H2B3_CHLRE
ID H2B3_CHLRE Reviewed; 153 AA.
AC P54346;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Histone H2B.3;
DE AltName: Full=H2B-III;
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 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; U16725; AAA98450.1; -; Genomic_DNA.
DR PIR; S59587; S59587.
DR RefSeq; XP_001690724.1; XM_001690672.1.
DR RefSeq; XP_001691541.1; XM_001691489.1.
DR AlphaFoldDB; P54346; -.
DR SMR; P54346; -.
DR EnsemblPlants; PNW70180; PNW70180; CHLRE_17g709150v5.
DR GeneID; 5717161; -.
DR Gramene; PNW70180; PNW70180; CHLRE_17g709150v5.
DR KEGG; cre:CHLRE_17g709150v5; -.
DR eggNOG; KOG1744; Eukaryota.
DR HOGENOM; CLU_075666_2_0_1; -.
DR OMA; YLQIAFX; -.
DR OrthoDB; 1536672at2759; -.
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.3"
FT /id="PRO_0000071912"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..60
FT /note="Basic and acidic residues"
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:0000250"
SQ SEQUENCE 153 AA; 16557 MW; 2092413E04E1F49C CRC64;
MAPKKDEKPA TAEAGAEAPA KAEAKPKAEK AGKKAKKEPA KKAAKEPKGD GEKKDKKKKK
SAVETYKLYI YKVLKQVHPD TGISSKAMSI MNSFINDIFE KVATEASKLS RYNKKPTVTS
REIQTAVRLV LPGELAKHAV SEGTKAVTKF TSG
