H2B_MARGL
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 03-AUG-2022, entry version 89.
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}.
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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 GO; GO:0030527; F:structural constituent of chromatin; 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 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