+ |
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 |
+ |
RPS6KA3 | down-regulates activity
phosphorylation
|
H3C1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-70436 |
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-138475 |
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. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-119229 |
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. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
RPS6KA3 | down-regulates activity
phosphorylation
|
H3-3A |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-138471 |
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. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-119225 |
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-70432 |
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. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
RPS6KA3 | up-regulates activity
phosphorylation
|
CREB1 |
0.716 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248951 |
Ser119 |
EILSRRPsYRKILND |
Homo sapiens |
|
pmid |
sentence |
8688081 |
MAPK activates CREB kinase, which in turn phosphorylates and activates CREB. Purification, sequencing, and biochemical characterization of CREB kinase revealed that it is identical to a member of the pp90(RSK) family, RSK2. RSK2 was shown to mediate growth factor induction of CREB serine-133 phosphorylation both in vitro and in vivo. These findings identify a cellular function for RSK2 and define a mechanism whereby growth factor signals mediated by RAS and MAPK are transmitted to the nucleus to activate gene expression |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RPS6KA3 | up-regulates
phosphorylation
|
ESR1 |
0.412 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-182958 |
Ser167 |
GGRERLAsTNDKGSM |
Homo sapiens |
Breast Cancer Cell |
pmid |
sentence |
19112174 |
S6k1 regulates estrogen receptor alpha (eralpha) by phosphorylating it on serine 167, leading to transcriptional activation of eralpha. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RPS6KA3 | down-regulates
phosphorylation
|
CIC |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-169887 |
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 |
+ |
AKT1 | down-regulates activity
phosphorylation
|
RPS6KA3 |
0.268 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277548 |
Ser19 |
KMAVESPsDSAENGQ |
Homo sapiens |
MDA-MB-231 Cell |
pmid |
sentence |
33574926 |
Akt interacts with and phosphorylates RSK2 at S19. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RPS6KA3 | down-regulates activity
phosphorylation
|
HMGN1 |
0.371 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249100 |
Ser21 |
KEEPKRRsARLSAKP |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
11438671 |
We report here that the NBD of the HMGN1 and -N2 protein family is highly and specifically phosphorylated during mitosis and that this phosphorylation has a major functional consequence: it abolishes the interaction of the proteins with its chromatin targets. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249101 |
Ser25 |
KRRSARLsAKPPAKV |
Homo sapiens |
|
pmid |
sentence |
11438671 |
We report here that the NBD of the HMGN1 and -N2 protein family is highly and specifically phosphorylated during mitosis and that this phosphorylation has a major functional consequence: it abolishes the interaction of the proteins with its chromatin targets. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
RPS6KA3 | down-regulates activity
phosphorylation
|
GSK3A |
0.268 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-110827 |
Ser21 |
SGRARTSsFAEPGGG |
Homo sapiens |
Neutrophil |
pmid |
sentence |
11583116 |
P90-rsk and akt may promote rapid phosphorylation/inactivation of glycogen synthase kinase 3 in chemoattractant-stimulated neutrophils. These reactions were monitored with a phosphospecific antibody that only recognized the alpha- or beta-isoforms of GSK-3 when these proteins were phosphorylated on serine residues 21 and 9, respectively. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PDPK1 | up-regulates
phosphorylation
|
RPS6KA3 |
0.639 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-161924 |
Ser227 |
DHEKKAYsFCGTVEY |
Homo sapiens |
|
pmid |
sentence |
19956600 |
We characterize two monoclonal antibodies raised against phosphorylated forms of the n- and c-terminal domain of rsk2 (p-s227 and p-t577, respectively). Using these two antibodies, we show that stress signals, such as uv light, induce phosphorylation and activation of the three rsks. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-70612 |
Ser227 |
DHEKKAYsFCGTVEY |
Homo sapiens |
|
pmid |
sentence |
10480933 |
We characterize two monoclonal antibodies raised against phosphorylated forms of the n- and c-terminal domain of rsk2 (p-s227 and p-t577, respectively). Using these two antibodies, we show that stress signals, such as uv light, induce phosphorylation and activation of the three rsks. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
ERK1/2 | up-regulates
phosphorylation
|
RPS6KA3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-244692 |
Ser227 |
DHEKKAYsFCGTVEY |
Homo sapiens |
|
pmid |
sentence |
10980595 |
We have generated two monoclonal antibodies that recognize two phosphorylated sites, p-ser227 and p-thr577, in the n- and c-terminal kinase domains of rsk2, respectively. phosphorylation and activation of rsk2 by uv light involves the erk pathway |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-244696 |
Thr577 |
AENGLLMtPCYTANF |
Homo sapiens |
|
pmid |
sentence |
10980595 |
We have generated two monoclonal antibodies that recognize two phosphorylated sites, p-ser227 and p-thr577, in the n- and c-terminal kinase domains of rsk2, respectively. phosphorylation and activation of rsk2 by uv light involves the erk pathway |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-244699 |
|
|
Homo sapiens |
|
pmid |
sentence |
19282669 |
Erk-activates the rsk family of serine/threonine kinases,rsk1, rsk2, and rsk3. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
PPM1D | down-regulates activity
dephosphorylation
|
RPS6KA3 |
0.369 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248320 |
Ser227 |
DHEKKAYsFCGTVEY |
Mus musculus |
|
pmid |
sentence |
15206906 |
RSK2 (p90 ribosomal S6 kinase 2) is activated via the ERK (extracellular-signal-regulated kinase) pathway by phosphorylation on four sites: Ser227 in the activation loop of the N-terminal kinase domain, Ser369 in the linker, Ser386 in the hydrophobic motif and Thr577 in the C-terminal kinase domain of RSK2. In the present study, we demonstrate that RSK2 is associated in vivo with PP2Cdelta (protein phosphatase 2Cdelta). In epidermal growth factorstimulated cells, RSK2 is partially dephosphorylated on all four sites in an Mn2+-dependent manner, leading to reduced protein kinase activity |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248321 |
Ser369 |
TAKTPKDsPGIPPSA |
Mus musculus |
|
pmid |
sentence |
15206906 |
RSK2 (p90 ribosomal S6 kinase 2) is activated via the ERK (extracellular-signal-regulated kinase) pathway by phosphorylation on four sites: Ser227 in the activation loop of the N-terminal kinase domain, Ser369 in the linker, Ser386 in the hydrophobic motif and Thr577 in the C-terminal kinase domain of RSK2. In the present study, we demonstrate that RSK2 is associated in vivo with PP2Cdelta (protein phosphatase 2Cdelta). In epidermal growth factorstimulated cells, RSK2 is partially dephosphorylated on all four sites in an Mn2+-dependent manner, leading to reduced protein kinase activity |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248322 |
Ser386 |
HQLFRGFsFVAITSD |
Mus musculus |
|
pmid |
sentence |
15206906 |
RSK2 (p90 ribosomal S6 kinase 2) is activated via the ERK (extracellular-signal-regulated kinase) pathway by phosphorylation on four sites: Ser227 in the activation loop of the N-terminal kinase domain, Ser369 in the linker, Ser386 in the hydrophobic motif and Thr577 in the C-terminal kinase domain of RSK2. In the present study, we demonstrate that RSK2 is associated in vivo with PP2Cdelta (protein phosphatase 2Cdelta). In epidermal growth factorstimulated cells, RSK2 is partially dephosphorylated on all four sites in an Mn2+-dependent manner, leading to reduced protein kinase activity |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248323 |
Thr577 |
AENGLLMtPCYTANF |
Mus musculus |
|
pmid |
sentence |
15206906 |
RSK2 (p90 ribosomal S6 kinase 2) is activated via the ERK (extracellular-signal-regulated kinase) pathway by phosphorylation on four sites: Ser227 in the activation loop of the N-terminal kinase domain, Ser369 in the linker, Ser386 in the hydrophobic motif and Thr577 in the C-terminal kinase domain of RSK2. In the present study, we demonstrate that RSK2 is associated in vivo with PP2Cdelta (protein phosphatase 2Cdelta). In epidermal growth factorstimulated cells, RSK2 is partially dephosphorylated on all four sites in an Mn2+-dependent manner, leading to reduced protein kinase activity |
|
Publications: |
4 |
Organism: |
Mus Musculus |
+ |
MAPK3 | up-regulates
phosphorylation
|
RPS6KA3 |
0.717 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-81460 |
Ser227 |
DHEKKAYsFCGTVEY |
Homo sapiens |
|
pmid |
sentence |
10980595 |
We have generated two monoclonal antibodies that recognize two phosphorylated sites, p-ser227 and p-thr577, in the n- and c-terminal kinase domains of rsk2, respectively. phosphorylation and activation of rsk2 by uv light involves the erk pathway |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-81464 |
Thr577 |
AENGLLMtPCYTANF |
Homo sapiens |
|
pmid |
sentence |
10980595 |
We have generated two monoclonal antibodies that recognize two phosphorylated sites, p-ser227 and p-thr577, in the n- and c-terminal kinase domains of rsk2, respectively. phosphorylation and activation of rsk2 by uv light involves the erk pathway |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-184583 |
|
|
Homo sapiens |
|
pmid |
sentence |
19282669 |
Erk-activates the rsk family of serine/threonine kinases,rsk1, rsk2, and rsk3. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
RPS6KA3 | up-regulates
phosphorylation
|
ATF4 |
0.623 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-124436 |
Ser245 |
TRGSPNRsLPSPGVL |
Homo sapiens |
|
pmid |
sentence |
15109498 |
Here, we show that rsk2 is required for osteoblast differentiation and function. We identify the transcription factor atf4 as a critical substrate of rsk2 that is required for the timely onset of osteoblast differentiation, for terminal differentiation of osteoblasts, and for osteoblast-specific gene expression |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RPS6KA3 | down-regulates activity
phosphorylation
|
HMGN2 |
0.293 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249102 |
Ser25 |
KDEPQRRsARLSAKP |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
11438671 |
We report here that the NBD of the HMGN1 and -N2 protein family is highly and specifically phosphorylated during mitosis and that this phosphorylation has a major functional consequence: it abolishes the interaction of the proteins with its chromatin targets. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249103 |
Ser29 |
QRRSARLsAKPAPPK |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
11438671 |
We report here that the NBD of the HMGN1 and -N2 protein family is highly and specifically phosphorylated during mitosis and that this phosphorylation has a major functional consequence: it abolishes the interaction of the proteins with its chromatin targets. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
RPS6KA3 | up-regulates
phosphorylation
|
NFATC4 |
0.395 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-234465 |
Ser281 |
SGTPSSAsPALSRRG |
Mus musculus |
|
pmid |
sentence |
17213202 |
Serines 281 and 285 of the nfat3 protein might be target amino acids of rsk2 phosphorylationrsk2 induced nuclear localization of nfat3. Rsk2 phosphorylated nfat3 in vitro (km=3.559 microm), and activation of nfat3 by rsk2 enhanced the promoter activity of nfat3 downstream target genes in vivo. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-234469 |
Ser285 |
SSASPALsRRGSLGE |
Mus musculus |
|
pmid |
sentence |
17213202 |
Serines 281 and 285 of the nfat3 protein might be target amino acids of rsk2 phosphorylationrsk2 induced nuclear localization of nfat3. Rsk2 phosphorylated nfat3 in vitro (km=3.559 microm), and activation of nfat3 by rsk2 enhanced the promoter activity of nfat3 downstream target genes in vivo. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-234473 |
Ser289 |
PALSRRGsLGEEGSE |
Mus musculus |
|
pmid |
sentence |
17213202 |
The results indicated that rsk2 phosphorylated two additional sites at ser289 (peptide 2) and ser344 (peptide 3)rsk2 induced nuclear localization of nfat3. Rsk2 phosphorylated nfat3 in vitro (km=3.559 microm), and activation of nfat3 by rsk2 enhanced the promoter activity of nfat3 downstream target genes in vivo. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-235652 |
Ser344 |
QAVALPRsEEPASCN |
Mus musculus |
C2C12 Cell, Myoblast |
pmid |
sentence |
17213202 |
The results indicated that rsk2 phosphorylated two additional sites at ser289 (peptide 2) and ser344 (peptide 3)rsk2 induced nuclear localization of nfat3. Rsk2 phosphorylated nfat3 in vitro (km=3.559 microm), and activation of nfat3 by rsk2 enhanced the promoter activity of nfat3 downstream target genes in vivo. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-133283 |
Ser676 |
SNGRRKRsPTQSFRF |
Homo sapiens |
|
pmid |
sentence |
15657420 |
We demonstrate that p90 ribosomal s6 kinase (rsk) is recruited to the nfat-dna transcription complex upon activation.Bound Rsk phosphorylates ser(676) and potentiates nfatc4 dna binding. Ser(676) is also targeted by the erk map kinase. |
|
Publications: |
5 |
Organism: |
Mus Musculus, Homo Sapiens |
Tissue: |
Muscle, Skeletal Muscle, Myotube |
+ |
RPS6KA3 |
phosphorylation
|
TINF2 |
0.351 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-202532 |
Ser295 |
FPFRNLGsPTQVISK |
Homo sapiens |
|
pmid |
sentence |
23977114 |
Phosphorylation of serines 295 and 330 appeared to be mediated, at least in part, by the mitotic kinase rsk2. The consequence of tin2 phosphorylation during mitosis remains to be determined |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-202536 |
Ser330 |
ASTGKSKsPCQTLGG |
Homo sapiens |
|
pmid |
sentence |
23977114 |
Phosphorylation of serines 295 and 330 appeared to be mediated, at least in part, by the mitotic kinase rsk2. The consequence of tin2 phosphorylation during mitosis remains to be determined |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
RPS6KA3 |
phosphorylation
|
H2BC3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-174026 |
Ser33 |
DGKKRKRsRKESYSI |
Homo sapiens |
|
pmid |
sentence |
21646345 |
Here, we studied the histone h2b core domain and found that phosphorylation of h2b serine 32 occurs in normal cycling and mitogen-stimulated cells. Notably, this phosphorylation is elevated in skin cancer cell lines and tissues compared with normal counterparts. We identified ribosomal s6 kinase 2 (rsk2) as the kinase responsible for h2bs32 phosphorylation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RPS6KA3 |
phosphorylation
|
NR4A1 |
0.477 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249295 |
Ser351 |
GRRGRLPsKPKQPPD |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
16223362 |
In the present paper, we have re-examined the phosphorylation of Nur77 on Ser354. Using a combination of cell-permeable kinase inhibitors and mouse knockin mutations, we show that Nur77 is phosphorylated by RSK in response to mitogenic stimulation of cells. Phosphorylation of Nur77 on Ser354 did not, however, appear to affect the transcriptional activity of Nur77, or its ability to bind 14-3-3 proteins in vivo. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RPS6KA3 | down-regulates quantity by destabilization
phosphorylation
|
FOXN2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273840 |
Ser365 |
EDDPLGDsGYASQPC |
Homo sapiens |
NCI-H1299 Cell |
pmid |
sentence |
29396548 |
Importantly, we identified RSK2 kinase as the upstream kinase for the FOXN2 phosphodegron. The Ser365 and Ser369 sites in a conserved DSGYAS motif are responsible for the ubiquitination of FOXN2 by β-Trcp. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273841 |
Ser369 |
LGDSGYAsQPCAKIS |
Homo sapiens |
NCI-H1299 Cell |
pmid |
sentence |
29396548 |
Importantly, we identified RSK2 kinase as the upstream kinase for the FOXN2 phosphodegron. The Ser365 and Ser369 sites in a conserved DSGYAS motif are responsible for the ubiquitination of FOXN2 by β-Trcp. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
RPS6KA3 | up-regulates activity
phosphorylation
|
KCNK3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-172470 |
Ser393 |
GLMKRRSsV |
Homo sapiens |
|
pmid |
sentence |
21357689 |
The chaperone protein, 14-3-3, binds to a critical phosphorylated serine in the channel c termini of k2p3.1 and k2p9.1 (ser(393) and ser(373), respectively) and overcomes retention in the endoplasmic reticulum by ?COP. We sought to identify the kinase responsible for phosphorylation of the terminal serine in human and rat variants of k2p3.1 and k2p9.1. Adopting a bioinformatic approach, three candidate protein kinases were identified: camp-dependent protein kinase, ribosomal s6 kinase, and protein kinase c. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RPS6KA3 | up-regulates
phosphorylation
|
TH |
0.271 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-95483 |
Ser40 |
GQGAPGPsLTGSPWP |
Homo sapiens |
|
pmid |
sentence |
12421349 |
Mitogen-activated protein-kinase (map) kinase-activated protein kinases 1 and 2 (mapkap kinase-1, mapkap kinase-2), were found to phosphorylate bacterially expressed human tyrosine hydroxylaserecombinant human tyrosine hydroxylase (hth1) was found to be phosphorylated by mitogen and stress-activated protein kinase 1 (msk1) at ser40 and by p38 regulated/activated kinase (prak) on ser19. Phosphorylation by msk1 induced an increase in vmax |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-34682 |
Ser40 |
GQGAPGPsLTGSPWP |
Homo sapiens |
|
pmid |
sentence |
7901013 |
Mitogen-activated protein-kinase (map) kinase-activated protein kinases 1 and 2 (mapkap kinase-1, mapkap kinase-2), were found to phosphorylate bacterially expressed human tyrosine hydroxylaserecombinant human tyrosine hydroxylase (hth1) was found to be phosphorylated by mitogen and stress-activated protein kinase 1 (msk1) at ser40 and by p38 regulated/activated kinase (prak) on ser19. Phosphorylation by msk1 induced an increase in vmax |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-34686 |
Ser71 |
RFIGRRQsLIEDARK |
Homo sapiens |
|
pmid |
sentence |
7901013 |
Mitogen-activated protein-kinase (map) kinase-activated protein kinases 1 and 2 (mapkap kinase-1, mapkap kinase-2), were found to phosphorylate bacterially expressed human tyrosine hydroxylaserecombinant human tyrosine hydroxylase (hth1) was found to be phosphorylated by mitogen and stress-activated protein kinase 1 (msk1) at ser40 and by p38 regulated/activated kinase (prak) on ser19. Phosphorylation by msk1 induced an increase in vmax |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-95487 |
Ser71 |
RFIGRRQsLIEDARK |
Homo sapiens |
|
pmid |
sentence |
12421349 |
Mitogen-activated protein-kinase (map) kinase-activated protein kinases 1 and 2 (mapkap kinase-1, mapkap kinase-2), were found to phosphorylate bacterially expressed human tyrosine hydroxylaserecombinant human tyrosine hydroxylase (hth1) was found to be phosphorylated by mitogen and stress-activated protein kinase 1 (msk1) at ser40 and by p38 regulated/activated kinase (prak) on ser19. Phosphorylation by msk1 induced an increase in vmax |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
+ |
RPS6KA3 | up-regulates activity
phosphorylation
|
PFKFB2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-23753 |
Ser466 |
PVRMRRNsFTPLSSS |
Homo sapiens |
|
pmid |
sentence |
2846551 |
Heart 6-phosphofructo-2-kinase activation by insulin results from ser-466 and ser-483 phosphorylation and requires 3-phosphoinositide-dependent kinase-1, but not protein kinase b. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-49367 |
Ser466 |
PVRMRRNsFTPLSSS |
Homo sapiens |
|
pmid |
sentence |
9211863 |
Heart 6-phosphofructo-2-kinase activation by insulin results from ser-466 and ser-483 phosphorylation and requires 3-phosphoinositide-dependent kinase-1, but not protein kinase b. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Tissue: |
Heart |
+ |
RPS6KA3 |
phosphorylation
|
KRT18 |
0.304 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248895 |
Ser53 |
ISVSRSTsFRGGMGS |
in vitro |
|
pmid |
sentence |
7523419 |
Ser-52 in K18 is not glycosylated and matches consensus sequences for phosphorylation by CAM kinase, S6 kinase and protein kinase C, and all these kinases can phosphorylate K18 in vitro predominantly at that site. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
RPS6KA3 | up-regulates quantity
phosphorylation
|
RANBP3 |
0.336 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276148 |
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 |
+ |
RPS6KA3 |
phosphorylation
|
HMGN1 |
0.371 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249215 |
Ser7 |
sSAEGAAK |
Mus musculus |
|
pmid |
sentence |
12773393 |
The results presented here show that MSK2 and, to a lesser extent, MSK1 are the major protein kinases required for the phosphorylation of histone H3 at both Ser10 and Ser28 and HMG-14 at Ser6 after stimulation of primary embryonic fibroblasts by TPA or anisomycin. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
RPS6KA3 | down-regulates
phosphorylation
|
BAD |
0.393 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-184595 |
Ser75 |
EIRSRHSsYPAGTED |
Homo sapiens |
|
pmid |
sentence |
19282669 |
The rsks catalyze the phosphorylation of the pro-apoptotic protein bad at serine 112 to promote cell survival. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RPS6KA3 | down-regulates quantity
phosphorylation
|
FGFR1 |
0.363 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276599 |
Ser789 |
DTRSSTCsSGEDSVF |
Homo sapiens |
U2-OS Cell |
pmid |
sentence |
24141780 |
Both in vitro and in vivo experiments confirmed the interaction and we show that phosphorylated RSK2 binds to and phosphorylates serine 789 in the C-terminal tail of FGFR1.prevention of FGFR1 phosphorylation by inhibition of RSK2 activity or mutation of serine 789 to alanine reduced FGFR1 endocytosis and ubiquitination explaining mechanistically the prolonged signaling activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RPS6KA3 | down-regulates activity
phosphorylation
|
MAP3K5 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276464 |
Ser83 |
ATRGRGSsVGGGSRR |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
23608533 |
We provide evidence to show that RSK2 inhibits ASK1 by phosphorylating S83, T1109, and T1326 through a novel mechanism in which phospho-T1109/T1326 inhibits ATP binding to ASK1, while phospho-S83 attenuates ASK1 substrate MKK6 binding. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276463 |
Thr1109 |
DRKIIATtLSKLKLE |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
23608533 |
We provide evidence to show that RSK2 inhibits ASK1 by phosphorylating S83, T1109, and T1326 through a novel mechanism in which phospho-T1109/T1326 inhibits ATP binding to ASK1, while phospho-S83 attenuates ASK1 substrate MKK6 binding. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276462 |
Thr1326 |
VNGADEDtISRFLAE |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
23608533 |
We provide evidence to show that RSK2 inhibits ASK1 by phosphorylating S83, T1109, and T1326 through a novel mechanism in which phospho-T1109/T1326 inhibits ATP binding to ASK1, while phospho-S83 attenuates ASK1 substrate MKK6 binding. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
RPS6KA3 | down-regulates activity
phosphorylation
|
VGLL1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273842 |
Ser84 |
PNQWRYSsPWTKPQP |
Homo sapiens |
NUGC-3 Cell |
pmid |
sentence |
33069758 |
Site-directed mutagenesis and immunoprecipitation experiments revealed that RSK2 phosphorylated VGLL1 at S84 in the presence of TGF-β. Mutation of VGLL1 at S84 suppressed VGLL1-TEAD4 binding and the subsequent transcriptional activation of matrix metalloprotease 9 (MMP9). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RPS6KA3 | up-regulates
phosphorylation
|
WWC1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-203302 |
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. Rsk-mediated phosphorylation is required for kibra binding to rsk1, but not rsk2. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-203306 |
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 |
+ |
RPS6KA3 | down-regulates quantity by destabilization
phosphorylation
|
CASP8 |
0.378 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272997 |
Thr263 |
SIRDRNGtHLDAGAL |
|
|
pmid |
sentence |
21183680 |
The ribosomal S6 kinase 2 (RSK2) is a member of the p90 ribosomal S6 kinase (p90RSK) family of proteins and plays a critical role in proliferation, cell cycle, and cell transformation. Here, we report that RSK2 phosphorylates caspase-8, and Thr-263 was identified as a novel caspase-8 phosphorylation site. In addition, we showed that EGF induces caspase-8 ubiquitination and degradation through the proteasome pathway, and phosphorylation of Thr-263 is associated with caspase-8 stability. |
|
Publications: |
1 |
+ |
RPS6KA3 | up-regulates
phosphorylation
|
EIF2AK2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-154183 |
Thr451 |
KRTRSKGtLRYMSPE |
Homo sapiens |
Skin Cancer Cell |
pmid |
sentence |
17404396 |
Our data indicated that phosphorylation of pkr at thr(451) is mediated through erk2 and rsk2, but not through p38 kinase. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SRC |
phosphorylation
|
RPS6KA3 |
0.362 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-160056 |
Tyr488 |
DVYDDGKyVYVVTEL |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
18156174 |
The results showed that tyr-488 is a major site of src but mutations at tyr-529 or tyr-707 did not significantly decrease src-dependent tyrosine phosphorylation of rsk2 (fig. 4c). However, we have previously characterized the tyr-488 site that is also phosphorylated by fgfr3 (14), and substitution of tyr-488 did not affect rsk2 activation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SRC | up-regulates
phosphorylation
|
RPS6KA3 |
0.362 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-160052 |
Tyr529 |
TITKTVEyLHAQGVV |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
18156174 |
Together, our findings suggest that src-dependent phosphorylation at tyr-529 facilitates inactive erk binding to rsk2, which might be a general requirement for rsk2 activation by egf through the mek/erk pathway. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FYN | up-regulates
phosphorylation
|
RPS6KA3 |
0.332 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-160048 |
Tyr529 |
TITKTVEyLHAQGVV |
Homo sapiens |
|
pmid |
sentence |
18156174 |
Epidermal growth factor stimulates rsk2 activation through activation of the mek/erk pathway and src-dependent tyrosine phosphorylation of rsk2 at tyr-529. By mass spectroscopy-based studies, we identified src tyrosine kinase family members src and fyn as upstream kinases of rsk2 tyr-529. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FLT4 | down-regulates
phosphorylation
|
RPS6KA3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-98708 |
Tyr707 |
KGAMAATySALNRNQ |
Homo sapiens |
|
pmid |
sentence |
12601080 |
Upon truncation of this c-terminal stretch, or mutation of the tyr-707 residue alone, autoinhibition is attenuated, and the kinase becomes constitutively active. Based on these findings we propose that phosphorylation of the tyr-707 represents a novel alternative regulatory mechanism for p90rsk activation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Gbeta | up-regulates
phosphorylation
|
RPS6KA3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270014 |
|
|
Homo sapiens |
|
pmid |
sentence |
10980595 |
We have generated two monoclonal antibodies that recognize two phosphorylated sites, p-ser227 and p-thr577, in the n- and c-terminal kinase domains of rsk2, respectively. phosphorylation and activation of rsk2 by uv light involves the erk pathway |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RPS6KA3 | down-regulates activity
phosphorylation
|
Histone H3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265347 |
|
|
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. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RPS6KA3 | up-regulates activity
|
MAD1L1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252038 |
|
|
Homo sapiens |
|
pmid |
sentence |
20383198 |
We also show that this kinase might also participate in the maintenance of the SAC in mammalian cells as Rsk2 knockdown in these cells prevents the kinetochore localization of Mad1, Mad2 and CENP-E under checkpoint conditions. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SL0101 | down-regulates
chemical inhibition
|
RPS6KA3 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-207075 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RPS6KA3 | up-regulates activity
|
CENPE |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252037 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
20383198 |
We also show that this kinase might also participate in the maintenance of the SAC in mammalian cells as Rsk2 knockdown in these cells prevents the kinetochore localization of Mad1, Mad2 and CENP-E under checkpoint conditions. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RPS6KA3 | up-regulates activity
|
MAD2L1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252039 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
20383198 |
We also show that this kinase might also participate in the maintenance of the SAC in mammalian cells as Rsk2 knockdown in these cells prevents the kinetochore localization of Mad1, Mad2 and CENP-E under checkpoint conditions. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAPK1 | up-regulates
phosphorylation
|
RPS6KA3 |
0.715 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-161518 |
|
|
Homo sapiens |
|
pmid |
sentence |
19282669 |
Erk-activates the rsk family of serine/threonine kinases,rsk1, rsk2, and rsk3. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |