| + |
RPS6KA1 | up-regulates 
phosphorylation
|
YBX1 |
0.545 |
| 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 |
| + |
RPS6KA1 | down-regulates activity 
phosphorylation
|
H3-3A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-70428 |
Ser11 |
TKQTARKsTGGKAPR |
Homo sapiens |
|
| pmid |
sentence |
| 10464286 |
Phosphorylation at ser-11 (h3s10ph) by rps6ka4 and rps6ka5 is important during interphase because it enables the transcription of genes following external stimulation, like mitogens, stress, growth factors or uv irradiation and result in the activation of genes, such as c-fos and c-jun. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-119221 |
Ser11 |
TKQTARKsTGGKAPR |
Homo sapiens |
|
| pmid |
sentence |
| 14625384 |
Phosphorylation at ser-11 (h3s10ph) by rps6ka4 and rps6ka5 is important during interphase because it enables the transcription of genes following external stimulation, like mitogens, stress, growth factors or uv irradiation and result in the activation of genes, such as c-fos and c-jun. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138467 |
Ser11 |
TKQTARKsTGGKAPR |
Homo sapiens |
|
| pmid |
sentence |
| 15994958 |
Phosphorylation at ser-11 (h3s10ph) by rps6ka4 and rps6ka5 is important during interphase because it enables the transcription of genes following external stimulation, like mitogens, stress, growth factors or uv irradiation and result in the activation of genes, such as c-fos and c-jun. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
RPS6KA1 | up-regulates activity
phosphorylation
|
L1CAM |
0.504 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248948 |
Ser1152 |
RSKGGKYsVKDKEDT |
Rattus norvegicus |
PC-12 Cell |
| pmid |
sentence |
| 8663493 |
Western blot analysis demonstrated that the L1 kinase activity from PC12 cells that phosphorylated this site was co-eluted with the S6 kinase, p90(rsk). Moreover, S6 kinase activity and p90(rsk) immunoreactivity co-immunoprecipitate with L1 from brain, and metabolic labeling studies have demonstrated that Ser1152 is phosphorylated in vivo in the developing rat brain. | These data demonstrate that the membrane-proximal 15 amino acids of the cytoplasmic domain of L1 are important for neurite outgrowth on L1, and the interactions it mediates may be regulated by phosphorylation of Ser1152. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
RPS6KA1 | down-regulates activity
phosphorylation
|
BAD |
0.396 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-78020 |
Ser118 |
GRELRRMsDEFVDSF |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 10837486 |
Rsk1, and survival factor signaling stimulate phosphorylation of bad at ser-155, blocking the binding of bad to bcl-xl. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249045 |
Ser153 |
SWTRVFQsWWDRNLG |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 10837486 |
We report here that the phosphorylation of BAD at Ser-155 within the BH3 domain is a second phosphorylation-dependent mechanism that inhibits the death-promoting activity of BAD. Protein kinase A, RSK1, and survival factor signaling stimulate phosphorylation of BAD at Ser-155, blocking the binding of BAD to Bcl-XL. RSK1 phosphorylates BAD at both Ser-112 and Ser-155 and rescues BAD-mediated cell death in a manner dependent upon phosphorylation at both sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-180910 |
Ser75 |
EIRSRHSsYPAGTED |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 10558990 |
The rsks catalyze the phosphorylation of the pro-apoptotic protein bad at serine 112 to promote cell survival. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160635 |
Ser75 |
EIRSRHSsYPAGTED |
Homo sapiens |
Melanoma Cell |
| pmid |
sentence |
| 18246127 |
To understand the mechanisms underlying B-RAF effects on cell survival we initially analysed the Bcl-2 family protein, Bad, that is phosphorylated by RSK1 at the inhibitory serine-75 residue in a MEK-dependent manner in melanoma cells |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| Pathways: | FLT3-ITD signaling, Inhibition of Apoptosis |
| + |
RPS6KA1 | up-regulates activity
phosphorylation
|
CREB1 |
0.747 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-72117 |
Ser119 |
EILSRRPsYRKILND |
Homo sapiens |
|
| pmid |
sentence |
| 10558990 |
The rsks phosphorylate the trascription factor creb at serine 133 to promote cell survival. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | AMPK Signaling, FLT3-ITD signaling, Inhibition of Apoptosis |
| + |
RPS6KA1 |
phosphorylation
|
RANBP3 |
0.32 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160904 |
Ser126 |
VKRERTSsLTQFPPS |
Homo sapiens |
|
| pmid |
sentence |
| 18280241 |
Rsk phosphorylates serine 58 of ranbp3 in vitro and in vivo |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KA1 | down-regulates
phosphorylation
|
MXD1 |
0.316 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178586 |
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 |
| + |
RPS6KA1 | up-regulates
phosphorylation
|
ESR1 |
0.496 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-34113 |
Ser167 |
GGRERLAsTNDKGSM |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 7838153 |
Serine 167 is the major phosphorylation site on the human estrogen receptor. Phosphorylation is mediated by casein kinase ii. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KA1 | down-regulates
phosphorylation
|
CIC |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-169883 |
Ser173 |
PGKRRTQsLSALPKE |
Homo sapiens |
Melanoma Cell |
| pmid |
sentence |
| 21087211 |
Specifically, 14-3-3 binds to p90(rsk)-phosphorylated ser?_??_ Of capic?_A thereby modulating dna binding to its hmg (high-mobility group) box, whereas erk phosphorylations prevent binding of a c-terminal nls (nuclear localization sequence) to importin ?4 (kpna3) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KA1 | down-regulates
phosphorylation
|
TSC2 |
0.767 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-128634 |
Ser1798 |
GQRKRLIsSVEDFTE |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15342917 |
The mitogen-activated protein kinase (mapk)-activated kinase, p90 ribosomal s6 kinase (rsk) 1, was found to interact with and phosphorylate tuberin at a regulatory site, ser-1798, located at the evolutionarily conserved c terminus of tuberin. Rsk1 phosphorylation of ser-1798 inhibits the tumor suppressor function of the tuberin/hamartin complex, resulting in increased mtor signaling to s6k1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KA1 | up-regulates activity
phosphorylation
|
ETV1 |
0.351 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249162 |
Ser191 |
HRFRRQLsEPCNSFP |
Homo sapiens |
|
| pmid |
sentence |
| 12213813 |
Here we describe that the 90-kDa ribosomal S6 kinase 1 (RSK1), a protein kinase downstream of the extracellular signal-regulated kinase (ERK) subclass of MAPKs, binds to ER81, phosphorylates it, and enhances ER81-dependent transcription. Two in vivo RSK1 phosphorylation sites within ER81, Ser(191) and Ser(216), were identified, whose mutation to alanine reduces ER81 activity upon ERK-MAPK stimulation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249163 |
Ser216 |
PMYQRQMsEPNIPFP |
Homo sapiens |
|
| pmid |
sentence |
| 12213813 |
Here we describe that the 90-kDa ribosomal S6 kinase 1 (RSK1), a protein kinase downstream of the extracellular signal-regulated kinase (ERK) subclass of MAPKs, binds to ER81, phosphorylates it, and enhances ER81-dependent transcription. Two in vivo RSK1 phosphorylation sites within ER81, Ser(191) and Ser(216), were identified, whose mutation to alanine reduces ER81 activity upon ERK-MAPK stimulation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
RPS6KA1 | down-regulates activity
phosphorylation
|
OSTF1 |
0.353 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273838 |
Ser202 |
TDAVRTLsNAEDYLD |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 21501342 |
SH3P2 was phosphorylated on Ser(202) by ribosomal S6 kinase (RSK) in an ERK pathway-dependent manner, and such phosphorylation inhibited the ability of SH3P2 to suppress cell motility. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KA1 | up-regulates
phosphorylation
|
FLNA |
0.384 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-123458 |
Ser2152 |
TRRRRAPsVANVGSH |
Homo sapiens |
Melanoma Cell |
| pmid |
sentence |
| 15024089 |
We show that the n-terminal kinase domain of rsk phosphorylates flna on ser(2152) in response to mitogens |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KA1 | up-regulates activity
phosphorylation
|
RPS6KA1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-162681 |
Ser221 |
DHEKKAYsFCGTVEY |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 20048145 |
Herein, we demonstrate that the n-terminal kinase domain (ntk) of rsk1 is necessary for interactions with pkarialpha. Substitution of the activation loop phosphorylation site (ser-221) in the ntk with the negatively charged asp residue abrogated the association between rsk1 and pkarialpha. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | AMPK Signaling, FLT3-ITD signaling, Inhibition of Apoptosis, MTOR Signaling |
| + |
ERK1/2 | up-regulates activity
phosphorylation
|
RPS6KA1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250553 |
Ser221 |
DHEKKAYsFCGTVEY |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 9430688 |
Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250554 |
Ser363 |
TSRTPKDsPGIPPSA |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 9430688 |
Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250555 |
Ser380 |
HQLFRGFsFVATGLM |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 9430688 |
Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250556 |
Ser732 |
RRVRKLPsTTL |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 9430688 |
Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250557 |
Thr359 |
DTEFTSRtPKDSPGI |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 9430688 |
Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250558 |
Thr573 |
AENGLLMtPCYTANF |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 9430688 |
Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733. |
|
| Publications: |
6 |
Organism: |
Chlorocebus Aethiops |
| Pathways: | AMPK Signaling, FLT3-ITD signaling, Inhibition of Apoptosis, MTOR Signaling |
| + |
PDPK1 | up-regulates activity
phosphorylation
|
RPS6KA1 |
0.629 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250270 |
Ser221 |
DHEKKAYsFCGTVEY |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 10480933 |
Full-length RSK1, RSK2, and RSK3 Are Activated when Coexpressed with PDK1 in COS7 Cells. Ser221 phosphorylation is increased 2–3-fold during ERK-mediated activation of RSK1 in COS1 cells |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| Pathways: | AMPK Signaling, FLT3-ITD signaling, MTOR Signaling |
| + |
MAPK1 | up-regulates activity
phosphorylation
|
RPS6KA1 |
0.759 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-219308 |
Ser221 |
DHEKKAYsFCGTVEY |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 9430688 |
Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-219312 |
Ser363 |
TSRTPKDsPGIPPSA |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 9430688 |
Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-219316 |
Ser380 |
HQLFRGFsFVATGLM |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 9430688 |
Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-219320 |
Ser732 |
RRVRKLPsTTL |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 9430688 |
Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-219324 |
Thr359 |
DTEFTSRtPKDSPGI |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 9430688 |
Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-219328 |
Thr573 |
AENGLLMtPCYTANF |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 9430688 |
Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-59363 |
Thr573 |
AENGLLMtPCYTANF |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 9687510 |
Thus, MAPK1/ERK1 and MAPK2/ERK2 activate three closely related protein kinases known as MAPK_activated protein kinases_1a, _1b and _1c (MAPKAP_K1a/b/c; also known as RSK1/2/3) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-102645 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12832467 |
Efficient rsk activation by erk requires its interaction through a docking site located near the c terminus of rsk |
|
| Publications: |
8 |
Organism: |
Chlorocebus Aethiops, Homo Sapiens |
| + |
MAPK3 | up-regulates activity
phosphorylation
|
RPS6KA1 |
0.717 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-219332 |
Ser221 |
DHEKKAYsFCGTVEY |
Chlorocebus aethiops |
COS-1 Cell |
| pmid |
sentence |
| 9430688 |
Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-219337 |
Ser363 |
TSRTPKDsPGIPPSA |
Chlorocebus aethiops |
COS-1 Cell |
| pmid |
sentence |
| 9430688 |
Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-219341 |
Ser380 |
HQLFRGFsFVATGLM |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 9430688 |
Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-219345 |
Ser732 |
RRVRKLPsTTL |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 9430688 |
Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-219349 |
Thr359 |
DTEFTSRtPKDSPGI |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 9430688 |
Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-219353 |
Thr573 |
AENGLLMtPCYTANF |
Chlorocebus aethiops |
COS-1 Cell |
| pmid |
sentence |
| 9430688 |
Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-38999 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 8387505 |
The pp90rsk phosphothreonine content paralleled the ERK1 activity more closely than the phosphoserine level. These results provide compelling evidence that in fibroblasts and PC12 cells ERK1 plays a direct role in the phosphorylation of pp90rsk and that pp90rsk represents a physiologically relevant substrate of extracellular-regulated kinases |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-102648 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12832467 |
Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity.Erk-activates the rsk family of serine/threonine kinases,rsk1, rsk2, and rsk3. |
|
| Publications: |
8 |
Organism: |
Chlorocebus Aethiops, Mus Musculus, Homo Sapiens |
| + |
RPS6KA1 | up-regulates
phosphorylation
|
RPS6 |
0.591 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-153618 |
Ser235 |
IAKRRRLsSLRASTS |
Homo sapiens |
|
| pmid |
sentence |
| 17360704 |
We demonstrate that while ribosomal s6 kinase 1 (s6k1) phosphorylates rps6 at all sites, rsk exclusively phosphorylates rps6 at ser(235/236) in vitro and in vivo using an mtor-independent mechanism. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-153622 |
Ser236 |
AKRRRLSsLRASTSK |
Homo sapiens |
|
| pmid |
sentence |
| 17360704 |
We demonstrate that while ribosomal s6 kinase 1 (s6k1) phosphorylates rps6 at all sites, rsk exclusively phosphorylates rps6 at ser(235/236) in vitro and in vivo using an mtor-independent mechanism. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-171243 |
Ser240 |
RLSSLRAsTSKSESS |
Homo sapiens |
|
| pmid |
sentence |
| 21233202 |
In response to mitogenic stimuli, rps6 undergoes ordered c-terminal phosphorylation by p70 s6 kinases and p90 ribosomal s6 kinases on four conserved ser residues (ser-235, ser-236, ser-240, and ser-244) whose modification potentiates rps6 cap binding activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-171247 |
Ser244 |
LRASTSKsESSQK |
Homo sapiens |
|
| pmid |
sentence |
| 21233202 |
In response to mitogenic stimuli, rps6 undergoes ordered c-terminal phosphorylation by p70 s6 kinases and p90 ribosomal s6 kinases on four conserved ser residues (ser-235, ser-236, ser-240, and ser-244) whose modification potentiates rps6 cap binding activity |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| Pathways: | MTOR Signaling |
| + |
RPS6KA1 | up-regulates
phosphorylation
|
CCT2 |
0.249 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-172986 |
Ser260 |
GSRVRVDsTAKVAEI |
Homo sapiens |
|
| pmid |
sentence |
| 21440620 |
Furthermore, both the s260a and s260d mutants showed a decreased folding capacity as compared to cells expressing the wild-type cct_ subunit ( fig.?_5e), suggesting that a cyclic phosphorylation of the s260 site by s6k1 is likely to be important for chaperonin function and that mutation of this site interferes with this process. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KA1 | down-regulates
phosphorylation
|
METTL1 |
0.325 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-135948 |
Ser27 |
YYRQRAHsNPMADHT |
Homo sapiens |
HEK-293 Cell, HeLa Cell |
| pmid |
sentence |
| 15861136 |
Pkb and ribosomal s6 kinase (rsk) both phosphorylated mettl1 at ser27 in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KA1 | down-regulates
phosphorylation
|
DEPTOR |
0.494 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176883 |
Ser286 |
SSMSSCGsSGYFSSS |
Homo sapiens |
|
| pmid |
sentence |
| 22017877 |
We found that deptor was rapidly phosphorylated on three serines in a conserved degron, facilitating binding and ubiquitylation by the f box protein _trcp, with consequent proteasomal degradation of deptor. Phosphorylation of the _trcp degron in deptor is executed by ck1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176887 |
Ser287 |
SMSSCGSsGYFSSSP |
Homo sapiens |
|
| pmid |
sentence |
| 22017877 |
We found that deptor was rapidly phosphorylated on three serines in a conserved degron, facilitating binding and ubiquitylation by the f box protein _trcp, with consequent proteasomal degradation of deptor. Phosphorylation of the _trcp degron in deptor is executed by ck1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176891 |
Ser291 |
CGSSGYFsSSPTLSS |
Homo sapiens |
|
| pmid |
sentence |
| 22017877 |
We found that deptor was rapidly phosphorylated on three serines in a conserved degron, facilitating binding and ubiquitylation by the f box protein _trcp, with consequent proteasomal degradation of deptor. Phosphorylation of the _trcp degron in deptor is executed by ck1 |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
RPS6KA1 | down-regulates
phosphorylation
|
CDC25A |
0.367 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-202113 |
Ser293 |
GSTKRRKsMSGASPK |
Homo sapiens |
|
| pmid |
sentence |
| 23708659 |
Rsk promotes g2/m transition through activating phosphorylation of cdc25a and cdc25b rsk is likely to be more active in mitotic cells than in interphase cells, as evidenced by the phosphorylation status of t359/s363 in rsk. Together, these findings indicate that rsk promotes g2/m transition in mammalian cells through activating phosphorylation of cdc25a and cdc25b. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-202117 |
Ser295 |
TKRRKSMsGASPKES |
Homo sapiens |
|
| pmid |
sentence |
| 23708659 |
Rsk promotes g2/m transition through activating phosphorylation of cdc25a and cdc25b rsk is likely to be more active in mitotic cells than in interphase cells, as evidenced by the phosphorylation status of t359/s363 in rsk. Together, these findings indicate that rsk promotes g2/m transition in mammalian cells through activating phosphorylation of cdc25a and cdc25b. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
RPS6KA1 | up-regulates
phosphorylation
|
CDC25B |
0.253 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-202121 |
Ser353 |
VQNKRRRsVTPPEEQ |
Homo sapiens |
|
| pmid |
sentence |
| 23708659 |
Rsk promotes g2/m transition through activating phosphorylation of cdc25a and cdc25b rsk is likely to be more active in mitotic cells than in interphase cells, as evidenced by the phosphorylation status of t359/s363 in rsk. Together, these findings indicate that rsk promotes g2/m transition in mammalian cells through activating phosphorylation of cdc25a and cdc25b. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-202125 |
Thr355 |
NKRRRSVtPPEEQQE |
Homo sapiens |
|
| pmid |
sentence |
| 23708659 |
Rsk promotes g2/m transition through activating phosphorylation of cdc25a and cdc25b rsk is likely to be more active in mitotic cells than in interphase cells, as evidenced by the phosphorylation status of t359/s363 in rsk. Together, these findings indicate that rsk promotes g2/m transition in mammalian cells through activating phosphorylation of cdc25a and cdc25b. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
RPS6KA1 | up-regulates activity
phosphorylation
|
FOS |
0.531 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-37154 |
Ser362 |
AAAHRKGsSSNEPSS |
Homo sapiens |
|
| pmid |
sentence |
| 8248197 |
We now provide evidence that two growth-regulated, nucleus- and cytoplasm-localized protein kinases, 90-kda ribosomal s6 kinase (rsk) and mitogen-activated protein kinase (map kinase), contribute to the serum-induced phosphorylation of c-fos. The major phosphopeptides derived from biosynthetically labeled c-fos correspond to phosphopeptides generated after phosphorylation of c-fos in vitro with both rsk and map kinase. The phosphorylation sites identified for rsk (ser-362) and map kinase (ser-374) are in the transrepression domain. Cooperative phosphorylation at these sites by both enzymes was observed in vitro and reflected in vivo by the predominance of the peptide phosphorylated on both sites, as opposed to singly phosphorylated peptides. This study suggests a role for nuclear rsk and map kinase in modulating newly synthesized c-fos phosphorylation and downstream signaling. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262999 |
Ser374 |
PSSDSLSsPTLLAL |
|
|
| pmid |
sentence |
| 16055710 |
Serine 374 and serine 362 are the primary sites targeted by Erk1/2 and the mitogen-activated protein kinase-activated kinases Rsk1/2 (12, 13, 37, 38, 41), respectively. Their phosphorylation leads to protein stabilization (3, 13, 20, 41). Threonine 325 and threonine 331 are secondary targets of Erk1/2; their modification occurs only when serines 362 and 374 are phosphorylated and Erk1/2 activation is sufficiently sustained (37, 38). This enhances the transcriptional activity of c-Fos |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, |
| + |
RPS6KA1 | down-regulates activity
phosphorylation
|
EEF2K |
0.515 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109708 |
Ser366 |
SPQVRTLsGSRPPLL |
Homo sapiens |
Embryonic Cell Line |
| pmid |
sentence |
| 11500364 |
We show that two such kinases, p70 s6 kinase (regulated via mtor) and p90(rsk1) (activated by erk), phosphorylate eef2k at a conserved serine and inhibit its activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KA1 |
phosphorylation
|
NR4A3 |
0.315 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249297 |
Ser376 |
GRRGRLPsKPKSPLQ |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16223362 |
We have established that two related proteins, Nurr1 and Nor1, are also phosphorylated on the equivalent site by RSK in cells in response to mitogenic stimulation. | Similar to Nur77, when FLAGNor1 was expressed in HEK-293 cells, its phosphorylation on Ser377 was stimulated by both PMA and EGF |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KA1 | down-regulates
phosphorylation
|
MITF |
0.411 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-174760 |
Ser409 |
HGLSLIPsTGLCSPD |
Homo sapiens |
|
| pmid |
sentence |
| 21749389 |
The current study reveals that c-kit signaling triggers two phosphorylation events on mi, which up-regulate transactivation potential yet simultaneously target mi for ubiquitin-dependent proteolysis. The specific activation/degradation signals derive from mapk/erk targeting of serine 73, whereas serine 409 serves as a substrate for p90 rsk-1. An unphosphorylatable double mutant at these two residues is at once profoundly stable and transcriptionally inert. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-75034 |
Ser409 |
HGLSLIPsTGLCSPD |
Homo sapiens |
|
| pmid |
sentence |
| 10673502 |
The current study reveals that c-kit signaling triggers two phosphorylation events on mi, which up-regulate transactivation potential yet simultaneously target mi for ubiquitin-dependent proteolysis. The specific activation/degradation signals derive from mapk/erk targeting of serine 73, whereas serine 409 serves as a substrate for p90 rsk-1. An unphosphorylatable double mutant at these two residues is at once profoundly stable and transcriptionally inert. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
RPS6KA1 | up-regulates
phosphorylation
|
EIF4B |
0.532 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-123993 |
Ser422 |
RERSRTGsESSQTGT |
Homo sapiens |
|
| pmid |
sentence |
| 15071500 |
S6k1/s6k2 specifically phosphorylate ser422 in vitro. Substitution of ser422 with ala results in a loss of activity in an in vivo translation assay, indicating that phosphorylation of this site plays an important role in eif4b function. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KA1 | down-regulates activity
phosphorylation
|
STK11 |
0.288 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-209871 |
Ser428 |
SSKIRRLsACKQQ |
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 25846811 |
Negative regulation of the LKB1/AMPK pathway by ERK in human acute myeloid leukemia cellsBRAFV600E activates downstream molecules, including ERK and p90 ribosomal S6 kinase (RSK), and leads to the phosphorylation of LKB-1 at Ser428 by these kinases. This cascade results in the dissociation of LKB1 from AMPK. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | AMPK Signaling, FLT3-ITD signaling |
| + |
RPS6KA1 | up-regulates activity
phosphorylation
|
PPP1R3A |
0.429 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249036 |
Ser46 |
PQPSRRGsDSSEDIY |
in vitro |
|
| pmid |
sentence |
| 10648825 |
The protein G(M), which targets protein phosphatase 1 (PP1) to the glycogen particles and sarcoplasmic reticulum (SR) of striated muscles, is known to be phosphorylated at Ser48 and Ser67 in vitro by adenosine 3',5' cyclic monophosphate-dependent protein kinase (PKA) and at Ser48 by MAP kinase-activated protein kinase-1 (MAPKAP-K1, also called p90 RSK). The phosphorylation of Ser48 increases the rate at which the glycogen-associated PP1.G(M) complex dephosphorylates (activates) glycogen synthase, but the phosphorylation of Ser67 has the opposite effect, suppressing the activity of PP1 toward glycogen-bound substrates. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
RPS6KA1 |
phosphorylation
|
CARHSP1 |
0.333 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-137482 |
Ser52 |
TRRTRTFsATVRASQ |
Homo sapiens |
|
| pmid |
sentence |
| 15910284 |
These and other results demonstrate that crhsp24 is phosphorylated at ser52 by pkbalpha in response to igf-1, at ser52 by pkbalpha and rsk in response to egf |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney |
| + |
RPS6KA1 | up-regulates quantity
phosphorylation
|
RANBP3 |
0.32 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276149 |
Ser57 |
HGTGHPEsAGEHALE |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 18280241 |
RSK phosphorylates RanBP3 at Serine 58 residue in vitro and in vivo.RanBP3 phosphorylation increases its affinity towards Ran |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KA1 | up-regulates
phosphorylation
|
SLC9A1 |
0.453 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-69171 |
Ser703 |
MSRARIGsDPLAYEP |
Homo sapiens |
|
| pmid |
sentence |
| 10400637 |
The results indicate that p90rsk phosphorylates serine 703 of nhe-1, and this phosphorylation is required for growth factor stimulation of na+/h+ exchange. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KA1 | up-regulates
phosphorylation
|
RPTOR |
0.549 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-180458 |
Ser719 |
PCTPRLRsVSSYGNI |
Homo sapiens |
|
| pmid |
sentence |
| 18722121 |
Ser719, ser721, and ser722 are the predominant rsk-dependent phosphorylation sites in raptor raptor phosphorylation regulates mtorc1 activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-180462 |
Ser721 |
TPRLRSVsSYGNIRA |
Homo sapiens |
|
| pmid |
sentence |
| 18722121 |
Ser719, ser721, and ser722 are the predominant rsk-dependent phosphorylation sites in raptor raptor phosphorylation regulates mtorc1 activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-180466 |
Ser722 |
PRLRSVSsYGNIRAV |
Homo sapiens |
|
| pmid |
sentence |
| 18722121 |
Ser719, ser721, and ser722 are the predominant rsk-dependent phosphorylation sites in raptor raptor phosphorylation regulates mtorc1 activity |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Pathways: | MTOR Signaling |
| + |
RPS6KA1 | up-regulates activity
phosphorylation
|
MAGI1 |
0.287 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273837 |
Ser741 |
QPLERKDsQNSSQHS |
Homo sapiens |
HUVEC Cell |
| pmid |
sentence |
| 30944250 |
We report herein that p90RSK associates with MAGI1 in ECs and executes 2 independently regulated PTMs of MAGI1: S741 phosphorylation and K931 deSUMOylation. MAGI1-S741 phosphorylation is vital for Rap1 activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KA1 | down-regulates
phosphorylation
|
GSK3B |
0.36 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-110917 |
Ser9 |
SGRPRTTsFAESCKP |
Homo sapiens |
|
| pmid |
sentence |
| 11584304 |
S6k then phosphorylates the same serine residue on gsk3 that is targeted by pkb/akt (fig. 1), thereby inhibiting its activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | FLT3-ITD signaling, MTOR Signaling |
| + |
RPS6KA1 | up-regulates
phosphorylation
|
WWC1 |
0.336 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203294 |
Ser947 |
CRLNRSDsDSSTLSK |
Homo sapiens |
|
| pmid |
sentence |
| 24269383 |
Moreover, we found that rsk1/2 specifically phosphorylates kibra at two highly conserved sites (thr(929) and ser(947)) in vitro and in cells. erk_rsk phosphorylation of kibra is required for proper cell proliferation and rsk-mediated phosphorylation also positively modulates kibra's migratory activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203298 |
Thr929 |
STIIRSKtFSPGPQS |
Homo sapiens |
|
| pmid |
sentence |
| 24269383 |
Moreover, we found that rsk1/2 specifically phosphorylates kibra at two highly conserved sites (thr(929) and ser(947)) in vitro and in cells. Rsk-mediated phosphorylation is required for kibra binding to rsk1, but not rsk2. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Breast |
| + |
RPS6KA1 | up-regulates activity
phosphorylation
|
SLC9A3R1 |
0.331 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278290 |
Thr156 |
ELRPRLCtMKKGPSG |
Homo sapiens |
|
| pmid |
sentence |
| 26862730 |
In summary, these results demonstrate that Ras-RSK1 signaling promotes nuclear localization of EBP50.|Specifically, RSK1 phosphorylates EBP50 at threonine 156 (T156) residue in a cell cycle dependent manner, which is important for nuclear translocation of EBP50 to facilitate cellular proliferation and transformation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KA1 | down-regulates quantity by destabilization
phosphorylation
|
CDC34 |
0.336 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277330 |
Thr162 |
KGKDREYtDIIRKQV |
in vitro |
|
| pmid |
sentence |
| 27786305 |
RSK1 phosphorylated Thr162 on UBE2R1.RSK1 induced self-ubiquitination and destabilisation of UBE2R1 by phosphorylation. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
RPS6KA1 | down-regulates
phosphorylation
|
VASP |
0.452 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-172899 |
Thr278 |
LARRRKAtQVGEKTP |
Homo sapiens |
Lung Cancer Cell |
| pmid |
sentence |
| 21423205 |
Rsk1 phosphorylated vasp on t278, a site regulating its binding to actin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KA1 | down-regulates activity
phosphorylation
|
SENP2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273839 |
Thr369 |
TDDLLELtEDMEKEI |
Homo sapiens |
HUVEC Cell |
| pmid |
sentence |
| 25689261 |
Here, we determined that d-flow activated the serine/threonine kinase p90RSK, which subsequently phosphorylated threonine 368 (T368) of SENP2. T368 phosphorylation promoted nuclear export of SENP2, leading to downregulation of eNOS expression and upregulation of proinflammatory adhesion molecule expression and apoptosis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Gbeta | up-regulates activity
phosphorylation
|
RPS6KA1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270002 |
|
|
Mus musculus |
Neuron |
| pmid |
sentence |
| 8387505 |
The pp90rsk phosphothreonine content paralleled the ERK1 activity more closely than the phosphoserine level. These results provide compelling evidence that in fibroblasts and PC12 cells ERK1 plays a direct role in the phosphorylation of pp90rsk and that pp90rsk represents a physiologically relevant substrate of extracellular-regulated kinases |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
LTN1 | down-regulates activity
ubiquitination
|
RPS6KA1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278757 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29540532 |
Ltn1 ubiquitylation of RSK1, RSK2, and TWY3 could either result in degradation or impart a regulatory function on target proteins distinct from degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KA1 | up-regulates
phosphorylation
|
mTORC1 |
0.46 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217553 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18722121 |
Ser719, ser721, and ser722 are the predominant rsk-dependent phosphorylation sites in raptor raptor phosphorylation regulates mtorc1 activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | AMPK Signaling |
| + |
RPS6KA1 | up-regulates 
|
Translational_regulation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268528 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17360704 |
Mutation of rpS6 at Ser(235/236) reveals that phosphorylation of these sites promotes its recruitment to the 7-methylguanosine cap complex, suggesting that Ras/ERK signaling regulates assembly of the translation preinitiation complex. These data demonstrate that RSK provides an mTOR-independent pathway linking the Ras/ERK signaling cascade to the translational machinery. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TP53 | up-regulates
|
RPS6KA1 |
0.358 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124038 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15073170 |
Rather, p53 expression stimulates the serine/threonine kinase ribosomal s6 kinase 1 (rsk1), which in turn phosphorylates the p65 subunit of nf-kb. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | FLT3-ITD signaling |
| + |
RPS6KA1 | down-regulates activity
phosphorylation
|
TSC |
0.722 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217900 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15342917 |
The mitogen-activated protein kinase (mapk)-activated kinase, p90 ribosomal s6 kinase (rsk) 1, was found to interact with and phosphorylate tuberin at a regulatory site, ser-1798, located at the evolutionarily conserved c terminus of tuberin. Rsk1 phosphorylation of ser-1798 inhibits the tumor suppressor function of the tuberin/hamartin complex, resulting in increased mtor signaling to s6k1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | AMPK Signaling, MTOR Signaling |
| + |
RPS6KA1 | down-regulates activity
phosphorylation
|
Histone H3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265346 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14625384 |
Phosphorylation at ser-11 (h3s10ph) by rps6ka4 and rps6ka5 is important during interphase because it enables the transcription of genes following external stimulation, like mitogens, stress, growth factors or uv irradiation and result in the activation of genes, such as c-fos and c-jun. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KA1 | down-regulates quantity by destabilization
phosphorylation
|
IRS1 |
0.359 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-175687 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21798082 |
Negative feedback involves s6k, which inactivates irs by phosphorylation at multiple sites, thus inducing its degradation and altered cell localization. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Skeletal Muscle |
| Pathways: | AMPK Signaling, MTOR Signaling |
3.0
RPS6KA1
- 
- 