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Switch #:
SWTI000040
Switch type:
Binary
Switch subtype:
Physicochemical compatibility

Description:
Phosphorylation of S63 in the Pin1-binding motif of Transcription factor AP-1 (JUN) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.

Participants:
(1) Transcription factor AP-1 (JUN)
(2) Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1)

Interactions
Interaction #1 JUN - PIN1

Interfaces
(1) DOC_WW_Pin1_4 motif (60LLTSPD65) in Transcription factor AP-1 (JUN)
(2) WW domain (7-37) in Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1)

Interaction Regulation
PTM-dependent Induction (Phosphorylation of S63 on Transcription factor AP-1 (JUN)) of the Transcription factor AP-1 (JUN) 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: S63 : Cyclin-dependent kinase 3 (CDK3), Mitogen-activated protein kinase 15 (MAPK15), Serine/threonine-protein kinase D1 (PRKD1), Serine/threonine-protein kinase PLK3 (PLK3), Mitogen-activated protein kinase 9 (MAPK9), Serine/threonine-protein kinase VRK1 (VRK1), Mitogen-activated protein kinase 8 (MAPK8).

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

(1) Pin1 is overexpressed in breast cancer and cooperates with Ras signaling in increasing the transcriptional activity of c-Jun towards cyclin D1.
Wulf et al. EMBO J. (2001)

See also

Other switches involving participants
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) - 55 more (view)
Transcription factor AP-1 (JUN) - 3 more (view)

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


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