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Switch #:
SWTI000053
Switch type:
Binary
Switch subtype:
Physicochemical compatibility

Description:
Phosphorylation of T450 in the Pin1-binding motif of RAC-alpha serine/threonine-protein kinase (AKT1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.

Participants:
(1) RAC-alpha serine/threonine-protein kinase (AKT1)
(2) Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1)

Interactions
Interaction #1 AKT1 - PIN1

Interfaces
(1) DOC_WW_Pin1_4 motif (447ITITPP452) in RAC-alpha serine/threonine-protein kinase (AKT1)
(2) WW domain (7-37) in Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1)

Interaction Regulation
PTM-dependent Induction (Phosphorylation of T450 on RAC-alpha serine/threonine-protein kinase (AKT1)) of the RAC-alpha serine/threonine-protein kinase (AKT1) DOC_WW_Pin1_4 motif - Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) WW domain interaction

Inferred Regulatory Enzymes for switch
Putative modifying enzymes for residue: T450 : Serine/threonine-protein kinase mTOR (MTOR).

Context
Switch localisation
ELM curated: nucleus, cytosol
Inferred: nucleoplasm
References

(1) Peptidyl-prolyl cis/trans isomerase Pin1 is critical for the regulation of PKB/Akt stability and activation phosphorylation.
Liao et al. Oncogene (2009)

See also

Other switches involving participants
RAC-alpha serine/threonine-protein kinase (AKT1) - 2 more (view)
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) - 55 more (view)

Other switches involving interfaces
DOC_WW_Pin1_4 - 90 more (view)
WW domain - 105 more (view)


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