H2BS2_PSAMI
ID H2BS2_PSAMI Reviewed; 143 AA.
AC Q27750;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Histone H2B.2, sperm;
OS Psammechinus miliaris (Green sea urchin) (Echinus miliaris).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Parechinidae;
OC Psammechinus.
OX NCBI_TaxID=7660;
RN [1]
RP PROTEIN SEQUENCE OF 2-44.
RX PubMed=708769; DOI=10.1016/0005-2795(78)90076-4;
RA Strickland M., Strickland W.N., Brandt W.F., von Holt C.;
RT "The partial amino acid sequences of the two H2B histones from sperm of the
RT sea urchin Psammechinus miliaris.";
RL Biochim. Biophys. Acta 536:289-297(1978).
RN [2]
RP PROTEIN SEQUENCE OF 17-27, AND PHOSPHORYLATION AT SER-14; SER-19 AND
RP SER-24.
RX PubMed=2311583; DOI=10.1002/j.1460-2075.1990.tb08177.x;
RA Hill C.S., Packman L.C., Thomas J.O.;
RT "Phosphorylation at clustered -Ser-Pro-X-Lys/Arg- motifs in sperm-specific
RT histones H1 and H2B.";
RL EMBO J. 9:805-813(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 41-143, AND DEVELOPMENTAL STAGE.
RC TISSUE=Testis;
RX PubMed=2412222; DOI=10.1073/pnas.82.17.5676;
RA Busslinger M., Barberis A.;
RT "Synthesis of sperm and late histone cDNAs of the sea urchin with a primer
RT complementary to the conserved 3' terminal palindrome: evidence for tissue-
RT specific and more general histone gene variants.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:5676-5680(1985).
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 -!- DEVELOPMENTAL STAGE: Expressed only during spermatogenesis.
CC {ECO:0000269|PubMed:2412222}.
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-137 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-129 promotes monoubiquitination of Lys-137.
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; M11087; AAA30021.1; -; mRNA.
DR AlphaFoldDB; Q27750; -.
DR SMR; Q27750; -.
DR iPTMnet; Q27750; -.
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: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; Nucleosome core; Nucleus; Phosphoprotein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:708769"
FT CHAIN 2..143
FT /note="Histone H2B.2, sperm"
FT /id="PRO_0000239651"
FT REGION 1..49
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 24..27
FT /note="SPKK motif 5"
FT COMPBIAS 14..49
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:2311583"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:2311583"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:2311583"
FT CARBOHYD 129
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CROSSLNK 137
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 143 AA; 15778 MW; E56220E97244845E CRC64;
MPKSPSKSSP RKGSPRKGSP RKGSPKRGGK GAKRAGKGGR RNVVKRRRRR RESYGIYIYK
VLKQVHPDTG ISSRGMSVMN SFVNDVFERI AGEASRLTSA NRRSTISSRE IQTAVRLLLP
GELAKHAVSE GTKAVTKYTT ARR
