H2BS1_STRPU
ID H2BS1_STRPU Reviewed; 140 AA.
AC P06145;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Histone H2B.1, sperm;
OS Strongylocentrotus purpuratus (Purple sea urchin).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC Strongylocentrotus.
OX NCBI_TaxID=7668;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Sperm;
RX PubMed=3786151; DOI=10.1093/nar/14.22.9218;
RA Lai Z.-C., Lieber T., Childs G.J.;
RT "The nucleotide sequence of the gene encoding the sperm specific histone
RT subtype H2B-1 from the sea urchin Strongylocentrotus purpuratus.";
RL Nucleic Acids Res. 14:9218-9218(1986).
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 -!- DOMAIN: Contains 3 SPKK motifs which may interact with the minor groove
CC of A/T-rich DNA sites. Phosphorylation of this motif may regulate DNA
CC binding. This motif is reiterated in both termini of histone H1 and in
CC the C-terminus of plant H2A, but its presence in the N-terminus seems
CC to be unique to sea urchin histones H2B.
CC -!- PTM: Monoubiquitination of Lys-135 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: Phosphorylated on SPKK motifs 2 and 3; which may regulate DNA
CC binding. Dephosphorylated during maturation of spermatids to mature
CC sperm and rephosphorylated at fertilization (By similarity).
CC {ECO:0000250}.
CC -!- PTM: GlcNAcylation at Ser-127 promotes monoubiquitination of Lys-135.
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 EMBL; X04681; CAA28385.1; -; Genomic_DNA.
DR EMBL; X04681; CAA28384.1; -; Genomic_DNA.
DR PIR; S07376; HSURBS.
DR RefSeq; NP_999706.1; NM_214541.1.
DR AlphaFoldDB; P06145; -.
DR SMR; P06145; -.
DR STRING; 7668.SPU_028171-tr; -.
DR iPTMnet; P06145; -.
DR EnsemblMetazoa; NM_214541; NP_999706; GeneID_373323.
DR GeneID; 373323; -.
DR KEGG; spu:373323; -.
DR CTD; 373323; -.
DR eggNOG; KOG1744; Eukaryota.
DR HOGENOM; CLU_075666_2_1_1; -.
DR OrthoDB; 1536672at2759; -.
DR PhylomeDB; P06145; -.
DR Proteomes; UP000007110; Unassembled WGS sequence.
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; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
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 3: Inferred from homology;
KW Chromosome; DNA-binding; Glycoprotein; Isopeptide bond; Nucleosome core;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..140
FT /note="Histone H2B.1, sperm"
FT /id="PRO_0000071896"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 6..9
FT /note="SPKK motif 1"
FT MOTIF 11..14
FT /note="SPKK motif 2"
FT MOTIF 16..19
FT /note="SPKK motif 3"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..47
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT CARBOHYD 127
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CROSSLNK 135
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 140 AA; 15562 MW; C693E335BF66E2DF CRC64;
MPSQRSPTKR SPTKRSPQKG AGKGGKGSKR GGKARRRGGA AVRRRRRRRE SYGIYIYKVL
KQVHPDTGIS SRGMSIMNSF VNDVFERVAA EASRLTKYNR RSTVSSREIQ TAVRLLLPGE
LAKHAVSEGT KAVTKYTTSR
