Relation Results

Summary

Name RPS6KB2
Full Name Ribosomal protein S6 kinase beta-2
Synonyms S6K-beta-2, S6K2, 70 kDa ribosomal protein S6 kinase 2, P70S6K2, p70-S6K 2, S6 kinase-related kinase, SRK, Serine/threonine-protein kinase 14B, p70 ribosomal S6 kinase beta, S6K-beta, p70 S6 kinase beta, p70 S6K-beta, p70 S6KB, p70-beta | STK14B
Primary ID Q9UBS0
Links - -
Type protein
Relations 22
Function Phosphorylates specifically ribosomal protein S6 (PubMed:29750193). Seems to act downstream of mTOR signaling in response to growth factors and nutrie ...
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Type: Score: Layout: SPV 
0.20.3360.6060.8340.20.20.20.2590.4680.3420.4420.530.595RPS6KB2MXD1TARBP2PDPK1MTORPRKCBPRKCAPRKCGPRKCDPRKCESRCPDCD4TSC2mTORC1

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▶Modifications Tables

Relations
Regulator
Mechanism
target
score ℹ
+ RPS6KB2down-regulates img/direct_inhibition.png phosphorylation MXD1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-178594 Ser145 IERIRMDsIGSTVSS Homo sapiens
pmid sentence
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
+ RPS6KB2up-regulates activity img/direct-activation.png phosphorylation TARBP2 0.336
Identifier Residue Sequence Organism Cell Line
SIGNOR-274066 Ser283 ILSLRSCsLGSLGAL in vitro
pmid sentence
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
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
+ PDPK1up-regulates activity img/direct-activation.png phosphorylation RPS6KB2 0.606
Identifier Residue Sequence Organism Cell Line
SIGNOR-250371 Ser370 TRQTPVDsPDDTALS in vitro
pmid sentence
 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
 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
 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
+ MTORup-regulates activity img/direct-activation.png phosphorylation RPS6KB2 0.834
Identifier Residue Sequence Organism Cell Line
SIGNOR-250293 Ser370 TRQTPVDsPDDTALS in vitro
pmid sentence
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
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
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 img/unknown.png phosphorylation RPS6KB2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-97283 Ser473 PPSGTKKsKRGRGRP Homo sapiens
pmid sentence
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 img/unknown.png phosphorylation RPS6KB2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-97279 Ser473 PPSGTKKsKRGRGRP Homo sapiens
pmid sentence
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 img/unknown.png phosphorylation RPS6KB2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-97295 Ser473 PPSGTKKsKRGRGRP Homo sapiens
pmid sentence
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 img/unknown.png phosphorylation RPS6KB2 0.259
Identifier Residue Sequence Organism Cell Line
SIGNOR-97287 Ser473 PPSGTKKsKRGRGRP Homo sapiens
pmid sentence
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 img/unknown.png phosphorylation RPS6KB2 0.468
Identifier Residue Sequence Organism Cell Line
SIGNOR-97291 Ser473 PPSGTKKsKRGRGRP Homo sapiens
pmid sentence
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
+ PDPK1up-regulates img/direct-activation.png phosphorylation RPS6KB2 0.606
Identifier Residue Sequence Organism Cell Line
SIGNOR-126076 Thr228 HEGAVTHtFCGTIEY Homo sapiens
pmid sentence
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-55371 Thr228 HEGAVTHtFCGTIEY Homo sapiens
pmid sentence
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 img/unknown.png phosphorylation RPS6KB2 0.342
Identifier Residue Sequence Organism Cell Line
SIGNOR-146292 Tyr45 GLEPVGHyEEVELTE Homo sapiens
pmid sentence
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
+ RPS6KB2down-regulates img/direct_inhibition.png phosphorylation PDCD4 0.442
Identifier Residue Sequence Organism Cell Line
SIGNOR-160992 Homo sapiens HEK-293 Cell
pmid sentence
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
+ MTORup-regulates img/direct-activation.png phosphorylation RPS6KB2 0.834
Identifier Residue Sequence Organism Cell Line
SIGNOR-201541 Homo sapiens
pmid sentence
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
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
+ TSC2down-regulates img/indirect_inhibition.png RPS6KB2 0.53
Identifier Residue Sequence Organism Cell Line
SIGNOR-91395 Homo sapiens
pmid sentence
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
+ mTORC1up-regulates img/direct-activation.png phosphorylation RPS6KB2 0.595
Identifier Residue Sequence Organism Cell Line
SIGNOR-217074 Homo sapiens
pmid sentence
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
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