Switches.ELM

Switch #:

SWTI000151

Switch type:
Binary

Switch subtype:
Physicochemical compatibility

Description:
Auto-phosphorylation of S386 in the PIF pocket-binding motif of Ribosomal protein S6 kinase alpha-3 (Rps6ka3) induces intramolecular binding and kinase cis-activation.

Participants:
(1) Ribosomal protein S6 kinase alpha-3 (Rps6ka3)

Interactions

Interaction #1 Rps6ka3 - Rps6ka3(intramolecular)
intramolecular
Interfaces
(1) DOC_AGCK_PIF_1 motif (₃₈₂FRGFSF₃₈₇) in Ribosomal protein S6 kinase alpha-3 (Rps6ka3)
(2) Protein kinase domain_(68-327) and _(422-679) in Ribosomal protein S6 kinase alpha-3 (Rps6ka3)

Interaction Regulation
PTM-dependent Induction (Phosphorylation of S₃₈₆ on Ribosomal protein S6 kinase alpha-3 (Rps6ka3)) of the Ribosomal protein S6 kinase alpha-3 (Rps6ka3) DOC_AGCK_PIF_1 motif - Ribosomal protein S6 kinase alpha-3 (Rps6ka3) Protein kinase domain interaction

Regulatory Enzymes for switch
Modifying enzymes for residue: S₃₈₆: Ribosomal protein S6 kinase alpha-3 (Rps6ka3)

Inferred Regulatory Enzymes for switch
Putative modifying enzymes for residue: S₃₈₆ : Mitogen-activated protein kinase 3 (Mapk3), 3-phosphoinositide-dependent protein kinase 1 (Pdpk1), Ribosomal protein S6 kinase alpha-3 (Rps6ka3).

Context

References

(1) A phosphoserine-regulated docking site in the protein kinase RSK2 that recruits and activates PDK1.
Frödin et al. EMBO J. (2000)