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Group by :Switch typeMotif classProteinEnzymePathway            Group Index    Colouring Info              Filtered: UNIPROT:Q9HC98 (2 hits) x
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  Domain hiding  Altered binding specificity  Motif hiding  Composite binding site formation
  Uncategorised  Rheostatic  Allostery  Avidity-sensing
  Physicochemical compatibility  Pre-translational  Competition

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DOC_WW_Pin1_4


ProteinStartEndSwitch TypeSwitch SubtypeSwitch DescriptionInformation

DOC_WW_Pin1_4 - The Class IV WW domain interaction motif is recognised primarily by the Pin1 phosphorylation-dependent prolyl isomerase.
NEK6_HUMAN212217BinaryPhysicochemical compatibilityPhosphorylation of S215 in the Pin1-binding motif of Serine/threonine-protein kinase Nek6 (NEK6) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
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NEK6_HUMAN242247BinaryPhysicochemical compatibilityPhosphorylation of S245 in the Pin1-binding motif of Serine/threonine-protein kinase Nek6 (NEK6) induces binding to the Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) protein.
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