H2B12_XENLA
ID H2B12_XENLA Reviewed; 126 AA.
AC P06900;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Histone H2B 1.2;
DE Short=H2B1.2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (GENE CLUSTER X1H1).
RX PubMed=3863963; DOI=10.1016/0022-2836(85)90065-8;
RA Perry M., Thomsen G.H., Roeder R.G.;
RT "Genomic organization and nucleotide sequence of two distinct histone gene
RT clusters from Xenopus laevis. Identification of novel conserved upstream
RT sequence elements.";
RL J. Mol. Biol. 185:479-499(1985).
RN [2]
RP PHOSPHORYLATION AT SER-15.
RX PubMed=12757711; DOI=10.1016/s0092-8674(03)00355-6;
RA Cheung W.L., Ajiro K., Samejima K., Kloc M., Cheung P., Mizzen C.A.,
RA Beeser A., Etkin L.D., Chernoff J., Earnshaw W.C., Allis C.D.;
RT "Apoptotic phosphorylation of histone H2B is mediated by mammalian sterile
RT twenty kinase.";
RL Cell 113:507-517(2003).
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: Monoubiquitination of Lys-121 by BRE1 gives a specific tag for
CC epigenetic transcriptional activation and is also prerequisite for
CC histone H3 'Lys-4' and 'Lys-79' methylation.
CC {ECO:0000250|UniProtKB:P33778}.
CC -!- PTM: Phosphorylated on Ser-15 during developmentally programmed
CC apoptosis; which may facilitate apoptotic chromatin condensation.
CC {ECO:0000269|PubMed:12757711}.
CC -!- PTM: GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121.
CC It fluctuates in response to extracellular glucose, and associates with
CC transcribed genes (By similarity). {ECO:0000250|UniProtKB:P62807}.
CC -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
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DR EMBL; X03017; CAA26811.1; -; Genomic_DNA.
DR EMBL; M21286; AAA49763.1; -; Genomic_DNA.
DR PIR; B24510; HSXLB2.
DR PIR; I51446; I51446.
DR RefSeq; XP_018098035.1; XM_018242546.1.
DR RefSeq; XP_018098037.1; XM_018242548.1.
DR RefSeq; XP_018098038.1; XM_018242549.1.
DR AlphaFoldDB; P06900; -.
DR SMR; P06900; -.
DR iPTMnet; P06900; -.
DR GeneID; 108705671; -.
DR GeneID; 108705673; -.
DR GeneID; 108705674; -.
DR KEGG; xla:108705671; -.
DR KEGG; xla:108705673; -.
DR KEGG; xla:108705674; -.
DR OrthoDB; 1536672at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 108705671; Expressed in oocyte and 7 other tissues.
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; DNA-binding; Glycoprotein; Isopeptide bond;
KW Nucleosome core; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..126
FT /note="Histone H2B 1.2"
FT /id="PRO_0000071855"
FT REGION 1..35
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"
FT MOD_RES 6
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P0C1H4"
FT MOD_RES 13
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P0C1H4"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12757711"
FT MOD_RES 16
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P0C1H4"
FT MOD_RES 21
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P0C1H4"
FT CARBOHYD 113
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250|UniProtKB:P62807"
FT CROSSLNK 121
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0C1H4"
SQ SEQUENCE 126 AA; 13905 MW; 24A035C504133AD8 CRC64;
MPEPAKSAPA PKKGSKKAVT KTPKKDGKKR RKSRKESYAI YVYKVMKQVH PDTGISSKAM
GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR LLLPGELAKH AVSEGTKAVT
KYTSAK
