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Group by :Switch type Motif class Protein Enzyme Pathway Group Index Colouring Info Filtered: UNIPROT:Q9HC98 (2 hits) x

x Coloured by switch type.

Domain hiding	Altered binding specificity	Motif hiding	Composite binding site formation
Uncategorised	Rheostatic	Allostery	Avidity-sensing
Physicochemical compatibility	Pre-translational	Competition

x Index

Type: Binary Subtype: Physicochemical compatibility

Protein

Motif

Start

End

Switch description

Information

*Type:* Binary *Subtype:* Physicochemical compatibility
PTM of a residue in a motif or in its flanking regions alters the physicochemical and/or structural compatibility of the motif with its binding partner. This can either induce or enhance an interaction, or result in inhibition or even abrogation of an interaction.
NEK6_HUMAN	DOC_WW_Pin1_4	212	217	Phosphorylation 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.	details
NEK6_HUMAN	DOC_WW_Pin1_4	242	247	Phosphorylation 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.	details

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