| + |
CSNK2A1 | down-regulates activity 
phosphorylation
|
CALM1 |
0.424 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266354 |
Ser102 |
KDGNGYIsAAELRHV |
in vitro |
|
| pmid |
sentence |
| 26675311 |
Phosphorylation of CaM at four sites by CK2 was found to follow a sequential order, with Ser81 as the first, Thr79 as the second, and Ser101 or Thr117 as the third. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266353 |
Ser82 |
RKMKDTDsEEEIREA |
in vitro |
|
| pmid |
sentence |
| 26675311 |
Phosphorylation of CaM at four sites by CK2 was found to follow a sequential order, with Ser81 as the first, Thr79 as the second, and Ser101 or Thr117 as the third. We found that in the complex between CaM and CaMKII, residue E115 of CaM is strongly interacting with K299 of the kinase through forming a salt-bridge (PDB entry 1WEL), it is quite likely that the phosphorylation induced structural change can disrupt this interaction and negatively affect the binding between the two proteins |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266355 |
Thr118 |
TNLGEKLtDEEVDEM |
in vitro |
|
| pmid |
sentence |
| 26675311 |
Phosphorylation of CaM at four sites by CK2 was found to follow a sequential order, with Ser81 as the first, Thr79 as the second, and Ser101 or Thr117 as the third. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266356 |
Thr80 |
MARKMKDtDSEEEIR |
in vitro |
|
| pmid |
sentence |
| 26675311 |
Phosphorylation of CaM at four sites by CK2 was found to follow a sequential order, with Ser81 as the first, Thr79 as the second, and Ser101 or Thr117 as the third. |
|
| Publications: |
4 |
Organism: |
In Vitro |
| + |
EGFR | down-regulates
phosphorylation
|
CALM1 |
0.406 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-34691 |
Tyr100 |
FDKDGNGyISAAELR |
Homo sapiens |
|
| pmid |
sentence |
| 7925415 |
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-24778 |
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: |
2 |
Organism: |
Homo Sapiens |
| + |
INSR | down-regulates
phosphorylation
|
CALM1 |
0.405 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-24782 |
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 |
| + |
CALM1 | up-regulates 
binding
|
PPP3CA |
0.754 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-114098 |
|
|
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 |
| Pathways: | T cell activation |
| + |
CCP110 | up-regulates activity
binding
|
CALM1 |
0.323 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265965 |
|
|
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 |
| + |
CALM1 | up-regulates
binding
|
CAMKK2 |
0.83 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-61922 |
|
|
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 |
| Pathways: | Thyroid Hormone Metabolism |
| + |
calcium(2+) | up-regulates
chemical activation
|
CALM1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-78915 |
|
|
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 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235590 |
|
|
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. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, Mus Musculus |
| Pathways: | B-cell activation, T cell activation, Thyroid Hormone Metabolism, VEGF Signaling |
| + |
CALM1 | up-regulates activity
binding
|
GEM |
0.335 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261716 |
|
|
Rattus norvegicus |
|
| 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-261726 |
|
|
Rattus norvegicus |
|
| 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 |
| + |
CALM1 | up-regulates activity
binding
|
KIF1A |
0.275 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266888 |
|
|
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. We show that Ca2+/CaM-dependent modulation on KIF1A allows for binding to vesicular cargo. Our results indicate that at low calcium concentrations, the tail domain of KIF1A does not bind to vesicular cargo, whereas at high calcium concentrations, CaM binds KIF1A, allowing for subsequent DCV motility. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
CALM1 | up-regulates
binding
|
PP2B |
0.764 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269892 |
|
|
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 |
| + |
CALM1 | up-regulates
binding
|
PPP3CB |
0.697 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-114101 |
|
|
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 |
| + |
CALM1 | up-regulates
binding
|
Calcineurin |
0.579 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252337 |
|
|
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 |
| Pathways: | B-cell activation, T cell activation |
| + |
CALM1 | up-regulates activity
binding
|
NOS3 |
0.762 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251615 |
|
|
Homo sapiens |
|
| 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 |
| Pathways: | VEGF Signaling |
| + |
CALM1 | down-regulates activity
binding
|
SCN8A |
0.456 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253410 |
|
|
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 |
| + |
CALM1 | up-regulates
binding
|
EEF2K |
0.468 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-82505 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11015200 |
The calmodulin-binding region is located between amino acids 51 and 96 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CALM1 | up-regulates
binding
|
PPP3CC |
0.662 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-114104 |
|
|
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 |
| + |
CALM1 | up-regulates
binding
|
CAMKK1 |
0.756 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-232178 |
|
|
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 |
4.0
CALM1
- 
- 