The primary structure of histone H2A from the sperm cell of the sea urchin Parechinus angulosus.
The 125 residues of the histone H2A from the sperm cells of the sea urchin Parechinus angulosus have been positioned. The N terminus is blocked by an acetyl group. Compared to the bovine histone, the sea urchin protein differs in 14 positions.
D000595:Amino Acid Sequence; D000818:Animals; D001974:Bromosuccinimide; D006657:Histones; D008297:Male; D010446:Peptide Fragments / Q000032:analysis; D010447:Peptide Hydrolases; D010669:Phenylthiohydantoin; D012617:Sea Urchins / Q000032:analysis*; D013094:Spermatozoa / Q000032:analysis*; D013820:Thermolysin; D014357:Trypsin
D006657:Histones; D010446:Peptide Fragments; D010669:Phenylthiohydantoin; D010447:Peptide Hydrolases; D014357:Trypsin; D013820:Thermolysin; D001974:Bromosuccinimide