| + |
RPS6KA5 | down-regulates activity 
phosphorylation
|
H3-3A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138479 |
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-70440 |
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-119233 |
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-178708 |
Ser29 |
ATKAARKsAPSTGGV |
Homo sapiens |
|
| pmid |
sentence |
| 18508628 |
In addition to ser10, msk was also found to phosphorylate a second site on h3, ser28 (75). It should be noted that while both ser10 and ser28 in h3 are extensively phosphorylated during mitosis, this is independent of msks and is catalysed by aurora kinases. In contrast, msks only phosphorylate a small proportion of the total cellular histone h3 in response to mitogens or stress. The spatial distribution of ser10 and ser28 phosphorylation is very tightly regulated in cells. In vitro, msk1 will phosphorylate one histone h3 molecule on both ser10 and ser28. Surprisingly it has been shown that in cells msk phosphorylates either ser10 or ser28 but not both on individual nucleosomes. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
RPS6KA5 |
phosphorylation
|
H3-4 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249213 |
Ser11 |
TKQTARKsTGGKAPR |
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 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249214 |
Ser29 |
ATKVARKsAPATGGV |
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 |
|
| Publications: |
2 |
Organism: |
Mus Musculus |
| + |
RPS6KA5 | down-regulates activity
phosphorylation
|
H3C1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-119237 |
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-70444 |
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-138483 |
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-163712 |
Ser29 |
ATKAARKsAPATGGV |
Homo sapiens |
|
| pmid |
sentence |
| 20129940 |
Upon activation of the erk and p38 mapk pathways, the msk1/2-mediated nucleosomal response, including h3 phosphorylation at serine 28 or 10, is coupled with the induction of immediate-early (ie) gene transcription. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
RPS6KA5 | up-regulates activity 
phosphorylation
|
H3-3A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178704 |
Ser11 |
TKQTARKsTGGKAPR |
Homo sapiens |
|
| pmid |
sentence |
| 18508628 |
In addition to ser10, msk was also found to phosphorylate a second site on h3, ser28 (75). It should be noted that while both ser10 and ser28 in h3 are extensively phosphorylated during mitosis, this is independent of msks and is catalysed by aurora kinases. In contrast, msks only phosphorylate a small proportion of the total cellular histone h3 in response to mitogens or stress. The spatial distribution of ser10 and ser28 phosphorylation is very tightly regulated in cells. In vitro, msk1 will phosphorylate one histone h3 molecule on both ser10 and ser28. Surprisingly it has been shown that in cells msk phosphorylates either ser10 or ser28 but not both on individual nucleosomes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KA5 | down-regulates activity
phosphorylation
|
BAD |
0.35 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262990 |
Ser118 |
GRELRRMsDEFVDSF |
|
|
| pmid |
sentence |
| 12213813 |
Phosphorylation of Bad at Ser112 in response to growth factors or cytokines is generally linked to cell survival. Knockdown of MSK1 suppressed Bad phosphorylation after calcium ionophore A23187 treatment in neuronal cells |
|
| Publications: |
1 |
| Pathways: | Malignant Melanoma |
| + |
RPS6KA5 | up-regulates
phosphorylation
|
CREB1 |
0.721 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-59458 |
Ser119 |
EILSRRPsYRKILND |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 9687510 |
Msk1 is localized in the nucleus of unstimulated or stimulated cells, and phosphorylates creb at ser133_ .MSK1 Is activated in vitro by mapk2/erk2 or sapk2/p38. Endogenous msk1 is activated in 293 cells by either growth factor/phorbol ester stimulation, or by exposure to uv radiation, and oxidative and chemical stres msk was the kinase responsible for phosphorylation of the transcription factor creb in response to tcr stimulation. Pka, ca2+-calmodulin-dependent kinase iv (camkiv), msk, p70s6k and rsk phosphorylate creb. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Adipogenesis, Malignant Melanoma, P38 Signaling |
| + |
RPS6KA5 | up-regulates
phosphorylation
|
H2AC11 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-123383 |
Ser2 |
sGRGKQGG |
Homo sapiens |
|
| pmid |
sentence |
| 15010469 |
We found that msk1 phosphorylated histone h2a on serine 1, and mutation of serine 1 to alanine blocked the inhibition of transcription by msk1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KA5 | up-regulates activity
phosphorylation
|
H2AW |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262942 |
Ser2 |
sGRGKQGG |
in vitro |
|
| pmid |
sentence |
| 15010469 |
We found that MSK1 phosphorylated histone H2A on serine 1, and mutation of serine 1 to alanine blocked the inhibition of transcription by MSK1. Furthermore, we found that acetylation of histone H3 by the p300 and CREB-binding protein associated factor, PCAF, suppressed the kinase-dependent inhibition of transcription. These results suggest that acetylation of histones may stimulate transcription by suppressing an inhibitory phosphorylation by a kinase as MSK1. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
RPS6KA5 | up-regulates activity
phosphorylation
|
RPS6KA5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-131387 |
Ser212 |
DETERAYsFCGTIEY |
Homo sapiens |
|
| pmid |
sentence |
| 15568999 |
Msk1 can autophosphorylate on at least six sites: ser-212, ser-376, ser-381, ser-750, ser-752 and ser-758. Of these sites, the n-terminal t-loop residue ser-212 and the 'hydrophobic motif' ser-376 are phosphorylated by the c-terminal kinase domain of msk1, and their phosphorylation is essential for the catalytic activity of the n-terminal kinase domain of msk1 and therefore for the phosphorylation of msk1 substrates in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-131391 |
Ser376 |
EKLFQGYsFVAPSIL |
Homo sapiens |
|
| pmid |
sentence |
| 15568999 |
Msk1 can autophosphorylate on at least six sites: ser-212, ser-376, ser-381, ser-750, ser-752 and ser-758. Of these sites, the n-terminal t-loop residue ser-212 and the 'hydrophobic motif' ser-376 are phosphorylated by the c-terminal kinase domain of msk1, and their phosphorylation is essential for the catalytic activity of the n-terminal kinase domain of msk1 and therefore for the phosphorylation of msk1 substrates in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-131395 |
Ser381 |
GYSFVAPsILFKRNA |
Homo sapiens |
|
| pmid |
sentence |
| 15568999 |
Msk1 can autophosphorylate on at least six sites: ser-212, ser-376, ser-381, ser-750, ser-752 and ser-758. Of these sites, the n-terminal t-loop residue ser-212 and the 'hydrophobic motif' ser-376 are phosphorylated by the c-terminal kinase domain of msk1, and their phosphorylation is essential for the catalytic activity of the n-terminal kinase domain of msk1 and therefore for the phosphorylation of msk1 substrates in vitro. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Pathways: | Adipogenesis, Malignant Melanoma, P38 Signaling |
| + |
RPS6KA5 | up-regulates activity
phosphorylation
|
ETV1 |
0.476 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262987 |
Ser216 |
PMYQRQMsEPNIPFP |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 12213813 |
Activated, overexpressed MSK1 was able to phosphorylate ER81 at Ser191 and Ser216. Mutation of these residues strongly impairs ER81-responsive promoter activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KA5 | up-regulates
phosphorylation
|
RELA |
0.706 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-99210 |
Ser276 |
SMQLRRPsDRELSEP |
Homo sapiens |
|
| pmid |
sentence |
| 12628924 |
Transcriptional activation of the nf-kappab p65 subunit by mitogen- and stress-activated protein kinase-1 (msk1)mutational analysis of p65 revealed ser276 as a target for phosphorylation and transactivation in response to tnf. Moreover, we identified msk1 as a nuclear kinase for p65, since msk1 associates with p65 in a stimulus-dependent way and phosphorylates p65 at ser276. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KA5 |
phosphorylation
|
NR4A1 |
0.391 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249296 |
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 |
| + |
MAPK11 | up-regulates
phosphorylation
|
RPS6KA5 |
0.597 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-59443 |
Ser360 |
TEMDPTYsPAALPQS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 9687510 |
Mitogen- and stress-activated protein kinase-1 (msk1) is directly activated by mapk and sapk2/p38, and may mediate activation of crebactivated by phosphorylation at ser-360, thr-581 and thr-700 by mapk1/erk2, mapk3/erk1 and mapk14/p38-alpha |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-59447 |
Thr581 |
PDNQPLKtPCFTLHY |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 9687510 |
Mitogen- and stress-activated protein kinase-1 (msk1) is directly activated by mapk and sapk2/p38, and may mediate activation of crebactivated by phosphorylation at ser-360, thr-581 and thr-700 by mapk1/erk2, mapk3/erk1 and mapk14/p38-alpha |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-59451 |
Thr700 |
LSSNPLMtPDILGSS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 9687510 |
Mitogen- and stress-activated protein kinase-1 (msk1) is directly activated by mapk and sapk2/p38, and may mediate activation of crebactivated by phosphorylation at ser-360, thr-581 and thr-700 by mapk1/erk2, mapk3/erk1 and mapk14/p38-alpha |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
MAPK3 | up-regulates
phosphorylation
|
RPS6KA5 |
0.567 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-131379 |
Ser360 |
TEMDPTYsPAALPQS |
Homo sapiens |
|
| pmid |
sentence |
| 15568999 |
In the present study, we show that, in addition to being phosphorylated on thr-581 and ser-360 by erk1/2 or p38, msk1 can autophosphorylate on at least six sites: ser-212, ser-376, ser-381, ser-750, ser-752 and ser-758. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-131383 |
Thr581 |
PDNQPLKtPCFTLHY |
Homo sapiens |
|
| pmid |
sentence |
| 15568999 |
In the present study, we show that, in addition to being phosphorylated on thr-581 and ser-360 by erk1/2 or p38, msk1 can autophosphorylate on at least six sites: ser-212, ser-376, ser-381, ser-750, ser-752 and ser-758. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ERK1/2 | up-regulates
phosphorylation
|
RPS6KA5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249572 |
Ser360 |
TEMDPTYsPAALPQS |
Homo sapiens |
|
| pmid |
sentence |
| 18267068 |
Together, our in vivo and in vitro studies indicate that the pkc/c-raf/mek/erk pathway plays a major role in the s6k1 activation in hypertrophic cardiac growth. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249573 |
Thr581 |
PDNQPLKtPCFTLHY |
Homo sapiens |
|
| pmid |
sentence |
| 18267068 |
Together, our in vivo and in vitro studies indicate that the pkc/c-raf/mek/erk pathway plays a major role in the s6k1 activation in hypertrophic cardiac growth. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Adipogenesis, Malignant Melanoma |
| + |
MAPK14 | up-regulates activity
phosphorylation
|
RPS6KA5 |
0.594 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-130736 |
Ser360 |
TEMDPTYsPAALPQS |
Homo sapiens |
|
| pmid |
sentence |
| 15568999 |
Msk1 (mitogen- and stress-activated protein kinase) is a kinase activated in cells downstream of both the erk1/2 (extracellular-signal-regulated kinase) and p38 mapk (mitogen-activated protein kinase) cascades. In the present study, we show that, in addition to being phosphorylated on thr-581 and ser-360 by erk1/2 or p38, msk1 can autophosphorylate on at least six sites |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249199 |
Ser376 |
EKLFQGYsFVAPSIL |
|
|
| pmid |
sentence |
| 15568999 |
In the present study, we show that, in addition to being phosphorylated on Thr-581 and Ser-360 by ERK1/2 or p38, MSK1 can autophosphorylate on at least six sites: Ser-212, Ser-376, Ser-381, Ser-750, Ser-752 and Ser-758. Of these sites, the N-terminal T-loop residue Ser-212 and the 'hydrophobic motif' Ser-376 are phosphorylated by the C-terminal kinase domain of MSK1, and their phosphorylation is essential for the catalytic activity of the N-terminal kinase domain of MSK1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-131375 |
Thr581 |
PDNQPLKtPCFTLHY |
Homo sapiens |
|
| pmid |
sentence |
| 15568999 |
Msk1 (mitogen- and stress-activated protein kinase) is a kinase activated in cells downstream of both the erk1/2 (extracellular-signal-regulated kinase) and p38 mapk (mitogen-activated protein kinase) cascades. In the present study, we show that, in addition to being phosphorylated on thr-581 and ser-360 by erk1/2 or p38, msk1 can autophosphorylate on at least six sites |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-59454 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 9687510 |
Mitogen- and stress-activated protein kinase-1 (msk1) is directly activated by mapk and sapk2/p38,. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens, |
| Pathways: | P38 Signaling |
| + |
MAPK1 | up-regulates
phosphorylation
|
RPS6KA5 |
0.6 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-59435 |
Ser360 |
TEMDPTYsPAALPQS |
Homo sapiens |
|
| pmid |
sentence |
| 9687510 |
Together, our in vivo and in vitro studies indicate that the pkc/c-raf/mek/erk pathway plays a major role in the s6k1 activation in hypertrophic cardiac growth. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-131311 |
Ser360 |
TEMDPTYsPAALPQS |
Homo sapiens |
|
| pmid |
sentence |
| 15568999 |
Together, our in vivo and in vitro studies indicate that the pkc/c-raf/mek/erk pathway plays a major role in the s6k1 activation in hypertrophic cardiac growth. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-116485 |
Ser360 |
TEMDPTYsPAALPQS |
Homo sapiens |
|
| pmid |
sentence |
| 11940578 |
Together, our in vivo and in vitro studies indicate that the pkc/c-raf/mek/erk pathway plays a major role in the s6k1 activation in hypertrophic cardiac growth. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-116489 |
Thr581 |
PDNQPLKtPCFTLHY |
Homo sapiens |
|
| pmid |
sentence |
| 11940578 |
Together, our in vivo and in vitro studies indicate that the pkc/c-raf/mek/erk pathway plays a major role in the s6k1 activation in hypertrophic cardiac growth. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160787 |
Thr581 |
PDNQPLKtPCFTLHY |
Homo sapiens |
|
| pmid |
sentence |
| 18267068 |
Together, our in vivo and in vitro studies indicate that the pkc/c-raf/mek/erk pathway plays a major role in the s6k1 activation in hypertrophic cardiac growth. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| + |
MAPK3 | up-regulates activity
phosphorylation
|
RPS6KA5 |
0.567 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249479 |
Ser376 |
EKLFQGYsFVAPSIL |
|
|
| pmid |
sentence |
| 15568999 |
In the present study, we show that, in addition to being phosphorylated on Thr-581 and Ser-360 by ERK1/2 or p38, MSK1 can autophosphorylate on at least six sites: Ser-212, Ser-376, Ser-381, Ser-750, Ser-752 and Ser-758. Of these sites, the N-terminal T-loop residue Ser-212 and the 'hydrophobic motif' Ser-376 are phosphorylated by the C-terminal kinase domain of MSK1, and their phosphorylation is essential for the catalytic activity of the N-terminal kinase domain of MSK1 |
|
| Publications: |
1 |
| + |
ERK1/2 | up-regulates activity
phosphorylation
|
RPS6KA5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249574 |
Ser376 |
EKLFQGYsFVAPSIL |
Homo sapiens |
|
| pmid |
sentence |
| 15568999 |
In the present study, we show that, in addition to being phosphorylated on Thr-581 and Ser-360 by ERK1/2 or p38, MSK1 can autophosphorylate on at least six sites: Ser-212, Ser-376, Ser-381, Ser-750, Ser-752 and Ser-758. Of these sites, the N-terminal T-loop residue Ser-212 and the 'hydrophobic motif' Ser-376 are phosphorylated by the C-terminal kinase domain of MSK1, and their phosphorylation is essential for the catalytic activity of the N-terminal kinase domain of MSK1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Adipogenesis, Malignant Melanoma |
| + |
MAPK1 | up-regulates activity
phosphorylation
|
RPS6KA5 |
0.6 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249445 |
Ser376 |
EKLFQGYsFVAPSIL |
|
|
| pmid |
sentence |
| 15568999 |
In the present study, we show that, in addition to being phosphorylated on Thr-581 and Ser-360 by ERK1/2 or p38, MSK1 can autophosphorylate on at least six sites: Ser-212, Ser-376, Ser-381, Ser-750, Ser-752 and Ser-758. Of these sites, the N-terminal T-loop residue Ser-212 and the 'hydrophobic motif' Ser-376 are phosphorylated by the C-terminal kinase domain of MSK1, and their phosphorylation is essential for the catalytic activity of the N-terminal kinase domain of MSK1 |
|
| Publications: |
1 |
| + |
RPS6KA5 | up-regulates
phosphorylation
|
ELK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-85514 |
Ser383 |
IHFWSTLsPIAPRSP |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 11145955 |
Phosphorylation on ser383 and ser389 of elk-1 by mapk enhances this basal binding but, most importantly, elk-1 exhibits new interactions with p300. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Ovary |
| + |
RPS6KA5 | up-regulates
phosphorylation
|
TH |
0.343 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-95491 |
Ser40 |
GQGAPGPsLTGSPWP |
Homo sapiens |
|
| pmid |
sentence |
| 12421349 |
Recombinant 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. studies on th from several species suggest that ser40 is the main site involved in direct activation of th |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KA5 | up-regulates activity
phosphorylation
|
ATF1 |
0.678 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249144 |
Ser63 |
GILARRPsYRKILKD |
Mus musculus |
Fibroblast |
| pmid |
sentence |
| 11909979 |
Using embryonic fibroblasts derived from these mice we were able to demonstrate an important role for these enzymes in the activation of CREB and the closely related transcription factor ATF1. | Our results clearly demonstrate that MSK1 and MSK2 are the major, if not the only, protein kinases that mediate the phosphorylation of CREB at Ser133 and of ATF1 at Ser63 in fibroblasts |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-95318 |
Ser63 |
GILARRPsYRKILKD |
Homo sapiens |
|
| pmid |
sentence |
| 12414794 |
We find that activation of the c-jun promoter through the atf1 site requires phosphorylation of atf1 at serine 63. atf1 can be phosphorylated by mitogen- and stress-activated protein kinase 1 (msk1), which is activated by egf and erk1/2. |
|
| Publications: |
2 |
Organism: |
Mus Musculus, Homo Sapiens |
| Pathways: | P38 Signaling |
| + |
RPS6KA5 | down-regulates activity
phosphorylation
|
EIF4EBP1 |
0.658 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262993 |
Ser65 |
FLMECRNsPVTKTPP |
|
|
| pmid |
sentence |
| 12213813 |
In response to UV-B irradiation, the translation factor 4E-BP1 (eukaryotic initiation factor 4E [eIF4E]-binding protein 1) was phosphorylated at Thr36, Thr45, Ser64 and Thr69. Using either p38 MAPK inhibitors or the MSK inhibitor H89, UV-B-irradiation-induced phosphorylation was blocked [43]. 4E-BP1 binds to eIF4E in resting cells to prevent formation of a functional eIF4F complex, which is essential for cap-dependent initiation of translation. Phosphorylation of 4E-BP1 leads to dissociation from eIF4E |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262991 |
Thr37 |
PPGDYSTtPGGTLFS |
|
|
| pmid |
sentence |
| 12213813 |
In response to UV-B irradiation, the translation factor 4E-BP1 (eukaryotic initiation factor 4E [eIF4E]-binding protein 1) was phosphorylated at Thr36, Thr45, Ser64 and Thr69. Using either p38 MAPK inhibitors or the MSK inhibitor H89, UV-B-irradiation-induced phosphorylation was blocked [43]. 4E-BP1 binds to eIF4E in resting cells to prevent formation of a functional eIF4F complex, which is essential for cap-dependent initiation of translation. Phosphorylation of 4E-BP1 leads to dissociation from eIF4E |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249131 |
Thr45 |
PGGTLFStTPGGTRI |
in vitro |
|
| pmid |
sentence |
| 11777913 |
Here, using mass spectrometry, we identify the serum-responsive, rapamycin-sensitive sites as Ser 65 and Thr 70. | Phosphorylation of Thr 37/Thr 46 is followed by Thr 70 phosphorylation, and Ser 65 is phosphorylated last. Finally, we show that phosphorylation of Ser 65 and Thr 70 alone is insufficient to block binding to eIF4E, indicating that a combination of phosphorylation events is necessary to dissociate 4E-BP1 from eIF4E. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262992 |
Thr46 |
GGTLFSTtPGGTRII |
|
|
| pmid |
sentence |
| 12213813 |
In response to UV-B irradiation, the translation factor 4E-BP1 (eukaryotic initiation factor 4E [eIF4E]-binding protein 1) was phosphorylated at Thr36, Thr45, Ser64 and Thr69. Using either p38 MAPK inhibitors or the MSK inhibitor H89, UV-B-irradiation-induced phosphorylation was blocked [43]. 4E-BP1 binds to eIF4E in resting cells to prevent formation of a functional eIF4F complex, which is essential for cap-dependent initiation of translation. Phosphorylation of 4E-BP1 leads to dissociation from eIF4E |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262994 |
Thr70 |
RNSPVTKtPPRDLPT |
|
|
| pmid |
sentence |
| 12213813 |
In response to UV-B irradiation, the translation factor 4E-BP1 (eukaryotic initiation factor 4E [eIF4E]-binding protein 1) was phosphorylated at Thr36, Thr45, Ser64 and Thr69. Using either p38 MAPK inhibitors or the MSK inhibitor H89, UV-B-irradiation-induced phosphorylation was blocked [43]. 4E-BP1 binds to eIF4E in resting cells to prevent formation of a functional eIF4F complex, which is essential for cap-dependent initiation of translation. Phosphorylation of 4E-BP1 leads to dissociation from eIF4E |
|
| Publications: |
5 |
Organism: |
, In Vitro |
| + |
RPS6KA5 | down-regulates activity
phosphorylation
|
HMGN1 |
0.604 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262988 |
Ser7 |
sSAEGAAK |
|
|
| pmid |
sentence |
| 12213813 |
HMGN1 (formerly known as HMG-14) phosphorylation at Ser6 occurs concomitantly with IE gene expression. | MSK2 seems to be the most important kinase responsible for this modification |Accordingly, it was suggested that HMGN1 phosphorylation reduces binding of the protein to the nucleosomes |
|
| Publications: |
1 |
| + |
RPS6KA5 | up-regulates
phosphorylation
|
STAT3 |
0.393 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-101251 |
Ser727 |
NTIDLPMsPRTLDSL |
Homo sapiens |
|
| pmid |
sentence |
| 12763138 |
The stat3-mediated transactivation was reduced by blocking the stat3 serine phosphorylation with the mek inhibitor u0126 or by expression of kinase-inactive msk1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166664 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20626350 |
Msk (mitogen- and stress-activated kinase) 1 and 2 can directly phosphorylate and activate transcription factors such as creb, atf1, the nf- b isoform p65 and stat (signal transducer and activator of transcription) 1 and 3 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
RPS6KA5 | up-regulates activity
phosphorylation
|
PLA2G4A |
0.359 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249051 |
Ser727 |
RQNPSRCsVSLSNVE |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 10978317 |
Serine 727 phosphorylation and activation of cytosolic phospholipase A2 by MNK1-related protein kinases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KA5 |
phosphorylation
|
RPS6KA5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-131399 |
Ser750 |
RRKMKKTsTSTETRS |
Homo sapiens |
|
| pmid |
sentence |
| 15568999 |
Msk1 can autophosphorylate on at least six sites: ser-212, ser-376, ser-381, ser-750, ser-752 and ser-758. ser-750, ser-752 and ser-758 are phosphorylated by the n-terminal kinase domain;however, their function is not known. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-131403 |
Ser752 |
KMKKTSTsTETRSSS |
Homo sapiens |
|
| pmid |
sentence |
| 15568999 |
Msk1 can autophosphorylate on at least six sites: ser-212, ser-376, ser-381, ser-750, ser-752 and ser-758. ser-750, ser-752 and ser-758 are phosphorylated by the n-terminal kinase domain;however, their function is not known. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-131407 |
Ser758 |
TSTETRSsSSESSHS |
Homo sapiens |
|
| pmid |
sentence |
| 15568999 |
Msk1 can autophosphorylate on at least six sites: ser-212, ser-376, ser-381, ser-750, ser-752 and ser-758. ser-750, ser-752 and ser-758 are phosphorylated by the n-terminal kinase domain;however, their function is not known. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Pathways: | Adipogenesis, Malignant Melanoma, P38 Signaling |
| + |
RPS6KA5 | down-regulates activity
phosphorylation
|
Histone H3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265348 |
|
|
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 |
| + |
Gbeta | up-regulates
phosphorylation
|
RPS6KA5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270076 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15568999 |
In the present study, we show that, in addition to being phosphorylated on thr-581 and ser-360 by erk1/2 or p38, msk1 can autophosphorylate on at least six sites: ser-212, ser-376, ser-381, ser-750, ser-752 and ser-758. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KA5 | down-regulates
phosphorylation
|
Histone H2A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265314 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15010469 |
We found that msk1 phosphorylated histone h2a on serine 1, and mutation of serine 1 to alanine blocked the inhibition of transcription by msk1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KA5 | up-regulates
phosphorylation
|
NfKb-p65/p50 |
0.604 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217424 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12628924 |
Transcriptional activation of the nf-kappab p65 subunit by mitogen- and stress-activated protein kinase-1 (msk1)mutational analysis of p65 revealed ser276 as a target for phosphorylation and transactivation in response to tnf. Moreover, we identified msk1 as a nuclear kinase for p65, since msk1 associates with p65 in a stimulus-dependent way and phosphorylates p65 at ser276. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
RPS6KA5
- 
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