| + |
YWHAG | up-regulates quantity by stabilization 
binding
|
GEM |
0.269 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261713 |
|
|
Chlorocebus aethiops |
|
| pmid |
sentence |
| 14701738 |
In order to address whether Gem binds specific isoforms of 14-3-3, we determined the coassociation of Gem and 14-3-3 in the neuroblastoma cell line SY5Y. 14-3-3ζ, -γ, -τ, and -β were observed to bind to Gem. 14-3-3-bound Gem has a twofold-longer half-life than nonbound Gem (Fig. (Fig.6).6). A similar increase in protein stability following 14-3-3 binding has been described for the Wee1 kinase |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261723 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 14701738 |
In order to address whether Gem binds specific isoforms of 14-3-3, we determined the coassociation of Gem and 14-3-3 in the neuroblastoma cell line SY5Y. 14-3-3ζ, -γ, -τ, and -β were observed to bind to Gem. 14-3-3-bound Gem has a twofold-longer half-life than nonbound Gem (Fig. (Fig.6).6). A similar increase in protein stability following 14-3-3 binding has been described for the Wee1 kinase |
|
| Publications: |
2 |
Organism: |
Chlorocebus Aethiops |
| + |
GEM | down-regulates activity 
binding
|
ROCK2 |
0.294 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261711 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14701738 |
Two functions for Gem have been demonstrated, including inhibition of voltage-gated calcium channel activity and inhibition of Rho kinase-mediated cytoskeletal reorganization, such as stress fiber formation and neurite retraction. These functions for Gem have been ascribed to its interaction with the calcium channel Β subunit and Rho kinase Β, respectively. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261717 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 16757346 |
We have found that Gem binds specifically to ROKβ in the coiled‐coil domain adjacent to the Rho binding site. The interaction between Gem and ROKβ leads to inhibition of MLC and MBS phosphorylation but not phosphorylation of LIMK, indicating that Gem exerts its effect by altering the substrate specificity of ROKβ |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261721 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14701738 |
Two functions for Gem have been demonstrated, including inhibition of voltage-gated calcium channel activity and inhibition of Rho kinase-mediated cytoskeletal reorganization, such as stress fiber formation and neurite retraction. These functions for Gem have been ascribed to its interaction with the calcium channel Β subunit and Rho kinase Β, respectively. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261707 |
|
|
Chlorocebus aethiops |
|
| pmid |
sentence |
| 16757346 |
We have found that Gem binds specifically to ROKβ in the coiled‐coil domain adjacent to the Rho binding site. The interaction between Gem and ROKβ leads to inhibition of MLC and MBS phosphorylation but not phosphorylation of LIMK, indicating that Gem exerts its effect by altering the substrate specificity of ROKβ |
|
| Publications: |
4 |
Organism: |
Homo Sapiens, Chlorocebus Aethiops |
| + |
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 |
| + |
YWHAZ | up-regulates quantity by stabilization
binding
|
GEM |
0.307 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261725 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 14701738 |
In order to address whether Gem binds specific isoforms of 14-3-3, we determined the coassociation of Gem and 14-3-3 in the neuroblastoma cell line SY5Y. 14-3-3ζ, -γ, -τ, and -β were observed to bind to Gem. 14-3-3-bound Gem has a twofold-longer half-life than nonbound Gem (Fig. (Fig.6).6). A similar increase in protein stability following 14-3-3 binding has been described for the Wee1 kinase |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261715 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 14701738 |
In order to address whether Gem binds specific isoforms of 14-3-3, we determined the coassociation of Gem and 14-3-3 in the neuroblastoma cell line SY5Y. 14-3-3ζ, -γ, -τ, and -β were observed to bind to Gem. 14-3-3-bound Gem has a twofold-longer half-life than nonbound Gem (Fig. (Fig.6).6). A similar increase in protein stability following 14-3-3 binding has been described for the Wee1 kinase |
|
| Publications: |
2 |
Organism: |
Chlorocebus Aethiops |
| + |
YWHAQ | up-regulates quantity by stabilization
binding
|
GEM |
0.269 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261714 |
|
|
Chlorocebus aethiops |
|
| pmid |
sentence |
| 14701738 |
In order to address whether Gem binds specific isoforms of 14-3-3, we determined the coassociation of Gem and 14-3-3 in the neuroblastoma cell line SY5Y. 14-3-3ζ, -γ, -τ, and -β were observed to bind to Gem. 14-3-3-bound Gem has a twofold-longer half-life than nonbound Gem (Fig. (Fig.6).6). A similar increase in protein stability following 14-3-3 binding has been described for the Wee1 kinase |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261724 |
|
|
Chlorocebus aethiops |
|
| pmid |
sentence |
| 14701738 |
In order to address whether Gem binds specific isoforms of 14-3-3, we determined the coassociation of Gem and 14-3-3 in the neuroblastoma cell line SY5Y. 14-3-3ζ, -γ, -τ, and -β were observed to bind to Gem. 14-3-3-bound Gem has a twofold-longer half-life than nonbound Gem (Fig. (Fig.6).6). A similar increase in protein stability following 14-3-3 binding has been described for the Wee1 kinase |
|
| Publications: |
2 |
Organism: |
Chlorocebus Aethiops |
| + |
CALM2 | up-regulates activity
binding
|
GEM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266325 |
|
|
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-266326 |
|
|
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 |
| + |
CALM1 | up-regulates activity
binding
|
GEM |
0.337 |
| 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. |
|
| 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. |
|
| Publications: |
2 |
Organism: |
Rattus Norvegicus |
| + |
GEM | down-regulates activity
binding
|
CACNB2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261710 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14701738 |
Two functions for Gem have been demonstrated, including inhibition of voltage-gated calcium channel activity and inhibition of Rho kinase-mediated cytoskeletal reorganization, such as stress fiber formation and neurite retraction. These functions for Gem have been ascribed to its interaction with the calcium channel Β subunit and Rho kinase Β, respectively. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261720 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14701738 |
Two functions for Gem have been demonstrated, including inhibition of voltage-gated calcium channel activity and inhibition of Rho kinase-mediated cytoskeletal reorganization, such as stress fiber formation and neurite retraction. These functions for Gem have been ascribed to its interaction with the calcium channel Β subunit and Rho kinase Β, respectively. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
3.0
GEM
- 
- 