Fig. 4: JMJD3 is a highly disordered protein.

a Disorder prediction of human JMJD3 using PONDR-VL3 algorithm. In the bottom panel, the disorder score and the lengths of the predicted disordered regions are indicated (length of disordered segments >50 amino acids). A schematic representation of JMJD3 described domains is shown on top of the graphic. b Analysis of the presence of low-complexity domains in JMJD3 using the SEG algorithm. The percentage of low complexity regions is indicated on the right side. Low complexity regions are depicted in yellow. A schematic representation of JMJD3 described domains is shown on top of the panel. c Amino acid composition of JMJD3 IDR, JMJD3 catalytic domain, mouse proteome and disordered proteins defined by the presence of a 50 residues fragment whose IUPRED median score is at least 0.55 and that is not found in Pfam (so that functional domains are avoided). The percentages of acid, basic, hydrophobic, and hydrophilic amino acids of JMJD3 are shown on the right panel. d JMJD3 hydrophobicity profile was determined using the ExPASy website with the Hopp and Woods scale and a sliding window of 21. e, f The potential of JMJD3 to phase separate was determined using catGRANULE (on the left) (e) and PSPredictor (on the right) (f) algorithms.