| + |
INSR | down-regulates 
phosphorylation
|
CALM3 |
0.383 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266336 |
Tyr100 |
FDKDGNGyISAAELR |
Homo sapiens |
|
| pmid |
sentence |
| 3415247 |
The in vitro phosphorylation of calmodulin by the insulin receptor tyrosine kinase. Phosphorylated calmodulin does not exhibit the characteristic ca2+ shift normally observed with calmodulin in electrophoretic gels, an observation that is consistent with this modification affecting the biological activity of the molecule. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EGFR | down-regulates
phosphorylation
|
CALM3 |
0.39 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266335 |
Tyr100 |
FDKDGNGyISAAELR |
Homo sapiens |
|
| pmid |
sentence |
| 3415247 |
Phosphorylation of calmodulin by the epidermal-growth-factor-receptor tyrosine kinase. Phosphorylated calmodulin does not exhibit the characteristic ca2+ shift normally observed with calmodulin in electrophoretic gels, an observation that is consistent with this modification affecting the biological activity of the molecule. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CALM3 | up-regulates activity 
binding
|
NOS3 |
0.581 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266339 |
|
|
Homo sapiens |
Vascular Endothelium |
| pmid |
sentence |
| 24379783 |
Electrons flow from the C-terminal reductase domain of one NOS monomer to the N-terminal oxygenase domain of the other NOS monomer (Siddhanta et al., 1998). The primary mode of enzyme activation is the binding of calcium-bound calmodulin to the N-terminal CaM-binding domain. This facilitates a structure change and the flow of electrons from NADPH through the flavins to the oxygenase domain of the other eNOS monomer |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CALM3 | up-regulates activity
binding
|
GEM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266342 |
|
|
Rattus norvegicus |
PC-12 Cell |
| pmid |
sentence |
| 14701738 |
Inhibition of voltage-gated calcium channels by Gem requires GTP and calmodulin binding, but not phosphorylation of serine 261 or 289. Calmodulin binding in the C-terminal extension of Gem is required for maximal inhibition of HVA Ca2+ channels by ectopically expressed Gem, as determined by measurement of electrical activity in primary neurons and by Ca2+-evoked secretion in PC12 cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266341 |
|
|
Rattus norvegicus |
PC-12 Cell |
| pmid |
sentence |
| 14701738 |
Inhibition of voltage-gated calcium channels by Gem requires GTP and calmodulin binding, but not phosphorylation of serine 261 or 289. Calmodulin binding in the C-terminal extension of Gem is required for maximal inhibition of HVA Ca2+ channels by ectopically expressed Gem, as determined by measurement of electrical activity in primary neurons and by Ca2+-evoked secretion in PC12 cells. |
|
| Publications: |
2 |
Organism: |
Rattus Norvegicus |
| + |
CALM3 | up-regulates
binding
|
PPP3CB |
0.593 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266338 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11796223 |
Calcium-bound calmodulin associates with calcineurin (cn), releasing the phosphatase from the repressive effects on an autoinhibitory domain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CALM3 | up-regulates
binding
|
PPP3CA |
0.644 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266343 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11796223 |
Calcium-bound calmodulin associates with calcineurin (cn), releasing the phosphatase from the repressive effects on an autoinhibitory domain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
calcium(2+) | up-regulates
chemical activation
|
CALM3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266334 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 10448861 |
Treatment with igf-1 or insulin and dexamethasone mobilizes intracellular calcium, activates the ca2+/calmodulin-dependent phosphatase calcineurin, and induces the nuclear translocation of the transcription factor nf-atc1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266333 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10884684 |
Calmodulin is the best studied and prototypical example of the e-f-hand family of ca2+-sensing proteins. In the event of a transient rise in Ca2+, the Ca2+ ion is coordinated in each Ca2+-binding loop of Ca2+–CaM by seven, primarily carboxylate, ligands. The binding of Ca2+ leads to substantial alterations in the interhelical angles within the E–F hands in each domain and dramatically changes the two domains of CaM to produce more ‘open’ conformations |
|
| Publications: |
2 |
Organism: |
Mus Musculus, Homo Sapiens |
| + |
CALM3 | up-regulates
binding
|
CAMKK1 |
0.626 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266344 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10770941 |
The binding of Ca2+/CaM to CaM-KK is absolutely required for its activation and efficient phosphorylation of target protein kinases |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CALM3 | down-regulates activity
binding
|
SCN8A |
0.46 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266346 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11807557 |
Here we show that calmodulin (CaM), a ubiquitous Ca2+-sensing protein, binds to the carboxy-terminal 'IQ' domain of the human cardiac Na channel (hH1) in a Ca2+-dependent manner. This binding interaction significantly enhances slow inactivation-a channel-gating process linked to life-threatening idiopathic ventricular arrhythmias. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CALM3 | up-regulates
binding
|
PPP3CC |
0.54 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266340 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11796223 |
Calcium-bound calmodulin associates with calcineurin (cn), releasing the phosphatase from the repressive effects on an autoinhibitory domain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CALM3 | up-regulates
binding
|
Calcineurin |
0.501 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266347 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11796223 |
Calcium-bound calmodulin associates with calcineurin (cn), releasing the phosphatase from the repressive effects on an autoinhibitory domain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CALM3 | up-regulates
binding
|
CAMKK2 |
0.606 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266345 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9822657 |
The ca2+-calmodulin-dependent protein kinase (cam kinase) cascade includes three kinases: cam-kinase kinase (camkk);and the cam kinases camki and camkiv, which are phosphorylated and activated by camkk. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CALM3 | up-regulates activity
binding
|
KIF1A |
0.273 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266890 |
|
|
Rattus norvegicus |
Pyramidal Neuron |
| pmid |
sentence |
| 30021165 |
To better understand how KIF1A-driven dense core vesicle (DCV) transport is regulated, we identified the KIF1A interactome and focused on three binding partners, the calcium binding protein calmodulin (CaM) and two synaptic scaffolding proteins: liprin-α and TANC2. We showed that calcium, acting via CaM, enhances KIF1A binding to DCVs and increases vesicle motility. In contrast, liprin-α and TANC2 are not part of the KIF1A-cargo complex but capture DCVs at dendritic spines. we can conclude that TANC2 and liprin-α are enriched in dendritic spines and interact with various synaptic proteins. TANC2 and Liprin-α2 Act as Immobile Postsynaptic Posts Able to Recruit KIF1A in a Subset of Dendritic Spines |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
CALM3 | up-regulates
binding
|
EEF2K |
0.472 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266337 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11015200 |
The calmodulin-binding region is located between amino acids 51 and 96 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CCP110 | up-regulates activity
binding
|
CALM3 |
0.334 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266348 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16760425 |
We report that CP110 interacts with two different Ca2+-binding proteins, calmodulin (CaM) and centrin, in vivo. our data demonstrate a functional role for CaM binding to CP110 and suggest that CP110 cooperates with CaM and centrin to regulate progression through cytokinesis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CALM3 | up-regulates
binding
|
PP2B |
0.66 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269891 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11796223 |
Calcium-bound calmodulin associates with calcineurin (cn), releasing the phosphatase from the repressive effects on an autoinhibitory domain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CALM3
- 
- 