H2BS2_STRPU
ID H2BS2_STRPU Reviewed; 144 AA.
AC P16887;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Histone H2B.2, 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 [MRNA].
RC TISSUE=Testis;
RX PubMed=3785204; DOI=10.1128/mcb.6.7.2602-2612.1986;
RA Lieber T., Weisser K., Childs G.;
RT "Analysis of histone gene expression in adult tissues of the sea urchins
RT Strongylocentrotus purpuratus and Lytechinus pictus: tissue-specific
RT expression of sperm histone genes.";
RL Mol. Cell. Biol. 6:2602-2612(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 5 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-139 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 3, 4 and 5; 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-131 promotes monoubiquitination of Lys-139.
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; M13634; AAA30058.1; -; mRNA.
DR PIR; A25381; HSURB1.
DR RefSeq; NP_999721.1; NM_214556.2.
DR AlphaFoldDB; P16887; -.
DR SMR; P16887; -.
DR STRING; 7668.SPU_016565-tr; -.
DR EnsemblMetazoa; NM_214556; NP_999721; LOC373351.
DR GeneID; 373351; -.
DR KEGG; spu:373351; -.
DR eggNOG; KOG1744; Eukaryota.
DR HOGENOM; CLU_531679_0_0_1; -.
DR InParanoid; P16887; -.
DR OMA; MAGGIRY; -.
DR OrthoDB; 1536672at2759; -.
DR PhylomeDB; P16887; -.
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 2: Evidence at transcript level;
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..144
FT /note="Histone H2B.2, sperm"
FT /id="PRO_0000071897"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 4..7
FT /note="SPKK motif 1"
FT MOTIF 9..12
FT /note="SPKK motif 2"
FT MOTIF 14..17
FT /note="SPKK motif 3"
FT MOTIF 19..22
FT /note="SPKK motif 4"
FT MOTIF 25..28
FT /note="SPKK motif 5"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..51
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT CARBOHYD 131
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 144 AA; 16004 MW; F8B3F75FD0A7247B CRC64;
MPRSPSKTSP RKGSPRRGSP SRKASPKRGG KGAKRAGKGG RRRNVVRRRR RRRESYGIYI
YKVLKQVHPD TGISSRGMSV MNSFVNDIFG RIAGEASRLT RANRRSTISS REIQTAVRLL
LPGELAKHAV SEGTKAVTKY TTSR
