Relation Results

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

Identifier	Residue	Sequence	Organism
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
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
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

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

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-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

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.

Publications:

4

Organism:

Homo Sapiens

Pathways:

FLT3-ITD signaling, Inhibition of Apoptosis

Identifier	Residue	Sequence	Organism
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

Identifier	Residue	Sequence	Organism
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

Identifier	Residue	Sequence	Organism
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

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

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

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

Identifier	Residue	Sequence	Organism
SIGNOR-280114	Ser19	DADEWCDsGLGSLGP	Homo sapiens
pmid	sentence
16822942	By using recombinant wild-type and mutant IkappaBbeta proteins, both active ERK2 and RSK1 were found to directly phosphorylate IkappaBbeta, but only active RSK1 phosphorylated IkappaBbeta on Ser19 and Ser23, two sites known to mediate the subsequent ubiquitination and degradation.

Identifier	Residue	Sequence	Organism
SIGNOR-280115	Ser23	WCDSGLGsLGPDAAA	Homo sapiens
pmid	sentence
16822942	By using recombinant wild-type and mutant IkappaBbeta proteins, both active ERK2 and RSK1 were found to directly phosphorylate IkappaBbeta, but only active RSK1 phosphorylated IkappaBbeta on Ser19 and Ser23, two sites known to mediate the subsequent ubiquitination and degradation.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
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
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

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

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

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

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
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-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-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	Organism
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

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

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

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
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
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
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	Organism
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.

Identifier	Residue	Organism
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

Publications:

8

Organism:

Chlorocebus Aethiops, Homo Sapiens, Mus Musculus

Identifier	Residue	Sequence	Organism
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
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
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
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

Identifier	Residue	Sequence	Organism
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

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

Identifier	Residue	Sequence	Organism
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
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
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

Identifier	Residue	Sequence	Organism
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
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

Identifier	Residue	Sequence	Organism
SIGNOR-279311	Ser32	LLDDRHDsGLDSMKD	Homo sapiens
pmid	sentence
10398585	Mitogen activated ribosomal S6 kinase (p90 rsk1) phosphorylates IkappaBalpha at S32, binds IkappaBalpha in vivo, and overexpression of dominant negative p90 rsk1 inhibits degradation of IkappaBalpha in response to TPA.

Publications:

1

Organism:

Homo Sapiens

Pathways:

FLT3-ITD signaling, Inhibition of Apoptosis

Identifier	Residue	Sequence	Organism
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
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

Identifier	Residue	Sequence	Organism
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
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,

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

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

Identifier	Residue	Sequence	Organism
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.

Identifier	Residue	Sequence	Organism
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.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
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

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

Identifier	Residue	Sequence	Organism
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

Identifier	Residue	Sequence	Organism
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

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

Identifier	Residue	Sequence	Organism
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

Identifier	Residue	Sequence	Organism
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
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
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

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

Identifier	Residue	Sequence	Organism
SIGNOR-280113	Ser897	RVSIRLPsTSGSEGV	Homo sapiens
pmid	sentence
32574556	These comprehensive analyses indicate that high matrix stiffness activates ERK/RSK1-mediated EPHA2 non-canonical signalling to induce LYN activation, TWIST1 nuclear localization, and cell invasion (Fig. 6M).\|We next knocked down the most abundant RSK family members and found that loss of RSK1, but not RSK2 or RSK3, drastically inhibited EPHA2 S897 phosphorylation, prevented ECM stiffness-induced LYN activation and recruitment to EPHA2, and inhibited cell EMT and invasion induced by increasing rigidities (Fig. 6F\u2013I and S6H\u2013L).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
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

Identifier	Residue	Sequence	Organism
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
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

Identifier	Residue	Sequence	Organism
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

Identifier	Residue	Sequence	Organism
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

Identifier	Residue	Sequence	Organism
SIGNOR-279653	Thr198	PGLRRRQt	Homo sapiens
pmid	sentence
19470470	As for other PI3K effectors, RSK1 phosphorylates p27 at T198.\|RSK1 overexpression increases p27pT198, p27-cyclin D1-Cdk4 complexes, and p27 stability.

Publications:

1

Organism:

Homo Sapiens

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

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

Identifier	Residue	Organism
SIGNOR-279280		Homo sapiens
pmid	sentence
25106868	These results indicate that RSK1 directly phosphorylates the C-terminus of ZFP36L1 downstream of ERK, and inhibits the Messenger RNA destabilization activity of ZFP36L1.\|These results indicate that RSK1 directly phosphorylates the C-terminus of ZFP36L1 downstream of ERK, and inhibits the mRNA destabilization activity of ZFP36L1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
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

Identifier	Residue	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

Identifier	Residue	Organism
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

Identifier	Residue	Organism
SIGNOR-280112		Homo sapiens
pmid	sentence
22068162	13 The data presented support previous findings that C/EBPbeta can be a molecular target of RSK1, 16 but provide the first indication that RSK1 can phosphorylate and activate C/EBPbeta to mediate the IL-6 signalling events in cholangiocarcinoma.\|As mentioned above, RSK1 has been shown to activate C/EBPbeta in hepatic stellate cells in an experimental model of liver fibrosis.

Publications:

1

Organism:

Homo Sapiens

Pathways:

FLT3-ITD signaling

Identifier	Residue	Organism
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

Identifier	Residue	Organism
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

Identifier	Residue	Organism
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

Identifier	Residue	Organism
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

Identifier	Residue	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

Name	RPS6KA1 View Modifications
Full Name	Ribosomal protein S6 kinase alpha-1
Synonyms	S6K-alpha-1, 90 kDa ribosomal protein S6 kinase 1, p90-RSK 1, p90RSK1, p90S6K, MAP kinase-activated protein kinase 1a, MAPK-activated protein kinase 1a, MAPKAP kinase 1a, MAPKAPK-1a, Ribosomal S6 kinase 1, RSK-1 \| MAPKAPK1A, RSK1
Primary ID	Q15418
Links	- -
Type	protein
Relations	94
Pathways	AMPK Signaling, FLT3-ITD signaling, Inhibition of Apoptosis, MTOR Signaling
Function	Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1. In fibroblast, is required for EGF-stimulated phosphorylation of CREB1, which results in the subsequent transcriptional activation of several immediate-early genes. In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP. Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity. Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the pre-initiation complex. In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation. Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway. Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function. Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4). Mediates induction of hepatocyte prolifration by TGFA through phosphorylation of CEBPB (By similarity). Is involved in cell cycle regulation by phosphorylating the CDK inhibitor CDKN1B, which promotes CDKN1B association with 14-3-3 proteins and prevents its translocation to the nucleus and inhibition of G1 progression. Phosphorylates EPHA2 at 'Ser-897', the RPS6KA-EPHA2 signaling pathway controls cell migration (PubMed:26158630).

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