| + |
CSNK2A2 |
phosphorylation
|
EEF1B2 |
0.342 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250987 |
Ser106 |
DDIDLFGsDDEEESE |
in vitro |
|
| pmid |
sentence |
| 8547318 |
EF-1 beta was highly phosphorylated by casein kinase II, with up to 1.3 mol of phosphate incorporated per mol protein. From microsequence analysis and manual Edman degradation, the majority of the phosphate was shown to be present in serine 106 in the peptide DLFGS106DDEEES112EEA. Serine 112 was also phosphorylated by casein kinase II, but to a lesser extent. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250988 |
Ser112 |
GSDDEEEsEEAKRLR |
in vitro |
|
| pmid |
sentence |
| 8547318 |
EF-1 beta was highly phosphorylated by casein kinase II, with up to 1.3 mol of phosphate incorporated per mol protein. From microsequence analysis and manual Edman degradation, the majority of the phosphate was shown to be present in serine 106 in the peptide DLFGS106DDEEES112EEA. Serine 112 was also phosphorylated by casein kinase II, but to a lesser extent. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
CSNK2A1 |
phosphorylation
|
EEF1B2 |
0.349 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250854 |
Ser106 |
DDIDLFGsDDEEESE |
in vitro |
|
| pmid |
sentence |
| 8547318 |
EF-1 beta was highly phosphorylated by casein kinase II, with up to 1.3 mol of phosphate incorporated per mol protein. From microsequence analysis and manual Edman degradation, the majority of the phosphate was shown to be present in serine 106 in the peptide DLFGS106DDEEES112EEA. Serine 112 was also phosphorylated by casein kinase II, but to a lesser extent. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250855 |
Ser112 |
GSDDEEEsEEAKRLR |
in vitro |
|
| pmid |
sentence |
| 8547318 |
EF-1 beta was highly phosphorylated by casein kinase II, with up to 1.3 mol of phosphate incorporated per mol protein. From microsequence analysis and manual Edman degradation, the majority of the phosphate was shown to be present in serine 106 in the peptide DLFGS106DDEEES112EEA. Serine 112 was also phosphorylated by casein kinase II, but to a lesser extent. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
EEF1B2 | form complex 
binding
|
EEF1B complex |
0.821 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269390 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23699257 |
An inactive eEF1A-GDP moiety leaves the ribosome and must be recycled to eEF1A-GTP before binding another aa-tRNA. This GTP exchange process is the function of the nucleotide exchange factor eEF1B complex, which exchanges GDP for GTP to regenerate active eEF1A. The requirement for a guanine nucleotide exchange factor, the eEF1B complex, which in metazoans is composed of the subunits α, δ, and γ (also called eEF1B, eEF1D, and eEF1G, respectively) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
EEF1B2
- 
- 