| + |
MAPK13 | down-regulates activity 
phosphorylation
|
EEF2K |
0.579 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109703 |
Ser359 |
GTEEKCGsPQVRTLS |
Homo sapiens |
|
| pmid |
sentence |
| 11500363 |
Sapk4/p38delta phosphorylated eef2k at ser359 in vitro, causing its inactivation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250089 |
Ser396 |
TFDSLPSsPSSATPH |
in vitro |
|
| pmid |
sentence |
| 11500363 |
eEF2 kinase is phosphorylated and inhibited by SAPK4/p38delta. eEF2K[S359A] was phosphorylated (presumably at Ser396) by the high concentrations of SAPK4/p38 used in this experiment. However, the inhibition of eEF2K under these conditions was reduced from 82% in the wild-type enzyme to 19% in eEF2K[S359A] |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, In Vitro |
| Tissue: |
Muscle, Skeletal Muscle |
| + |
MAPK13 | down-regulates
phosphorylation
|
EEF2K |
0.579 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-177986 |
Ser359 |
GTEEKCGsPQVRTLS |
Homo sapiens |
|
| pmid |
sentence |
| 18337751 |
The phosphorylation of eef2k at ser359 is of particular interest. First, the phosphorylation of this site strongly decreases the activity of eef2k even at high calcium concentrations (knebel et al, 2001), that is, desensitizes eef2k to the activating effects of elevated ca2+ levels. third, although p38 map kinase (also termed sapk4 can phosphorylate ser359 in vitro (knebel et al, 2001), this enzyme is not known to be active basally or to be regulated by amino acids. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK1 | down-regulates
phosphorylation
|
EEF2K |
0.367 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-177982 |
Ser359 |
GTEEKCGsPQVRTLS |
Homo sapiens |
|
| pmid |
sentence |
| 18337751 |
Phosphorylation at ser359 inhibits eef2k activity even at high calcium concentrations. we demonstrate that cdc2 contributes to controlling eef2 phosphorylation in cells. inactivation of eef2k by cdc2 may serve to keep eef2 active during mitosis |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6K | down-regulates activity
phosphorylation
|
EEF2K |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252775 |
Ser366 |
SPQVRTLsGSRPPLL |
Homo sapiens |
|
| pmid |
sentence |
| 11500364 |
We show that two such kinases, p70 s6 kinase (regulated via mtor) and p90(rsk1) (activated by erk), phosphorylate eef2k at a conserved serine and inhibit its activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKAA1 | down-regulates activity
phosphorylation
|
EEF2K |
0.493 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250402 |
Ser366 |
SPQVRTLsGSRPPLL |
in vitro |
|
| pmid |
sentence |
| 14709557 |
AMPK can phosphorylate three sites in eEF2 kinase in vitro. Of these, Ser-398 appears to be more efficiently phosphorylated than either Ser-78 or Ser-366. Ser-78 and Ser-366 do not appear to be phosphorylated by AMPK within cells. Ser-366 serves to decrease the activity of eEF2 kinase |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250314 |
Ser78 |
SSGSPANsFHFKEAW |
in vitro |
|
| pmid |
sentence |
| 14709557 |
AMPK can phosphorylate three sites in eEF2 kinase in vitro. Of these, Ser-398 appears to be more efficiently phosphorylated than either Ser-78 or Ser-366. Ser-78 and Ser-366 do not appear to be phosphorylated by AMPK within cells. Ser-366 serves to decrease the activity of eEF2 kinase |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PRKACA | up-regulates activity 
phosphorylation
|
EEF2K |
0.304 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250354 |
Ser366 |
SPQVRTLsGSRPPLL |
in vitro |
|
| pmid |
sentence |
| 11171059 |
EEF-2K can be phosphorylated in vitro by cAMP-dependent protein kinase (PKA) and that this induces significant Ca(2+)/calmodulin (CaM)-independent eEF-2K activity. sites of phosphorylation were Ser-365 and Ser-499 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250444 |
Ser500 |
RLHLPRAsAVALEVQ |
in vitro |
|
| pmid |
sentence |
| 11171059 |
EEF-2K can be phosphorylated in vitro by cAMP-dependent protein kinase (PKA) and that this induces significant Ca(2+)/calmodulin (CaM)-independent eEF-2K activity. sites of phosphorylation were Ser-365 and Ser-499 |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
RPS6KB1 | down-regulates activity
phosphorylation
|
EEF2K |
0.738 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109712 |
Ser366 |
SPQVRTLsGSRPPLL |
Homo sapiens |
|
| pmid |
sentence |
| 11500364 |
We show that two such kinases, p70 s6 kinase (regulated via mtor) and p90(rsk1) (activated by erk), phosphorylate eef2k at a conserved serine and inhibit its activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KA1 | down-regulates activity
phosphorylation
|
EEF2K |
0.513 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109708 |
Ser366 |
SPQVRTLsGSRPPLL |
Homo sapiens |
Embryonic Cell Line |
| pmid |
sentence |
| 11500364 |
We show that two such kinases, p70 s6 kinase (regulated via mtor) and p90(rsk1) (activated by erk), phosphorylate eef2k at a conserved serine and inhibit its activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKAA2 | down-regulates activity
phosphorylation
|
EEF2K |
0.499 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250319 |
Ser366 |
SPQVRTLsGSRPPLL |
in vitro |
|
| pmid |
sentence |
| 14709557 |
AMPK can phosphorylate three sites in eEF2 kinase in vitro. Of these, Ser-398 appears to be more efficiently phosphorylated than either Ser-78 or Ser-366. Ser-78 and Ser-366 do not appear to be phosphorylated by AMPK within cells. Ser-366 serves to decrease the activity of eEF2 kinase |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250321 |
Ser78 |
SSGSPANsFHFKEAW |
in vitro |
|
| pmid |
sentence |
| 14709557 |
AMPK can phosphorylate three sites in eEF2 kinase in vitro. Of these, Ser-398 appears to be more efficiently phosphorylated than either Ser-78 or Ser-366. Ser-78 and Ser-366 do not appear to be phosphorylated by AMPK within cells. Ser-366 serves to decrease the activity of eEF2 kinase |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
MAPKAPK3 |
phosphorylation
|
EEF2K |
0.323 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249709 |
Ser377 |
PPLLRPLsENSGDEN |
in vitro |
|
| pmid |
sentence |
| 12171600 |
Identification of Ser-377 as the site on eEF2 kinase phosphorylated in vitro by MAPKAP-K2, MAPKAP-K3 and MAPKAP-K5. Maximal phosphorylation of eEF2 kinase by MAPKAP-K2 (Figure 5) or MAPKAP-K5 (results not shown) had no effect on its activity. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MAPKAPK5 |
phosphorylation
|
EEF2K |
0.293 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249708 |
Ser377 |
PPLLRPLsENSGDEN |
in vitro |
|
| pmid |
sentence |
| 12171600 |
Identification of Ser-377 as the site on eEF2 kinase phosphorylated in vitro by MAPKAP-K2, MAPKAP-K3 and MAPKAP-K5. Maximal phosphorylation of eEF2 kinase by MAPKAP-K2 (Figure 5) or MAPKAP-K5 (results not shown) had no effect on its activity. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MAPKAPK2 |
phosphorylation
|
EEF2K |
0.35 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249710 |
Ser377 |
PPLLRPLsENSGDEN |
in vitro |
|
| pmid |
sentence |
| 12171600 |
Identification of Ser-377 as the site on eEF2 kinase phosphorylated in vitro by MAPKAP-K2, MAPKAP-K3 and MAPKAP-K5. Maximal phosphorylation of eEF2 kinase by MAPKAP-K2 (Figure 5) or MAPKAP-K5 (results not shown) had no effect on its activity. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MAPK14 | down-regulates activity
phosphorylation
|
EEF2K |
0.333 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249707 |
Ser396 |
TFDSLPSsPSSATPH |
in vitro |
|
| pmid |
sentence |
| 12171600 |
Inhibition of eEF2 kinase resulting from phosphorylation of Ser-396 by SAPK2a p38 was approx.25%. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MAPK12 |
phosphorylation
|
EEF2K |
0.327 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250137 |
Ser396 |
TFDSLPSsPSSATPH |
in vitro |
|
| pmid |
sentence |
| 12171600 |
We have also shown that JNK11, JNK22 and SAPK3 p38 phosphorylate eEF2 kinase very poorly at Ser-396 |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKAA2 | up-regulates activity
phosphorylation
|
EEF2K |
0.499 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250158 |
Ser398 |
DSLPSSPsSATPHSQ |
in vitro |
|
| pmid |
sentence |
| 14709557 |
Stimulation of the AMP-activated Protein Kinase Leads to Activation of Eukaryotic Elongation Factor 2 Kinase and to Its Phosphorylation at a Novel Site, Serine 398. phosphorylation of eEF2 kinase at Ser-398 leads to an increase in its activity. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKAA1 | up-regulates activity
phosphorylation
|
EEF2K |
0.493 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250157 |
Ser398 |
DSLPSSPsSATPHSQ |
in vitro |
|
| pmid |
sentence |
| 14709557 |
Stimulation of the AMP-activated Protein Kinase Leads to Activation of Eukaryotic Elongation Factor 2 Kinase and to Its Phosphorylation at a Novel Site, Serine 398. phosphorylation of eEF2 kinase at Ser-398 leads to an increase in its activity. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
AMPK | up-regulates
phosphorylation
|
EEF2K |
0.426 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216503 |
Ser398 |
DSLPSSPsSATPHSQ |
Homo sapiens |
|
| pmid |
sentence |
| 22669845 |
In response to genotoxic stress, eef2k was activated by ampk (adenosine monophosphate-activated protein kinase)-mediated phosphorylation on serine 398. Activated eef2k phosphorylated eef2 and induced a temporary ribosomal slowdown at the stage of elongation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKAA1 | up-regulates
phosphorylation
|
EEF2K |
0.493 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-197734 |
Ser398 |
DSLPSSPsSATPHSQ |
Homo sapiens |
|
| pmid |
sentence |
| 22669845 |
In response to genotoxic stress, eef2k was activated by ampk (adenosine monophosphate-activated protein kinase)-mediated phosphorylation on serine 398. Activated eef2k phosphorylated eef2 and induced a temporary ribosomal slowdown at the stage of elongation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EEF2K | down-regulates
phosphorylation
|
EEF2K |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-197725 |
Ser445 |
SGDSGYPsEKRGELD |
Homo sapiens |
|
| pmid |
sentence |
| 22669845 |
The combination of eef2k autophosphorylation (targeting ser445) and a yet to be identified kinase (targeting ser441) would be needed to generate the eef2k phosphodegron specifically in response to dna damage. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
mTORC1 | down-regulates activity
phosphorylation
|
EEF2K |
0.343 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277908 |
Ser70 |
LTKSERYsSSGSPAN |
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 35513296 |
Our phosphoproteomics analysis add to this body of knowledge as it indicates that mTORC1 modulates additional phosphorylation sites in eEF2K, such as Y69, S70, S72, and S74, which is consistent with our previous findings |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277906 |
Ser72 |
KSERYSSsGSPANSF |
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 35513296 |
Our phosphoproteomics analysis add to this body of knowledge as it indicates that mTORC1 modulates additional phosphorylation sites in eEF2K, such as Y69, S70, S72, and S74, which is consistent with our previous findings |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277907 |
Ser74 |
ERYSSSGsPANSFHF |
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 35513296 |
Our phosphoproteomics analysis add to this body of knowledge as it indicates that mTORC1 modulates additional phosphorylation sites in eEF2K, such as Y69, S70, S72, and S74, which is consistent with our previous findings |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277909 |
Tyr69 |
NLTKSERySSSGSPA |
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 35513296 |
Our phosphoproteomics analysis add to this body of knowledge as it indicates that mTORC1 modulates additional phosphorylation sites in eEF2K, such as Y69, S70, S72, and S74, which is consistent with our previous findings |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
TRPM7 | up-regulates activity
phosphorylation
|
EEF2K |
0.315 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277923 |
Ser78 |
SSGSPANsFHFKEAW |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21112387 |
TRPM7 interacts with, and phosphorylates mouse eEF2-k at serine site 77 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EEF2K | down-regulates
phosphorylation
|
EEF2 |
0.791 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-91751 |
Thr57 |
RAGETRFtDTRKDEQ |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12194824 |
The activation of eef2 kinase by ampk, resulting in the phosphorylation and inactivation of eef2, provides a novel mechanism for the inhibition of protein synthesis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-38552 |
Thr57 |
RAGETRFtDTRKDEQ |
Homo sapiens |
|
| pmid |
sentence |
| 8386634 |
The eef-2 kinase could phosphorylate a synthetic peptide based on residues 49-60 of eef-2 (ragetrftdtrk), albeit only at a very low rate, and with a very high km, compared to eef-2 itself. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-38556 |
Thr59 |
GETRFTDtRKDEQER |
Homo sapiens |
|
| pmid |
sentence |
| 8386634 |
Ef-2 kinase phosphorylates ef-2 at 3 threonine residues: thr-53, thr-56, thr-58. Phosphorylation of thr56 and thr58 was found to be an ordered process, modification of thr56 preceding, and apparently being required for, phosphorylation of thr58. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-22928 |
Thr59 |
GETRFTDtRKDEQER |
Homo sapiens |
|
| pmid |
sentence |
| 2261989 |
Ef-2 kinase phosphorylates ef-2 at 3 threonine residues: thr-53, thr-56, thr-58. Phosphorylation of thr56 and thr58 was found to be an ordered process, modification of thr56 preceding, and apparently being required for, phosphorylation of thr58. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
CALM1 | up-regulates
binding
|
EEF2K |
0.463 |
| 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 |
| + |
p38 | down-regulates activity
phosphorylation
|
EEF2K |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270127 |
|
|
in vitro |
|
| pmid |
sentence |
| 12171600 |
Inhibition of eEF2 kinase resulting from phosphorylation of Ser-396 by SAPK2a p38 was approx.25%. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CALM2 | up-regulates
binding
|
EEF2K |
0.459 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266321 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11015200 |
The calmodulin-binding region is located between amino acids 51 and 96 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CALM3 | up-regulates
binding
|
EEF2K |
0.459 |
| 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 |
| + |
FBXW11 | down-regulates
ubiquitination
|
EEF2K |
0.433 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-197730 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22669845 |
Eef2k was degraded by the ubiquitin-proteasome system through the ubiquitin ligase scf(__trcp) (skp1-cul1-f-box protein, __-transducin repeat-containing protein) to enable rapid resumption of translation elongation. This event required autophosphorylation of eef2k on a canonical __trcp-binding domain |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
EEF2K
- 
- 