| + |
OBSCN | up-regulates quantity 
relocalization
|
ANK2 |
0.512 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266726 |
|
|
Homo sapiens |
Cardiomyocyte Cell Line |
| pmid |
sentence |
| 19840192 |
Ankyrin-B is targeted to the M-line via its interaction with the C-terminal domain of the large sarcomeric protein obscurin. Obscurin is targeted to the M-line via its N-terminal interactions with myomesin and titin. This population of ankyrin-B recruits B56α, a regulatory subunit of protein phosphatase 2A, to the M-line where the phosphatase may regulate the phosphorylation status of contractile and signalling proteins. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NFASC | up-regulates quantity
relocalization
|
ANK2 |
0.682 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266716 |
|
|
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 |
| + |
ANK2 | up-regulates quantity
relocalization
|
DMD |
0.546 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266712 |
|
|
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 |
| + |
ANK2 | up-regulates quantity
binding
|
CACNA1B |
0.266 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266707 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 24394417 |
Here, we demonstrate that ankyrin-B associates with Cav2.1 and Cav2.2 in cortex, cerebellum, and brain stem. Additionally, using in vitro and in vivo techniques, we demonstrate that ankyrin-B, via its membrane-binding domain, associates with a highly conserved motif in the DII/III loop domain of Cav2.1 and Cav2.2. Collectively, our findings identify an interaction between ankyrin-B and both Cav2.1 and Cav2.2 at the amino acid level that is necessary for proper Cav2.1 and Cav2.2 targeting in vivo. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Brain |
| + |
ANK2 | up-regulates quantity
binding
|
CACNA1A |
0.266 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266706 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 24394417 |
Here, we demonstrate that ankyrin-B associates with Cav2.1 and Cav2.2 in cortex, cerebellum, and brain stem. Additionally, using in vitro and in vivo techniques, we demonstrate that ankyrin-B, via its membrane-binding domain, associates with a highly conserved motif in the DII/III loop domain of Cav2.1 and Cav2.2. Collectively, our findings identify an interaction between ankyrin-B and both Cav2.1 and Cav2.2 at the amino acid level that is necessary for proper Cav2.1 and Cav2.2 targeting in vivo. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
CHL1 | up-regulates quantity
relocalization
|
ANK2 |
0.418 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266722 |
|
|
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 |
| + |
NRCAM | up-regulates quantity
relocalization
|
ANK2 |
0.726 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266719 |
|
|
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 |
| + |
ANK2 | up-regulates quantity
relocalization
|
DCTN4 |
0.609 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266713 |
|
|
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 |
| + |
ANK2 | up-regulates quantity
relocalization
|
PPP2R5A |
0.287 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266729 |
|
|
Homo sapiens |
Cardiomyocyte Cell Line |
| pmid |
sentence |
| 19840192 |
Ankyrin-B is targeted to the M-line via its interaction with the C-terminal domain of the large sarcomeric protein obscurin. Obscurin is targeted to the M-line via its N-terminal interactions with myomesin and titin. This population of ankyrin-B recruits B56α, a regulatory subunit of protein phosphatase 2A, to the M-line where the phosphatase may regulate the phosphorylation status of contractile and signalling proteins. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
ANK2
- 
- 