| + |
ANK1 | form complex 
binding
|
Ankyrin complex |
0.365 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266013 |
|
|
Homo sapiens |
Erythrocyte |
| pmid |
sentence |
| 22465511 |
The ankyrin associated complex brings together proteins of both the band 3 tetrameric complex (band 3, glycophorin A (GPA), protein 4.2, carbonic anhydrase II) and the Rh complex (RhAG, RhCE, RhD, CD47, ICAM-4, glycophorin B (GPB)) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CHL1 | up-regulates quantity 
relocalization
|
ANK1 |
0.532 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266724 |
|
|
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 |
| + |
ANK1 | down-regulates activity 
binding
|
ATP2A1 |
0.294 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265927 |
|
|
Oryctolagus cuniculus |
|
| pmid |
sentence |
| 28487373 |
We recently reported that small ankyrin 1 (sAnk1) interacts with the sarco(endo)plasmic reticulum Ca2+-ATPase in skeletal muscle (SERCA1) to inhibit its activity. |
|
| Publications: |
1 |
Organism: |
Oryctolagus Cuniculus |
| + |
NFASC | up-regulates quantity
relocalization
|
ANK1 |
0.684 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266718 |
|
|
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 |
| + |
ANK1 | down-regulates activity
binding
|
SLN |
0.256 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265930 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28487373 |
These results suggest that sAnk1 interacts with SLN both directly and in complex with SERCA1 and reduces SLN's inhibitory effect on SERCA1 activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NRCAM | up-regulates quantity
relocalization
|
ANK1 |
0.543 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266721 |
|
|
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 |
3.0
ANK1
- 
- 