2BYV

Structure of the cAMP responsive exchange factor Epac2 in its auto- inhibited state

Functional Information from GO Data

Chain	GOid	namespace	contents
E	0000166	molecular_function	nucleotide binding
E	0005085	molecular_function	guanyl-nucleotide exchange factor activity
E	0005515	molecular_function	protein binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0005886	cellular_component	plasma membrane
E	0006887	biological_process	exocytosis
E	0007186	biological_process	G protein-coupled receptor signaling pathway
E	0007188	biological_process	adenylate cyclase-modulating G protein-coupled receptor signaling pathway
E	0007189	biological_process	adenylate cyclase-activating G protein-coupled receptor signaling pathway
E	0007264	biological_process	small GTPase-mediated signal transduction
E	0007265	biological_process	Ras protein signal transduction
E	0016020	cellular_component	membrane
E	0017156	biological_process	calcium-ion regulated exocytosis
E	0017157	biological_process	regulation of exocytosis
E	0030073	biological_process	insulin secretion
E	0030552	molecular_function	cAMP binding
E	0030674	molecular_function	protein-macromolecule adaptor activity
E	0031267	molecular_function	small GTPase binding
E	0032024	biological_process	positive regulation of insulin secretion
E	0035556	biological_process	intracellular signal transduction
E	0046879	biological_process	hormone secretion
E	0050714	biological_process	positive regulation of protein secretion
E	0050796	biological_process	regulation of insulin secretion
E	0098686	cellular_component	hippocampal mossy fiber to CA3 synapse
E	0098693	biological_process	regulation of synaptic vesicle cycle

Functional Information from PROSITE/UniProt

site_id	PS00720
Number of Residues	30
Details	RASGEF Ras Guanine-nucleotide exchange factors domain signature. IPFmPllIkDMtfthegnktfidnl.....................VNFeK

Chain	Residue	Details
E	ILE903-LYS932

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250|UniProtKB:O95398

Chain	Residue	Details
E	GLU422
E	LYS432

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