| + |
GRK2 | up-regulates 
phosphorylation
|
RPLP2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-94254 |
Ser102 |
KDEKKEEsEESDDDM |
Homo sapiens |
|
| pmid |
sentence |
| 12379128 |
The phosphorylation sites in grk2-phosphorylated p2 are identified (s102 and s105) and are identical to the sites known to regulate p2 activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-94258 |
Ser105 |
KKEESEEsDDDMGFG |
Homo sapiens |
|
| pmid |
sentence |
| 12379128 |
The phosphorylation sites in grk2-phosphorylated p2 are identified (s102 and s105) and are identical to the sites known to regulate p2 activity. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
RPLP2 | form complex 
binding
|
60S cytosolic large ribosomal subunit |
0.809 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262449 |
|
|
in vitro |
|
| pmid |
sentence |
| 25901680 |
Here we report the near-atomic structure of the human ribosome derived from high-resolution single-particle cryo-electron microscopy and atomic model building. The structure has an average resolution of 3.6 Å, reaching 2.9 Å resolution in the most stable regions. |The human ribosome (80S) has a molecular weight of 4.3 MDa: the large subunit (60S) consists of 28S, 5S and 5.8S rRNAs and 47 proteins, while the small subunit (40S) possesses a single 18S rRNA chain and 33 pro- teins. |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
RPLP2
- 
- 