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. 2010 Apr 5;9(10):2205–2224. doi: 10.1074/mcp.M000035-MCP201

Table II. Properties of intrinsically disordered domains in S. cerevisiae FG nucleoporins.

MG, molten globule; PMG, premolten globule.

Nucleoporin Disordered domain AAsa FG motifs Net charge pI Charged AAs (DEKR) Hydrophobic AAs (AILFWV) Charged to hydrophobic ratio Molecular mass Configuration at 30 °C Predicted Rh at 30 °Cb Predicted diameter Volume Number per NPC Volume × number FG domain interactionc
% % daltons nm nm nm3 nm3
Nup159 387–1071 16 −38 4.7 24 22 1.1 71,748 Relaxed coil 6.7 13.4 1,259 8 10,074 Repulsive
Nup42 1–382 20 +11 10.7 4 25 0.2 37,577 PMG 4.1 8.2 289 8 2,309 Cohesive
Nup116 172–764 42 +11 10.7 2 22 0.1 59,006 PMG 4.9 9.8 492 8 3,940 Cohesive
Nup116 765–960 0 −1 6.3 35 26 1.4 22,152 Relaxed coil 3.8 7.6 230 8 1,838 Repulsive
Nup100 1–610 43 +12 11.4 2 21 0.1 61,153 PMG 4.9 9.8 493 8 3,941 Cohesive
Nup100 611–800 0 0 7.2 26 25 1.0 20,842 Relaxed coil 3.7 7.4 212 8 1,697 Repulsive
Nsp1 1–186 13 +4 10.5 2 22 0.1 18,507 PMG 3.1 6.2 125 32 3,991 Cohesive
Nsp1 187–617 22 +4 8.7 36 24 1.5 44,749 Extended coil 6.2 12.4 998 32 31,930 Repulsive
Nup49 1–251 17 +7 10.7 3 24 0.1 24,320 MG 2.5 5.0 65 16 1,047 Cohesive
Nup57 1–255 15 +7 10.8 3 21 0.1 24,601 PMG 3.4 6.8 165 16 2,633 Cohesive
Nup145N 1–242 13 +6 10.4 3 17 0.2 23,931 MG 2.5 5.0 65 16 1,047 Cohesive
Nup145N 243–433 1 +2 8.8 24 27 0.9 20,930 PMG 3.2 6.4 137 16 2,195 Repulsive
Nup1 220–797 19 +12 9.3 26 24 1.1 61,634 Extended coil 6.8 13.6 1,316 8 10,531 Repulsive
Nup1 798–1076 10 +7 11.8 4 26 0.2 27,525 PMG 3.6 7.2 195 8 1,563 Cohesive
Nup60 389–539 4 −3 5.3 26 27 1.0 16,576 Relaxed coil 3.3 6.6 151 8 1,204 Repulsive
Nup2 160–600 15 −8 5.2 27 23 1.2 46,960 Extended coil 6.3 12.6 1,047 8 8,375 Repulsive

a Specific boundaries for the intrinsically disordered domains were defined in Denning and Rexach (22) according to a bimodal AA substitution rate in these nups during evolution. The boundaries for Nup1 and Nup2 were refined here according to the PONDR predictions shown in Fig. 1.

b The predicted Rh for each domain was derived from its molecular weight and its best match structural category using the scaling equations defined in Table I.

c These assignments are based on the interactions reported here or in Patel et al. (27); the assignments are consistent with the rules of cohesion discussed in the text.