+ |
PRKCD | up-regulates
phosphorylation
|
RPS3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-137967 |
Ser6 |
sKKRKFVA |
Homo sapiens |
|
pmid |
sentence |
15950189 |
It has been shown previously that ribosomal protein s3 (rps3) |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-182619 |
Ser6 |
sKKRKFVA |
Homo sapiens |
|
pmid |
sentence |
19059439 |
Here we show that pkcdelta phosphorylates rps3 resulting in its mobilization in the nucleus to repair damaged dna. pkc? Kinase assay then indicated that at least two residues, serine 6 and threonine 221, are phosphorylated by pkc? |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-182623 |
Thr221 |
KDEILPTtPISEQKG |
Homo sapiens |
|
pmid |
sentence |
19059439 |
Here we show that pkcdelta phosphorylates rps3 resulting in its mobilization in the nucleus to repair damaged dna. Phosphorylated rps3 was only detected in non-ribosomal rps3 and the repair endonuclease activity of rps3 was increased by its phosphorylation. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
PPP2CA | down-regulates
dephosphorylation
|
RPS3 |
0.402 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-137963 |
Ser6 |
sKKRKFVA |
Homo sapiens |
|
pmid |
sentence |
15950189 |
We identified that pp2a interacts with wild-type rps3, but not with mutants (s6a/t221a) (fig. 8), and that it associates with the n-terminal region of rps3 (fig. 2). From our results presented here, we conclude that pp2a is involved in the dephosphorylation of phosphorylated rps3 by pkc, and that serine 6 on the n-terminal region of rps3 appears to mediate the pp2a recruitment. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKCD | up-regulates activity
phosphorylation
|
RPS3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260894 |
Ser6 |
sKKRKFVA |
Homo sapiens |
|
pmid |
sentence |
19059439 |
Here we show that PKCδ phosphorylates rpS3 resulting in its mobilization in the nucleus to repair damaged DNA |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260895 |
Thr221 |
KDEILPTtPISEQKG |
Homo sapiens |
|
pmid |
sentence |
19059439 |
Here we show that PKCδ phosphorylates rpS3 resulting in its mobilization in the nucleus to repair damaged DNA |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CDK1 | up-regulates
phosphorylation
|
RPS3 |
0.371 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-176131 |
Thr221 |
KDEILPTtPISEQKG |
Homo sapiens |
|
pmid |
sentence |
21871177 |
These results suggest that the phosphorylation of rps3 by cdk1 occurs at thr221 during g2/m phase and, moreover, that this event is important for nuclear accumulation of rps3. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK1 |
phosphorylation
|
RPS3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-136075 |
Thr42 |
SGVEVRVtPTRTEII |
Homo sapiens |
|
pmid |
sentence |
15950189 |
Erk phosphorylates threonine 42 residue of ribosomal protein s3. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK1 | up-regulates
phosphorylation
|
RPS3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-137955 |
Thr42 |
SGVEVRVtPTRTEII |
Homo sapiens |
|
pmid |
sentence |
15950189 |
Erk phosphorylates threonine 42 residue of ribosomal protein s3. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK3 | up-regulates
phosphorylation
|
RPS3 |
0.359 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-137175 |
Thr42 |
SGVEVRVtPTRTEII |
Homo sapiens |
|
pmid |
sentence |
15950189 |
Erk phosphorylates threonine 42 residue of ribosomal protein s3. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK3 |
phosphorylation
|
RPS3 |
0.359 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-137959 |
Thr42 |
SGVEVRVtPTRTEII |
Homo sapiens |
|
pmid |
sentence |
15950189 |
Erk phosphorylates threonine 42 residue of ribosomal protein s3. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AKT1 | up-regulates activity
phosphorylation
|
RPS3 |
0.377 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-259815 |
Thr70 |
GRRIRELtAVVQKRF |
Rattus norvegicus |
PC12-AC Cell |
pmid |
sentence |
20605787 |
Here, we show that human RPS3 is a physiological target of Akt kinase and a novel mediator of neuronal apoptosis. NGF stimulation resulted in phosphorylation of threonine 70 of RPS3 by Akt, and this phosphorylation was required for Akt binding to RPS3.our experiment demonstrated that Akt up-regulates the endonuclease activity of RPS3 via phosphorylation and led us to believe that Akt phosphorylation of RPS3 after DNA damage is an antiapoptotic signal or a molecular switch that extends the life of a cell after DNA damage. |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |
+ |
AKT | up-regulates activity
phosphorylation
|
RPS3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-259816 |
Thr70 |
GRRIRELtAVVQKRF |
Rattus norvegicus |
PC12-AC Cell |
pmid |
sentence |
20605787 |
Here, we show that human RPS3 is a physiological target of Akt kinase and a novel mediator of neuronal apoptosis. NGF stimulation resulted in phosphorylation of threonine 70 of RPS3 by Akt, and this phosphorylation was required for Akt binding to RPS3.our experiment demonstrated that Akt up-regulates the endonuclease activity of RPS3 via phosphorylation and led us to believe that Akt phosphorylation of RPS3 after DNA damage is an antiapoptotic signal or a molecular switch that extends the life of a cell after DNA damage. |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |
+ |
ERK1/2 |
phosphorylation
|
RPS3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270145 |
|
|
Homo sapiens |
|
pmid |
sentence |
15950189 |
Erk phosphorylates threonine 42 residue of ribosomal protein s3. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RPS3 | form complex
binding
|
40S cytosolic small ribosomal subunit |
0.889 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262421 |
|
|
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 |
+ |
Gbeta |
phosphorylation
|
RPS3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270019 |
|
|
Homo sapiens |
|
pmid |
sentence |
15950189 |
Erk phosphorylates threonine 42 residue of ribosomal protein s3. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Host translation inhibitor nsp1 | down-regulates activity
binding
|
RPS3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262507 |
|
|
in vitro |
|
pmid |
sentence |
33188728 |
Nsp1 Locks the 40S in a Conformation Incompatible with mRNA Loading and Disrupts Initiation Factor Binding. Molecular interactions between C-Nsp1 and 40S ribosome components, including uS3, h18, and uS5. |
|
Publications: |
1 |
Organism: |
In Vitro |