H2B_ROSNE
ID H2B_ROSNE Reviewed; 136 AA.
AC Q8J1K2;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Histone H2B;
GN Name=hh2b; Synonyms=htb1;
OS Rosellinia necatrix (White root-rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Rosellinia.
OX NCBI_TaxID=77044;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=W20;
RX PubMed=12652911; DOI=10.1080/1042517021000019287;
RA Aimi T., Taguchi H., Morinaga T.;
RT "Primary structure of the histone 2B gene in the white root rot fungus,
RT Rosellinia necatrix.";
RL DNA Seq. 13:383-386(2002).
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 -!- PTM: Monoubiquitinated to form H2BK123ub1. H2BK123ub1 gives a specific
CC tag for epigenetic transcriptional activation and is also prerequisite
CC for H3K4me and H3K79me formation. H2BK123ub1 also modulates the
CC formation of double-strand breaks during meiosis and is a prerequisite
CC for DNA-damage checkpoint activation (By similarity). {ECO:0000250}.
CC -!- PTM: Acetylated by GCN5 to form H2BK11ac and H2BK16ac. H2BK16ac can
CC also be formed by ESA1. Acetylation of N-terminal lysines and
CC particularly formation of H2BK11acK16ac has a positive effect on
CC transcription (By similarity). {ECO:0000250}.
CC -!- PTM: Sumoylation to form H2BK6su or H2BK7su, and probably also H2BK16su
CC or H2BK17su, occurs preferentially near the telomeres and represses
CC gene transcription. {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-8; H2BK6su = sumoylated Lys-8; H2BK7ac = acetylated Lys-
CC 9; H2BK7su = sumoylated Lys-9; H2BK11ac = acetylated Lys-13; H2BK16ac =
CC acetylated Lys-23; H2BK16su = sumoylated Lys-23; H2BK17su = sumoylated
CC Lys-24; H2BK123ub1 = monoubiquitinated Lys-130. {ECO:0000305}.
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DR EMBL; AB085854; BAC54259.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8J1K2; -.
DR SMR; Q8J1K2; -.
DR PRIDE; Q8J1K2; -.
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 Acetylation; Chromosome; DNA-binding; Isopeptide bond; Nucleosome core;
KW Nucleus; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..136
FT /note="Histone H2B"
FT /id="PRO_0000071936"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 9
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 13
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 23
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 8
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 9
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 23
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 24
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 130
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 136 AA; 14798 MW; 24668AF8AC6A53CD CRC64;
MPPKAADKKP AAKAPVASKA PEKKDAGKKT ASTGEKKKRT KARRETYSSY IYKVLKQVHP
DTGISNRAMS ILNSFVNDIF ERVATEASKL AAYNKKSTIS SREIQTSVRL ILPGELAKHA
VSEGTKAVTK YSSSTK
