ID   H2B_LILLO               Reviewed;         158 AA.
AC   Q9MBF7;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Histone H2B.1;
DE   AltName: Full=GH2B;
OS   Lilium longiflorum (Trumpet lily).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Liliales; Liliaceae; Lilium.
OX   NCBI_TaxID=4690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 69-77, TISSUE SPECIFICITY,
RP   AND DEVELOPMENTAL STAGE.
RX   PubMed=10794571; DOI=10.1007/s004120050401;
RA   Ueda K., Kinoshita Y., Xu Z.-J., Ide N., Ono M., Akahori Y., Tanaka I.,
RA   Inoue M.;
RT   "Unusual core histones specifically expressed in male gametic cells of
RT   Lilium longiflorum.";
RL   Chromosoma 108:491-500(2000).
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 {ECO:0000250}. Chromosome {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in the generative cell within the
CC       bicellular pollen. Not detected in other reproductive or vegetative
CC       tissues. {ECO:0000269|PubMed:10794571}.
CC   -!- DEVELOPMENTAL STAGE: Associated with the differentiation of male
CC       gametic cells during pollen maturation. {ECO:0000269|PubMed:10794571}.
CC   -!- PTM: Can be acetylated to form H2BK6ac and H2BK33ac. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
CC   -!- CAUTION: To ensure consistency between histone entries, we follow the
CC       'Brno' nomenclature for histone modifications, with positions referring
CC       to those used in the literature for the 'closest' model organism. Due
CC       to slight variations in histone sequences between organisms and to the
CC       presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the
CC       actual positions of modified amino acids in the sequence generally
CC       differ. In this entry the following conventions are used: H2BK6ac =
CC       acetylated Lys-7; H2BK33ac = acetylated Lys-25. {ECO:0000305}.
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DR   EMBL; AB003780; BAA96095.1; -; mRNA.
DR   AlphaFoldDB; Q9MBF7; -.
DR   SMR; Q9MBF7; -.
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: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   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR23428; PTHR23428; 1.
DR   Pfam; PF00125; Histone; 1.
DR   PRINTS; PR00621; HISTONEH2B.
DR   SMART; SM00427; H2B; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chromosome; Direct protein sequencing; DNA-binding;
KW   Nucleosome core; Nucleus.
FT   CHAIN           1..158
FT                   /note="Histone H2B.1"
FT                   /id="PRO_0000240655"
FT   REGION          26..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          135..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         7
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         25
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   158 AA;  17249 MW;  37A96D6D9117A0BD CRC64;
     MPPRRKKKAA AAAAAAAAAA AAAGKAAAGK DGKAGIMTPK KPKKGKKKIP LMKYRVYIRR
     VLTQVRPELG ISSKSMLIMN NFVVHNFQNI AKEASILAQY SKKKTITVKE LKAAVKLVLP
     HQLLEYADRD GDRAVHNFES ETSKKNSQGR KRGRGQQT