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   18-SEP-2019, entry version 58.
DE   RecName: Full=Histone H2B;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii;
OC   Salmoniformes; 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-
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. Chromosome.
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.
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-
CC       119. It fluctuates in response to extracellular glucose, and
CC       associates with transcribed genes (By similarity).
CC       {ECO:0000250|UniProtKB:P62807}.
CC   -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
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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;
KW   Phosphoprotein; Ubl conjugation.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:4506069}.
FT   CHAIN         2    124       Histone H2B.
FT                                /FTId=PRO_0000071851.
FT   MOD_RES       6      6       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:4506069}.
FT   MOD_RES      11     11       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:4506069}.
FT   MOD_RES      13     13       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P06900}.
FT   MOD_RES      14     14       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:4506069}.
FT   MOD_RES      19     19       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:4506069}.
FT   CARBOHYD    111    111       O-linked (GlcNAc) serine.
FT                                {ECO:0000250|UniProtKB:P62807}.
FT   CROSSLNK    119    119       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:P0C1H4}.
FT   CONFLICT     29     30       KR -> RK (in Ref. 1; CAA26673).
FT                                {ECO:0000305}.
SQ   SEQUENCE   124 AA;  13596 MW;  30097D5582BE0B84 CRC64;
     MPEPAKSAPK KGSKKAVTKT AGKGGKKRKR SRKESYAIYV YKVLKQVHPD TGISSKAMGI
     MNSFVNDIFE RIAGESSRLA HYNKRSTITS REIQTAVRLL LPGELAKHAV SEGTKAVTKY
     TSSK
//