+ |
ANK3 | up-regulates activity
binding
|
GABARAP |
0.454 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266709 |
|
|
Mus musculus |
Pyramidal Neuron |
pmid |
sentence |
30504823 |
Importantly, the 480 kDa ankyrin-G isoform has also been shown to stabilize GABAergic synapses on the soma and AIS of excitatory pyramidal neurons by interacting with the GABAA receptor-associated protein (GABARAP) to inhibit GABAA receptor endocytosis |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
ANK3 | up-regulates quantity
relocalization
|
DAG1 |
0.262 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266714 |
|
|
Mus musculus |
|
pmid |
sentence |
19109891 |
We present evidence for an ankyrin-based mechanism for sarcolemmal localization of dystrophin and beta-DG. Ankyrin-B thus is an adaptor required for sarcolemmal localization of dystrophin, as well as dynactin-4. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
Tissue: |
Skeletal Muscle |
+ |
CHL1 | up-regulates quantity
relocalization
|
ANK3 |
0.422 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266723 |
|
|
Rattus norvegicus |
|
pmid |
sentence |
7961622 |
Neurofascin, L1, NrCAM, NgCAM, and neuroglian are membrane-spanning cell adhesion molecules with conserved cytoplasmic domains that are believed to play important roles in development of the nervous system. This report presents biochemical evidence that the cytoplasmic domains of these molecules associate directly with ankyrins, a family of spectrin-binding proteins located on the cytoplasmic surface of specialized plasma membrane domains. |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |
Tissue: |
Central Nervous System |
+ |
ANK3 | up-regulates activity
binding
|
SPTBN1 |
0.63 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266711 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
17620337 |
Ankyrin-G is a molecular partner of E-cadherin in epithelial cells and early embryos. Ankyrin-G also recruits beta-2-spectrin to E-cadherin-beta-catenin complexes, thus providing a direct connection between E-cadherin and the spectrin/actin skeleton. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ANK3 | up-regulates activity
binding
|
CDH1 |
0.33 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266710 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
17620337 |
Ankyrin-G is a molecular partner of E-cadherin in epithelial cells and early embryos. Ankyrin-G also recruits beta-2-spectrin to E-cadherin-beta-catenin complexes, thus providing a direct connection between E-cadherin and the spectrin/actin skeleton. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ANK3 | up-regulates quantity
relocalization
|
DMD |
0.375 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266715 |
|
|
Mus musculus |
|
pmid |
sentence |
19109891 |
We present evidence for an ankyrin-based mechanism for sarcolemmal localization of dystrophin and beta-DG. Ankyrin-B thus is an adaptor required for sarcolemmal localization of dystrophin, as well as dynactin-4. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
Tissue: |
Skeletal Muscle |
+ |
GLDN | up-regulates quantity
relocalization
|
ANK3 |
0.421 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266725 |
|
|
Homo sapiens |
|
pmid |
sentence |
19840192 |
Ankyrin-G is recruited to the nodes of Ranvier by gliomedin, which is produced by Schwann cells and accumulates in the perinodal extracellular matrix. As a ligand for neurofascin-186, gliomedin causes the nodal clustering of this cell adhesion molecule, which in turn recruits to the nodal plasma membrane an ankyrin-G protein network consisting of voltage-gated sodium or potassium channels (KCNQ2/3) and β4-spectrin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Central Nervous System |
+ |
NRCAM | up-regulates quantity
relocalization
|
ANK3 |
0.711 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266720 |
|
|
Rattus norvegicus |
|
pmid |
sentence |
7961622 |
Neurofascin, L1, NrCAM, NgCAM, and neuroglian are membrane-spanning cell adhesion molecules with conserved cytoplasmic domains that are believed to play important roles in development of the nervous system. This report presents biochemical evidence that the cytoplasmic domains of these molecules associate directly with ankyrins, a family of spectrin-binding proteins located on the cytoplasmic surface of specialized plasma membrane domains. |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |
Tissue: |
Central Nervous System |
+ |
ELAVL3 | down-regulates quantity
post transcriptional regulation
|
ANK3 |
0.253 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266861 |
|
|
Homo sapiens |
Neuron |
pmid |
sentence |
29614249 |
NElavl (composed of Elavl2, Elavl3, and Elavl4) proteins are the RNA-binding proteins that is specifically expressed in neurons, regulate the alternative splicing of target RNAs, and promote neuronal differentiation and maturation. Here, we found that the alternative splicing of AnkyrinG exon 34 was misregulated in the cerebella of Elavl3-/- mice. AnkyrinG is an essential factor for the formation of neuronal polarity and is required for normal neuronal functions. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NFASC | up-regulates quantity
relocalization
|
ANK3 |
0.736 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266717 |
|
|
Rattus norvegicus |
|
pmid |
sentence |
7961622 |
Neurofascin, L1, NrCAM, NgCAM, and neuroglian are membrane-spanning cell adhesion molecules with conserved cytoplasmic domains that are believed to play important roles in development of the nervous system. This report presents biochemical evidence that the cytoplasmic domains of these molecules associate directly with ankyrins, a family of spectrin-binding proteins located on the cytoplasmic surface of specialized plasma membrane domains. |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |
Tissue: |
Central Nervous System |