Relation Results

Summary

Name KCNA4
Full Name Potassium voltage-gated channel subfamily A member 4
Synonyms HPCN2, Voltage-gated K(+, Voltage-gated potassium channel HBK4, Voltage-gated potassium channel HK1, Voltage-gated potassium channel subunit Kv1.4 | KCNA4L
Primary ID P22459
Links - -
Type protein
Relations 3
Function Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. Forms tetrameric potassium-selective channels ...
View More

Viewer

Type: Score: Layout: SPV 
0.20.283PKAKCNA4LNX1

Search Tools

Refine search:

  • by mechanism


  • by effect
  • by organism:


  • by tissue:


  • by cell-line

▶Modifications Tables

Relations
Regulator
Mechanism
target
score ℹ
+ PKAdown-regulates quantity by destabilization img/direct_inhibition.png phosphorylation KCNA4 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-276037 Thr601 LKKFRSStSSSLGDK Homo sapiens HEK-293 Cell
pmid sentence
In parallel experiments, it was shown that recombinant PKA catalytic subunits (Fig. 3A) or cell extracts from GIP-stimulated GIPR-HEK293-KV cells (Fig. 3B) increased phosphorylation of KV1.4, and active PKA phosphorylated Thr-601 in the C terminus of KV1.4 (Fig. 3D). These results therefore provide compelling evidence for a role for GIP-induced down-regulation of KV1.4, via phosphorylation-dependent endocytosis of the channel protein, in the modulation of insulin secretion.
Publications: 1 Organism: Homo Sapiens
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation KCNA4 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-273778 Thr601 LKKFRSStSSSLGDK Homo sapiens HEK-293 Cell
pmid sentence
 In GIP receptor-expressing HEK293 cells, GIP reduced A-type peak ionic current amplitude of K(V)1.4 via activation of protein kinase A (PKA). Using mutant forms of K(V)1.4 with Ala-Ser/Thr substitutions in a potential PKA phosphorylation site, C-terminal phosphorylation was shown to be linked to GIP-mediated current amplitude decreases.
Publications: 1 Organism: Homo Sapiens
+ LNX1down-regulates quantity by destabilization img/direct_inhibition.png ubiquitination KCNA4 0.283
Identifier Residue Sequence Organism Cell Line
SIGNOR-272899 in vitro
pmid sentence
We used the Ligand of Numb protein X (LNX) family of E3s, a group of PDZ domain-containing RING-type E3 ubiquitin ligases, to demonstrate the feasibility of this strategy. Many potential substrates of LNX E3s were identified. Eight of the nine selected candidates were ubiquitinated in vitro, and two novel endogenous substrates, PDZ-binding kinase (PBK) and breakpoint cluster region protein (BCR), were confirmed in vivo.The C-terminal LNX1 PDZ1-binding motifs of the ATP-binding cassette, subfamily A member 1 (ABC-1), PBK, glutamate receptor, ionotropic, N-methyl d-aspartate 1 (GRIN1), and Claudin-17 significantly promoted the ubiquitination of the corresponding artificial degrons by LNX1ΔPDZ234.
Publications: 1 Organism: In Vitro
a simple tooltip