+ |
EIF3F | up-regulates
deubiquitination
|
NOTCH1 |
0.431 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-170158 |
Lys1759 |
CGVLLSRkRRRQHGQ |
Homo sapiens |
|
pmid |
sentence |
21124883 |
The activated form of notch needs to be deubiquitinated before being processed by the gamma-secretase activity and entering the nucleus, where it fulfills its transcriptional function. The enzyme accounting for this deubiquitinase activity is eif3f, known so far as a translation initiation factor. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK11B | down-regulates
phosphorylation
|
EIF3F |
0.531 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-95762 |
Ser46 |
PAAAPASsSDPAAAA |
Homo sapiens |
|
pmid |
sentence |
12446680 |
The interaction between cdk11p46 and eif3 p47 occurs in vitro and in vivo. In addition, cdk11 protein kinase isolated from cells undergoing apoptosis can phosphorylate eif3 p47in vitro, and serine phosphorylation of eif3 p47 occurs in cells during apoptosis.Purified recombinant cdk11p46 inhibited translation of a reporter gene in vitro in a dose-dependent manner.These data suggest that the function of the caspase-processed cdk11p110 isoform may be to inhibit translation during apoptosis. However, whether or not this inhibition of protein translation occurs in an eif3 p47-dependent or -independent manner remains to be clarified. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CyclinD3/CDK11B | up-regulates activity
phosphorylation
|
EIF3F |
0.531 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273134 |
Ser46 |
PAAAPASsSDPAAAA |
|
|
pmid |
sentence |
19245811 |
EIF3f is phosphorylated by CDK11p46 at Ser46 during apoptosis.|Phosphorylation of eIF3f plays an important role in regulating its function in translation and apoptosis. Phosphorylation of eIF3f enhances the association of eIF3f with the core eIF3 subunits during apoptosis. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273132 |
Thr119 |
GAARVIGtLLGTVDK |
|
|
pmid |
sentence |
19245811 |
Here, we identified a second eIF3f phosphorylation site (Thr119) by CDK11(p46) during apoptosis. We demonstrated that eIF3f is directly phosphorylated by CDK11(p46) in vivo. Phosphorylation of eIF3f plays an important role in regulating its function in translation and apoptosis. Phosphorylation of eIF3f enhances the association of eIF3f with the core eIF3 subunits during apoptosis. |
|
Publications: |
2 |
+ |
CDK11B | up-regulates activity
phosphorylation
|
EIF3F |
0.531 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273133 |
Ser46 |
PAAAPASsSDPAAAA |
|
|
pmid |
sentence |
19245811 |
EIF3f is phosphorylated by CDK11p46 at Ser46 during apoptosis.|Phosphorylation of eIF3f plays an important role in regulating its function in translation and apoptosis. Phosphorylation of eIF3f enhances the association of eIF3f with the core eIF3 subunits during apoptosis. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273131 |
Thr119 |
GAARVIGtLLGTVDK |
|
|
pmid |
sentence |
19245811 |
Here, we identified a second eIF3f phosphorylation site (Thr119) by CDK11(p46) during apoptosis. We demonstrated that eIF3f is directly phosphorylated by CDK11(p46) in vivo. Phosphorylation of eIF3f plays an important role in regulating its function in translation and apoptosis. Phosphorylation of eIF3f enhances the association of eIF3f with the core eIF3 subunits during apoptosis. |
|
Publications: |
2 |
+ |
CDK11B |
phosphorylation
|
EIF3F |
0.531 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-184185 |
Thr119 |
GAARVIGtLLGTVDK |
Homo sapiens |
|
pmid |
sentence |
19245811 |
Here, we identified a second eif3f phosphorylation site (thr119) by cdk11p46 during apoptosis.Thr119 is located in the mov34 domain of eif3f which is important for both the translational inhibitory function of eif3ffurther studies of how eif3f phosphorylation regulates its function will refine insights into the mechanism and regulation of translation initiation, apoptotic signaling, and tumorigenesis. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
EIF3F | up-regulates
deubiquitination
|
NOTCH |
0.431 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-254327 |
|
|
Homo sapiens |
|
pmid |
sentence |
21124883 |
The activated form of notch needs to be deubiquitinated before being processed by the gamma-secretase activity and entering the nucleus, where it fulfills its transcriptional function. The enzyme accounting for this deubiquitinase activity is eif3f, known so far as a translation initiation factor. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Cullin 1-RBX1-Skp1 | down-regulates quantity by destabilization
binding
|
EIF3F |
0.356 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271767 |
|
|
Mus musculus |
C2C12 Cell |
pmid |
sentence |
18354498 |
Mediation of eIF3-f polyubiquitination by the SCFMAFbx. The association of MAFbx with the essential Skp1, Roc 1 and Cul1 proteins, specific components of an E3 ubiquitin–protein ligase (SCFMAFbx), was previously described. Here, we present evidence that during muscle atrophy MAFbx targets the eukaryotic initiation factor 3 subunit 5 (eIF3-f) for ubiquitination and degradation by the proteasome. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
FBXO33 | down-regulates quantity by destabilization
polyubiquitination
|
EIF3F |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271768 |
|
|
Mus musculus |
C2C12 Cell |
pmid |
sentence |
18354498 |
Mediation of eIF3-f polyubiquitination by the SCFMAFbx. The association of MAFbx with the essential Skp1, Roc 1 and Cul1 proteins, specific components of an E3 ubiquitin–protein ligase (SCFMAFbx), was previously described. Here, we present evidence that during muscle atrophy MAFbx targets the eukaryotic initiation factor 3 subunit 5 (eIF3-f) for ubiquitination and degradation by the proteasome. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
S | down-regulates activity
binding
|
EIF3F |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260255 |
|
|
Homo sapiens |
|
pmid |
sentence |
18231581 |
Coronavirus spike protein inhibits host cell translation by interaction with eIF3f |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
EIF3F | form complex
binding
|
EIF3_complex |
0.921 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266395 |
|
|
in vitro |
|
pmid |
sentence |
16920360 |
Consistent with its diverse functions, eIF3 is the largest and most complex initiation factor: the mammalian version, for example, contains 13 nonidentical subunits that are designated eIF3a to eIF3m 8, 9, 10, 11, 12, 13 (Table 1). |
|
Publications: |
1 |
Organism: |
In Vitro |