Table 3. Overview of the amino acid changes in the 33 predicted sites of type II functional divergence.
Residue position (Human IκBα) | Amino acid change | Property change |
40* [635]# | Q → K | Hydrophilic/+ |
44 [639] | H → Q | +/Hydrophilic |
49 [644] | T → A | Hydrophilic/Hydrophobic |
63 [660] | C → A | Hydrophilic/Hydrophobic |
64 [661] | D → Q | −/Hydrophilic |
73 [670] | N → R | Hydrophilic/+ |
79 [676] | A → C | Hydrophobic/Hydrophilic |
80 [677] | C → A | Hydrophilic/Hydrophobic |
117 [785] | L → C | Hydrophobic/Hydrophilic |
119 [787] | S → V | Hydrophilic/Hydrophobic |
122 [790] | G → H | Hydrophilic/+ |
123 [791] | Y → N | Hydrophilic/Hydrophilic |
128 [823] | E → K | −/+ |
138 [833] | N → E | Hydrophilic/− |
139 [834] | A → S | Hydrophobic/Hydrophilic |
143 [859] | C → K | Hydrophilic/+ |
154 [870] | D → Q | −/Hydrophilic |
155 [871] | L → E | Hydrophobic/− |
156 [872] | Q → A | Hydrophilic/Hydrophobic |
170 [891] | D → F | −/Hydrophobic |
172 [893] | N → D | Hydrophilic/− |
174 [895] | V → K | Hydrophobic/+ |
175 [896] | T → A | Hydrophilic/Hydrophobic |
176 [897] | Y → H | Hydrophilic/+ |
179 [900] | Y → N | Hydrophilic/Hydrophilic |
181 [902] | P → A | Hydrophilic/Hydrophobic |
183 [904] | Q → H | Hydrophilic/+ |
185 [906] | T → A | Hydrophilic/Hydrophobic |
187 [912] | G → R | Hydrophilic/+ |
194 [919] | Q → V | Hydrophilic/Hydrophobic |
205 [930] | L → S | Hydrophobic/Hydrophilic |
208 [933] | L → N | Hydrophobic/Hydrophilic |
209 [934] | P → L | Hydrophilic/Hydrophobic |
Sites of radical change were detected in pairwise type II functional analysis of vertebrate IκB taxonomic groups. The residue positions are provided based on the human IκBα reference sequence. The amino acid changes between subfamilies along with their property changes are provided.
+ represents positively charged amino acids; − represents negatively charged amino acids;
represents the residue position based on the human IκBα reference sequence;
represents the residue position in the full vertebrate IκB alignment.