEQUENCE   123 AA;  13629 MW;  62AA1E0EB712905C CRC64;
     MPAKAQPAGK KGSKKAKAPR PSGGKKRRRR RKESYGIYIY KVLKQVHPDT GISSRAMSIM
     NSFVNDVFER IAAEASRLAH YNKKSTITSR EVQTVVRLLL PGELAKHAVS EGTKAVTKYT
     TSK