Table 1.
Diverse ankyrin repeat sequences are substrates for FIH
| Peptide sequence | Protein | Activity relative to HIF-1α peptide, % |
|---|---|---|
| DESGLPQLTSYDCEVNAPI | HIF-1α (788–806) | 100 |
| SLPCLLLLVAAGADVNAQEQK | p105 (663–683) | 125 |
| YLGIVELLVSLGADVNAQEPC | IκBα (195–215) | 127 |
| NPDLVSLLLKCGADVNRVTY | IκBα (229–248) | 120 |
| NALVTKLLLDCGAEVNAVDNE | FEM1β (511–531) | 112 |
| FLDTLKVLVEHGADVNVPDG | p19-INK4d (86–105) | 124 |
| HASIVEVLLKHGADVNAKDM | GABP-β (83–102) | 107 |
| NLEVAEYLLEHGADVNAQDK | Tankyrase-1 (849–868) | 107 |
| RDEIVKALLGKGAQVNAVNQ | Gankyrin (85–104) | 116 |
| YTEVLKLLIQAGYDVNIKDV | MYPT1 (211–230) | 122 |
| QLEILEFLLLKGADINAPDK | Myotrophin (46–65) | 124 |
| NTRVASFLLQHDADINAQTK | FGIF (153–172) | 168 |
| HRDIVQKLLQYKADINAVNEH | ILK-1 (79–99) | 45 |
2-OG decarboxylation assays illustrating the ability of peptides derived from different ARD proteins to act as FIH substrates. Activity is normalized to that of the HIF-1α peptide. Target Asn residues are in bold.