H2B1_DANRE
ID H2B1_DANRE Reviewed; 124 AA.
AC Q5BJA5;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Histone H2B 1/2;
GN ORFNames=zgc:112234;
GN and
GN ORFNames=zgc:114046;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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-119 by the 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 during apoptosis; which facilitates apoptotic
CC chromatin condensation. {ECO:0000250|UniProtKB:P06900}.
CC -!- PTM: GlcNAcylation at Ser-111 promotes monoubiquitination of Lys-119.
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; BC091558; AAH91558.1; -; mRNA.
DR EMBL; BC095697; AAH95697.1; -; mRNA.
DR RefSeq; NP_001013481.1; NM_001013463.1.
DR RefSeq; XP_002666990.1; XM_002666944.4.
DR RefSeq; XP_005163256.1; XM_005163199.3.
DR RefSeq; XP_005170789.1; XM_005170732.3.
DR RefSeq; XP_005172456.1; XM_005172399.3.
DR RefSeq; XP_009301957.1; XM_009303682.2.
DR RefSeq; XP_017209639.1; XM_017354150.1.
DR RefSeq; XP_017212661.1; XM_017357172.1.
DR AlphaFoldDB; Q5BJA5; -.
DR SMR; Q5BJA5; -.
DR STRING; 7955.ENSDARP00000050236; -.
DR PaxDb; Q5BJA5; -.
DR Ensembl; ENSDART00000109316; ENSDARP00000101525; ENSDARG00000075482.
DR Ensembl; ENSDART00000126590; ENSDARP00000111194; ENSDARG00000091728.
DR Ensembl; ENSDART00000152766; ENSDARP00000127042; ENSDARG00000070297.
DR Ensembl; ENSDART00000169756; ENSDARP00000139362; ENSDARG00000104501.
DR Ensembl; ENSDART00000190053; ENSDARP00000151365; ENSDARG00000114180.
DR GeneID; 100329290; -.
DR GeneID; 100329560; -.
DR GeneID; 100333496; -.
DR GeneID; 100334559; -.
DR GeneID; 100334869; -.
DR GeneID; 541335; -.
DR GeneID; 561322; -.
DR KEGG; dre:100329290; -.
DR KEGG; dre:100329560; -.
DR KEGG; dre:100333496; -.
DR KEGG; dre:100334559; -.
DR KEGG; dre:541335; -.
DR KEGG; dre:561322; -.
DR CTD; 255626; -.
DR eggNOG; KOG1744; Eukaryota.
DR GeneTree; ENSGT01050000244921; -.
DR HOGENOM; CLU_075666_2_1_1; -.
DR InParanoid; Q5BJA5; -.
DR OMA; FETKSAP; -.
DR OrthoDB; 1536672at2759; -.
DR PhylomeDB; Q5BJA5; -.
DR TreeFam; TF300212; -.
DR PRO; PR:Q5BJA5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 25.
DR Proteomes; UP000814640; Chromosome 7.
DR Bgee; ENSDARG00000070297; Expressed in gastrula and 7 other tissues.
DR ExpressionAtlas; Q5BJA5; baseline and differential.
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; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
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 2: Evidence at transcript 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..124
FT /note="Histone H2B 1/2"
FT /id="PRO_0000244867"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..32
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 11
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P0C1H4"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06900"
FT MOD_RES 14
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P0C1H4"
FT MOD_RES 19
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P0C1H4"
FT CARBOHYD 111
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250|UniProtKB:P62807"
FT CROSSLNK 119
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0C1H4"
SQ SEQUENCE 124 AA; 13578 MW; 6EAC690D72B48363 CRC64;
MPEPAKAAPK KGSKKAVTKT AGKGGKKRKR TRKESYAIYV YKVLKQVHPD TGISSKAMGI
MNSFVNDIFE RIAGEASRLA HYNKRSTITS REIQTAVRLL LPGELAKHAV SEGTKAVTKY
TSSK
