Table 1.

Intrinsically-disordered protein domains potentially involved in membrane shaping. Values of predicted % disorder (human sequences) come from Pietrosemoli et al., PLOS Computational Biology 2013 [104]. CME: clathrin-mediated endocytosis.

Protein	Function	Membrane interaction	% Disorder (location)	Major binding partners
Epsin1	Cargo adaptor in CME [20, 94]	ENTH domain [20]	78 (C-term.)	AP2, clathrin, cargo [63]
AP180	Cargo adaptor in CME [94, 95]	ANTH domain [115]	28 (C-term.)	AP2, clathrin, cargo [63]
Intersectin1	CME initiation [42]	PH, C2 domains [116]	28 (middle)	AP2, clathrin, Eps15, FCHo1/2 [63, 116]
FCHo1	CME initiation [42]	F-BAR domain [117]	48 (middle)	Eps15, intersectin [42]
Amphiphysin	Dynamin recruitment [106]	N-BAR domain [38]	61 (middle)	Dynamin, AP2, clathrin [63]
SNX9	Dynamin recruitment [109]	PX-BAR domain [110]	27 (middle)	Dynamin, AP2, clathrin [63]
Auxilin	Clathrin uncoating [118]	n/a	45 (middle)	HSC70, clathrin, dynamin [63]
Sec16A	COPII accessory [113]	n/a	71 (N and C-term.)	Sec13/31, Sec23/24, Sar1 [113, 119]
Sec31A	COPII coat component [114]	n/a	34 (middle)	Sec13, Sec23/24, Sec16 [114, 119]