| + |
DPH5 | down-regulates activity 
methylation
|
EEF2 |
0.75 |
| 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 |
0.79 |
| 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 |
0.405 |
| 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 |
| + |
CSK | down-regulates quantity
phosphorylation
|
EEF2 |
0.264 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279698 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24648518 |
C-terminal Src kinase (Csk)-mediated phosphorylation of eukaryotic elongation factor 2 (eEF2) promotes proteolytic cleavage and nuclear translocation of eEF2.|In this report, we show that eukaryotic elongation factor 2 (eEF2) is a new protein substrate of Csk and could locate in the nucleus. |
|
| 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 |
| + |
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
|
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 |
| + |
2-(3-amino-3-carboxypropyl)histidine synthase complex | down-regulates activity
chemical modification
|
EEF2 |
0.844 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281500 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31463593 |
Diphthamide, the target of diphtheria toxin, is a post-translationally modified histidine residue found in archaeal and eukaryotic translation elongation factor 2 (EF2). In the first step of diphthamide biosynthesis, a [4Fe-4S] cluster-containing radical SAM enzyme, Dph1-Dph2 heterodimer in eukaryotes or Dph2 homodimer in archaea, cleaves S-adenosylmethionine and transfers the 3-amino-3-carboxypropyl group to EF2. Dph1-Dph2 heterodimer is a non-canonical radical SAM enzyme that transfers the ACP group from SAM to EF2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
EEF2
- 
- 