ID A0A2K5MJK6_CERAT Unreviewed; 134 AA.
AC A0A2K5MJK6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Histone H2B {ECO:0000256|RuleBase:RU000451};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000025399.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000025399.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 {ECO:0000256|ARBA:ARBA00002001}.
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. {ECO:0000256|RuleBase:RU000451}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU000451}.
CC -!- SIMILARITY: Belongs to the histone H2B family.
CC {ECO:0000256|ARBA:ARBA00006846, ECO:0000256|RuleBase:RU000451}.
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DR AlphaFoldDB; A0A2K5MJK6; -.
DR STRING; 9531.ENSCATP00000025399; -.
DR Ensembl; ENSCATT00000049629.1; ENSCATP00000025399.1; ENSCATG00000036173.1.
DR GeneTree; ENSGT01100000263506; -.
DR OMA; ARKETWA; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000036173; Expressed in bone marrow and 12 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
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; Histone, subunit A; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR000558; Histone_H2B.
DR PANTHER; PTHR23428; HISTONE H2B; 1.
DR PANTHER; PTHR23428:SF326; HISTONE H2B TYPE 2-E; 1.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00621; HISTONEH2B.
DR SMART; SM00427; H2B; 1.
DR SUPFAM; SSF47113; Histone-fold; 1.
DR PROSITE; PS00357; HISTONE_H2B; 1.
PE 3: Inferred from homology;
KW Chromosome {ECO:0000256|RuleBase:RU000451};
KW DNA-binding {ECO:0000256|RuleBase:RU000451};
KW Nucleosome core {ECO:0000256|RuleBase:RU000451};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU000451};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060}.
FT DOMAIN 11..101
FT /note="Histone H2A/H2B/H3"
FT /evidence="ECO:0000259|Pfam:PF00125"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..35
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 134 AA; 14736 MW; 43A593683A60B603 CRC64;
MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSV YVYKVLKQVH PDTGISSKAM
GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR LLLPGELAKH AVSEGTKAVT
KYTSQFNLAI VTAS
//
