| + |
CDK1 | down-regulates activity 
phosphorylation
|
STIP1 |
0.267 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262729 |
Ser189 |
LLGVDLGsMDEEEEI |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 14754904 |
Inactivation and phosphorylation mimicking of potential phosphorylation sites in mSTI1 altered the nuclear translocation. Mimicking of phosphorylation at the mSTI1 CKII phosphorylation site (S189E) promoted nuclear localization of mSTI1-EGFP. Mimicking phosphorylation at the cdc2 kinase phosphorylation site (T198E) promoted cytoplasmic localization of mSTI1-EGFP at the G1/S-phase transition,whereas removal of this site (T198A) promoted the nuclear localization of mSTI1-EGFP under the same conditions. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262727 |
Thr198 |
DEEEEIAtPPPPPPP |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 14754904 |
Inactivation and phosphorylation mimicking of potential phosphorylation sites in mSTI1 altered the nuclear translocation. Mimicking of phosphorylation at the mSTI1 CKII phosphorylation site (S189E) promoted nuclear localization of mSTI1-EGFP. Mimicking phosphorylation at the cdc2 kinase phosphorylation site (T198E) promoted cytoplasmic localization of mSTI1-EGFP at the G1/S-phase transition,whereas removal of this site (T198A) promoted the nuclear localization of mSTI1-EGFP under the same conditions. A lower level of phosphorylation was observed for the double mutant, suggesting that T332 might also be phosphorylated by cdc2 kinase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262728 |
Thr332 |
KSLAEHRtPDVLKKC |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 14754904 |
Inactivation and phosphorylation mimicking of potential phosphorylation sites in mSTI1 altered the nuclear translocation. Mimicking of phosphorylation at the mSTI1 CKII phosphorylation site (S189E) promoted nuclear localization of mSTI1-EGFP. Mimicking phosphorylation at the cdc2 kinase phosphorylation site (T198E) promoted cytoplasmic localization of mSTI1-EGFP at the G1/S-phase transition,whereas removal of this site (T198A) promoted the nuclear localization of mSTI1-EGFP under the same conditions. A lower level of phosphorylation was observed for the double mutant, suggesting that T332 might also be phosphorylated by cdc2 kinase. |
|
| Publications: |
3 |
Organism: |
Mus Musculus |
| + |
STIP1 | down-regulates activity
binding
|
HSP90AB1 |
0.848 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261412 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 27353360 |
Hsp90 chaperone cycle is tightly regulated by another group of proteins referred to as ‘co-chaperones'. Their stability does not depend on Hsp90 function but they interact with distinct Hsp90 conformational states, providing directionality to the Hsp90 cycle4. Furthermore, certain co-chaperones, such as HOP and Cdc37p50 inhibit the Hsp90 chaperone cycle, assisting in delivery of distinct sets of client proteins (steroid hormone receptors and kinases, respectively) to the Hsp90 chaperone machine. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STIP1 | down-regulates activity
binding
|
HSP90AA1 |
0.932 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261411 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 27353360 |
Hsp90 chaperone cycle is tightly regulated by another group of proteins referred to as ‘co-chaperones'. Their stability does not depend on Hsp90 function but they interact with distinct Hsp90 conformational states, providing directionality to the Hsp90 cycle. Furthermore, certain co-chaperones, such as HOP and Cdc37p50 inhibit the Hsp90 chaperone cycle, assisting in delivery of distinct sets of client proteins (steroid hormone receptors and kinases, respectively) to the Hsp90 chaperone machine. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
STIP1
- 
- 