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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.

(1) DNA repair protein RAD9 (RAD9)
(2) Serine/threonine-protein kinase RAD53 (RAD53)

Interaction #1 RAD9 - RAD53

(1) LIG_FHA_2 motif (190EVTEADA196) in DNA repair protein RAD9 (RAD9)
(2) FHA domain (66-133) in Serine/threonine-protein kinase RAD53 (RAD53)

Interaction Regulation
PTM-dependent Induction (Phosphorylation of T192 on DNA repair protein RAD9 (RAD9)) of the DNA repair protein RAD9 (RAD9) LIG_FHA_2 motif - Serine/threonine-protein kinase RAD53 (RAD53) FHA domain interaction

Additional Information
Affinity : 0.3 µM
Structural information: 1K3Q

(1) Solution structures of two FHA1-phosphothreonine peptide complexes provide insight into the structural basis of the ligand specificity of FHA1 from yeast Rad53.
Yuan et al. J. Mol. Biol. (2001)

See also

Other switches involving participants
DNA repair protein RAD9 (RAD9) - 2 more (view)
Serine/threonine-protein kinase RAD53 (RAD53) - 3 more (view)

Other switches involving interfaces
FHA domain - 11 more (view)
LIG_FHA_2 - 9 more (view)

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