H2B4_VOLCA
ID H2B4_VOLCA Reviewed; 155 AA.
AC P16868;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Histone H2B.4;
DE AltName: Full=H2B-IV;
OS Volvox carteri (Green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Volvox.
OX NCBI_TaxID=3067;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=f. Nagariensis / HK10;
RX PubMed=2227431; DOI=10.1016/0378-1119(90)90221-c;
RA Mueller K., Lindauer A., Bruederlein M., Schmitt R.;
RT "Organization and transcription of Volvox histone-encoding genes:
RT similarities between algal and animal genes.";
RL Gene 93:167-175(1990).
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: Monoubiquitinated to form H2BK143ub1; may give a specific tag for
CC epigenetic transcriptional activation. {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: H2BK143ub1 =
CC monoubiquitinated Lys-151. {ECO:0000305}.
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DR EMBL; M31922; AAA34250.1; -; Genomic_DNA.
DR PIR; JQ0797; JQ0797.
DR AlphaFoldDB; P16868; -.
DR SMR; P16868; -.
DR PRIDE; P16868; -.
DR OMA; KHAINEG; -.
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 3: Inferred from homology;
KW Chromosome; DNA-binding; Isopeptide bond; Nucleosome core; Nucleus;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..155
FT /note="Histone H2B.4"
FT /id="PRO_0000071923"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 151
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 155 AA; 16842 MW; 56AC3D9C7A6F5940 CRC64;
MAPKTKEEKP ASEAVEPKAE AKPKAEKAPK KKEKKAPAKK SAKEPAAGDA AEGDKKKKKA
KVAKSETYKL YIYKVLKQVH PDTGISSKAM SIMNSFINDI FEKVATEASK LSRYNKKPTV
TSREIQTAVR LVLPGELAKH AVSEGTKAVT KFTSA
