Domain hiding |   Altered binding specificity |   Motif hiding |   Composite binding site formation |
  Uncategorised |   Rheostatic |   Allostery |   Avidity-sensing |
  Physicochemical compatibility |   Pre-translational |   Competition |
Motif | Start | End | Switch Type | Switch Subtype | Switch Description | Information |
DNA repair protein RAD9 - RAD9 -  Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | |||||||
LIG_FHA_1 | 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. | ||
RNA-binding protein PIN4 - PIN4 -  Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | |||||||
LIG_FHA_1 | 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. | ||
Receptor protein kinase CLAVATA1 - CLV1 -  Arabidopsis thaliana | |||||||
LIG_FHA_1 | 866 | 872 | Binary | Physicochemical compatibility | Phosphorylation of T868 in the FHA-binding motif of Receptor protein kinase CLAVATA1 (CLV1) induces binding to the Protein phosphatase 2C 70 (KAPP) protein. | ||
Serine/threonine-protein kinase Chk2 - CHEK2 -  Homo sapiens | |||||||
LIG_FHA_1 | 66 | 72 | Binary | Physicochemical compatibility | Phosphorylation of T68 in the FHA-binding motif of Serine/threonine-protein kinase Chk2 (CHEK2) induces binding to the Serine/threonine-protein kinase Chk2 (CHEK2) protein. | ||
Uncharacterized protein Rv1827/MT1875 - Rv1827 -  Mycobacterium tuberculosis | |||||||
LIG_FHA_1 | 19 | 25 | Binary | Physicochemical compatibility | Phosphorylation of T21 in the FHA-binding motif of Uncharacterized protein Rv1827/MT1875 (Rv1827) by Probable serine/threonine-protein kinase pknG (pknG) results in auto-inhibition due to an intramolecular interaction with the FHA domain. As a result, phosphorylation-independent interactions of the FHA domain with metabolic enzymes, which regulate the catalytic activity of these enzymes, are blocked (See also switch details). | ||
LIG_FHA_1 | 20 | 26 | Binary | Physicochemical compatibility | Phosphorylation of T22 in the FHA-binding motif of Uncharacterized protein Rv1827/MT1875 (Rv1827) by Serine/threonine-protein kinase pknB (pknB) results in auto-inhibition due to an intramolecular interaction with the FHA domain. As a result, phosphorylation-independent interactions of the FHA domain with metabolic enzymes, which regulate the catalytic activity of these enzymes, are blocked (See also switch details). |