| + |
DPH5 | down-regulates activity 
methylation
|
EEF2 |
0.74 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261146 |
His715 |
TLHADAIhRGGGQII |
Homo sapiens |
|
| pmid |
sentence |
| 23486472 |
Analysis of EF2 in the mutant cells revealed a novel form of diphthamide with an additional methyl group that prevented ADP-ribosylation and inactivation of EF2. The abnormal methylation appeared to be catalyzed by DPH5. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EEF2K | down-regulates
phosphorylation
|
EEF2 |
0.782 |
| 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-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-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. |
|
| 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. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
PPP2CA | up-regulates 
dephosphorylation
|
EEF2 |
0.415 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-38561 |
Thr57 |
RAGETRFtDTRKDEQ |
Homo sapiens |
|
| pmid |
sentence |
| 8386634 |
Protein phosphatases-2a and -2c (pp-2a and pp-2c) can each efficiently dephosphorylate phosphorylated eef-2 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-38566 |
Thr59 |
GETRFTDtRKDEQER |
Homo sapiens |
|
| pmid |
sentence |
| 8386634 |
Protein phosphatases-2a and -2c (pp-2a and pp-2c) can each efficiently dephosphorylate phosphorylated eef-2 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
EEF2 | up-regulates 
|
Translational_elongation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269396 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14709557 |
In mammalian cells, peptide chain elongation requires two main elongation factors, eEF1A and eEF2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EEF2 | up-regulates
|
Translational_regulation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268628 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30082469 |
… several key regulators of nervous system translation, including eukaryotic initiation factor 2α (eIF2α), the mechanistic (or mammalian) target of rapamycin complex 1 (mTORC1), and the eukaryotic elongation factor 2 (eEF2). These pathways regulate the overall rate of protein synthesis in neurons and have selective effects on the translation of specific messenger RNAs (mRNAs |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EEF2 | up-regulates activity
binding
|
80S_cytosolic_ribosome |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269397 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14709557 |
In mammalian cells, peptide chain elongation requires two main elongation factors, eEF1A and eEF2. The latter mediates the translocation step of elongation in which the ribosome moves by the equivalent of one codon relative to the mRNA, and the peptidyl-tRNA shifts from the A- into the P-site on the ribosomend eEF2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Translation elongation and termination |
3.0
EEF2
- 
- 