| + |
ERK1/2 | up-regulates quantity by stabilization 
phosphorylation
|
PCBP2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262668 |
Ser173 |
MLETLSQsPPKGVTI |
Mus musculus |
K-562 Cell |
| pmid |
sentence |
| 17475908 |
All together, these data indicate that ERK-dependent phosphorylation of hnRNP-E2 at serines 173, 189, and 272, and threonine 213 is responsible for increased hnRNP-E2 protein stability in BCR/ABL-transformed cells. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
MAPK3 | up-regulates quantity by stabilization
phosphorylation
|
PCBP2 |
0.329 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262914 |
Ser173 |
MLETLSQsPPKGVTI |
Homo sapiens |
K-562 Cell |
| pmid |
sentence |
| 17475908 |
We also identified 4 hnRNP-E2 MAPKERK1/2 phosphorylation sites and demonstrated that hnRNP-E2 is a bona fide MAPKERK1/2 substrate and that MAPKERK1/2-dependent phosphorylation of hnRNP-E2 at these amino acid residues is essential for increased hnRNP-E2 expression in BCR/ABL-expressing cells. Serine/threonine to alanine substitution abolishes hnRNP-E2 phosphorylation and markedly decreases its stability in BCR/ABL-expressing myeloid precursors. Consistent with the existence of a BCR/ABL-MAPK pathway that posttranslationally regulates hnRNP-E2 expression, sequence analysis of hnRNP-E2 revealed the presence of 4 consensus ERK phosphorylation sites (S/T-P)35,36 at amino acid residues 173, 189, 213, and 272 (Figure 2B). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262915 |
Ser189 |
YRPKPSSsPVIFAGG |
Homo sapiens |
|
| pmid |
sentence |
| 17475908 |
We also identified 4 hnRNP-E2 MAPKERK1/2 phosphorylation sites and demonstrated that hnRNP-E2 is a bona fide MAPKERK1/2 substrate and that MAPKERK1/2-dependent phosphorylation of hnRNP-E2 at these amino acid residues is essential for increased hnRNP-E2 expression in BCR/ABL-expressing cells. Serine/threonine to alanine substitution abolishes hnRNP-E2 phosphorylation and markedly decreases its stability in BCR/ABL-expressing myeloid precursors. Consistent with the existence of a BCR/ABL-MAPK pathway that posttranslationally regulates hnRNP-E2 expression, sequence analysis of hnRNP-E2 revealed the presence of 4 consensus ERK phosphorylation sites (S/T-P)35,36 at amino acid residues 173, 189, 213, and 272 (Figure 2B). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262916 |
Ser272 |
FSGIESSsPEVKGYW |
Homo sapiens |
|
| pmid |
sentence |
| 17475908 |
We also identified 4 hnRNP-E2 MAPKERK1/2 phosphorylation sites and demonstrated that hnRNP-E2 is a bona fide MAPKERK1/2 substrate and that MAPKERK1/2-dependent phosphorylation of hnRNP-E2 at these amino acid residues is essential for increased hnRNP-E2 expression in BCR/ABL-expressing cells. Serine/threonine to alanine substitution abolishes hnRNP-E2 phosphorylation and markedly decreases its stability in BCR/ABL-expressing myeloid precursors. Consistent with the existence of a BCR/ABL-MAPK pathway that posttranslationally regulates hnRNP-E2 expression, sequence analysis of hnRNP-E2 revealed the presence of 4 consensus ERK phosphorylation sites (S/T-P)35,36 at amino acid residues 173, 189, 213, and 272 (Figure 2B). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262917 |
Thr213 |
SASFPHTtPSMCLNP |
Homo sapiens |
K-562 Cell |
| pmid |
sentence |
| 17475908 |
We also identified 4 hnRNP-E2 MAPKERK1/2 phosphorylation sites and demonstrated that hnRNP-E2 is a bona fide MAPKERK1/2 substrate and that MAPKERK1/2-dependent phosphorylation of hnRNP-E2 at these amino acid residues is essential for increased hnRNP-E2 expression in BCR/ABL-expressing cells. Serine/threonine to alanine substitution abolishes hnRNP-E2 phosphorylation and markedly decreases its stability in BCR/ABL-expressing myeloid precursors. Consistent with the existence of a BCR/ABL-MAPK pathway that posttranslationally regulates hnRNP-E2 expression, sequence analysis of hnRNP-E2 revealed the presence of 4 consensus ERK phosphorylation sites (S/T-P)35,36 at amino acid residues 173, 189, 213, and 272 (Figure 2B). |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
MAPK1 | up-regulates quantity by stabilization
phosphorylation
|
PCBP2 |
0.324 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262910 |
Ser173 |
MLETLSQsPPKGVTI |
Homo sapiens |
|
| pmid |
sentence |
| 17475908 |
We also identified 4 hnRNP-E2 MAPKERK1/2 phosphorylation sites and demonstrated that hnRNP-E2 is a bona fide MAPKERK1/2 substrate and that MAPKERK1/2-dependent phosphorylation of hnRNP-E2 at these amino acid residues is essential for increased hnRNP-E2 expression in BCR/ABL-expressing cells. Serine/threonine to alanine substitution abolishes hnRNP-E2 phosphorylation and markedly decreases its stability in BCR/ABL-expressing myeloid precursors. Consistent with the existence of a BCR/ABL-MAPK pathway that posttranslationally regulates hnRNP-E2 expression, sequence analysis of hnRNP-E2 revealed the presence of 4 consensus ERK phosphorylation sites (S/T-P)35,36 at amino acid residues 173, 189, 213, and 272 (Figure 2B). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262911 |
Ser189 |
YRPKPSSsPVIFAGG |
Homo sapiens |
K-562 Cell |
| pmid |
sentence |
| 17475908 |
We also identified 4 hnRNP-E2 MAPKERK1/2 phosphorylation sites and demonstrated that hnRNP-E2 is a bona fide MAPKERK1/2 substrate and that MAPKERK1/2-dependent phosphorylation of hnRNP-E2 at these amino acid residues is essential for increased hnRNP-E2 expression in BCR/ABL-expressing cells. Serine/threonine to alanine substitution abolishes hnRNP-E2 phosphorylation and markedly decreases its stability in BCR/ABL-expressing myeloid precursors. Consistent with the existence of a BCR/ABL-MAPK pathway that posttranslationally regulates hnRNP-E2 expression, sequence analysis of hnRNP-E2 revealed the presence of 4 consensus ERK phosphorylation sites (S/T-P)35,36 at amino acid residues 173, 189, 213, and 272 (Figure 2B). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262912 |
Ser272 |
FSGIESSsPEVKGYW |
Homo sapiens |
K-562 Cell |
| pmid |
sentence |
| 17475908 |
We also identified 4 hnRNP-E2 MAPKERK1/2 phosphorylation sites and demonstrated that hnRNP-E2 is a bona fide MAPKERK1/2 substrate and that MAPKERK1/2-dependent phosphorylation of hnRNP-E2 at these amino acid residues is essential for increased hnRNP-E2 expression in BCR/ABL-expressing cells. Serine/threonine to alanine substitution abolishes hnRNP-E2 phosphorylation and markedly decreases its stability in BCR/ABL-expressing myeloid precursors. Consistent with the existence of a BCR/ABL-MAPK pathway that posttranslationally regulates hnRNP-E2 expression, sequence analysis of hnRNP-E2 revealed the presence of 4 consensus ERK phosphorylation sites (S/T-P)35,36 at amino acid residues 173, 189, 213, and 272 (Figure 2B). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262913 |
Thr213 |
SASFPHTtPSMCLNP |
Homo sapiens |
K-562 Cell |
| pmid |
sentence |
| 17475908 |
We also identified 4 hnRNP-E2 MAPKERK1/2 phosphorylation sites and demonstrated that hnRNP-E2 is a bona fide MAPKERK1/2 substrate and that MAPKERK1/2-dependent phosphorylation of hnRNP-E2 at these amino acid residues is essential for increased hnRNP-E2 expression in BCR/ABL-expressing cells. Serine/threonine to alanine substitution abolishes hnRNP-E2 phosphorylation and markedly decreases its stability in BCR/ABL-expressing myeloid precursors. Consistent with the existence of a BCR/ABL-MAPK pathway that posttranslationally regulates hnRNP-E2 expression, sequence analysis of hnRNP-E2 revealed the presence of 4 consensus ERK phosphorylation sites (S/T-P)35,36 at amino acid residues 173, 189, 213, and 272 (Figure 2B). |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
LPAR | up-regulates quantity by stabilization
phosphorylation
|
PCBP2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262669 |
Ser189 |
YRPKPSSsPVIFAGG |
Mus musculus |
KB Cell |
| pmid |
sentence |
| 17475908 |
All together, these data indicate that ERK-dependent phosphorylation of hnRNP-E2 at serines 173, 189, and 272, and threonine 213 is responsible for increased hnRNP-E2 protein stability in BCR/ABL-transformed cells. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
Ggamma | up-regulates quantity by stabilization
phosphorylation
|
PCBP2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262670 |
Ser272 |
FSGIESSsPEVKGYW |
Mus musculus |
LoVo Cell |
| pmid |
sentence |
| 17475908 |
All together, these data indicate that ERK-dependent phosphorylation of hnRNP-E2 at serines 173, 189, and 272, and threonine 213 is responsible for increased hnRNP-E2 protein stability in BCR/ABL-transformed cells. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
Gbeta | up-regulates quantity by stabilization
phosphorylation
|
PCBP2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262671 |
Thr213 |
SASFPHTtPSMCLNP |
Mus musculus |
Keratinocyte |
| pmid |
sentence |
| 17475908 |
All together, these data indicate that ERK-dependent phosphorylation of hnRNP-E2 at serines 173, 189, and 272, and threonine 213 is responsible for increased hnRNP-E2 protein stability in BCR/ABL-transformed cells. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PCBP2 | up-regulates activity
binding
|
ITCH |
0.599 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260361 |
|
|
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 19881509 |
Only AIP4 associated with PCBP2 and caused MAVS degradation. The interaction between PCBP2 and AIP4 was abrogated when the linker region or WB2 of PCBP2 was deleted, which confirmed our previous data indicating that this region was critical for PCBP2-mediated degradation of MAVS |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NLRX1 | up-regulates activity
binding
|
PCBP2 |
0.411 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260359 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28956771 |
Moreover, poly(rC) binding protein 2 (PCBP2) interacts with NLRX1 to participate in the NLRX1-induced degradation of MAVS and the inhibition of antiviral responses during HCV infection. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PCBP2 | down-regulates quantity by destabilization 
binding
|
MAVS |
0.631 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260360 |
|
|
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 19881509 |
PCBP2 mediates degradation of the adaptor MAVS via the HECT ubiquitin ligase AIP4. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PCBP2
- 
- 