Literature summary extracted from

Dai, Y.; Walker, S.A.; de Vet, E.; Cook, S.; Welch, H.C.; Lockyer, P.J.
Ca2+-dependent monomer and dimer formation switches CAPRI Protein between Ras GTPase-activating protein (GAP) and RapGAP activities (2011), J. Biol. Chem., 286, 19905-19916.

Activating Compound

EC Number	Activating Compound	Comment	Organism	Structure
3.6.5.2	CAPRI	a member of the GAP1 family of GTPase-activating proteins, GAPs, for small G proteins functioning as an amplitude sensor for intracellular Ca2+ levels stimulated by extracellular signals. It has a catalytic domain with dual Ras-GAP and RapGAP activities, and acts as dimer and monomer. CAPRI switches between its two GAP activities, RasGAP and Rap1GAP, mechanism, overview. Structure and activity of the C-terminal tail of Mus musclus CAPRI, activities on endogenous Rap1 in vivo of the recombinant full-length and C-terminal part of murine CAPRI in CHO cells, overview. Wild-type and monomeric CAPRI translocate to the plasma membrane similarly, but monomers are stronger RasGAPs at the membrane level	Cricetulus griseus

Localization

EC Number	Localization	Comment	Organism	GeneOntology No.	Textmining
3.6.5.2	plasma membrane	-	Cricetulus griseus	5886	-

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.6.5.2	Cricetulus griseus	-	-	-

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
3.6.5.2	CHO cell	-	Cricetulus griseus	-

Synonyms

EC Number	Synonyms	Comment	Organism
3.6.5.2	Rap1	-	Cricetulus griseus

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Release 2023.1 (January 2023)