ID   H2B1_CHLRE              Reviewed;         153 AA.
AC   P50565;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Histone H2B.1;
DE   AltName: Full=H2B-I;
GN   Name=H2B;
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=137c / CC-125;
RX   PubMed=7479007; DOI=10.1093/nar/23.18.3756;
RA   Walther Z., Hall J.L.;
RT   "The uni chromosome of Chlamydomonas: histone genes and nucleosome
RT   structure.";
RL   Nucleic Acids Res. 23:3756-3763(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 61-101 AND 106-152, AND UBIQUITINATION AT LYS-149.
RC   STRAIN=cw15;
RX   PubMed=1312804; DOI=10.1016/0003-9861(92)90157-r;
RA   Shimogawara K., Muto S.;
RT   "Purification of Chlamydomonas 28-kDa ubiquitinated protein and its
RT   identification as ubiquitinated histone H2B.";
RL   Arch. Biochem. Biophys. 294:193-199(1992).
RN   [3]
RP   UBIQUITINATION, ACETYLATION, AND DEVELOPMENTAL STAGE.
RC   STRAIN=cw15;
RX   PubMed=7480339; DOI=10.1104/pp.109.2.393;
RA   Waterborg J.H., Robertson A.J., Tatar D.L., Borza C.M., Davie J.R.;
RT   "Histones of Chlamydomonas reinhardtii. Synthesis, acetylation, and
RT   methylation.";
RL   Plant Physiol. 109:393-407(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   -!- DEVELOPMENTAL STAGE: Up-regulated during the dark period.
CC       {ECO:0000269|PubMed:7480339}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- PTM: Can be acetylated to form H2BK33ac and H2BK34ac (By similarity).
CC       Acetylated mainly on the ubiquitinated form. {ECO:0000250,
CC       ECO:0000269|PubMed:1312804, ECO:0000269|PubMed:7480339}.
CC   -!- PTM: Monoubiquitinated to form H2BK143ub1; which is increased during
CC       the light period and may give a specific tag for epigenetic
CC       transcriptional activation.
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: H2BK33ac =
CC       acetylated Lys-41; H2BK34ac = acetylated Lys-42; H2BK143ub1 =
CC       monoubiquitinated Lys-149. {ECO:0000305}.
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DR   EMBL; L41841; AAA99967.1; -; Genomic_DNA.
DR   PIR; S59125; S59125.
DR   AlphaFoldDB; P50565; -.
DR   SMR; P50565; -.
DR   STRING; 3055.EDP08533; -.
DR   iPTMnet; P50565; -.
DR   PRIDE; P50565; -.
DR   ProMEX; P50565; -.
DR   eggNOG; KOG1744; Eukaryota.
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   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   Acetylation; Chromosome; Direct protein sequencing; DNA-binding;
KW   Isopeptide bond; Nucleosome core; Nucleus; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000305"
FT   CHAIN           2..153
FT                   /note="Histone H2B.1"
FT                   /id="PRO_0000071910"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         41
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         42
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        149
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000305|PubMed:1312804"
SQ   SEQUENCE   153 AA;  16727 MW;  B4D79F264B4544EF CRC64;
     MAPKKDEKPP TQEAGAEAPA KAERKPKAEK AAKKAKKEPS KKAAKEPKGS GEKKDKKKKK
     SAVETYKLYI YKVLKQVHPD TGISSKAMSI MNSFINDIFE KVATEASKLS RYNKKPTVTS
     REIQTAVRLV LPGELAKHAV SEGTKAVTKF TSG