Search results for KCNIP1

Showing 4 results out of 4

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Species

Types

Compartments

Search properties

Protein (1 results from a total of 1)

Identifier: R-HSA-5577236
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: KCNIP1: Q9NZI2

Set (1 results from a total of 1)

Identifier: R-HSA-5577094
Species: Homo sapiens
Compartment: plasma membrane

Interactor (1 results from a total of 1)

Identifier: Q9NZI2-2
Species: Homo sapiens
Primary external reference: UniProt: Q9NZI2-2

Reaction (1 results from a total of 1)

Identifier: R-HSA-5577234
Species: Homo sapiens
Compartment: plasma membrane, cytosol, extracellular region
In phase 1 of the action potential, the fast Na+ channels are inactivated. This happens by net outward currents Ito1 and Ito2 caused by efflux of K+ and Cl- ions respectively. Potassium voltage-gated channel subfamily D members 1, 2 and 3 (KCND1, 2 and 3) are pore-forming (alpha) subunits of voltage-gated, rapidly inactivating A-type K+ channels (Isbrandt et al. 2000) that produce the Ito1 current. They may also contribute to the ISa current in neurons. KCND1 is functional as either a homo- or hetero-tetramer with KCND2 and/or KCND3. KCNDs associate with the regulatory subunits KCNIP1-4 (Scannevin et al. 2004, Pioletti et al. 2006). KCNIPs form homodimers and/or homotetramers (Lin et al. 2004). KCNIPs and KCNDs together modulate the density, inactivation kinetics and rate of recovery from inactivation of KCNDs (An et al. 2000, Nakamura et al. 2001, Shibata et al. 2003, Wang et al. 2007).
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