ID H2B_MARGL Reviewed; 121 AA. AC P02285; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 25-MAY-2022, entry version 88. DE RecName: Full=Histone H2B, sperm; OS Marthasterias glacialis (Spiny starfish). OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Asterozoa; Asteroidea; OC Forcipulatacea; Forcipulatida; Asteriidae; Marthasterias. OX NCBI_TaxID=7609; RN [1] RP PROTEIN SEQUENCE OF 2-121. RX PubMed=7398625; DOI=10.1111/j.1432-1033.1980.tb04601.x; RA Strickland M., Strickland W.N., von Holt C.; RT "The histone H2B from the sperm cell of the starfish Marthasterias RT glacialis."; RL Eur. J. Biochem. 106:541-548(1980). 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-116 gives a specific tag for epigenetic CC transcriptional activation and is also prerequisite for histone H3 CC 'Lys-4' and 'Lys-79' methylation. {ECO:0000250}. CC -!- PTM: GlcNAcylation at Ser-108 promotes monoubiquitination of Lys-116. CC It fluctuates in response to extracellular glucose, and associates with CC transcribed genes (By similarity). {ECO:0000250}. 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 PIR; A02612; HSSF2M. DR AlphaFoldDB; P02285; -. DR SMR; P02285; -. 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:0044877; F:protein-containing complex binding; ISS:UniProtKB. 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 Chromosome; Direct protein sequencing; DNA-binding; Glycoprotein; KW Isopeptide bond; Methylation; Nucleosome core; Nucleus; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:7398625" FT CHAIN 2..121 FT /note="Histone H2B, sperm" FT /id="PRO_0000071887" FT REGION 1..30 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 9..30 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N,N-dimethylproline" FT /evidence="ECO:0000250|UniProtKB:P02286" FT CARBOHYD 108 FT /note="O-linked (GlcNAc) serine" FT /evidence="ECO:0000250" FT CROSSLNK 116 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250" SQ SEQUENCE 121 AA; 13481 MW; C7B97F69B7911824 CRC64; MPPKSGKGQK KAGKAKGAPR SDKKRRRKRK ESYGIYIYKV MKQVHPDTGI SSRAMSIMNS FVNDIFERIA AEASRLAHYN KKSTITSREV QTAVRLLLPG ELAKHAVSEG TKAVTKYTTS K //