Fig. 2 

Protein features annotations. A Regions. Long, medium, short and three repeats are shown. At the moment, ProToDeviseR assigns regions colours anew for each protein. A rainbow gradient is used by default, where regions with the same name will have the same colour. Please note that, although coloured the same within one protein, regions may have another colour assigned to them in another protein. Shapes are: pointed: long regions (> 200 amino acids), curved: medium-sized regions (35–200 amino acids), straight: small regions (< 35 amino acids), jagged: regions designated as repeats. B Motifs. Signal peptide (1), coiled coil (2), low complexity (3), intrinsic disorder (4), intrinsically disordered binding (5), charged or polar amino acids patch (6), phosphorylation motif (7), glycosylation motif (8), transmembrane part (9), lipidation motif (10), cleavage motif (11), degradation motif (12), targeting motif (13), nuclear localisation or export motif (14), docking, ligand or binding motif (15), activity-related motif (16), other motif (17). C Markups. N-glycosylation (1), O-glycosylation (2), glycosaminoglycan (3), C-mannosylation (4), O-fucosylation (5), glycosylation unspecified (6), hydroxylation (7), prenylated (8), acylated (9), gpi (10), lipidation (11), acetylation (12), methylation (13), amidation (14), pyrrolidone carboxylic acid (15), sulfation (16), D-isomerization (17), di-sulfide bond (18), cross-linking (19), sumoylation (20), ubiquitination (21), degradation (22), cleavage (23), sorting (24), targeting (25), retaining (26), absorption (27), nuclear import (28), nuclear export (29), nuclear receptor (30), nuclear-related (31), DNA-binding (32), binding site (33), ligand binding (34), ligand site (35), docking (36), interacts with (37), flavin-binding (38), co-factor (39), active site (40), catalytic activity (41), activity regulation (42), phospho-serine (43), phospho-threonine (44), phospho-tyrosine (45), phosphorylation unspecified (46), other motif (47)