+ |
MAPK1 | up-regulates activity
phosphorylation
|
KCND2 |
0.376 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262934 |
Ser616 |
EGDDRPEsPEYSGGN |
Rattus norvegicus |
Hippocampus |
pmid |
sentence |
11080179 |
We determined that the Kv4.2 C-terminal cytoplasmic domain is an effective ERK2 substrate, and that it is phosphorylated at three sites: Thr(602), Thr(607), and Ser(616). Phosphorylation of the Kv4.2 channel by ERK during LTP induction may lead to increased excitability and membrane depolarization of neurons, which would increase the magnitude of the calcium influx and the probability of triggering LTP. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262935 |
Thr602 |
TAIISIPtPPVTTPE |
Rattus norvegicus |
Hippocampus |
pmid |
sentence |
11080179 |
We determined that the Kv4.2 C-terminal cytoplasmic domain is an effective ERK2 substrate, and that it is phosphorylated at three sites: Thr(602), Thr(607), and Ser(616). Phosphorylation of the Kv4.2 channel by ERK during LTP induction may lead to increased excitability and membrane depolarization of neurons, which would increase the magnitude of the calcium influx and the probability of triggering LTP. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262936 |
Thr607 |
IPTPPVTtPEGDDRP |
Rattus norvegicus |
Hippocampus |
pmid |
sentence |
11080179 |
We determined that the Kv4.2 C-terminal cytoplasmic domain is an effective ERK2 substrate, and that it is phosphorylated at three sites: Thr(602), Thr(607), and Ser(616). Phosphorylation of the Kv4.2 channel by ERK during LTP induction may lead to increased excitability and membrane depolarization of neurons, which would increase the magnitude of the calcium influx and the probability of triggering LTP. |
|
Publications: |
3 |
Organism: |
Rattus Norvegicus |
+ |
DPP10 | up-regulates activity
relocalization
|
KCND2 |
0.55 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269006 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
15454437 |
Coexpression of DPP10 changes the subcellular localization of Kv4.2 expressed in COS-7 cells by promoting surface trafficking.DPP10 accelerates Kv4.2 inactivation at high and low voltages |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
DPP6 | up-regulates activity
relocalization
|
KCND2 |
0.565 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269005 |
|
|
Xenopus laevis |
Oocyte |
pmid |
sentence |
17130523 |
DPPX-S reduced energy barriers of the voltage-dependent transitions; therefore, this auxiliary subunit may exert a catalytic effect on voltage-dependent gating of Kv4.2 channels. DPPX-S may also accelerate coupled inactivation indirectly |
|
Publications: |
1 |
Organism: |
Xenopus Laevis |
+ |
KCNIP4 | up-regulates activity
relocalization
|
KCND2 |
0.765 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269004 |
|
|
Xenopus laevis |
Oocyte |
pmid |
sentence |
24811166 |
KChIP4 increased the current amplitude of Kv4.2, decelerated the inactivation, and accelerated the recovery from inactivation of Kv4.2. KChIP.is known to promote the translocation of Kv4.2 from the endoplasmic reticulum or Golgi to the cell surface |
|
Publications: |
1 |
Organism: |
Xenopus Laevis |
+ |
IRX5 | down-regulates quantity by repression
transcriptional regulation
|
KCND2 |
0.503 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266045 |
|
|
Mus musculus |
Endocardium |
pmid |
sentence |
16239150 |
Irx5 Directly Represses the Kcnd2 Promoter |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
FLNA | up-regulates activity
binding
|
KCND2 |
0.36 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269003 |
|
|
Rattus norvegicus |
|
pmid |
sentence |
11102480 |
Filamin may function as a scaffold protein in the postsynaptic density, mediating a direct link between Kv4.2 and the actin cytoskeleton, and that this interaction is essential for the generation of appropriate Kv4.2 current densities. |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |
Tissue: |
Cerebellum |