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Switch #:
SWTI000124
Switch type:
Binary
Switch subtype:
Physicochemical compatibility

Description:
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.

Participants:
(1) Serine/threonine-protein kinase Chk2 (CHEK2)

Interactions
Interaction #1 CHEK2 - CHEK2(intramolecular)
intramolecular
Interfaces
(1) LIG_FHA_1 motif (66VSTQELY72) in Serine/threonine-protein kinase Chk2 (CHEK2)
(2) FHA domain (113-192) in Serine/threonine-protein kinase Chk2 (CHEK2)

Interaction Regulation
PTM-dependent Induction (Phosphorylation of T68 on Serine/threonine-protein kinase Chk2 (CHEK2)) of the Serine/threonine-protein kinase Chk2 (CHEK2) LIG_FHA_1 motif - Serine/threonine-protein kinase Chk2 (CHEK2) FHA domain interaction

Inferred Regulatory Enzymes for switch
Putative modifying enzymes for residue: T68 : Serine-protein kinase ATM (ATM), ATM, Serine/threonine-protein kinase ATR (ATR), DNA-dependent protein kinase catalytic subunit (PRKDC), Mitogen-activated protein kinase kinase kinase MLT (MLTK), Serine/threonine-protein kinase Chk2 (CHEK2), Serine/threonine-protein kinase PLK1 (PLK1), Dual specificity protein kinase TTK (TTK).

Context
Switch localisation
ELM curated: nucleus
References

(1) Structural and functional versatility of the FHA domain in DNA-damage signaling by the tumor suppressor kinase Chk2.
Li et al. Mol. Cell (2002)

See also

Other switches involving interfaces
LIG_FHA_1 - 5 more (view)
FHA domain - 11 more (view)


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