| + |
PAK1 | up-regulates 
phosphorylation
|
FLNA |
0.782 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-92065 |
Ser2152 |
TRRRRAPsVANVGSH |
Homo sapiens |
|
| pmid |
sentence |
| 12198493 |
In flna, the pak1-binding site involves tandem repeat 23 in the carboxyl terminus and phosphorylation takes place on serine 2152. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KA1 | up-regulates
phosphorylation
|
FLNA |
0.393 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-123458 |
Ser2152 |
TRRRRAPsVANVGSH |
Homo sapiens |
Melanoma Cell |
| pmid |
sentence |
| 15024089 |
We show that the n-terminal kinase domain of rsk phosphorylates flna on ser(2152) in response to mitogens |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP3CA | down-regulates 
dephosphorylation
|
FLNA |
0.262 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143979 |
Ser2152 |
TRRRRAPsVANVGSH |
Homo sapiens |
|
| pmid |
sentence |
| 16442073 |
We report that a purified c-terminal recombinant region of filamin is a suitable substrate for calcineurin in vitro. Furthermore, 1 microm cyclosporin a (csa), a specific calcineurin inhibitor, reduced the dephosphorylation of the recombinant fragment in 293ft cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKACA | up-regulates
phosphorylation
|
FLNA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-126659 |
Ser2152 |
TRRRRAPsVANVGSH |
Homo sapiens |
|
| pmid |
sentence |
| 15228085 |
Site-directed mutagenesis analysis indicated that serine 2152 is the unique substrate in the c-terminal region of abp for endogenously activated pka. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, SARS-CoV ATTACHMENT AND ENTRY |
| + |
PPP3CC | down-regulates quantity by destabilization
dephosphorylation
|
FLNA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248507 |
Ser2152 |
TRRRRAPsVANVGSH |
Homo sapiens |
|
| pmid |
sentence |
| 16442073 |
Filamin is a phosphoprotein that organizes actin filaments into networks. We report that a purified C-terminal recombinant region of filamin is a suitable substrate for calcineurin |Mutagenesis analysis showed that a dephosphorylation step occurred in Ser 2152, which was previously shown to provide resistance to calpain cleavage when endogenous PKA is activated. In contrast, phosphorylation of Ser 2152 was recently reported to be necessary for membrane dynamic changes. In this regard, we found that CsA protects filamin in platelets from calpain degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6K | up-regulates
phosphorylation
|
FLNA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252790 |
Ser2152 |
TRRRRAPsVANVGSH |
Homo sapiens |
Melanoma Cell |
| pmid |
sentence |
| 15024089 |
We show that the n-terminal kinase domain of rsk phosphorylates flna on ser(2152) in response to mitogens |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Calcineurin | down-regulates
dephosphorylation
|
FLNA |
0.27 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252339 |
Ser2152 |
TRRRRAPsVANVGSH |
Homo sapiens |
|
| pmid |
sentence |
| 16442073 |
We report that a purified c-terminal recombinant region of filamin is a suitable substrate for calcineurin in vitro. Furthermore, 1 microm cyclosporin a (csa), a specific calcineurin inhibitor, reduced the dephosphorylation of the recombinant fragment in 293ft cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP3CB | down-regulates quantity by destabilization
dephosphorylation
|
FLNA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248362 |
Ser2152 |
TRRRRAPsVANVGSH |
Homo sapiens |
|
| pmid |
sentence |
| 16442073 |
Filamin is a phosphoprotein that organizes actin filaments into networks. We report that a purified C-terminal recombinant region of filamin is a suitable substrate for calcineurin |Mutagenesis analysis showed that a dephosphorylation step occurred in Ser 2152, which was previously shown to provide resistance to calpain cleavage when endogenous PKA is activated. In contrast, phosphorylation of Ser 2152 was recently reported to be necessary for membrane dynamic changes. In this regard, we found that CsA protects filamin in platelets from calpain degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAMK2G |
phosphorylation
|
FLNA |
0.438 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250696 |
Ser2523 |
VTGPRLVsNHSLHET |
|
Pulmonary Artery Endothelial Cell |
| pmid |
sentence |
| 11290523 |
Our TER experiments using a CaM peptide, which functions as a specific competitive inhibitor of nonmuscle filamin phosphorylation by CaM kinase II, strongly suggest that filamin phosphorylation is involved in endothelial cell barrier regulation, although the exact mechanism is not clear and consequent signaling events are not well understood. |
|
| Publications: |
1 |
| + |
GPIb-IX-V complex | up-regulates activity
relocalization
|
FLNA |
0.561 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261846 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16293600 |
The cytoplasmic domain of GPIbα of the GPIb-IX-V complex binds to actin filaments through FLNa|This immediately means that clustering of the GPIb-IX-V complex and anchoring of FLNa to actin filaments by activation could also increase avidity, which could withstand high shear stress. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ROR2 | up-regulates
binding
|
FLNA |
0.415 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179668 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18667433 |
Additionally, the association of ror2 with the actin-binding protein filamin a is required for wnt5a-induced jnk activation and polarized cell migration. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FLNA | up-regulates
binding
|
MAP2K4 |
0.507 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-45887 |
|
|
Homo sapiens |
Melanoma Cell |
| pmid |
sentence |
| 9006895 |
Sek-1 binds directly and specifically to the actin-binding protein abp-280. As a consequence, active sek-1 is capable of phosphorylating and activating in vitro added bacterial recombinant sapk. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, SARS-CoV ATTACHMENT AND ENTRY |
| + |
FLNA | up-regulates quantity by stabilization
binding
|
F-actin_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261851 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11706047 |
We conclude that FLNa is essential in cells that express it for stabilizing orthogonal actin networks suitable for locomotion. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FLNA | up-regulates activity 
|
MAPK8 |
0.488 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258973 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18667433 |
Additionally, the association of Ror2 with the actin-binding protein filamin A is required for Wnt5a-induced JNK activation and polarized cell migration. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, SARS-CoV ATTACHMENT AND ENTRY |
| + |
FBLIM1 | up-regulates activity
binding
|
FLNA |
0.884 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266105 |
|
|
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 24165133 |
Kindlin binds migfilin tandem LIM domains and regulates migfilin focal adhesion localization and recruitment dynamics. Two integrin-binding proteins present in FAs, kindlin-1 and kindlin-2, are important for integrin activation, FA formation, and signaling. By binding filamin, migfilin provides a link between kindlin and the actin cytoskeleton. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
FLNA | up-regulates activity
binding
|
MAP2K4 |
0.507 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260629 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20156194 |
We used Filamin-A-deficient cells to show that Filamin A enhances MKK7 activation and is important for synergistic stress-induced JNK activation in vivo. Thus Filamin A is a novel member of the group of scaffold proteins whose function is to link two MAPKKs together and promote JNK activation. The present study provides evidence that Filamin A is one of the ‘binder’ molecules presumed to directly and closely connect MKK4 and MKK7 so that they can mediate this tyrosine/threonine phosphorylation. We showed that Filamin A (as well as Filamin B and C) associate with MKK7 and MKK4, but not with JNK1 itself |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, SARS-CoV ATTACHMENT AND ENTRY |
| + |
MAS1 | up-regulates activity
binding
|
FLNA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260627 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26460884 |
We further determined that GPCRs, AT1R, and MAS directly recruited FLNa and promoted its phosphorylation by cellular S/T kinases in an agonist-dependent manner. Our studies thus provide a structural framework for filamin in GPCR signaling, potentially regulating a variety of cellular responses. MAS likely binds filamin constitutively and hence leads to constitutive filamin phosphorylation. These results emphasize that it is the active receptor that mediates filamin phosphorylation by PKA or other cellular S/T kinases |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, SARS-CoV ATTACHMENT AND ENTRY |
| + |
calcium(2+) | down-regulates activity
chemical inhibition
|
FLNA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261845 |
|
|
Homo sapiens |
Blood Platelet |
| pmid |
sentence |
| 27871158 |
Gelsolin is an actin binding protein that severs and caps the barbed-end actin filaments to prevent actin monomer exchange upon intracellular calcium increase in the initial step. Cofilin also binds to actin and contributes to the disassembly of actin filaments and the subsequent release of actin monomers. The actin cross-linking complex, GP1b/IX-filamin, translocates from the plasma membrane to the cytoskeleton during this step. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PP2B | down-regulates quantity by destabilization
dephosphorylation
|
FLNA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269986 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16442073 |
Filamin is a phosphoprotein that organizes actin filaments into networks. We report that a purified C-terminal recombinant region of filamin is a suitable substrate for calcineurin |Mutagenesis analysis showed that a dephosphorylation step occurred in Ser 2152, which was previously shown to provide resistance to calpain cleavage when endogenous PKA is activated. In contrast, phosphorylation of Ser 2152 was recently reported to be necessary for membrane dynamic changes. In this regard, we found that CsA protects filamin in platelets from calpain degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FLNA | up-regulates activity
binding
|
MAP2K7 |
0.262 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260628 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20156194 |
We used Filamin-A-deficient cells to show that Filamin A enhances MKK7 activation and is important for synergistic stress-induced JNK activation in vivo. Thus Filamin A is a novel member of the group of scaffold proteins whose function is to link two MAPKKs together and promote JNK activation. The present study provides evidence that Filamin A is one of the ‘binder’ molecules presumed to directly and closely connect MKK4 and MKK7 so that they can mediate this tyrosine/threonine phosphorylation. We showed that Filamin A (as well as Filamin B and C) associate with MKK7 and MKK4, but not with JNK1 itself |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, SARS-CoV ATTACHMENT AND ENTRY |
| + |
ASB2 | down-regulates quantity by destabilization
polyubiquitination
|
FLNA |
0.453 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271740 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 18799729 |
ASB2 is the specificity subunit of an E3 ubiquitin ligase complex and is proposed to exert its effects by regulating the turnover of specific proteins; however, no ASB2 substrates had been identified. Here, we report that ASB2 targets the actin-binding proteins filamin A and B for proteasomal degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FLNA | up-regulates activity
binding
|
KCND2 |
0.36 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269003 |
|
|
Rattus norvegicus |
|
| pmid |
sentence |
| 11102480 |
Filamin may function as a scaffold protein in the postsynaptic density, mediating a direct link between Kv4.2 and the actin cytoskeleton, and that this interaction is essential for the generation of appropriate Kv4.2 current densities. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| Tissue: |
Cerebellum |
3.0
FLNA
- 
- 