| + |
PTPN1 | down-regulates activity 
dephosphorylation
|
ACTN1 |
0.34 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270539 |
Tyr12 |
DSQQTNDyMQPEEDW |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 16291744 |
Here we report that protein-tyrosine phosphatase 1B (PTP 1B) is an alpha-actinin phosphatase. PTP 1B-dependent dephosphorylation of alpha-actinin was seen in COS-7 cells|No dephosphorylation was observed in cells coexpressing the alpha-actinin phosphorylation mutant Y12F and PTP 1B. |A reversible interaction between alpha-actinin and Src enables the dephosphorylation of alpha-actinin by PTP 1B, releasing Src |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
PTK2 | down-regulates activity
phosphorylation
|
ACTN1 |
0.555 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-108329 |
Tyr12 |
DSQQTNDyMQPEEDW |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 11369769 |
The cytoskeletal/non-muscle isoform of alpha-actinin is phosphorylated on its actin-binding domain by the focal adhesion kinase tyrosine 12 is the site of phosphorylation. The wild type recombinant protein was not phosphorylated in cells lacking the focal adhesion kinase (fak).Tyrosine phosphorylation reduced the amount of alpha-actinin that cosedimented with actin filaments. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| Pathways: | Axon guidance |
| + |
PTPN1 | up-regulates 
dephosphorylation
|
ACTN1 |
0.34 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-141634 |
Tyr12 |
DSQQTNDyMQPEEDW |
Homo sapiens |
|
| pmid |
sentence |
| 16291744 |
Here we report that protein-tyrosine phosphatase 1b (ptp 1b) is an ?-Actinin phosphatase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTK2 | down-regulates
phosphorylation
|
ACTN1 |
0.555 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-192126 |
Tyr12 |
DSQQTNDyMQPEEDW |
Homo sapiens |
|
| pmid |
sentence |
| 23454549 |
Phosphorylation at y12 by fak reduces _-actinin1's affinity for actin . |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Axon guidance |
| + |
ACTN1 | up-regulates quantity by stabilization
binding
|
F-actin_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261852 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27871158 |
Actin exists in polymer where filamin and α-actinin act as cross-linkers with approximately 1:10 ratios |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Axon guidance |
| + |
ACTN1 | down-regulates activity
binding
|
PTK2 |
0.555 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261799 |
|
|
Chlorocebus aethiops |
|
| pmid |
sentence |
| 16291744 |
Consistent with the results obtained with COS-7 cells, coexpression of wild-type α-actinin with PTP 1B in PTP 1B-null cells resulted in Src/α-actinin binding and limited the interaction between FAK and Src |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| Pathways: | Axon guidance |
| + |
SHANK1 | up-regulates activity
relocalization
|
ACTN1 |
0.277 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264583 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 28179641 |
SHANK proteins are ‘master’ scaffolding proteins that tether and organize intermediate scaffolding proteins. They are located at excitatory synapses, where they are crucial for proper synaptic development and function. SAPAP proteins subsequently bind to the PDZ domain of members of the SHANK protein family. SHANK proteins then bind to the actin cytoskeleton and to Homer protein, which in turn interacts with mGluRs. Through these extended links, PSD95, SAPAP, SHANK and Homer proteins form a quaternary complex that brings together mGluR and NMDAR complexes in the PSD (FIG. 3). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glutamatergic synapse |
| + |
SHANK3 | up-regulates activity
relocalization
|
ACTN1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264585 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 28179641 |
SHANK proteins are ‘master’ scaffolding proteins that tether and organize intermediate scaffolding proteins. They are located at excitatory synapses, where they are crucial for proper synaptic development and function. SAPAP proteins subsequently bind to the PDZ domain of members of the SHANK protein family. SHANK proteins then bind to the actin cytoskeleton and to Homer protein, which in turn interacts with mGluRs. Through these extended links, PSD95, SAPAP, SHANK and Homer proteins form a quaternary complex that brings together mGluR and NMDAR complexes in the PSD (FIG. 3). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glutamatergic synapse |
| + |
ACTN1 | up-regulates 
|
Actin_cytoskeleton_reorganization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264618 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17243894 |
On most principal neurons in the mammalian brain (e.g., pyramidal neurons of cortex and hippocampus, Purkinje cells of cerebellum, medium spiny neurons of striatum), the postsynaptic specialization is housed on tiny actin rich protrusions called dendritic spines The size, shape, motility, and stability of dendritic spines depend largely on actin, the primary cytoskeleton within spines. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Axon guidance, Glutamatergic synapse |
| + |
SHANK2 | up-regulates activity
relocalization
|
ACTN1 |
0.301 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264584 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 28179641 |
SHANK proteins are ‘master’ scaffolding proteins that tether and organize intermediate scaffolding proteins. They are located at excitatory synapses, where they are crucial for proper synaptic development and function. SAPAP proteins subsequently bind to the PDZ domain of members of the SHANK protein family. SHANK proteins then bind to the actin cytoskeleton and to Homer protein, which in turn interacts with mGluRs. Through these extended links, PSD95, SAPAP, SHANK and Homer proteins form a quaternary complex that brings together mGluR and NMDAR complexes in the PSD (FIG. 3). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
ACTN1
- 
- 