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Group by :Switch type Motif class Protein Enzyme Pathway Group Index Colouring Info Filtered: UNIPROT:Q99814 (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.
EPAS1_HUMAN	DEG_ODPH_VHL_1	403	416	Hydroxylation of P405 in the VHL-binding motif of Endothelial PAS domain-containing protein 1 (EPAS1) induces binding to the Von Hippel-Lindau disease tumor suppressor (VHL) protein.	details
EPAS1_HUMAN	DEG_ODPH_VHL_1	529	542	Hydroxylation of P531 in the VHL-binding motif of Endothelial PAS domain-containing protein 1 (EPAS1) induces binding to the Von Hippel-Lindau disease tumor suppressor (VHL) protein.	details

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