Domain hiding |   Altered binding specificity |   Motif hiding |   Composite binding site formation |
  Uncategorised |   Rheostatic |   Allostery |   Avidity-sensing |
  Physicochemical compatibility |   Pre-translational |   Competition |
Protein | Start | End | Switch Type | Switch Subtype | Switch Description | Information |
DOC_WW_Pin1_4 - The Class IV WW domain interaction motif is recognised primarily by the Pin1 phosphorylation-dependent prolyl isomerase. | |||||||
NR4A1_HUMAN | 137 | 142 | Binary | Physicochemical compatibility | Phosphorylation of S140 in the Pin1-binding motif of Nuclear receptor subfamily 4 group A member 1 (NR4A1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein. | ||
NR4A1_HUMAN | 428 | 433 | Binary | Physicochemical compatibility | Phosphorylation of S431 in the Pin1-binding motif of Nuclear receptor subfamily 4 group A member 1 (NR4A1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein. | ||
NR4A1_HUMAN | 92 | 97 | Binary | Physicochemical compatibility | Phosphorylation of S95 in the Pin1-binding motif of Nuclear receptor subfamily 4 group A member 1 (NR4A1) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein. |