ID H2B_ONCMY Reviewed; 124 AA. AC P69069; P02282; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 11-DEC-2019, entry version 59. DE RecName: Full=Histone H2B; OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes; OC Salmonidae; Salmoninae; Oncorhynchus. OX NCBI_TaxID=8022; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2997457; DOI=10.1007/bf02105800; RA Winkfein R.J., Connor W., Mezquita J., Dixon G.H.; RT "Histone H4 and H2B genes in rainbow trout (Salmo gairdnerii)."; RL J. Mol. Evol. 22:1-19(1985). RN [2] RP PROTEIN SEQUENCE OF 2-23, AND ACETYLATION AT LYS-6; LYS-11; LYS-14 AND RP LYS-19. RX PubMed=4506069; DOI=10.1073/pnas.69.8.2015; RA Candido E.P.M., Dixon G.H.; RT "Amino-terminal sequences and sites of in vivo acetylation of trout-testis RT histones 3 and IIb 2."; RL Proc. Natl. Acad. Sci. U.S.A. 69:2015-2019(1972). 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 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X02916; CAA26673.1; -; Genomic_DNA. DR PIR; A92961; HSTR2B. DR SMR; P69069; -. DR iPTMnet; P69069; -. DR PRIDE; P69069; -. 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 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; Direct protein sequencing; DNA-binding; KW Glycoprotein; Isopeptide bond; Nucleosome core; Nucleus; Phosphoprotein; KW Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:4506069" FT CHAIN 2..124 FT /note="Histone H2B" FT /id="PRO_0000071851" FT MOD_RES 6 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:4506069" FT MOD_RES 11 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:4506069" FT MOD_RES 13 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P06900" FT MOD_RES 14 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:4506069" FT MOD_RES 19 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:4506069" 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" FT CONFLICT 29..30 FT /note="KR -> RK (in Ref. 1; CAA26673)" FT /evidence="ECO:0000305" SQ SEQUENCE 124 AA; 13596 MW; 30097D5582BE0B84 CRC64; MPEPAKSAPK KGSKKAVTKT AGKGGKKRKR SRKESYAIYV YKVLKQVHPD TGISSKAMGI MNSFVNDIFE RIAGESSRLA HYNKRSTITS REIQTAVRLL LPGELAKHAV SEGTKAVTKY TSSK //