TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
*8.A.10.1.1









Slow voltage-dependent K+ channel auxiliary protein (β-subunit), MinK or K2NE1. KCNQ1-KCNE1 complexes may interact intermittently with the actin cytoskeleton via the C-terminal region (Mashanov et al., 2010; Coey et al., 2011).  The transmembrane region and the C-terminal cytoplasmic domains that abuts the KCNE1 TMS both interact with and regulate the KCNQ1 channel (Lvov et al. 2010; Zheng et al. 2010). Mutations in KCNE1 can cause Meniere's disease (Zheng et al. 2010). Mutations in KCNE1 can cause Meniere's disease (Doi et al. 2005).

Eukaryota
Metazoa
MinK of Rattus norvegicus (130 aas; P15383)
*8.A.10.1.2









Potassium voltage-gated channel Isk-related family member 1, of 129 aas and one TMS, KCNE1 (Sahu et al. 2015).  Mutations can give rise to hearing disorders including chronic tinitus (Sand et al. 2010).  KCNE proteins modulate both homomeric Kv.2.1 and heteromeric Kv2.1/Kv6.4 channels (David et al. 2015). Slow-activating channel complexes formed by KCNQ1 and KCNE1 are essential for human ventricular myocyte repolarization, while constitutively active KCNQ1-KCNE3 channels are important in the intestine. Inherited sequence variants in human KCNE1 and KCNE3 cause cardiac arrhythmias by different mechanisms (Abbott 2015). KCNE confers pH sensitivity to KCNQ1 (Heitzmann et al. 2007). State-dependent interactions between KCNE1 and KCNQ1 have been demonstrated (Westhoff et al. 2017).

Eukaryota
Metazoa
KCNE1 of Homo sapiens
*8.A.10.2.1









K+ voltage-gated channel subfamily E member 2 (KCNE2) or minimum K+ channel-related peptide (MinK; MiRP1) (β-subunit) [associates with KCNH2/ERG1 and KCNQ1/KVLQT1 (McCrossan et al. 2009), as well as KCNQ2 and KCNQ3] (Eldstrom and Fedida, 2011Roepke et al., 2006). Regulated by PKCδ phosphorylation (O'Mahony et al., 2007).  A mutation (hERG T473P) in the transmembrane non-pore region  causes clinical manifestations of long QT syndrome (Liu et al. 2012).  Exhibits an array of functions in the heart, stomach, thyroid and choroid plexus. A variety of interconnected disease manifestations caused by KCNE2 disruption involve both excitable cells such as cardiomyocytes, and non-excitable, polarized epithelia (Abbott 2015).  It's secondary structure has been determined (Abbott et al. 2008). Deletion of the Kcne2 structural gene in mice and humans gives rise to impaired insulin secretion as well as type 2 diabetes mellitus (Lee et al. 2017).

Eukaryota
Metazoa
KCNE2 of Mus musculus (123 aas; Q9D808)
*8.A.10.3.1









KCNE3 (β-subunit) constitutively opens outwardly rectifying KCNQ1 (Kv7.1) K+ channels by abolishing their voltage-dependent gating. KCNQ1/KCNE3 heteromers are present in basolateral membranes of intestinal and tracheal epithelial cells where they may facilitate transepithelial Cl- secretion (Preston et al., 2010).  Mutations cause Meniere's disease and tinnitus.  KCNE3 regulates Kv4.2 in spiral gangion neurons (Wang et al. 2014) and other voltage-gated ion channels (Kroncke et al. 2016). KCNE3 induces the constitutive activation of KCNQ1 in a process involving interactions in both sides of the membrane (Kroncke et al. 2016).

Eukaryota
Metazoa
KCNE3 of Mus musculus (103 aas; AAH04629)
*8.A.10.3.2









Potassium voltage-gated channel subfamily E regulatory subunit 5, KCNE5 of 142 aas and 1 TMS. It is a potassium channel ancillary subunit of that is essential for the generation of some native K+ currents by virtue of the formation of heteromeric ion channel complexes with voltage-gated potassium (Kv) channel pore-forming alpha subunits. It functions as an inhibitory beta-subunit of the repolarizing cardiac potassium ion channel KCNQ1 (Angelo et al. 2002).

Eukaryota
Metazoa
KCNE5 of Homo sapiens
*8.A.10.4.1









MinK-related peptide 3 (MiRK3) or KCNE4 (β-subunit)
Eukaryota
Metazoa
MiRP3 or KCNE4 of Mus musculus (170 aas; Q9WTW3)