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Physicochemical compatibility

Phosphorylation of Y170 in the WW-binding motif of Transcription factor AP-1 (Jun) by Tyrosine-protein kinase ABL1 (Abl1) blocks binding to the E3 ubiquitin-protein ligase Itchy (Itch). As a result, Transcription factor AP-1 (Jun) is not ubiquitylated by E3 ubiquitin-protein ligase Itchy (Itch), and thus not targeted for proteasomal degradation. Regulation of transcriptional activity of Transcription factor AP-1 (Jun) by Tyrosine-protein kinase ABL1 (Abl1) required translocation of the kinase to the nucleus, which was triggered by T cell activation.

(1) Transcription factor AP-1 (Jun)
(2) E3 ubiquitin-protein ligase Itchy (Itch)

Interaction #1 Jun - Itch

(1) LIG_WW_1 motif (167PPVY170) in Transcription factor AP-1 (Jun)
(2) WW domain (289-318) and (321-350) and (401-430) and (441-470) in E3 ubiquitin-protein ligase Itchy (Itch)

Interaction Regulation
PTM-dependent Abrogation (Phosphorylation of Y170 on Transcription factor AP-1 (Jun)) of the Transcription factor AP-1 (Jun) LIG_WW_1 motif - E3 ubiquitin-protein ligase Itchy (Itch) WW domain interaction

Regulatory Enzymes for switch
Modifying enzymes for residue: Y170: Tyrosine-protein kinase ABL1 (Abl1)


(1) The tyrosine kinase c-Abl protects c-Jun from ubiquitination-mediated degradation in T cells.
Gao et al. J. Biol. Chem. (2006)

See also

Other switches involving participants
E3 ubiquitin-protein ligase Itchy (Itch) - 3 more (view)

Other switches involving interfaces
WW domain - 105 more (view)
LIG_WW_1 - 17 more (view)

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