Domain hiding |   Altered binding specificity |   Motif hiding |   Composite binding site formation |
  Uncategorised |   Rheostatic |   Allostery |   Avidity-sensing |
  Physicochemical compatibility |   Pre-translational |   Competition |
Protein | Start | End | Switch Type | Switch Subtype | Switch Description | Information |
LIG_FHA_1 - Phosphothreonine motif binding a subset of FHA domains that show a preference for a large aliphatic amino acid at the pT+3 position. | |||||||
RAD9_YEAST | 601 | 607 | Binary | Physicochemical compatibility | Phosphorylation of T603 in the FHA-binding motif of DNA repair protein RAD9 (RAD9) induces binding to the Serine/threonine-protein kinase RAD53 (RAD53) protein. | ||
PIN4_YEAST | 303 | 309 | Binary | Physicochemical compatibility | Phosphorylation of T305 in the FHA-binding motif of RNA-binding protein PIN4 (PIN4) induces binding to the Serine/threonine-protein kinase RAD53 (RAD53) protein. | ||
LIG_FHA_2 - Phosphothreonine motif binding a subset of FHA domains that have a preference for an acidic amino acid at the pT+3 position. | |||||||
RAD9_YEAST | 153 | 159 | Binary | Physicochemical compatibility | Phosphorylation of T155 in the FHA-binding motif of DNA repair protein RAD9 (RAD9) induces binding to the Serine/threonine-protein kinase RAD53 (RAD53) protein. | ||
RAD9_YEAST | 190 | 196 | Binary | Physicochemical compatibility | Phosphorylation of T192 in the FHA-binding motif of DNA repair protein RAD9 (RAD9) induces binding to the Serine/threonine-protein kinase RAD53 (RAD53) protein. |