+ |
AKT | up-regulates
phosphorylation
|
YBX1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-182493 |
Ser102 |
NPRKYLRsVGDGETV |
Homo sapiens |
Breast Cancer Cell |
pmid |
sentence |
19036157 |
Phosphorylation of yb-1 at the serine 102 residue is required for transcriptional activation of growth-enhancing genes, such as egfr. Herein, we illustrate that activated akt binds to and phosphorylates the yb-1 cold shock domain at ser102 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RPS6K | up-regulates
phosphorylation
|
YBX1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252804 |
Ser102 |
NPRKYLRsVGDGETV |
Homo sapiens |
Breast Cancer Cell |
pmid |
sentence |
19036157 |
We therefore conclude that rsk1/rsk2 are novel activators of yb-1, able to phosphorylate the serine 102 residue. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AKT1 | up-regulates
phosphorylation
|
YBX1 |
0.576 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252521 |
Ser102 |
NPRKYLRsVGDGETV |
Homo sapiens |
Breast Cancer Cell |
pmid |
sentence |
19036157 |
Phosphorylation of yb-1 at the serine 102 residue is required for transcriptional activation of growth-enhancing genes, such as egfr. Herein, we illustrate that activated akt binds to and phosphorylates the yb-1 cold shock domain at ser102 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252475 |
Ser102 |
NPRKYLRsVGDGETV |
Homo sapiens |
Breast Cancer Cell |
pmid |
sentence |
15806160 |
Phosphorylation of yb-1 at the serine 102 residue is required for transcriptional activation of growth-enhancing genes, such as egfr. Herein, we illustrate that activated akt binds to and phosphorylates the yb-1 cold shock domain at ser102 |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
RPS6KA1 | up-regulates
phosphorylation
|
YBX1 |
0.56 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-182497 |
Ser102 |
NPRKYLRsVGDGETV |
Homo sapiens |
Breast Cancer Cell |
pmid |
sentence |
19036157 |
We therefore conclude that rsk1/rsk2 are novel activators of yb-1, able to phosphorylate the serine 102 residue. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RPS6KA3 | up-regulates
phosphorylation
|
YBX1 |
0.555 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-182165 |
Ser102 |
NPRKYLRsVGDGETV |
Homo sapiens |
Breast Cancer Cell |
pmid |
sentence |
19036157 |
We therefore conclude that rsk1/rsk2 are novel activators of yb-1, able to phosphorylate the serine 102 residue. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKDC | up-regulates activity
phosphorylation
|
YBX1 |
0.343 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277611 |
Thr89 |
EDVFVHQtAIKKNNP |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
36475703 |
The DNA-PK subunits and YB-1 phosphorylated at T89 were found colocalized suggesting their in vivo interaction.DNA-PK directly phosphorylates YB-1 and, this way, modulates YB-1 function. Point mutation of YB-1 at this residue abrogated the translocation of YB-1 into the nucleus. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
YBX1 | up-regulates quantity by expression
transcriptional regulation
|
ABCB1 |
0.393 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-253873 |
|
|
Homo sapiens |
|
pmid |
sentence |
10644769 |
these results indicate a role for both NF-Y and Sp1 in the transcriptional activation of the MDR1 gene by genotoxic stress, and indicate that YB-1, if involved, is not sufficient to mediate this activation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
YBX1 | down-regulates quantity by repression
transcriptional regulation
|
MMP13 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255615 |
|
|
Homo sapiens |
|
pmid |
sentence |
17822788 |
YB-1 binds to the MMP-13 promoter sequence and represses MMP-13 transactivation via the AP-1 site. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
YBX1 | up-regulates quantity by expression
transcriptional regulation
|
NDRG1 |
0.25 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255612 |
|
|
Homo sapiens |
|
pmid |
sentence |
17072343 |
YB-1 knockdown by siRNA upregulated 344 genes, including MDR1, thymidylate synthetase, S100 calcium binding protein and cyclin B, and downregulated 534 genes, including CXCR4, N-myc downstream regulated gene 1, E-cadherin and phospholipase C. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
YBX1 | down-regulates quantity by repression
transcriptional regulation
|
TYMS |
0.25 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255613 |
|
|
Homo sapiens |
Ovary Cancer Cell |
pmid |
sentence |
17072343 |
YB-1 knockdown by siRNA upregulated 344 genes, including MDR1, thymidylate synthetase, S100 calcium binding protein and cyclin B, and downregulated 534 genes, including CXCR4, N-myc downstream regulated gene 1, E-cadherin and phospholipase C. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
YBX1 | down-regulates quantity by repression
transcriptional regulation
|
ABCB1 |
0.393 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255614 |
|
|
Homo sapiens |
Ovary Cancer Cell |
pmid |
sentence |
17072343 |
YB-1 knockdown by siRNA upregulated 344 genes, including MDR1, thymidylate synthetase, S100 calcium binding protein and cyclin B, and downregulated 534 genes, including CXCR4, N-myc downstream regulated gene 1, E-cadherin and phospholipase C. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SCF-betaTRCP | down-regulates quantity by destabilization
polyubiquitination
|
YBX1 |
0.327 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271606 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
16797541 |
Here we identify FBX33 as a component of an SCF E3-ubiquitin ligase that targets the multifunctional regulator Y-box binding protein 1 (YB-1)/dbpB/p50 for polyubiquitination and destruction by the proteasome. By targeting YB-1 for proteasomal degradation, FBX33 negatively interferes with YB-1 mediated functions. FBX33 recruits Skp-1/Cul1 to YB-1 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RBBP6 | down-regulates quantity by destabilization
ubiquitination
|
YBX1 |
0.322 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271773 |
|
|
Homo sapiens |
|
pmid |
sentence |
18851979 |
RBBP6 interacts with multifunctional protein YB-1 through its RING finger domain, leading to ubiquitination and proteosomal degradation of YB-1 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
YBX1 | up-regulates quantity by expression
transcriptional regulation
|
CDH1 |
0.329 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255610 |
|
|
Homo sapiens |
Ovary Cancer Cell |
pmid |
sentence |
17072343 |
YB-1 knockdown by siRNA upregulated 344 genes, including MDR1, thymidylate synthetase, S100 calcium binding protein and cyclin B, and downregulated 534 genes, including CXCR4, N-myc downstream regulated gene 1, E-cadherin and phospholipase C. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
YBX1 | up-regulates quantity by expression
transcriptional regulation
|
CXCR4 |
0.272 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255611 |
|
|
Homo sapiens |
|
pmid |
sentence |
17072343 |
YB-1 knockdown by siRNA upregulated 344 genes, including MDR1, thymidylate synthetase, S100 calcium binding protein and cyclin B, and downregulated 534 genes, including CXCR4, N-myc downstream regulated gene 1, E-cadherin and phospholipase C. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FBXO33 | down-regulates quantity by destabilization
binding
|
YBX1 |
0.39 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271604 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
16797541 |
Here we identify FBX33 as a component of an SCF E3-ubiquitin ligase that targets the multifunctional regulator Y-box binding protein 1 (YB-1)/dbpB/p50 for polyubiquitination and destruction by the proteasome. By targeting YB-1 for proteasomal degradation, FBX33 negatively interferes with YB-1 mediated functions. FBX33 recruits Skp-1/Cul1 to YB-1 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MECP2 | up-regulates activity
binding
|
YBX1 |
0.521 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277700 |
|
|
|
|
pmid |
sentence |
16251272 |
In this study, we show that MeCP2 interacts with the RNA-binding protein Y box-binding protein 1 and regulates splicing of reporter minigenes. Importantly, we found aberrant alternative splicing patterns in a mouse model of RTT. Thus, we uncovered a previously uncharacterized function of MeCP2 that involves regulation of splicing, in addition to its role as a transcriptional repressor. |
|
Publications: |
1 |