Literature summary for 3.1.3.16 extracted from

Martinez-Martinez, S.; Genesca, L.; Rodriguez, A.; Raya, A.; Salichs, E.; Were, F.; Lopez-Maderuelo, M.D.; Redondo, J.M.; de la Luna, S.
The RCAN carboxyl end mediates calcineurin docking-dependent inhibition via a site that dictates binding to substrates and regulators (2009), Proc. Natl. Acad. Sci. USA, 106, 6117-6122.

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Protein Variants

Protein Variants	Comment	Organism
additional information	mutation of key residues within the hydrophobic docking-cleft of the calcineurin catalytic domain impairs binding to all human RCAN proteins and to the calcineurin interacting proteins Cabin1 and AKAP79, overview	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
RCAN proteins	RCAN inhibition of CN phosphatase activity is mediated by the extreme C-terminal region	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	dependent on	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Homo sapiens	physical and functional interaction of the phosphatase calcineurin with a group of modulators, the RCAN protein family, e.g. proteins Cabin1 and AKAP79, a valine-rich region within the RCAN carboxyl region is essential for binding to the docking site in calcineurin, overview. Competition by substrates and modulators for a common docking site appears to be an essential mechanism in the regulation of Ca2+-calcineurin signaling	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	physical and functional interaction of the phosphatase calcineurin with a group of modulators, the RCAN protein family, e.g. proteins Cabin1 and AKAP79, a valine-rich region within the RCAN carboxyl region is essential for binding to the docking site in calcineurin, overview. Competition by substrates and modulators for a common docking site appears to be an essential mechanism in the regulation of Ca2+-calcineurin signaling	Homo sapiens	?	-	?

Subunits

Subunits	Comment	Organism
More	the CnA hydrophobic cleft, containing the NIR site, defines a common docking site for CN regulators, motifs involved in calcineurin inetractions with RCAN proteins, overview. The CnA beta-strand 14 is required for binding to the RCAN EV-motif. The EV-motif blocks CN/NFAT signaling but does not inhibit calcineurin phosphatase activity	Homo sapiens

Synonyms

Synonyms	Comment	Organism
calcineurin	-	Homo sapiens
CN phosphatase	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	Ca2+-calcineurin signaling	Homo sapiens

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Release 2023.1 (January 2023)