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 05-MAY-2009, entry version 30. DE RecName: Full=Histone H2B; OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; OC Protacanthopterygii; Salmoniformes; Salmonidae; Salmoninae; OC Oncorhynchus. OX NCBI_TaxID=8022; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=86037261; 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. RX MEDLINE=72259090; 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- RT testis 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 CC compact DNA into chromatin, limiting DNA accessibility to the CC cellular machineries which require DNA as a template. Histones CC thereby play a central role in transcription regulation, DNA CC repair, DNA replication and chromosomal stability. DNA CC accessibility is regulated via a complex set of post-translational CC modifications of histones, also called histone code, and CC nucleosome remodeling. CC -!- SUBUNIT: The nucleosome is a histone octamer containing two CC molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 CC heterotetramer and two H2A-H2B heterodimers. The octamer wraps CC approximately 147 bp of DNA. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- PTM: Monoubiquitination of Lys-119 by BRE1 gives a specific tag CC for epigenetic transcriptional activation and is also prerequisite CC for histone H3 'Lys-4' and 'Lys-79' methylation (By similarity). CC -!- PTM: Phosphorylated during apoptosis; which facilitates apoptotic CC chromatin condensation (By similarity). CC -!- SIMILARITY: Belongs to the histone H2B family. 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 HSSP; P02281; 1KX3. DR SMR; P69069; 8-124. DR HOVERGEN; P69069; -. DR GO; GO:0000786; C:nucleosome; IEA:InterPro. DR GO; GO:0005634; C:nucleus; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro. DR InterPro; IPR009072; Histone-fold. DR InterPro; IPR007125; Histone_core_D. DR InterPro; IPR000558; Histone_H2B. DR Gene3D; G3DSA:1.10.20.10; Histone-fold; 1. DR PANTHER; PTHR23428; Histone_H2B; 1. DR Pfam; PF00125; Histone; 1. DR PRINTS; PR00621; HISTONEH2B. DR ProDom; PD000497; Histone_H2B; 1. DR SMART; SM00427; H2B; 1. DR PROSITE; PS00357; HISTONE_H2B; 1. PE 1: Evidence at protein level; KW Acetylation; Chromosomal protein; Direct protein sequencing; KW DNA-binding; Isopeptide bond; Nucleosome core; Nucleus; KW Phosphoprotein; Ubl conjugation. FT INIT_MET 1 1 Removed. FT CHAIN 2 124 Histone H2B. FT /FTId=PRO_0000071851. FT MOD_RES 6 6 N6-acetyllysine. FT MOD_RES 11 11 N6-acetyllysine. FT MOD_RES 13 13 Phosphoserine (By similarity). FT MOD_RES 14 14 N6-acetyllysine. FT MOD_RES 19 19 N6-acetyllysine. FT CROSSLNK 119 119 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin) (By FT similarity). FT CONFLICT 29 30 KR -> RK (in Ref. 1; CAA26673). SQ SEQUENCE 124 AA; 13596 MW; 30097D5582BE0B84 CRC64; MPEPAKSAPK KGSKKAVTKT AGKGGKKRKR SRKESYAIYV YKVLKQVHPD TGISSKAMGI MNSFVNDIFE RIAGESSRLA HYNKRSTITS REIQTAVRLL LPGELAKHAV SEGTKAVTKY TSSK //