| + |
DDX3X | up-regulates activity 
binding
|
PABPC1 |
0.588 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269194 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21883093 |
In the present study, we indentified the SG marker PABP1 [poly(A)-binding protein 1] as another direct interaction partner of DDX3. Interestingly, down-regulation of DDX3 interfered with SG assembly, led to nuclear accumulation of PABP1 and reduced cell viability following stress. Conversely, supplementation with a shRNA (short hairpin RNA)-resistant DDX3 restored SG formation, the translocation of PABP1 into SGs and cell survival. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269201 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21883093 |
In the present study, we indentified the SG marker PABP1 [poly(A)-binding protein 1] as another direct interaction partner of DDX3. Interestingly, down-regulation of DDX3 interfered with SG assembly, led to nuclear accumulation of PABP1 and reduced cell viability following stress. Conversely, supplementation with a shRNA (short hairpin RNA)-resistant DDX3 restored SG formation, the translocation of PABP1 into SGs and cell survival. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
LARP4B | up-regulates activity
binding
|
PABPC1 |
0.571 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260940 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20573744 |
Here we show that LARP4B is a cytoplasmic protein that co-sediments with polysomes and accumulates upon stress induction in stress granules. Biochemical studies further show that the protein interacts with two key factors of the translational machinery, namely, the cytoplasmic poly(A) binding protein (PABPC1) and the receptor for activated C Kinase (RACK1). The biochemical and functional data of LARP4B presented in this study suggest a possible mode of action of LARP4B in translation. Assuming that LARP4B interacts with mRNA-associated PABPC1 and RACK1 simultaneously, it may form a bridge between the 3′ end of mRNAs and the initiating ribosome. This process would lead to mRNA circularization, possibly in an analogous way as it has been described for PABPC1 and eIF4G, the scaffold protein of the cap-binding complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, SARS-CoV STRESS GRANULES |
| + |
PABPC1 | up-regulates quantity by stabilization
binding
|
messenger RNA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268318 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25480299 |
As poly(A)+ mRNAs are associated with poly(A) binding protein (PABP) in cells|his result suggests that PABPC1 binds preferentially to long poly(A) tails and protects them from TUT4/7 and thereby enhances the selectivity of uridylation according to poly(A) tail length. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | mRNA maturation, mRNA maturation |
| + |
NFX1 | up-regulates activity
binding
|
PABPC1 |
0.35 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-226011 |
|
|
Homo sapiens |
HFK Cell |
| pmid |
sentence |
| 17267499 |
NFX1-123 augments the activation of hTERT expression through interactions with PABPCs |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PABPC1 | up-regulates activity
binding
|
NFX1 |
0.35 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261052 |
|
|
Homo sapiens |
Culture Condition:3-hydroxybenzoate-grown Cell |
| pmid |
sentence |
| 17267499 |
We identifiednew protein partners of NFX1-123, including several cytoplasmic poly(A) binding proteins (PABPCs) thatinteracted with NFX1-123 through its N-terminal PAM2 motif. Central to our findings were our observations that PABPCs copurify with NFX1-123, that a PAM2 motif is present in NFX1, and this motif and the PABPCs are important in the enhancement of hTERT activity by NFX1-123. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MKRN1 | up-regulates activity
ubiquitination
|
PABPC1 |
0.357 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272215 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 31640799 |
We show that MKRN1 directly binds to the cytoplasmic poly(A)-binding protein (PABPC1) and associates with polysomes. MKRN1 is positioned upstream of poly(A) tails in mRNAs in a PABPC1-dependent manner. Ubiquitin remnant profiling and in vitro ubiquitylation assays uncover PABPC1 and ribosomal protein RPS10 as direct ubiquitylation substrates of MKRN1.Our data show that MKRN1 associates with polysomes and ubiquitylates RPS10, indicating a role in translational control. We hypothesize that ribosomes encountering the MKRN1-PABPC1 complex are stalled, possibly via ubiquitylation of RPS10 on K107 and other MKRN1 substrates. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PABPC1 | up-regulates activity
binding
|
EIF4E |
0.799 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260968 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30209168 |
The binding of PABP to mRNA poly(A) tails is followed by interactions with eukaryotic initiation factor (eIF4G) and other translation factors, including eIF4E, to constitute a translation initiation complex, which mediates cellular mRNA circularization and enhances cap-dependent translation by facilitating ribosome recycling |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, SARS-CoV STRESS GRANULES |
| + |
PABPC1 | up-regulates activity
binding
|
eIF4F_complex |
0.82 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260943 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30209168 |
The binding of PABP to mRNA poly(A) tails is followed by interactions with eukaryotic initiation factor (eIF4G) and other translation factors, including eIF4E, to constitute a translation initiation complex, which mediates cellular mRNA circularization and enhances cap-dependent translation by facilitating ribosome recycling |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PABPC1
- 
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