| + |
RPS6KB2 | down-regulates 
phosphorylation
|
MXD1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178594 |
Ser145 |
IERIRMDsIGSTVSS |
Homo sapiens |
|
| pmid |
sentence |
| 18451027 |
In this study, we showed that mad1 is a substrate of p90 ribosomal kinase (rsk) and p70 s6 kinase (s6k). Both rsk and s6k phosphorylate serine 145 of mad1 upon serum or insulin stimulation. Ser-145 phosphorylation of mad1 accelerates the ubiquitination and degradation of mad1 through the 26s proteasome pathway |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KB2 | up-regulates activity 
phosphorylation
|
TARBP2 |
0.341 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274066 |
Ser283 |
ILSLRSCsLGSLGAL |
in vitro |
|
| pmid |
sentence |
| 27407113 |
We demonstrate that S6 kinases can phosphorylate the extended C-terminal domain of TRBP and interact with TRBP in situ in primary cells. TRBP serines 283/286 are essential for S6K-mediated TRBP phosphorylation, optimal expression of TRBP, and the S6K-TRBP interaction in human primary cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274069 |
Ser286 |
LRSCSLGsLGALGPA |
in vitro |
|
| pmid |
sentence |
| 27407113 |
We demonstrate that S6 kinases can phosphorylate the extended C-terminal domain of TRBP and interact with TRBP in situ in primary cells. TRBP serines 283/286 are essential for S6K-mediated TRBP phosphorylation, optimal expression of TRBP, and the S6K-TRBP interaction in human primary cells. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PDPK1 | up-regulates activity
phosphorylation
|
RPS6KB2 |
0.595 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250371 |
Ser370 |
TRQTPVDsPDDTALS |
in vitro |
|
| pmid |
sentence |
| 11733037 |
Mutational analysis revealed that the phosphorylation of Thr241 and Thr401 in p70beta1 was indispensable for the kinase activity. In contrast, a p70beta1 mutant in which Ser383 was substituted with Gly (S383G) still retained nearly the half maximal activity. Sequential phosphorylation of wild-type and S383G mutant of p70beta1 with mTOR and 3-phosphoinositide-dependent protein kinase 1 (PDK1) in vitro synergistically activated their kinase activities. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250273 |
Thr228 |
HEGAVTHtFCGTIEY |
in vitro |
|
| pmid |
sentence |
| 11733037 |
Mutational analysis revealed that the phosphorylation of Thr241 and Thr401 in p70beta1 was indispensable for the kinase activity. In contrast, a p70beta1 mutant in which Ser383 was substituted with Gly (S383G) still retained nearly the half maximal activity. Sequential phosphorylation of wild-type and S383G mutant of p70beta1 with mTOR and 3-phosphoinositide-dependent protein kinase 1 (PDK1) in vitro synergistically activated their kinase activities. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250272 |
Thr388 |
NQAFLGFtYVAPSVL |
in vitro |
|
| pmid |
sentence |
| 11733037 |
Mutational analysis revealed that the phosphorylation of Thr241 and Thr401 in p70beta1 was indispensable for the kinase activity. In contrast, a p70beta1 mutant in which Ser383 was substituted with Gly (S383G) still retained nearly the half maximal activity. Sequential phosphorylation of wild-type and S383G mutant of p70beta1 with mTOR and 3-phosphoinositide-dependent protein kinase 1 (PDK1) in vitro synergistically activated their kinase activities. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
MTOR | up-regulates activity
phosphorylation
|
RPS6KB2 |
0.831 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250293 |
Ser370 |
TRQTPVDsPDDTALS |
in vitro |
|
| pmid |
sentence |
| 11733037 |
In vitro phosphorylation and activation of p70β by mTOR and PDK1. replacement of Ser383 to Gly (S383G) reduced but still retained nearly half of the kinase activity of the wild-type. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250294 |
Thr228 |
HEGAVTHtFCGTIEY |
in vitro |
|
| pmid |
sentence |
| 11733037 |
In vitro phosphorylation and activation of p70β by mTOR and PDK1. We observed that the replacement of either Thr241 or Thr401 to Ala in p70β1(T241A, T401A) severely decreased the kinase activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250295 |
Thr388 |
NQAFLGFtYVAPSVL |
in vitro |
|
| pmid |
sentence |
| 11733037 |
In vitro phosphorylation and activation of p70β by mTOR and PDK1. We observed that the replacement of either Thr241 or Thr401 to Ala in p70β1(T241A, T401A) severely decreased the kinase activity. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
PRKCB |
phosphorylation
|
RPS6KB2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-97283 |
Ser473 |
PPSGTKKsKRGRGRP |
Homo sapiens |
|
| pmid |
sentence |
| 12529391 |
Pkc-mediated phosphorylation at s486 does not affect s6k activity but eliminates the function of its nuclear localization signal and causes retention of an activated form of the kinase in the cytoplasm. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCA |
phosphorylation
|
RPS6KB2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-97279 |
Ser473 |
PPSGTKKsKRGRGRP |
Homo sapiens |
|
| pmid |
sentence |
| 12529391 |
Pkc-mediated phosphorylation at s486 does not affect s6k activity but eliminates the function of its nuclear localization signal and causes retention of an activated form of the kinase in the cytoplasm. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCE |
phosphorylation
|
RPS6KB2 |
0.478 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-97291 |
Ser473 |
PPSGTKKsKRGRGRP |
Homo sapiens |
|
| pmid |
sentence |
| 12529391 |
Pkc-mediated phosphorylation at s486 does not affect s6k activity but eliminates the function of its nuclear localization signal and causes retention of an activated form of the kinase in the cytoplasm. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCG |
phosphorylation
|
RPS6KB2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-97295 |
Ser473 |
PPSGTKKsKRGRGRP |
Homo sapiens |
|
| pmid |
sentence |
| 12529391 |
Pkc-mediated phosphorylation at s486 does not affect s6k activity but eliminates the function of its nuclear localization signal and causes retention of an activated form of the kinase in the cytoplasm. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCD |
phosphorylation
|
RPS6KB2 |
0.262 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-97287 |
Ser473 |
PPSGTKKsKRGRGRP |
Homo sapiens |
|
| pmid |
sentence |
| 12529391 |
Pkc-mediated phosphorylation at s486 does not affect s6k activity but eliminates the function of its nuclear localization signal and causes retention of an activated form of the kinase in the cytoplasm. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PDPK1 | up-regulates
phosphorylation
|
RPS6KB2 |
0.595 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-55371 |
Thr228 |
HEGAVTHtFCGTIEY |
Homo sapiens |
|
| pmid |
sentence |
| 9445476 |
A regulatory link between p70s6k and pkb was demonstrated, as pdk1 was found to selectively phosphorylate p70s6k at thr229. More importantly, pdk1 activated p70s6k in vitro and in vivo, whereas the catalytically inactive pdk1 blocked insulin-induced activation of p70s6k. one of the most studied signalling events controlled by ptdins(3,4,5)p3, comprises the activation of a group of agc family protein kinases, including isoforms of protein kinase b (pkb)/akt, p70 ribosomal s6 kinase (s6k), serum- and glucocorticoid-induced protein kinase (sgk) and protein kinase c (pkc), which play crucial roles in regulating physiological processes relevant to metabolism, growth, proliferation and survival. Here, we review recent biochemical, genetic and structural studies on the 3-phosphoinositide-dependent protein kinase-1 (pdk1), which phosphorylates and activates the agc kinase members regulated by pi 3-kinase. We also discuss whether inhibitors of pdk1 might have chemotherapeutic potential in the treatment of cancers in which the pdk1-regulated agc kinases are constitutively activated. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-126076 |
Thr228 |
HEGAVTHtFCGTIEY |
Homo sapiens |
|
| pmid |
sentence |
| 15209375 |
A regulatory link between p70s6k and pkb was demonstrated, as pdk1 was found to selectively phosphorylate p70s6k at thr229. More importantly, pdk1 activated p70s6k in vitro and in vivo, whereas the catalytically inactive pdk1 blocked insulin-induced activation of p70s6k. one of the most studied signalling events controlled by ptdins(3,4,5)p3, comprises the activation of a group of agc family protein kinases, including isoforms of protein kinase b (pkb)/akt, p70 ribosomal s6 kinase (s6k), serum- and glucocorticoid-induced protein kinase (sgk) and protein kinase c (pkc), which play crucial roles in regulating physiological processes relevant to metabolism, growth, proliferation and survival. Here, we review recent biochemical, genetic and structural studies on the 3-phosphoinositide-dependent protein kinase-1 (pdk1), which phosphorylates and activates the agc kinase members regulated by pi 3-kinase. We also discuss whether inhibitors of pdk1 might have chemotherapeutic potential in the treatment of cancers in which the pdk1-regulated agc kinases are constitutively activated. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
SRC |
phosphorylation
|
RPS6KB2 |
0.347 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-146292 |
Tyr45 |
GLEPVGHyEEVELTE |
Homo sapiens |
|
| pmid |
sentence |
| 16640565 |
Src kinase phosphorylates s6k in the n-terminus. tyrosine y39/45 in s6k1/2 is a substrate for src kinase in vitro. tyrosine y39/45 in s6k1/2 is a substrate for src kinase in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KB2 | down-regulates
phosphorylation
|
PDCD4 |
0.45 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160992 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 18296647 |
Both akt and p70(s6k) phosphorylate pdcd4, allowing for binding of the e3-ubiquitin ligase beta-trcp and consequently ubiquitylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Skin |
| + |
MTOR | up-regulates
phosphorylation
|
RPS6KB2 |
0.831 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-201541 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23486913 |
These results indicate that arg, leu, and gln act coordinately to stimulate proliferation of ptr cells through activation of the mtor-rps6k-rps6-eif4ebp1 signal transduction pathway. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-154821 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17510057 |
In response to insulin and nutrients, mtorc1, consisting of mtor, raptor (regulatory-associated protein of mtor), and mlst8, is activated and phosphorylates eukaryotic initiation factor 4e-binding protein (4ebp) and p70 s6 kinase to promote protein synthesis and cell size. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
TSC2 | down-regulates 
|
RPS6KB2 |
0.542 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-91395 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12172553 |
Here, we show that tsc1-tsc2 inhibits the p70 ribosomal protein s6 kinase 1 (an activator of translation) and activates the eukaryotic initiation factor 4e binding protein 1 (4e-bp1, an inhibitor of translational initiation). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
mTORC1 | up-regulates
phosphorylation
|
RPS6KB2 |
0.586 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217074 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17510057 |
In response to insulin and nutrients, mtorc1, consisting of mtor, raptor (regulatory-associated protein of mtor), and mlst8, is activated and phosphorylates eukaryotic initiation factor 4e-binding protein (4ebp) and p70 s6 kinase to promote protein synthesis and cell size. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
RPS6KB2
- 
- 