Literature summary for 3.6.5.2 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.

Search for more literature for 3.6.5.2

Activating Compound

Activating Compound	Comment	Organism	Structure
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

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

Organism

Organism	UniProt	Comment	Textmining
Cricetulus griseus	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
CHO cell	-	Cricetulus griseus	-

Synonyms

Synonyms	Comment	Organism
Rap1	-	Cricetulus griseus

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)