H2B2_CHLRE
ID H2B2_CHLRE Reviewed; 156 AA.
AC P54345;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Histone H2B.2;
DE AltName: Full=H2B-II;
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].
RX PubMed=8590479; DOI=10.1007/bf00326431;
RA Fabry S., Mueller K., Lindauer A., Park P.B., Cornelius T., Schmitt R.;
RT "The organization structure and regulatory elements of Chlamydomonas
RT histone genes reveal features linking plant and animal genes.";
RL Curr. Genet. 28:333-345(1995).
RN [2]
RP PROTEIN SEQUENCE OF 64-104 AND 109-155, AND UBIQUITINATION AT LYS-152.
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-40; H2BK34ac = acetylated Lys-41; H2BK143ub1 =
CC monoubiquitinated Lys-152. {ECO:0000305}.
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DR EMBL; U16724; AAA98446.1; -; Genomic_DNA.
DR PIR; S59583; S59583.
DR AlphaFoldDB; P54345; -.
DR SMR; P54345; -.
DR STRING; 3055.EDP08976; -.
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..156
FT /note="Histone H2B.2"
FT /id="PRO_0000071911"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 40
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 41
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT CROSSLNK 152
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 156 AA; 16932 MW; 2EA4FA6E15DDDB5E CRC64;
MAPKKDEKPA TRAATQEAGV EATAKAEAKP KAEKAAKKAK KEPAKKAAKE PKGDGEKKDK
KKKSAVETYK LYIYKVLKQV HPDTGISSKA MSIMNSFIND IFEKVATEAS KLSRYNKKPT
VTSREIQTAV RLVLPGELAK HAVSEGTKAV TKFTSG
