Relation Results

Identifier	Residue	Sequence	Organism
SIGNOR-196034	Ser100	LGLLKLAsPELERLI	Homo sapiens
pmid	sentence
22327296	Menin binds the jun family transcription factor jund and inhibits its transcriptional activity. The menin-jund interaction blocks jun n-terminal kinase (jnk)-mediated jund phosphorylation and suppresses jund-induced transcription. We found a role for phosphorylation of the ser100 residue of jund;jund phosphorylation were prevented by inhibitors of calcium, calmodulin, or erk1/2 kinase.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-202698	Ser1035	DHQTPPTsPVQGTTP	Homo sapiens
pmid	sentence
24089523	Histone deacetylase 6 (hdac6) is well known for its ability to promote cell migrationextracellular signal-regulated kinase (erk) phosphorylates histone deacetylase 6 (hdac6) at serine 1035 to stimulate cell migrationwe have identified two novel erk-mediated phosphorylation sites: threonine 1031 and serine 1035 in hdac6. Both sites were phosphorylated by erk1

Identifier	Residue	Sequence	Organism
SIGNOR-202702	Thr1031	ASSTDHQtPPTSPVQ	Homo sapiens
pmid	sentence
24089523	Histone deacetylase 6 (hdac6) is well known for its ability to promote cell migrationextracellular signal-regulated kinase (erk) phosphorylates histone deacetylase 6 (hdac6) at serine 1035 to stimulate cell migrationwe have identified two novel erk-mediated phosphorylation sites: threonine 1031 and serine 1035 in hdac6. Both sites were phosphorylated by erk1

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-178141	Ser104	FPPLNSVsPSPLMLL	Homo sapiens
pmid	sentence
18372406	In several estrogen response element-containing genes, the s118a mutation strongly reduced induction by e(2), and u0126 did not further reduce expression. Here, we show that serines 104 (s104) and 106 (s106) are also phosphorylated by mapk in vitro and upon stimulation of mapk activity in vivo.Phosphorylation at serines 104 and 106 by erk1/2 mapk is important for estrogen receptor-alpha activity

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-156860	Ser104	FPPLNSVsPSPLMLL	Homo sapiens	HeLa Cell
pmid	sentence
17615152	In several estrogen response element-containing genes, the s118a mutation strongly reduced induction by e(2), and u0126 did not further reduce expression. Here, we show that serines 104 (s104) and 106 (s106) are also phosphorylated by mapk in vitro and upon stimulation of mapk activity in vivo.Phosphorylation at serines 104 and 106 by erk1/2 mapk is important for estrogen receptor-alpha activity

Identifier	Residue	Sequence	Organism
SIGNOR-178145	Ser106	PLNSVSPsPLMLLHP	Homo sapiens
pmid	sentence
18372406	In several estrogen response element-containing genes, the s118a mutation strongly reduced induction by e(2), and u0126 did not further reduce expression. Here, we show that serines 104 (s104) and 106 (s106) are also phosphorylated by mapk in vitro and upon stimulation of mapk activity in vivo.Phosphorylation at serines 104 and 106 by erk1/2 mapk is important for estrogen receptor-alpha activity

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-156864	Ser106	PLNSVSPsPLMLLHP	Homo sapiens	HeLa Cell
pmid	sentence
17615152	In several estrogen response element-containing genes, the s118a mutation strongly reduced induction by e(2), and u0126 did not further reduce expression. Here, we show that serines 104 (s104) and 106 (s106) are also phosphorylated by mapk in vitro and upon stimulation of mapk activity in vivo.Phosphorylation at serines 104 and 106 by erk1/2 mapk is important for estrogen receptor-alpha activity

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-156868	Ser118	LHPPPQLsPFLQPHG	Homo sapiens	HeLa Cell
pmid	sentence
17615152	In several estrogen response element-containing genes, the s118a mutation strongly reduced induction by e(2), and u0126 did not further reduce expression. Here, we show that serines 104 (s104) and 106 (s106) are also phosphorylated by mapk in vitro and upon stimulation of mapk activity in vivo.

Publications:

5

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-32757	Ser1044	WNLVSPDsPRSIDSN	Homo sapiens
pmid	sentence
7777512	Thus, our results identify the human lifr as a substrate for mapk and suggest a mechanism of heterologous receptor regulation of lifr signaling occurring at ser-1044.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277449	Ser1051	NRSEIGHsPPPAYTP	Homo sapiens	HEK-293 Cell
pmid	sentence
31053301	We also identified Ser-1026 as an ErbB4-specific ERK target site in the CYT-1 region. Moreover, double mutations (Thr-674/Ser-1026 to Ala) significantly upregulated ErbB4 activation, indicating that Thr-674 and Ser-1026 are cooperatively involved in negative feedback regulation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277448	Thr699	TELVEPLtPSGTAPN	Homo sapiens	HEK-293 Cell
pmid	sentence
31053301	We also identified Ser-1026 as an ErbB4-specific ERK target site in the CYT-1 region. Moreover, double mutations (Thr-674/Ser-1026 to Ala) significantly upregulated ErbB4 activation, indicating that Thr-674 and Ser-1026 are cooperatively involved in negative feedback regulation.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-192101	Ser111	ESNSDGAsPEPCTVT	Homo sapiens
pmid	sentence
23024368	Phosphorylation of this site downregulates nanog, sox2, rex1 and upregulates bmp4, gata6, ddlx5.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-179404	Ser112	AIKVEPAsPPYYSEK	Homo sapiens
pmid	sentence
11733495	Moreover, the inhibition of erks 1 and 2 with a mek inhibitor, u1026, lead to an inhibition in the decay of ppargamma proteins, indicating that serine phosphorylation influences the degradation of ppargamma in fat cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-43939	Ser1132	TLPHGPRsASVSSIS	Homo sapiens
pmid	sentence
8816480	In this report, we describe the identification of five MAP kinase sites (S-1137, S-1167, S-1178, S-1193, and S-1197) on hSos1.Replacing the MAP kinase phosphorylation sites with alanine residues results in an increase in the binding affinity of Grb2 to hSos1

Identifier	Residue	Sequence	Organism
SIGNOR-43943	Ser1167	ESAPAESsPSKIMSK	Homo sapiens
pmid	sentence
8816480	In this report, we describe the identification of five map kinase sites (s-1137, s-1167, s-1178, s-1193, and s-1197) on hsos1

Identifier	Residue	Sequence	Organism
SIGNOR-43947	Ser1178	IMSKHLDsPPAIPPR	Homo sapiens
pmid	sentence
8816480	In this report, we describe the identification of five map kinase sites (s-1137, s-1167, s-1178, s-1193, and s-1197) on hsos1

Identifier	Residue	Sequence	Organism
SIGNOR-43951	Ser1193	QPTSKAYsPRYSISD	Homo sapiens
pmid	sentence
8816480	In this report, we describe the identification of five map kinase sites (s-1137, s-1167, s-1178, s-1193, and s-1197) on hsos1

Identifier	Residue	Organism
SIGNOR-26338		Homo sapiens
pmid	sentence
7478566	For example, inactivation of sos through phosphorylation by the downstream mapk

Publications:

5

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-80096	Ser117	YPSMPAFsPGPGIKE	Homo sapiens	Hep-G2 Cell
pmid	sentence
10915800	Map kinases erk1/2 phosphorylate sterol regulatory element-binding protein (srebp)-1a at serine 117 in vitro. mutation of serine 117 to alanine abolished erk2-mediated phosphorylation in vitro and the map kinase-related transcriptional activation of srebp-1a by insulin and platelet-derived growth factor in vivo.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-91139	Ser1185	GTPPASTsPFSQLAA	Homo sapiens	Prostate Gland Cancer Cell
pmid	sentence
12163482	Mapk also directly phosphorylates src-1 at thr1179 and ser1185. Phosphorylation of src-1 by mitogen-activated protein kinase (mapk) is required for optimal progesterone receptor-dependent transcription and for functional cooperation with camp response element-binding protein-binding protein

Identifier	Residue	Sequence	Organism
SIGNOR-91143	Thr1179	NYGTNPGtPPASTSP	Homo sapiens
pmid	sentence
12163482	Mapk also directly phosphorylates src-1 at thr1179 and ser1185. Phosphorylation of src-1 by mitogen-activated protein kinase (mapk) is required for optimal progesterone receptor-dependent transcription and for functional cooperation with camp response element-binding protein-binding protein

Publications:

2

Organism:

Homo Sapiens

Pathways:

Glucocorticoid receptor Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-249473	Ser12	ESPLCPLsPLEAGDL	Homo sapiens
pmid	sentence
10187842	We now demonstrate that amino acids 1-92 of hPPARalpha contain an activation function (AF)-1-like domain, which is further activated by insulin through a pathway involving the mitogen-activated protein kinases p42 and p44. Further analysis of the amino-terminal region of PPARalpha revealed that the insulin-induced trans-activation occurs through the phosphorylation of two mitogen-activated protein kinase sites at positions 12 and 21, both of which are conserved across evolution.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249474	Ser21	LEAGDLEsPLSEEFL	Homo sapiens	Hep-G2 Cell
pmid	sentence
10187842	We now demonstrate that amino acids 1-92 of hPPARalpha contain an activation function (AF)-1-like domain, which is further activated by insulin through a pathway involving the mitogen-activated protein kinases p42 and p44. Further analysis of the amino-terminal region of PPARalpha revealed that the insulin-induced trans-activation occurs through the phosphorylation of two mitogen-activated protein kinase sites at positions 12 and 21, both of which are conserved across evolution.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-116153	Ser122	DGRMVQLsPPALAAP	Homo sapiens
pmid	sentence
11904294	We report here that the important proangiogenic stimulus hypoxia stimulates phosphorylation, ubiquitination, and proteasomal breakdown of tal1 in endothelial cells. A specific serine in the putative transactivation domain of the protein, ser122, is preferentially phosphorylated by mapk in vitro.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-280027	Ser124	FARTVARsPVAPARG	Homo sapiens
pmid	sentence
25219500	By contrast, MAFG-S124A was not phosphorylated, indicating that ERK1 phosphorylates MAFG at S124.\|Notably, cotransfection of ERK1 increased total levels of wild-type MAFG and MAFG-T3A but not MAFG-S124A, indicating that phosphorylation increased MAFG stability.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-169879	Ser1409	SAPEDPTsPKRKMRR	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)[...] These results suggest that erk phosphorylation of ser1382 and ser1409 masks the nls and prevents its binding to kpna3

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-102224	Ser142	IQKNLHPsYSCKYEG	Homo sapiens
pmid	sentence
12809513	We concluded that serine 142 of the tr dbd is the likely site of phosphorylation by t(4)-activated mapk and that the docking site on tr for activated mapk includes residues 128-133 (kgffrr), a basic amino acid-enriched motif novel for mapk substrates. Tr mutations in the proposed mapk docking domain and at residue 142 modulated t(4)-conditioned shedding of co-repressor and recruitment of co-activator proteins by the receptor, and they altered transcriptional activity of tr in a thyroid hormone response element-luciferase reporter assay.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-100270	Ser15	PSVEPPLsQETFSDL	Homo sapiens
pmid	sentence
12955074	Mutant p53 is constitutively phosphorylated at serine 15 in uv-induced mouse skin tumors: involvement of erk1/2 map kinase.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-138171	Ser150	PELCGPGsPPVLTPG	Homo sapiens
pmid	sentence
15952796	Phosphorylation of grb10 by mitogen-activated protein kinase: identification of ser150 and ser476 of human grb10zeta as major phosphorylation sitesreplacing ser(150) and ser(476) with alanines reduced the inhibitory effect of human grb10zeta on insulin-stimulated irs1 tyrosine phosphorylation

Identifier	Residue	Sequence	Organism
SIGNOR-138175	Ser476	MNILGSQsPLHPSTL	Homo sapiens
pmid	sentence
15952796	Phosphorylation of grb10 by mitogen-activated protein kinase: identification of ser150 and ser476 of human grb10zeta as major phosphorylation sitesreplacing ser(150) and ser(476) with alanines reduced the inhibitory effect of human grb10zeta on insulin-stimulated irs1 tyrosine phosphorylation

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-259921	Ser151	VARSNPKsPQKPIVR	Homo sapiens	Melanoma Cell
pmid	sentence
21478863	We show that overactivation of the MAPK pathway, induced by the oncogenic Ras in melanoma, induces constitutive phosphorylation of BRAF on Ser151 by ERK, which inhibits NRAS-BRAF interaction

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-88728	Ser152	PASSVSSsPSPPFGH	Homo sapiens
pmid	sentence
12050114	Biochemical analyses have then shown that erk mapk (erk2) and jnk/sapk (jnk2) bind to and phosphorylate tob in vitro. Erk catalyzes the phosphorylation more efficiently than jnk

Identifier	Residue	Sequence	Organism
SIGNOR-88732	Ser154	SSVSSSPsPPFGHSA	Homo sapiens
pmid	sentence
12050114	Tob is rapidly phosphorylated at Ser 152, Ser 154, and Ser 164 by Erk1 and Erk2 upon growth-factor stimulation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-91059	Ser154	SSVSSSPsPPFGHSA	Homo sapiens	T-lymphocyte
pmid	sentence
12151396	Biochemical analyses have then shown that erk mapk (erk2) and jnk/sapk (jnk2) bind to and phosphorylate tob in vitro. Erk catalyzes the phosphorylation more efficiently than jnk

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-91063	Ser164	FGHSAAVsPTFMPRS	Homo sapiens	T-lymphocyte
pmid	sentence
12151396	Biochemical analyses have then shown that erk mapk (erk2) and jnk/sapk (jnk2) bind to and phosphorylate tob in vitro. Erk catalyzes the phosphorylation more efficiently than jnk

Identifier	Residue	Sequence	Organism
SIGNOR-88736	Ser164	FGHSAAVsPTFMPRS	Homo sapiens
pmid	sentence
12050114	Biochemical analyses have then shown that erk mapk (erk2) and jnk/sapk (jnk2) bind to and phosphorylate tob in vitro. Erk catalyzes the phosphorylation more efficiently than jnk

Publications:

5

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-188164	Ser158	KSDGACDsPSSDKEN	Homo sapiens
pmid	sentence
19776015	Wstf, a specific component of two chromatin remodeling complexes (swi/snf-type winac and iswi-type wich), was phosphorylated by the stimulation of mapk cascades in vitro and in vivo. Ser-158 residue in the wac (wstf/acf1/cbpq46) domain, located close to the n terminus of wstf, was identified as a major phosphorylation target

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-132975	Ser159	DGSCSSSsPPLPVLG	Homo sapiens
pmid	sentence
15632084	Phosphorylation of serines 159 and 197 by erk1/2 enhances proteasomal degradation of mkp-3

Identifier	Residue	Sequence	Organism
SIGNOR-132979	Ser197	SATDSDGsPLSNSQP	Homo sapiens
pmid	sentence
15632084	Phosphorylation of serines 159 and 197 by erk1/2 enhances proteasomal degradation of mkp-3

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-120172	Ser1619	SPSYSPTsPSYSPTS	Homo sapiens
pmid	sentence
14662762	Erk1/2 are major ser-5 kinases after h2o2 treatment. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination.

Identifier	Residue	Sequence	Organism
SIGNOR-120176	Ser1626	SPSYSPTsPSYSPTS	Homo sapiens
pmid	sentence
14662762	Erk1/2 are major ser-5 kinases after h2o2 treatment. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination.

Identifier	Residue	Sequence	Organism
SIGNOR-120180	Ser1647	SPSYSPTsPSYSPTS	Homo sapiens
pmid	sentence
14662762	Erk1/2 are major ser-5 kinases after h2o2 treatment. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination.

Identifier	Residue	Sequence	Organism
SIGNOR-120184	Ser1654	SPSYSPTsPSYSPTS	Homo sapiens
pmid	sentence
14662762	Erk1/2 are major ser-5 kinases after h2o2 treatment. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination.

Identifier	Residue	Sequence	Organism
SIGNOR-120188	Ser1668	SPSYSPTsPSYSPTS	Homo sapiens
pmid	sentence
14662762	Erk1/2 are major ser-5 kinases after h2o2 treatment. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination.

Identifier	Residue	Sequence	Organism
SIGNOR-120192	Ser1675	SPSYSPTsPSYSPTS	Homo sapiens
pmid	sentence
14662762	Erk1/2 are major ser-5 kinases after h2o2 treatment. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination.

Identifier	Residue	Sequence	Organism
SIGNOR-120196	Ser1696	SPSYSPTsPSYSPTS	Homo sapiens
pmid	sentence
14662762	Erk1/2 are major ser-5 kinases after h2o2 treatment. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination.

Identifier	Residue	Sequence	Organism
SIGNOR-120200	Ser1717	SPSYSPTsPSYSPTS	Homo sapiens
pmid	sentence
14662762	Erk1/2 are major ser-5 kinases after h2o2 treatment. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination.

Identifier	Residue	Sequence	Organism
SIGNOR-120204	Ser1724	SPSYSPTsPSYSPTS	Homo sapiens
pmid	sentence
14662762	Erk1/2 are major ser-5 kinases after h2o2 treatment. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination.

Identifier	Residue	Sequence	Organism
SIGNOR-120208	Ser1738	SPSYSPTsPSYSPTS	Homo sapiens
pmid	sentence
14662762	Erk1/2 are major ser-5 kinases after h2o2 treatment. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination.

Identifier	Residue	Sequence	Organism
SIGNOR-120212	Ser1766	SPSYSPTsPSYSPTS	Homo sapiens
pmid	sentence
14662762	Erk1/2 are major ser-5 kinases after h2o2 treatment. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination.

Identifier	Residue	Sequence	Organism
SIGNOR-120216	Ser1787	SPNYSPTsPSYSPTS	Homo sapiens
pmid	sentence
14662762	Erk1/2 are major ser-5 kinases after h2o2 treatment. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination.

Identifier	Residue	Sequence	Organism
SIGNOR-120220	Ser1864	SPKYSPTsPKYSPTS	Homo sapiens
pmid	sentence
14662762	Erk1/2 are major ser-5 kinases after h2o2 treatment. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination.

Identifier	Residue	Sequence	Organism
SIGNOR-120224	Ser1871	SPKYSPTsPKYSPTS	Homo sapiens
pmid	sentence
14662762	Erk1/2 are major ser-5 kinases after h2o2 treatment. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination.

Identifier	Residue	Sequence	Organism
SIGNOR-120228	Ser1882	SPTSPTYsPTTPKYS	Homo sapiens
pmid	sentence
14662762	Erk1/2 are major ser-5 kinases after h2o2 treatment. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination.

Identifier	Residue	Sequence	Organism
SIGNOR-120232	Ser1892	TPKYSPTsPTYSPTS	Homo sapiens
pmid	sentence
14662762	Erk1/2 are major ser-5 kinases after h2o2 treatment. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination.

Identifier	Residue	Sequence	Organism
SIGNOR-120236	Ser1899	SPTYSPTsPVYTPTS	Homo sapiens
pmid	sentence
14662762	Erk1/2 are major ser-5 kinases after h2o2 treatment. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination.

Identifier	Residue	Sequence	Organism
SIGNOR-120240	Ser1913	SPKYSPTsPTYSPTS	Homo sapiens
pmid	sentence
14662762	Erk1/2 are major ser-5 kinases after h2o2 treatment. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination.

Identifier	Residue	Sequence	Organism
SIGNOR-120244	Ser1920	SPTYSPTsPKYSPTS	Homo sapiens
pmid	sentence
14662762	Erk1/2 are major ser-5 kinases after h2o2 treatment. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination.

Identifier	Residue	Sequence	Organism
SIGNOR-120248	Ser1927	SPKYSPTsPTYSPTS	Homo sapiens
pmid	sentence
14662762	Erk1/2 are major ser-5 kinases after h2o2 treatment. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination.

Identifier	Residue	Sequence	Organism
SIGNOR-120252	Ser1934	SPTYSPTsPKGSTYS	Homo sapiens
pmid	sentence
14662762	Erk1/2 are major ser-5 kinases after h2o2 treatment. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination.

Identifier	Residue	Sequence	Organism
SIGNOR-120256	Ser1944	GSTYSPTsPGYSPTS	Homo sapiens
pmid	sentence
14662762	Erk1/2 are major ser-5 kinases after h2o2 treatment. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination.

Identifier	Residue	Sequence	Organism
SIGNOR-120260	Ser1951	SPGYSPTsPTYSLTS	Homo sapiens
pmid	sentence
14662762	Erk1/2 are major ser-5 kinases after h2o2 treatment. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination.

Publications:

23

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-79519	Ser165	LFQLGPPsPVKMPSP	Homo sapiens
pmid	sentence
10906323	Pttg is phosphorylated in vitro on ser(162) by map kinase and this phosphorylation site plays an essential role in pttg transactivation function.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249478	Ser167	FLISPPAsPPVGWKQ	Mus musculus	C2C12 Cell
pmid	sentence
12063245	Consensus phosphorylation sites for p42/44 MAPK and GSK-3 are present in the SP repeat of MCIP1 at serine 112 and serine 108, respectively \|Several endogenous proteins are capable of inhibiting the catalytic activity of calcineurin. Modulatory calcineurin interacting protein 1 (MCIP1) is unique among these proteins on the basis of its pattern of expression and its function in a negative feedback loop to regulate calcineurin activity. Here we show that MCIP1 can be phosphorylated by MAPK and glycogen synthase kinase-3 and that phosphorylated MCIP1 is a substrate for calcineurin.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-74564	Ser172	YRDPSCLsPASSLSS	Homo sapiens
pmid	sentence
10652349	We show that jnk, erk, and p38 physically associate with the nfatc n-terminal regulatory domain and can directly phosphorylate functionally important residues involved in regulating nfatc subcellular localization, namely ser(172) and the conserved nfatc ser-pro repeats.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262914	Ser173	MLETLSQsPPKGVTI	Homo sapiens	K-562 Cell
pmid	sentence
17475908	We also identified 4 hnRNP-E2 MAPKERK1/2 phosphorylation sites and demonstrated that hnRNP-E2 is a bona fide MAPKERK1/2 substrate and that MAPKERK1/2-dependent phosphorylation of hnRNP-E2 at these amino acid residues is essential for increased hnRNP-E2 expression in BCR/ABL-expressing cells. Serine/threonine to alanine substitution abolishes hnRNP-E2 phosphorylation and markedly decreases its stability in BCR/ABL-expressing myeloid precursors. Consistent with the existence of a BCR/ABL-MAPK pathway that posttranslationally regulates hnRNP-E2 expression, sequence analysis of hnRNP-E2 revealed the presence of 4 consensus ERK phosphorylation sites (S/T-P)35,36 at amino acid residues 173, 189, 213, and 272 (Figure 2B).

Identifier	Residue	Sequence	Organism
SIGNOR-262915	Ser189	YRPKPSSsPVIFAGG	Homo sapiens
pmid	sentence
17475908	We also identified 4 hnRNP-E2 MAPKERK1/2 phosphorylation sites and demonstrated that hnRNP-E2 is a bona fide MAPKERK1/2 substrate and that MAPKERK1/2-dependent phosphorylation of hnRNP-E2 at these amino acid residues is essential for increased hnRNP-E2 expression in BCR/ABL-expressing cells. Serine/threonine to alanine substitution abolishes hnRNP-E2 phosphorylation and markedly decreases its stability in BCR/ABL-expressing myeloid precursors. Consistent with the existence of a BCR/ABL-MAPK pathway that posttranslationally regulates hnRNP-E2 expression, sequence analysis of hnRNP-E2 revealed the presence of 4 consensus ERK phosphorylation sites (S/T-P)35,36 at amino acid residues 173, 189, 213, and 272 (Figure 2B).

Identifier	Residue	Sequence	Organism
SIGNOR-262916	Ser272	FSGIESSsPEVKGYW	Homo sapiens
pmid	sentence
17475908	We also identified 4 hnRNP-E2 MAPKERK1/2 phosphorylation sites and demonstrated that hnRNP-E2 is a bona fide MAPKERK1/2 substrate and that MAPKERK1/2-dependent phosphorylation of hnRNP-E2 at these amino acid residues is essential for increased hnRNP-E2 expression in BCR/ABL-expressing cells. Serine/threonine to alanine substitution abolishes hnRNP-E2 phosphorylation and markedly decreases its stability in BCR/ABL-expressing myeloid precursors. Consistent with the existence of a BCR/ABL-MAPK pathway that posttranslationally regulates hnRNP-E2 expression, sequence analysis of hnRNP-E2 revealed the presence of 4 consensus ERK phosphorylation sites (S/T-P)35,36 at amino acid residues 173, 189, 213, and 272 (Figure 2B).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262917	Thr213	SASFPHTtPSMCLNP	Homo sapiens	K-562 Cell
pmid	sentence
17475908	We also identified 4 hnRNP-E2 MAPKERK1/2 phosphorylation sites and demonstrated that hnRNP-E2 is a bona fide MAPKERK1/2 substrate and that MAPKERK1/2-dependent phosphorylation of hnRNP-E2 at these amino acid residues is essential for increased hnRNP-E2 expression in BCR/ABL-expressing cells. Serine/threonine to alanine substitution abolishes hnRNP-E2 phosphorylation and markedly decreases its stability in BCR/ABL-expressing myeloid precursors. Consistent with the existence of a BCR/ABL-MAPK pathway that posttranslationally regulates hnRNP-E2 expression, sequence analysis of hnRNP-E2 revealed the presence of 4 consensus ERK phosphorylation sites (S/T-P)35,36 at amino acid residues 173, 189, 213, and 272 (Figure 2B).

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-188466	Ser174	ESPSPPQsPQEESFS	Homo sapiens	Melanoma Cell
pmid	sentence
19828458	Mage-11 ser-174 appears to be a post-translational regulatory site phosphorylated by erk1, based on the inhibitory effect of the s174a mutation in the context of shorter ar nh2-terminal fragments (19), and the greater transcriptional activity of gal-mage-11 fusion proteins containing the s174d phosphomimetic.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-120467	Ser175	EEEEDLSsPPGLPEP	Homo sapiens
pmid	sentence
14697653	Thus, fe65 has at least two apparently disparate functions and may also be involved in the pathogenesis of alzheimer's disease. The mechanisms by which fe65 trafficking and metabolism are regulated to fulfil these different roles are unclear. Our findings reported here, which demonstrate that fe65 is a phosphoprotein that is targeted by erk1/2 and which identify four in vivo phosphorylation sites, provide one possible mechanism whereby functional diversity might be achieved.

Identifier	Residue	Sequence	Organism
SIGNOR-120475	Ser287	WEPPGRAsPSQGSSP	Homo sapiens
pmid	sentence
14697653	Thus, fe65 has at least two apparently disparate functions and may also be involved in the pathogenesis of alzheimer's disease. The mechanisms by which fe65 trafficking and metabolism are regulated to fulfil these different roles are unclear. Our findings reported here, which demonstrate that fe65 is a phosphoprotein that is targeted by erk1/2 and which identify four in vivo phosphorylation sites, provide one possible mechanism whereby functional diversity might be achieved.

Identifier	Residue	Sequence	Organism
SIGNOR-120479	Ser347	TFPAQSLsPEPLPQE	Homo sapiens
pmid	sentence
14697653	Thus, fe65 has at least two apparently disparate functions and may also be involved in the pathogenesis of alzheimer's disease. The mechanisms by which fe65 trafficking and metabolism are regulated to fulfil these different roles are unclear. Our findings reported here, which demonstrate that fe65 is a phosphoprotein that is targeted by erk1/2 and which identify four in vivo phosphorylation sites, provide one possible mechanism whereby functional diversity might be achieved.

Identifier	Residue	Sequence	Organism
SIGNOR-120483	Thr709	PKRLGAHtP	Homo sapiens
pmid	sentence
14697653	Thus, fe65 has at least two apparently disparate functions and may also be involved in the pathogenesis of alzheimer's disease. The mechanisms by which fe65 trafficking and metabolism are regulated to fulfil these different roles are unclear. Our findings reported here, which demonstrate that fe65 is a phosphoprotein that is targeted by erk1/2 and which identify four in vivo phosphorylation sites, provide one possible mechanism whereby functional diversity might be achieved.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-249620	Ser180	PGSSAPNsPMAMLTL
pmid	sentence
10841026	More interestingly, ERK-dependent phosphorylation of MITF at Ser 73 is essential for MITF ubiquitinilation and degradation (87). Putting together all these findings, it can be proposed that MAPK activation inhibits melanogenesis due to an increased MITF degradation which is dependent on the MAPK-induced MITF phosphorylation and ubiquitinilation. In summary, although the phosphorylation of MITF at Ser73 increases its intrinsic transcriptional activity, this phosphorylation also targets MITF to the proteasome for its degradation. Consequently, the decrease in MITF levels leads to a down-regulation of melanogenic enzymes expression and to an inhibition of melanogenesis.

Publications:

1

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-269086	Ser189 Ser283	SGILGITsPSADTNK DMKANLAsPTPADIG	Homo sapiens	RAMOS (RA.1) Cell
pmid	sentence
22593617	In this study, we demonstrated that PAX5 was phosphorylated by ERK1/2 in vitro and in vivo at serines 189 and 283. This phosphorylation attenuated the transcriptional repression of BLIMP1 by PAX5.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276102	Ser196	EKSPSVCsPLNMTSS	Homo sapiens	M1 Melanoma Cell
pmid	sentence
22798426	Taken together, these data suggest that ERK1/2 directly phosphorylates the MR on several serine residues present in its NTD, that the upward shift of MR is mainly due to receptor phosphorylation, and finally that these sites represent the major aldosterone-inducible targets for MR phosphorylation.MR phosphorylation limits the transcriptional activity.Taken together, these results provide evidence that MR phosphorylation plays a role in aldosterone-mediated ubiquitylation and degradation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276111	Ser227	FGSFPVHsPITQGTP	Homo sapiens	M1 Melanoma Cell
pmid	sentence
22798426	Taken together, these data suggest that ERK1/2 directly phosphorylates the MR on several serine residues present in its NTD, that the upward shift of MR is mainly due to receptor phosphorylation, and finally that these sites represent the major aldosterone-inducible targets for MR phosphorylation.MR phosphorylation limits the transcriptional activity.Taken together, these results provide evidence that MR phosphorylation plays a role in aldosterone-mediated ubiquitylation and degradation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276112	Ser238	QGTPLTCsPNVENRG	Homo sapiens	M1 Melanoma Cell
pmid	sentence
22798426	Taken together, these data suggest that ERK1/2 directly phosphorylates the MR on several serine residues present in its NTD, that the upward shift of MR is mainly due to receptor phosphorylation, and finally that these sites represent the major aldosterone-inducible targets for MR phosphorylation.MR phosphorylation limits the transcriptional activity.Taken together, these results provide evidence that MR phosphorylation plays a role in aldosterone-mediated ubiquitylation and degradation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276108	Ser263	NVGSPLSsPLSSMKS	Homo sapiens	M1 Melanoma Cell
pmid	sentence
22798426	Taken together, these data suggest that ERK1/2 directly phosphorylates the MR on several serine residues present in its NTD, that the upward shift of MR is mainly due to receptor phosphorylation, and finally that these sites represent the major aldosterone-inducible targets for MR phosphorylation.MR phosphorylation limits the transcriptional activity.Taken together, these results provide evidence that MR phosphorylation plays a role in aldosterone-mediated ubiquitylation and degradation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276110	Ser287	SVKSPVSsPNNVTLR	Homo sapiens	M1 Melanoma Cell
pmid	sentence
22798426	Taken together, these data suggest that ERK1/2 directly phosphorylates the MR on several serine residues present in its NTD, that the upward shift of MR is mainly due to receptor phosphorylation, and finally that these sites represent the major aldosterone-inducible targets for MR phosphorylation.MR phosphorylation limits the transcriptional activity.Taken together, these results provide evidence that MR phosphorylation plays a role in aldosterone-mediated ubiquitylation and degradation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276106	Ser361	TLRDVVPsPDTQEKG	Homo sapiens	M1 Melanoma Cell
pmid	sentence
22798426	Taken together, these data suggest that ERK1/2 directly phosphorylates the MR on several serine residues present in its NTD, that the upward shift of MR is mainly due to receptor phosphorylation, and finally that these sites represent the major aldosterone-inducible targets for MR phosphorylation.MR phosphorylation limits the transcriptional activity.Taken together, these results provide evidence that MR phosphorylation plays a role in aldosterone-mediated ubiquitylation and degradation.

Publications:

6

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277337	Ser200	EEEEEIHsPTLLPEA	Homo sapiens	HeLa Cell
pmid	sentence
28179426	Here we show that Lin28a is directly phosphorylated by ERK1/2 kinases at Ser-200.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-186125	Ser207	PYEITLLsPCLHMLP	Homo sapiens
pmid	sentence
19524539	Lysrs serves as a key signaling molecule in the immune response by regulating gene expression. Lysrs was phosphorylated on serine 207 in a mapk-dependent manner, released from the multisynthetase complex, and translocated into the nucleus.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-120570	Ser21	PMSSHLQsPPHAPSS	Homo sapiens	Monocyte
pmid	sentence
14701740	Ccaat/enhancer-binding protein alpha (c/ebpalpha) is one of the key transcription factors that mediate lineage specification and differentiation of multipotent myeloid progenitors into mature granulocytes.Here we report that inducers of monocyte differentiation inhibit the alternate cell fate choice, that of granulopoiesis, through inhibition of c/ebpalpha. This inhibition is mediated by extracellular signal-regulated kinases 1 and/or 2 (erk1/2), which interact with c/ebpalpha through an fxfp docking site and phosphorylate serine 21.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-264773	Ser21	KRTSSPRsPPSSSEI	Homo sapiens
pmid	sentence
25728771	When phosphorylated by ERK, MCRIP1 dissociates from CtBP, allowing CtBP to interact with ZEB1. In this manner, the CtBP co-repressor complex is recruited to, and silences, the E-cadherin promoter by inducing chromatin modifications.\| While substitution of S4 or S18 with Ala did not affect the phosphorylation of MCRIP1 by ERK, substitution of either S21 or T30 significantly reduced MCRIP1 phosphorylation

Identifier	Residue	Sequence	Organism
SIGNOR-264772	Thr30	PSSSEIFtPAHEENV	Homo sapiens
pmid	sentence
25728771	When phosphorylated by ERK, MCRIP1 dissociates from CtBP, allowing CtBP to interact with ZEB1. In this manner, the CtBP co-repressor complex is recruited to, and silences, the E-cadherin promoter by inducing chromatin modifications.\| While substitution of S4 or S18 with Ala did not affect the phosphorylation of MCRIP1 by ERK, substitution of either S21 or T30 significantly reduced MCRIP1 phosphorylation

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-123656	Ser213	DNMIRRLsPAERAQG	Mus musculus
pmid	sentence
15060146	Tel became phosphorylated by erk on two serine residues, ser213 and ser257, in the internal domain between the hlh and ets domains. Tel lost its abilities to repress transcription through the phosphorylation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-260085	Ser257	ESHPKPSsPRQESTR	Mus musculus	NIH-3T3 Cell
pmid	sentence
15060146	Tel became phosphorylated by erk on two serine residues, ser213 and ser257, in the internal domain between the hlh and ets domains. Tel lost its abilities to repress transcription through the phosphorylation.

Publications:

2

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-280257	Ser220	NTIRKALsQLKGGGL	Homo sapiens	U-87MG Cell
pmid	sentence
40467571	Mechanistically, glucose deprivation-activated ERK1 phosphorylates GLYCTK2 at serine 220 directly, which prevents STUB1 (ubiquitin E3 ligase) binding, thereby abrogating the ubiquitination and degradation of GLYCTK2. ERK1 phosphorylates GLYCTK2 at S220 to promotes its stability

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-188151	Ser221	KVAAETQsPSLFGST	Homo sapiens
pmid	sentence
19767751	Erk phosphorylates nup50 at ser221 and ser315 erk phosphorylation of the fg repeat region of nup50 reduced its affinity for importin-beta family proteins, importin-beta and transportin.

Publications:

1

Organism:

Homo Sapiens

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-38999		Mus musculus
pmid	sentence
8387505	The pp90rsk phosphothreonine content paralleled the ERK1 activity more closely than the phosphoserine level. These results provide compelling evidence that in fibroblasts and PC12 cells ERK1 plays a direct role in the phosphorylation of pp90rsk and that pp90rsk represents a physiologically relevant substrate of extracellular-regulated kinases

Identifier	Residue	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.

Publications:

8

Organism:

Chlorocebus Aethiops, Mus Musculus, Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252758	Ser221	DHEKKAYsFCGTVEY	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-252759	Ser363	TSRTPKDsPGIPPSA	Chlorocebus aethiops	COS-1 Cell
pmid	sentence
9430688	Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252756	Ser380	HQLFRGFsFVATGLM	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-252761	Ser732	RRVRKLPsTTL	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-252755	Thr359	DTEFTSRtPKDSPGI	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-252757	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-252762		Mus musculus
pmid	sentence
8387505	The pp90rsk phosphothreonine content paralleled the ERK1 activity more closely than the phosphoserine level. These results provide compelling evidence that in fibroblasts and PC12 cells ERK1 plays a direct role in the phosphorylation of pp90rsk and that pp90rsk represents a physiologically relevant substrate of extracellular-regulated kinases

Identifier	Residue	Organism	Cell Line
SIGNOR-252760		Homo sapiens	HEK-293 Cell
pmid	sentence
12832467	Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity.Erk-activates the rsk family of serine/threonine kinases,rsk1, rsk2, and rsk3.

Publications:

8

Organism:

Chlorocebus Aethiops, Mus Musculus, Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-172881	Ser225	ARLGSQHsPGRTASL	Homo sapiens
pmid	sentence
21419341	We show that erk colocalizes with the wrc at lamellipodial leading edges and directly phosphorylates two wrc components: wave2 and abi1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-118550	Ser225	VGSKTPAsPVVVQQG	Homo sapiens
pmid	sentence
14532121	Activation of sphingosine kinase 1 by erk1/2-mediated phosphorylation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-154409	Ser226	IDENCLLsPLAGEDD	in vitro
pmid	sentence
9199329	Cyclin-dependent kinase (CDK) and mitogen-activated protein kinase (MAPK) phosphorylate the rat glucocorticoid receptor in vitro at distinct sites that together correspond to the major phosphorylated receptor residues observed in vivo; MAPK phosphorylates receptor residues threonine 171 and serine 246, whereas multiple CDK complexes modify serines 224 and 232.\|MAPKs and CDKs exert opposite effects on receptor transcriptional enhancement. From our results, we speculate that activators of the MAPK pathway, such as growth factors, insulin, and certain oncoproteins, or inhibitors of CDK function, such as tumor growth factor beta (TGF_), p21, and p27, might attenuate receptor-induced transcrip- tional responses. In contrast, negative regulators of MAPK, such as pKA, as well as activators of CDK, such as the cyclins or CAKs, should potentiate receptor action.

Publications:

1

Organism:

In Vitro

Pathways:

Glucocorticoid receptor Signaling

Identifier	Residue	Sequence	Organism
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
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	Organism
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

Identifier	Residue	Sequence	Organism
SIGNOR-277587	Ser235	MELLNEKsPSSQETH	in vitro
pmid	sentence
35216969	Screening the DEPTOR interactome identified that the association of USP-7 deubiquitinase with DEPTOR was dependent upon S235 phosphorylation. Inhibition of USP-7 activity resulted in DEPTOR polyubiquitination and degradation. A scansite search suggested that ERK1 may be responsible for S235 phosphorylation, which was confirmed through the use of inhibitors, ERK1 knockdown, and an in vitro kinase assay.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276003	Ser244	QPVSAPPsPRDISME	Homo sapiens	HEK-293 Cell
pmid	sentence
14712216	We have characterized the H4(D10S170) gene product, showing that it is a ubiquitously expressed 55 KDa nuclear and cytosolic protein that is phosphorylated following serum stimulation. This phosphorylation was found to depend on mitogen-activated protein kinase (MAPK) Erk1/2 activity and to be associated to the relocation of H4(D10S170) from the nucleus to the cytosol. S244 is the major target residue of ERK1

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-66759	Ser245	NQSMDTGsPAELSPT	Homo sapiens
pmid	sentence
10197981	These results suggest that oncogenic ras, acting through mek1 and erk kinases, induces the phosphorylation of smad2 and smad3 .we show that phosphorylation of smad2, a mediator of the activin/transforming growth factor-beta signal, by activated extracellular signal-regulated kinase 1 (erk1) increases the amount of smad2 protein and leads to enhanced transcriptional activity

Identifier	Residue	Sequence	Organism
SIGNOR-182988	Ser245	NQSMDTGsPAELSPT	Homo sapiens
pmid	sentence
19115199	These results suggest that oncogenic ras, acting through mek1 and erk kinases, induces the phosphorylation of smad2 and smad3 .we show that phosphorylation of smad2, a mediator of the activin/transforming growth factor-beta signal, by activated extracellular signal-regulated kinase 1 (erk1) increases the amount of smad2 protein and leads to enhanced transcriptional activity

Identifier	Residue	Sequence	Organism
SIGNOR-91730	Ser245	NQSMDTGsPAELSPT	Homo sapiens
pmid	sentence
12193595	These results suggest that oncogenic ras, acting through mek1 and erk kinases, induces the phosphorylation of smad2 and smad3 .we show that phosphorylation of smad2, a mediator of the activin/transforming growth factor-beta signal, by activated extracellular signal-regulated kinase 1 (erk1) increases the amount of smad2 protein and leads to enhanced transcriptional activity

Identifier	Residue	Sequence	Organism
SIGNOR-91734	Ser250	TGSPAELsPTTLSPV	Homo sapiens
pmid	sentence
12193595	These results suggest that oncogenic ras, acting through mek1 and erk kinases, induces the phosphorylation of smad2 and smad3 .we show that phosphorylation of smad2, a mediator of the activin/transforming growth factor-beta signal, by activated extracellular signal-regulated kinase 1 (erk1) increases the amount of smad2 protein and leads to enhanced transcriptional activity

Identifier	Residue	Sequence	Organism
SIGNOR-182992	Ser250	TGSPAELsPTTLSPV	Homo sapiens
pmid	sentence
19115199	These results suggest that oncogenic ras, acting through mek1 and erk kinases, induces the phosphorylation of smad2 and smad3 .we show that phosphorylation of smad2, a mediator of the activin/transforming growth factor-beta signal, by activated extracellular signal-regulated kinase 1 (erk1) increases the amount of smad2 protein and leads to enhanced transcriptional activity

Identifier	Residue	Sequence	Organism
SIGNOR-66763	Ser250	TGSPAELsPTTLSPV	Homo sapiens
pmid	sentence
10197981	These results suggest that oncogenic ras, acting through mek1 and erk kinases, induces the phosphorylation of smad2 and smad3 .we show that phosphorylation of smad2, a mediator of the activin/transforming growth factor-beta signal, by activated extracellular signal-regulated kinase 1 (erk1) increases the amount of smad2 protein and leads to enhanced transcriptional activity

Identifier	Residue	Sequence	Organism
SIGNOR-182996	Ser255	ELSPTTLsPVNHSLD	Homo sapiens
pmid	sentence
19115199	These results suggest that oncogenic ras, acting through mek1 and erk kinases, induces the phosphorylation of smad2 and smad3 .we show that phosphorylation of smad2, a mediator of the activin/transforming growth factor-beta signal, by activated extracellular signal-regulated kinase 1 (erk1) increases the amount of smad2 protein and leads to enhanced transcriptional activity

Identifier	Residue	Sequence	Organism
SIGNOR-91738	Ser255	ELSPTTLsPVNHSLD	Homo sapiens
pmid	sentence
12193595	These results suggest that oncogenic ras, acting through mek1 and erk kinases, induces the phosphorylation of smad2 and smad3 .we show that phosphorylation of smad2, a mediator of the activin/transforming growth factor-beta signal, by activated extracellular signal-regulated kinase 1 (erk1) increases the amount of smad2 protein and leads to enhanced transcriptional activity

Identifier	Residue	Sequence	Organism
SIGNOR-66767	Ser255	ELSPTTLsPVNHSLD	Homo sapiens
pmid	sentence
10197981	These results suggest that oncogenic ras, acting through mek1 and erk kinases, induces the phosphorylation of smad2 and smad3 .we show that phosphorylation of smad2, a mediator of the activin/transforming growth factor-beta signal, by activated extracellular signal-regulated kinase 1 (erk1) increases the amount of smad2 protein and leads to enhanced transcriptional activity

Identifier	Residue	Sequence	Organism
SIGNOR-66771	Thr220	QSNYIPEtPPPGYIS	Homo sapiens
pmid	sentence
10197981	These results suggest that oncogenic ras, acting through mek1 and erk kinases, induces the phosphorylation of smad2 and smad3 .we show that phosphorylation of smad2, a mediator of the activin/transforming growth factor-beta signal, by activated extracellular signal-regulated kinase 1 (erk1) increases the amount of smad2 protein and leads to enhanced transcriptional activity

Identifier	Residue	Sequence	Organism
SIGNOR-183000	Thr220	QSNYIPEtPPPGYIS	Homo sapiens
pmid	sentence
19115199	These results suggest that oncogenic ras, acting through mek1 and erk kinases, induces the phosphorylation of smad2 and smad3 .we show that phosphorylation of smad2, a mediator of the activin/transforming growth factor-beta signal, by activated extracellular signal-regulated kinase 1 (erk1) increases the amount of smad2 protein and leads to enhanced transcriptional activity

Identifier	Residue	Sequence	Organism
SIGNOR-91742	Thr220	QSNYIPEtPPPGYIS	Homo sapiens
pmid	sentence
12193595	These results suggest that oncogenic ras, acting through mek1 and erk kinases, induces the phosphorylation of smad2 and smad3 .we show that phosphorylation of smad2, a mediator of the activin/transforming growth factor-beta signal, by activated extracellular signal-regulated kinase 1 (erk1) increases the amount of smad2 protein and leads to enhanced transcriptional activity

Identifier	Residue	Sequence	Organism
SIGNOR-66775	Thr8	MSSILPFtPPVVKRL	Homo sapiens
pmid	sentence
10197981	These results suggest that oncogenic ras, acting through mek1 and erk kinases, induces the phosphorylation of smad2 and smad3 .we show that phosphorylation of smad2, a mediator of the activin/transforming growth factor-beta signal, by activated extracellular signal-regulated kinase 1 (erk1) increases the amount of smad2 protein and leads to enhanced transcriptional activity

Identifier	Residue	Sequence	Organism
SIGNOR-183004	Thr8	MSSILPFtPPVVKRL	Homo sapiens
pmid	sentence
19115199	These results suggest that oncogenic ras, acting through mek1 and erk kinases, induces the phosphorylation of smad2 and smad3 .we show that phosphorylation of smad2, a mediator of the activin/transforming growth factor-beta signal, by activated extracellular signal-regulated kinase 1 (erk1) increases the amount of smad2 protein and leads to enhanced transcriptional activity

Identifier	Residue	Sequence	Organism
SIGNOR-91746	Thr8	MSSILPFtPPVVKRL	Homo sapiens
pmid	sentence
12193595	These results suggest that oncogenic ras, acting through mek1 and erk kinases, induces the phosphorylation of smad2 and smad3 .we show that phosphorylation of smad2, a mediator of the activin/transforming growth factor-beta signal, by activated extracellular signal-regulated kinase 1 (erk1) increases the amount of smad2 protein and leads to enhanced transcriptional activity

Publications:

15

Organism:

Homo Sapiens

Tissue:

Lung, Breast, Lung

Identifier	Residue	Sequence	Organism
SIGNOR-249482	Ser25	QAFELILsPRSKESV	Homo sapiens
pmid	sentence
9731215	Stress-induced stathmin phosphorylation is not de- pendent on ERK. Stathmin is also known to be phos- phorylated by ERK on Ser-25 and Ser-38 (17). Thus, it is possible that ERK phosphorylates stathmin in 293 cells\|In subsequent reports (28, 29) it was shown that phosphorylation of stathmin blocks its ability to destabilize MTs.

Identifier	Residue	Sequence	Organism
SIGNOR-249483	Ser38	SVPEFPLsPPKKKDL	Homo sapiens
pmid	sentence
9731215	Stress-induced stathmin phosphorylation is not de- pendent on ERK. Stathmin is also known to be phos- phorylated by ERK on Ser-25 and Ser-38 (17). Thus, it is possible that ERK phosphorylates stathmin in 293 cells\|In subsequent reports (28, 29) it was shown that phosphorylation of stathmin blocks its ability to destabilize MTs.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-279071	Ser251	VKSEASSsPPVVTSS	Homo sapiens
pmid	sentence
29556337	Mass spectrum analysis was employed after an in vitro kinase assay in which cells were incubated with or without ERK1-active kinase, and the results demonstrated that Sox2 was phosphorylated by ERK1 directly at S251, which was further verified by western blotting for the specific antibody targeting S251 phosphorylated Sox2 after the in vitro kinase assay.\|Mechanistically, ERK1 kinase promoted autophagic degradation of Sox2 via phosphorylation of Sox2 at Ser251 and further SUMOylation of Sox2 at Lys245 in non CSCs.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249465	Ser255	HATSGALsPAKDCGS	Homo sapiens
pmid	sentence
9535909	These studies confirm that connexin-43 is a MAP kinase substrate in vivo and that phosphorylation on Ser255, Ser279, and/or Ser282 initiates the down-regulation of gap junctional communication. Studies with connexin-43 mutants suggest that MAP kinase phosphorylation at one or more of the tandem Ser279/Ser282 sites is sufficient to disrupt gap junctional intercellular communication.

Identifier	Residue	Sequence	Organism
SIGNOR-249466	Ser279	SSPTAPLsPMSPPGY	Homo sapiens
pmid	sentence
9535909	These studies confirm that connexin-43 is a MAP kinase substrate in vivo and that phosphorylation on Ser255, Ser279, and/or Ser282 initiates the down-regulation of gap junctional communication. Studies with connexin-43 mutants suggest that MAP kinase phosphorylation at one or more of the tandem Ser279/Ser282 sites is sufficient to disrupt gap junctional intercellular communication.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249467	Ser282	TAPLSPMsPPGYKLV	Homo sapiens	HeLa Cell
pmid	sentence
9535909	These studies confirm that connexin-43 is a MAP kinase substrate in vivo and that phosphorylation on Ser255, Ser279, and/or Ser282 initiates the down-regulation of gap junctional communication. Studies with connexin-43 mutants suggest that MAP kinase phosphorylation at one or more of the tandem Ser279/Ser282 sites is sufficient to disrupt gap junctional intercellular communication.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-88662	Ser260	NMGLNPSsPNDPVTN	Homo sapiens
pmid	sentence
17604322	In colon cancer cells, the Ras/mitogen‐activated protein kinase (MAPK) pathway phosphorylates RXRalpha, which impairs its function as a heterodimeric partner for PPARgamma\|A point‐mutated RXRalpha T82A/S260A, which mimics the unphosphorylated form of RXRalpha, can form a heterodimer with PPARgamma and thereby activate target gene expression by binding to the PPRE

Identifier	Residue	Sequence	Organism
SIGNOR-262959	Thr82	HSMSVPTtPTLGFST	Homo sapiens
pmid	sentence
17604322	In colon cancer cells, the Ras/mitogen‐activated protein kinase (MAPK) pathway phosphorylates RXRalpha, which impairs its function as a heterodimeric partner for PPARgamma\|A point‐mutated RXRalpha T82A/S260A, which mimics the unphosphorylated form of RXRalpha, can form a heterodimer with PPARgamma and thereby activate target gene expression by binding to the PPRE

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-275434	Ser267	RVQSKIGsLDNITHV	in vitro
pmid	sentence
10090741	We have studied the relationship between the phosphorylation oftau by several kinases (MARK, PKA, MAPK, GSK3) and its assembly into PHFs. By contrast, MARK and PKA phosphorylate several sites within the repeats (notably theKXGS motifs including Ser262, Ser324, and Ser356, plus Ser320); in addition PKA phosphorylates somesites in the flanking domains, notably Ser214. This type of phosphorylation strongly reduces tau’s affinityfor microtubules, and at the same time inhibits tau’s assembly into PHFs.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-197932	Ser27	PFRDSPLsSRLLDDG	Homo sapiens
pmid	sentence
22721717	Hsp22 is phosphorylated by protein kinase c (at residues ser(14) and thr(63)) and by p44 mitogen-activated protein kinase (at residues ser(27) and thr(87)). Concerning the possible function of hsp22, no definitive conclusions can be drawn with the available data, although its function might be to bind to and modulate the activity of hsp27.Some Studies claimed that phosphorylation is required for the translocation

Identifier	Residue	Sequence	Organism
SIGNOR-197936	Thr87	GVPAEGRtPPPFPGE	Homo sapiens
pmid	sentence
22721717	Hsp22 is phosphorylated by protein kinase c (at residues ser(14) and thr(63)) and by p44 mitogen-activated protein kinase (at residues ser(27) and thr(87)). Concerning the possible function of hsp22, no definitive conclusions can be drawn with the available data, although its function might be to bind to and modulate the activity of hsp27.Some Studies claimed that phosphorylation is required for the translocation

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-107676	Ser27	PFRDSPLsSRLLDDG	Homo sapiens
pmid	sentence
11342557	Hsp22 is phosphorylated by protein kinase c (at residues ser(14) and thr(63)) and by p44 mitogen-activated protein kinase (at residues ser(27) and thr(87)). Concerning the possible function of hsp22, no definitive conclusions can be drawn with the available data, although its function might be to bind to and modulate the activity of hsp27.Some Studies claimed that phosphorylation is required for the translocation

Identifier	Residue	Sequence	Organism
SIGNOR-107680	Thr87	GVPAEGRtPPPFPGE	Homo sapiens
pmid	sentence
11342557	Hsp22 is phosphorylated by protein kinase c (at residues ser(14) and thr(63)) and by p44 mitogen-activated protein kinase (at residues ser(27) and thr(87)). Concerning the possible function of hsp22, no definitive conclusions can be drawn with the available data, although its function might be to bind to and modulate the activity of hsp27.Some Studies claimed that phosphorylation is required for the translocation

Publications:

2

Organism:

Homo Sapiens

Tissue:

Muscle

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264441	Ser272	CSLERQLsLEQEVQQ	Homo sapiens	HeLa Cell
pmid	sentence
12670876	Intriguingly, a significant difference in the potency of nonredox-type inhibitors (but not of BWA4C) was determined between wild-type 5-LO and the mutant S271A/S663A-5-LO (lacking phosphorylation sites for ERK1/2 and MAPKAPK-2) in HeLa cells. Collectively, our data suggest that compared with Ca2+-mediated 5-LO product formation, enzyme activation involving 5-LO phosphorylation events specifically and strongly alters the susceptibility of 5-LO toward nonredox-type inhibitors in intact cells.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264440	Ser664	QLPYYYLsPDRIPNS	Homo sapiens	HeLa Cell
pmid	sentence
12670876	Intriguingly, a significant difference in the potency of nonredox-type inhibitors (but not of BWA4C) was determined between wild-type 5-LO and the mutant S271A/S663A-5-LO (lacking phosphorylation sites for ERK1/2 and MAPKAPK-2) in HeLa cells. Collectively, our data suggest that compared with Ca2+-mediated 5-LO product formation, enzyme activation involving 5-LO phosphorylation events specifically and strongly alters the susceptibility of 5-LO toward nonredox-type inhibitors in intact cells.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275978	Ser277	ASPGSLHsPQQLAEE	Mus musculus	AtT-20 Cell
pmid	sentence
11466319	The MAPKs extracellular signal-regulated kinases 1 and 2 physically interact with ICER and mediated the phosphorylation of ICER on a critical serine residue (Ser-41). A mutant form of ICER in which Ser-41 was substituted by alanine had a half-life 4-5 h longer than its wild-type counterpart. This alteration in stability was due to the inability of the Ser-41-mutant ICER to be efficiently ubiquitinated and degraded via the ubiquitin-proteasome pathway.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-150545	Ser280	TVHGLPTsPDRPGST	Homo sapiens	T-lymphocyte, Macrophage
pmid	sentence
17095509	We found that in these cells, lipopolysaccharide stimulates the expression of mhc ii genes via the activation of erk1/2, which is mediated by toll-like receptor 4. Erk1/2 then phosphorylates the serine at position 357, which is located in a degron of ciita isoform 1 that leads to its monoubiquitylation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-164231	Ser282	VGKQAPLsPGLPAMG	Homo sapiens
pmid	sentence
20230789	Accumulating evidence indicates that protein phosphorylation regulates nox activity. In this report, we show that serine282 residue of nox activator 1 (noxa1) is phosphorylated by erk in response to egf resulting in desensitization of nox1 activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-145375	Ser284	RRDYDDMsPRRGPPP	Homo sapiens
pmid	sentence
16564677	Erk phosphorylation drives cytoplasmic accumulation of hnrnp-k and inhibition of mrna translation mitogen-activated protein kinase/extracellular-signal-regulated kinase (mapk/erk) efficiently phosphorylates hnrnp-k both in vitro and in vivo at serines 284 and 353.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-105238	Ser284	RRDYDDMsPRRGPPP	Homo sapiens
pmid	sentence
11231586	Erk phosphorylation drives cytoplasmic accumulation of hnrnp-k and inhibition of mrna translation mitogen-activated protein kinase/extracellular-signal-regulated kinase (mapk/erk) efficiently phosphorylates hnrnp-k both in vitro and in vivo at serines 284 and 353.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-160617	Ser288	PDRPGSTsPFAPSAT	Homo sapiens
pmid	sentence
18245089	In this study we show that the extracellular signal-regulated kinases 1 and 2 (erk1/2) interact directly with ciita, targeting serine residues in the amino terminus of the protein, including serine 288. These data suggest a model whereby erk1/2-mediated phosphorylation of ciita down-regulates ciita activity by priming it for nuclear export, thus providing a means for cells to tightly regulate the extent of antigen presentation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-143688	Ser289	RSHSESAsPSALSSS	Mus musculus
pmid	sentence
15664191	Here, we identify six residues of Raf-1 (S29, S43, S289, S296, S301, and S642) that become hyperphosphorylated in a manner coincident with Raf-1 inactivation. \| Five of the identified sites are proline-directed targets of activated ERK, and phosphorylation of all six sites requires MEK signaling, indicating a negative feedback mechanism. Hyperphosphorylation of these six sites inhibits the Ras/Raf-1 interaction and desensitizes Raf-1 to additional stimuli.\|FLAG-Raf-1 phosphorylated by activated ERK2

Identifier	Residue	Sequence	Organism
SIGNOR-143692	Ser296	SPSALSSsPNNLSPT	Mus musculus
pmid	sentence
15664191	Here, we identify six residues of Raf-1 (S29, S43, S289, S296, S301, and S642) that become hyperphosphorylated in a manner coincident with Raf-1 inactivation. \| Five of the identified sites are proline-directed targets of activated ERK, and phosphorylation of all six sites requires MEK signaling, indicating a negative feedback mechanism. Hyperphosphorylation of these six sites inhibits the Ras/Raf-1 interaction and desensitizes Raf-1 to additional stimuli.\|FLAG-Raf-1 phosphorylated by activated ERK2

Publications:

2

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-184176	Ser291	TYVNNSPsPGFNSSH	Homo sapiens
pmid	sentence
19237534	We previously established that phosphorylation of lsf in early g1 at ser-291 and ser-309 inhibits its transcriptional activity and that dephosphorylation later in g1 is required for its reactivation. At the peak activities of erk and cyclin c/cdk2 in early g1, lsf is efficiently phosphorylated on ser-291 and ser-309.

Identifier	Residue	Sequence	Organism
SIGNOR-184180	Ser309	SLGEGNGsPNHQPEP	Homo sapiens
pmid	sentence
19237534	We previously established that phosphorylation of lsf in early g1 at ser-291 and ser-309 inhibits its transcriptional activity and that dephosphorylation later in g1 is required for its reactivation. At the peak activities of erk and cyclin c/cdk2 in early g1, lsf is efficiently phosphorylated on ser-291 and ser-309.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-126867	Ser293	PAPARPRsPSQTRKG	Homo sapiens
pmid	sentence
15262992	Thus, we propose that mapk phosphorylation of amphiphysin1 controls ngf receptor/trka-mediated endocytosis by terminating the amphiphysin1-ap-2 interaction.Our results indicate that phosphorylation of amphiphysin 1 at ser-285 and/or ser-293 affects the function of amphiphysin1.Mapk phosphorylation of ser-285 and ser-293 could modulate the interaction between prd and ap-2, resulting in the dissociation of amphiphysin1 from ap-2.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252961	Ser294	QLSKWPGsPTSRSSD	Homo sapiens
pmid	sentence
19282669	Phosphorylation of foxo3a by erk1/2 at residues ser 294, ser 344 and ser 425 increases foxo3amdm2 interaction and enhances foxo3a degradation via an mdm2-dependent ubiquitin-proteasome pathway

Identifier	Residue	Sequence	Organism
SIGNOR-252962	Ser344	QDDDAPLsPMLYSSS	Homo sapiens
pmid	sentence
19282669	Phosphorylation of foxo3a by erk1/2 at residues ser 294, ser 344 and ser 425 increases foxo3amdm2 interaction and enhances foxo3a degradation via an mdm2-dependent ubiquitin-proteasome pathway

Identifier	Residue	Sequence	Organism
SIGNOR-252963	Ser425	TKGSGLGsPTSSFNS	Homo sapiens
pmid	sentence
19282669	Phosphorylation of foxo3a by erk1/2 at residues ser 294, ser 344 and ser 425 increases foxo3amdm2 interaction and enhances foxo3a degradation via an mdm2-dependent ubiquitin-proteasome pathway

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-74716	Ser294	APMAPGRsPLATTVM	Homo sapiens	Breast Cancer Cell
pmid	sentence
10655479	Specifically, down-regulation of mature prs occurs by a mechanism in which ligand binding activates pr phosphorylation by mapks at a unique serine residue, which then targets the receptors for degradation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-188343	Ser294	DPRQAQSsPPWSYDQ	Homo sapiens
pmid	sentence
19801668	In this study, we identified two phosphorylation sites in runx2 at ser301 and ser319 that are required for mapk-dependent activation of runx2 transcriptional activity and osteoblast differentiation.

Identifier	Residue	Sequence	Organism
SIGNOR-188347	Ser312	SYLSQMTsPSIHSTT	Homo sapiens
pmid	sentence
19801668	In this study, we identified two phosphorylation sites in runx2 at ser301 and ser319 that are required for mapk-dependent activation of runx2 transcriptional activity and osteoblast differentiation.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-184569	Ser294	QLSKWPGsPTSRSSD	Homo sapiens
pmid	sentence
19282669	Phosphorylation of foxo3a by erk1/2 at residues ser 294, ser 344 and ser 425 increases foxo3amdm2 interaction and enhances foxo3a degradation via an mdm2-dependent ubiquitin-proteasome pathway

Identifier	Residue	Sequence	Organism
SIGNOR-184573	Ser344	QDDDAPLsPMLYSSS	Homo sapiens
pmid	sentence
19282669	Phosphorylation of foxo3a by erk1/2 at residues ser 294, ser 344 and ser 425 increases foxo3amdm2 interaction and enhances foxo3a degradation via an mdm2-dependent ubiquitin-proteasome pathway

Identifier	Residue	Sequence	Organism
SIGNOR-184577	Ser425	TKGSGLGsPTSSFNS	Homo sapiens
pmid	sentence
19282669	Phosphorylation of foxo3a by erk1/2 at residues ser 294, ser 344 and ser 425 increases foxo3amdm2 interaction and enhances foxo3a degradation via an mdm2-dependent ubiquitin-proteasome pathway

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-126871	Ser295	PARPRSPsQTRKGPP	Homo sapiens
pmid	sentence
15262992	Thus, we propose that mapk phosphorylation of amphiphysin1 controls ngf receptor/trka-mediated endocytosis by terminating the amphiphysin1-ap-2 interaction.Our results indicate that phosphorylation of amphiphysin 1 at ser-285 and/or ser-293 affects the function of amphiphysin1.Mapk phosphorylation of ser-285 and ser-293 could modulate the interaction between prd and ap-2, resulting in the dissociation of amphiphysin1 from ap-2.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Brain

Identifier	Residue	Sequence	Organism
SIGNOR-141605	Ser296	KQRRSIIsPNFSFMG	Homo sapiens
pmid	sentence
16286470	The dual-specificity mapk phosphatase mkp-1/cl100/dusp1 is an inducible nuclear protein controlled by p44/42 mapk (erk1/2) in a negative feedback mechanism to inhibit kinase activity. Here, we report on the molecular basis for a novel positive feedback mechanism to sustain erk activation by triggering mkp-1 proteolysis. Active erk2 docking to the def motif (fxfp, residues 339-342) of n-terminally truncated mkp-1 in vitro initiated phosphorylation at the ser(296)/ser(323) domain

Identifier	Residue	Sequence	Organism
SIGNOR-141609	Ser323	HCSAEAGsPAMAVLD	Homo sapiens
pmid	sentence
16286470	The dual-specificity mapk phosphatase mkp-1/cl100/dusp1 is an inducible nuclear protein controlled by p44/42 mapk (erk1/2) in a negative feedback mechanism to inhibit kinase activity. Here, we report on the molecular basis for a novel positive feedback mechanism to sustain erk activation by triggering mkp-1 proteolysis. Active erk2 docking to the def motif (fxfp, residues 339-342) of n-terminally truncated mkp-1 in vitro initiated phosphorylation at the ser(296)/ser(323) domain

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-143696	Ser301	SSSPNNLsPTGWSQP	Homo sapiens
pmid	sentence
16407412	Using mass spectrometry, we identified raf-1 phosphorylation on three sp motif sites: s289/s296/s301. These sites were phosphorylated by extracellular signal-regulated kinase (erk)-1 in vitro, and their phosphorylation in vivo was dependent on endogenous erk activity. Functionally, erk-1 expression sustains raf-1 activation in a manner dependent on raf-1 phosphorylation on the identified sites, and s289/296/301a substitution markedly decreases the in vivo activity of raf-1 s259a.

Identifier	Residue	Organism
SIGNOR-133345		Homo sapiens
pmid	sentence
15664191	Mapkerk1/2 is also able to phopshorylate the egf receptor, the ras exchange factor sos, mkkkraf1, and mkkmek1. The phosphorylation of each of these proteins by mapkerk1/2 is believed to reduce their catalytic activity. previous studies have shown that phosphorylation is required for raf-1 activation, and here, we identify six phosphorylation sites that contribute to the downregulation of raf-1 after mitogen stimulation. Five of the identified sites are proline-directed targets of activated erk

Identifier	Residue	Organism
SIGNOR-64172		Homo sapiens
pmid	sentence
9922370	Mapkerk1/2 is also able to phopshorylate the egf receptor, the ras exchange factor sos, mkkkraf1, and mkkmek1. The phosphorylation of each of these proteins by mapkerk1/2 is believed to reduce their catalytic activity. previous studies have shown that phosphorylation is required for raf-1 activation, and here, we identify six phosphorylation sites that contribute to the downregulation of raf-1 after mitogen stimulation. Five of the identified sites are proline-directed targets of activated erk

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-44999	Ser307	EPPSPPQsPRVEEAS	Homo sapiens
pmid	sentence
8940068	Sequential phosphorylation of hsf1 by mitogen-activated protein kinase and glycogen synthase kinase 3 at ser-303 and ser-307 represses transcriptional activation by heat shock factor-1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-134841	Ser315	GRMLQAIsPKQSPSS	Homo sapiens
pmid	sentence
15788406	Oxysterols inhibit phosphatidylcholine synthesis via erk docking and phosphorylation of ctp:phosphocholine cytidylyltransferase. Mutagenesis of ser315 within cctalpha was both required and sufficient to confer significant resistance to 22-hc/9-cis-ra inhibition of ptdcho synthesis.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Lung

Identifier	Residue	Sequence	Organism
SIGNOR-187378	Ser315	TQSKPVSsPFPTKPL	Homo sapiens
pmid	sentence
19767751	Erk phosphorylates nup50 at ser221 and ser315 phosphorylation of nup50 reduces affinity for importin-beta

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-263060	Ser317	TPQGSRTsPGAPPPA	in vitro
pmid	sentence
15133517	To identify the phosphorylated residue, we introduced a serine-to-alanine substitution at residues 294 and 326 and a threonine-to-alanine substitution at residue 331 in Irx2(291–356). Erk1 phosphorylated S294A and T331A, but not S326A (Fig. 4b), indicating that Ser326 is the bona fide MAP kinase target.

Identifier	Residue	Sequence	Organism
SIGNOR-263061	Ser325	PGAPPPAsKPKLWSL	in vitro
pmid	sentence
15133517	To identify the phosphorylated residue, we introduced a serine-to-alanine substitution at residues 294 and 326 and a threonine-to-alanine substitution at residue 331 in Irx2(291–356). Erk1 phosphorylated S294A and T331A, but not S326A (Fig. 4b), indicating that Ser326 is the bona fide MAP kinase target.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-34653	Ser324	RDLELPLsPSLLGGP	Homo sapiens
pmid	sentence
7889942	Erki phosphorylates five c-terminal sites in elk-i (s324, t336, s383, s389 and s422) with varying degrees of efficiency.

Identifier	Residue	Sequence	Organism
SIGNOR-34657	Ser383	IHFWSTLsPIAPRSP	Homo sapiens
pmid	sentence
7889942	Erki phosphorylates five c-terminal sites in elk-i (s324, t336, s383, s389 and s422) with varying degrees of efficiency.

Identifier	Residue	Sequence	Organism
SIGNOR-34661	Ser389	LSPIAPRsPAKLSFQ	Homo sapiens
pmid	sentence
7889942	Erki phosphorylates five c-terminal sites in elk-i (s324, t336, s383, s389 and s422) with varying degrees of efficiency.

Identifier	Residue	Sequence	Organism
SIGNOR-34665	Ser422	LSTPVVLsPGPQKP	Homo sapiens
pmid	sentence
7889942	Erki phosphorylates five c-terminal sites in elk-i (s324, t336, s383, s389 and s422) with varying degrees of efficiency.

Identifier	Residue	Sequence	Organism
SIGNOR-34669	Thr336	GGPGPERtPGSGSGS	Homo sapiens
pmid	sentence
7889942	Erki phosphorylates five c-terminal sites in elk-i (s324, t336, s383, s389 and s422) with varying degrees of efficiency.

Identifier	Residue	Organism
SIGNOR-29923		Homo sapiens
pmid	sentence
7618106	The tcf protein elk-1 is phosphorylated by the jnk and erk groups of mitogen-activated protein (map) kinases causing increased dna binding, ternary complex formation, and transcriptional activation

Publications:

6

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-58489	Ser333	KGLVSPQsPQKSDCQ	Homo sapiens	T-lymphocyte, Lymphoma Cell
pmid	sentence
9649500	Here we show that antigen receptor activation leads to bcl-6 phosphorylation by mitogen-activated protein kinase (mapk). Phosphorylation, in turn, targets bcl-6 for rapid degradation by the ubiquitin/proteasome pathway.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-58493	Ser343	KSDCQPNsPTESCSS	Homo sapiens	T-lymphocyte, Lymphoma Cell
pmid	sentence
9649500	Here we show that antigen receptor activation leads to bcl-6 phosphorylation by mitogen-activated protein kinase (mapk). Phosphorylation, in turn, targets bcl-6 for rapid degradation by the ubiquitin/proteasome pathway.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-144317	Ser337	QLAKCVSsPHFQVAE	Homo sapiens
pmid	sentence
16456541	Iex-1 binds to b56 subunits and perk independently, enhances b56 phosphorylation by erk at a conserved ser/pro site in this complex and triggers dissociation from the catalytic subunit.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-277185	Ser343	PTDEVGQsPAAVGLG	Homo sapiens
pmid	sentence
26459638	We found that CDK1 phosphorylates Ser343 of ERK1c, thereby allowing the binding of phosphorylated ERK1c to a complex that consists of PI4KIIIβ (also known as PI4KB) and the 14-3-3γ dimer (encoded by YWHAB).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-40821	Ser345	QARPGPQsPGSPLEE	Homo sapiens
pmid	sentence
8626435	Upon activation, several serine residues on the cytosolic oxidase subunit p47phox become phosphorylated. Mitogen-activated protein kinase phophorylated only the peptide containing ser345/348.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-147174	Ser345	QARPGPQsPGSPLEE	Homo sapiens	Neutrophil
pmid	sentence
16778989	Inhibitors of the erk1/2 pathway abrogated gm-csf-induced phosphorylation of ser345, while p38 mapk inhibitor abrogated tnf-alpha-induced phosphorylation of ser345.These results show that the ala-mutated p47phox acts as a dominant-negative inhibitor of endogenous p47phox and clearly indicate that phosphorylation of ser345 is required for the priming of nadph oxidase activity in neutrophil-like cells.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-73629	Ser359	SALSYLQsPITTSPS	Homo sapiens
pmid	sentence
10617468	Mkp-1 was a target in vivo and in vitro for p42(mapk) or p44(mapk), which phosphorylates mkp-1 on two carboxyl-terminal serine residues, serine 359 and serine 364. This phosphorylation did not modify mkp-1's intrinsic ability to dephosphorylate p44(mapk) but led to stabilization of the protein.

Identifier	Residue	Sequence	Organism
SIGNOR-73633	Ser364	LQSPITTsPSC	Homo sapiens
pmid	sentence
10617468	Mkp-1 was a target in vivo and in vitro for p42(mapk) or p44(mapk), which phosphorylates mkp-1 on two carboxyl-terminal serine residues, serine 359 and serine 364. This phosphorylation did not modify mkp-1's intrinsic ability to dephosphorylate p44(mapk) but led to stabilization of the protein.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
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
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

Identifier	Residue	Sequence
SIGNOR-262997	Ser362	AAAHRKGsSSNEPSS
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

Identifier	Residue	Sequence	Organism
SIGNOR-118023	Ser374	PSSDSLSsPTLLAL	Homo sapiens
pmid	sentence
12972619	In a previous study we have observed that exposure of nih 3t3 cells to pdgf or serum leads to c-fos phosphorylation by erk on specific residues, thr232, thr325, thr331, and ser374, within the cooh-terminal c-fos tad we have recently shown that erk phosphorylates multiple residues within the carboxylterminal transactivation domain (tad) of c-fos, thus resulting in its increased transcriptional activity.

Identifier	Residue	Sequence
SIGNOR-263012	Thr325	TELEPLCtPVVTCTP
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

Identifier	Residue	Sequence	Organism
SIGNOR-118027	Thr325	TELEPLCtPVVTCTP	Homo sapiens
pmid	sentence
12972619	In a previous study we have observed that exposure of nih 3t3 cells to pdgf or serum leads to c-fos phosphorylation by erk on specific residues, thr232, thr325, thr331, and ser374, within the cooh-terminal c-fos tad we have recently shown that erk phosphorylates multiple residues within the carboxylterminal transactivation domain (tad) of c-fos, thus resulting in its increased transcriptional activity.

Identifier	Residue	Sequence
SIGNOR-263008	Thr331	CTPVVTCtPSCTAYT
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

Identifier	Residue	Sequence	Organism
SIGNOR-118031	Thr331	CTPVVTCtPSCTAYT	Homo sapiens
pmid	sentence
12972619	In a previous study we have observed that exposure of nih 3t3 cells to pdgf or serum leads to c-fos phosphorylation by erk on specific residues, thr232, thr325, thr331, and ser374, within the cooh-terminal c-fos tad we have recently shown that erk phosphorylates multiple residues within the carboxylterminal transactivation domain (tad) of c-fos, thus resulting in its increased transcriptional activity.

Publications:

6

Organism:

, Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-272241	Ser371	RIRRSGVsPLHLAAE
pmid	sentence
24044920	Indeed, using mass spectrometry, we showed for the first time that ASB2a is phosphorylated and that phosphorylation of serine-323 (Ser-323) of ASB2a is crucial for the targeting of the actin-binding protein filamin A (FLNa) to degradation. \|Moreover, inhibition of the extracellular signal-regulated kinases 1 and 2 (Erk1/2) activity reduced ASB2a-mediated FLNa degradation.

Publications:

1

Identifier	Residue	Sequence
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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277318	Ser377	PVPCPPPsPGPSAVP	Homo sapiens	HEK-293T Cell
pmid	sentence
34215846	We further demonstrated BAG3, a HSP70 co-chaperone, is a bona fide substrate of SCFFBXO22. FBXO22 mediates BAG3 ubiquitination and degradation that requires ERK-dependent BAG3 phosphorylation at S377.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249459	Ser381	CIPTAGMsPSRSNTI	Cricetulus griseus	CHO Cell
pmid	sentence
15379552	Our results demonstrate that ERK1/2 phosphorylate Gab1 at six serine/threonine residues (T312, S381, S454, T476, S581, S597) in consensus motifs for MAP kinase phosphorylation. \|serine and threonine phosphorylation are capable of modulating the initial signal

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249460	Ser454	YVPMNPNsPPRQHSS	Cricetulus griseus	CHO Cell
pmid	sentence
15379552	Our results demonstrate that ERK1/2 phosphorylate Gab1 at six serine/threonine residues (T312, S381, S454, T476, S581, S597) in consensus motifs for MAP kinase phosphorylation. \|serine and threonine phosphorylation are capable of modulating the initial signal

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249461	Ser551	ELQAPVRsPITRSFA	Cricetulus griseus	CHO Cell
pmid	sentence
15379552	Our results demonstrate that ERK1/2 phosphorylate Gab1 at six serine/threonine residues (T312, S381, S454, T476, S581, S597) in consensus motifs for MAP kinase phosphorylation. \|serine and threonine phosphorylation are capable of modulating the initial signal

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249462	Ser567	DSSRFPMsPRPDSVH	Cricetulus griseus	CHO Cell
pmid	sentence
15379552	Our results demonstrate that ERK1/2 phosphorylate Gab1 at six serine/threonine residues (T312, S381, S454, T476, S581, S597) in consensus motifs for MAP kinase phosphorylation. \|serine and threonine phosphorylation are capable of modulating the initial signal

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249463	Thr312	ISYDIPPtPGNTYQI	Cricetulus griseus	CHO Cell
pmid	sentence
15379552	Our results demonstrate that ERK1/2 phosphorylate Gab1 at six serine/threonine residues (T312, S381, S454, T476, S581, S597) in consensus motifs for MAP kinase phosphorylation. \|serine and threonine phosphorylation are capable of modulating the initial signal

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249464	Thr476	EANYVPMtPGTFDFS	Cricetulus griseus	CHO Cell
pmid	sentence
15379552	Our results demonstrate that ERK1/2 phosphorylate Gab1 at six serine/threonine residues (T312, S381, S454, T476, S581, S597) in consensus motifs for MAP kinase phosphorylation. \|serine and threonine phosphorylation are capable of modulating the initial signal

Publications:

6

Organism:

Cricetulus Griseus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-153387	Ser387	PATVEPAsPTPAHSL	Homo sapiens	Breast Cancer Cell
pmid	sentence
17311928	Sphingosine kinase type 2 activation by erk-mediated phosphorylation. site-directed mutagenesis indicated that hsphk2 is phosphorylated on ser-351 and thr-578 by erk1

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-153391	Thr614	AFRLEPLtPRGVLTV	Homo sapiens	Breast Cancer Cell
pmid	sentence
17311928	Sphingosine kinase type 2 activation by erk-mediated phosphorylation. site-directed mutagenesis indicated that hsphk2 is phosphorylated on ser-351 and thr-578 by erk1

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-203480	Ser387	YLEMDLSsPQTRYIP	Homo sapiens
pmid	sentence
24342355	We demonstrate that perk 1/2 can phosphorylate pro-caspase-8 at s387 by knocking-down the endogenous pro-caspase-8 using rnai and replacing it with its non-phosphorylatable counterpart (s387a), a significant increase in caspase-8 activity

Publications:

1

Organism:

Homo Sapiens

Tissue:

Breast

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-169682	Ser405	KTQTPPVsPAPQPTE	Homo sapiens	Neuron
pmid	sentence
21079800	Cortactin is regulated by multiple phosphorylation events, including phosphorylation of s405 and s418 by extracellular regulated kinases (erk)1/2. Erk1/2 phosphorylation of cortactin has emerged as an important positive regulatory modification, enabling cortactin to bind and activate the arp2/3 regulator neuronal wiskott-aldrich syndrome protein (n-wasp), promoting actin polymerization and enhancing tumor cell movement.

Identifier	Residue	Sequence	Organism
SIGNOR-165208	Ser405	KTQTPPVsPAPQPTE	Homo sapiens
pmid	sentence
20444238	Cortactin is regulated by multiple phosphorylation events, including phosphorylation of s405 and s418 by extracellular regulated kinases (erk)1/2. Erk1/2 phosphorylation of cortactin has emerged as an important positive regulatory modification, enabling cortactin to bind and activate the arp2/3 regulator neuronal wiskott-aldrich syndrome protein (n-wasp), promoting actin polymerization and enhancing tumor cell movement.

Identifier	Residue	Sequence	Organism
SIGNOR-165212	Ser418	TEERLPSsPVYEDAA	Homo sapiens
pmid	sentence
20444238	Cortactin is regulated by multiple phosphorylation events, including phosphorylation of s405 and s418 by extracellular regulated kinases (erk)1/2. Erk1/2 phosphorylation of cortactin has emerged as an important positive regulatory modification, enabling cortactin to bind and activate the arp2/3 regulator neuronal wiskott-aldrich syndrome protein (n-wasp), promoting actin polymerization and enhancing tumor cell movement.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-169686	Ser418	TEERLPSsPVYEDAA	Homo sapiens	Neuron
pmid	sentence
21079800	Cortactin is regulated by multiple phosphorylation events, including phosphorylation of s405 and s418 by extracellular regulated kinases (erk)1/2. Erk1/2 phosphorylation of cortactin has emerged as an important positive regulatory modification, enabling cortactin to bind and activate the arp2/3 regulator neuronal wiskott-aldrich syndrome protein (n-wasp), promoting actin polymerization and enhancing tumor cell movement.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-67634	Ser412	EEEDGTGsPQLNNR	Homo sapiens
pmid	sentence
10347142	Erk1 and erk2 phosphorylate beta-arrestin1 at ser-412 in vitro. . in the resting state, cytosolic arrestin1 proteins are constitutively phosphorylated by extracellular signal-regulated kinase (erk) at ser412, located within their distal c terminus. erk-phosphorylated arrestin1 is unable to associate with clathrin cages, whereas this constraint is removed upon its dephosphorylation

Identifier	Residue	Sequence	Organism
SIGNOR-183484	Ser412	EEEDGTGsPQLNNR	Homo sapiens
pmid	sentence
19153083	Erk1 and erk2 phosphorylate beta-arrestin1 at ser-412 in vitro. . in the resting state, cytosolic arrestin1 proteins are constitutively phosphorylated by extracellular signal-regulated kinase (erk) at ser412, located within their distal c terminus. erk-phosphorylated arrestin1 is unable to associate with clathrin cages, whereas this constraint is removed upon its dephosphorylation

Identifier	Residue	Sequence	Organism
SIGNOR-129589	Ser412	EEEDGTGsPQLNNR	Homo sapiens
pmid	sentence
15456867	Erk1 and erk2 phosphorylate beta-arrestin1 at ser-412 in vitro. . in the resting state, cytosolic arrestin1 proteins are constitutively phosphorylated by extracellular signal-regulated kinase (erk) at ser412, located within their distal c terminus. erk-phosphorylated arrestin1 is unable to associate with clathrin cages, whereas this constraint is removed upon its dephosphorylation

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262979	Ser416	GFPSKTDsPSCEYSR	Homo sapiens	HEK-293 Cell
pmid	sentence
27846390	Here we show that ERK suppresses pre-miRNA export from the nucleus through phosphorylation of exportin-5 (XPO5) at T345/S416/S497. After phosphorylation by ERK, conformation of XPO5 is altered by prolyl isomerase Pin1, resulting in reduction of pre-miRNA loading.

Identifier	Residue	Sequence	Organism
SIGNOR-262982	Ser497	GSLCSVFsPSFVQWE	Homo sapiens
pmid	sentence
27846390	Here we show that ERK suppresses pre-miRNA export from the nucleus through phosphorylation of exportin-5 (XPO5) at T345/S416/S497. After phosphorylation by ERK, conformation of XPO5 is altered by prolyl isomerase Pin1, resulting in reduction of pre-miRNA loading.

Identifier	Residue	Sequence	Organism
SIGNOR-262985	Thr345	GADSDVEtPSNFGKY	Homo sapiens
pmid	sentence
27846390	Here we show that ERK suppresses pre-miRNA export from the nucleus through phosphorylation of exportin-5 (XPO5) at T345/S416/S497. After phosphorylation by ERK, conformation of XPO5 is altered by prolyl isomerase Pin1, resulting in reduction of pre-miRNA loading.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249406	Ser418	QQRKALLsPFSTPVR	in vitro
pmid	sentence
15952796	We identified Ser150, Ser418, and Ser476 of human Grb10 as MAPK-mediated in vitro phosphorylation sites.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-209880	Ser428	SSKIRRLsACKQQ	Homo sapiens
pmid	sentence
25846811	Directly and/or through the activation of p90RSK, ERK phosphorylates LKB-1 at Ser325 and Ser428. The phosphorylation of LKB-1 causes the dissociation of LKB-1 from AMPK, resulting in the impaired activation of AMPK.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-265949	Ser43	RNPEAALsPTFRSDS	Homo sapiens	HEK-293 Cell
pmid	sentence
33217317	Mass spectrometry analysis showed that ERK phosphorylates METTL3 at three highly conserved residues: S43, S50, and S525 (Figures 2D and 2E). Mutational analysis further confirmed these three sites as main ERK phosphorylation sites (Figure 2F). Phosphorylation of METTL3 increases interaction with USP5, decreasing ubiquitination to stabilize the m6 A methyltransferase complex.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-265945	Ser50	SPTFRSDsPVPTAPT	Homo sapiens	HEK-293 Cell
pmid	sentence
33217317	Mass spectrometry analysis showed that ERK phosphorylates METTL3 at three highly conserved residues: S43, S50, and S525 (Figures 2D and 2E). Mutational analysis further confirmed these three sites as main ERK phosphorylation sites (Figure 2F). Phosphorylation of METTL3 increases interaction with USP5, decreasing ubiquitination to stabilize the m6 A methyltransferase complex.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-265947	Ser525	YGMIERLsPGTRKIE	Homo sapiens	HEK-293 Cell
pmid	sentence
33217317	Mass spectrometry analysis showed that ERK phosphorylates METTL3 at three highly conserved residues: S43, S50, and S525 (Figures 2D and 2E). Mutational analysis further confirmed these three sites as main ERK phosphorylation sites (Figure 2F). Phosphorylation of METTL3 increases interaction with USP5, decreasing ubiquitination to stabilize the m6 A methyltransferase complex.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-123049	Ser432	NQNVLLMsPPASDSG	Homo sapiens
pmid	sentence
14988395	Insulin-activated erk-mitogen-activated protein kinases phosphorylate sterol regulatory element-binding protein-2 at serine residues 432 and 455 in vivo.Further characterization by electrophoretic mobility shift assay and promoter reporter gene analyses revealed that phosphorylation does not influence protein/dna interaction, but enhances trans-activity.

Identifier	Residue	Sequence	Organism
SIGNOR-123053	Ser455	SIDSEPGsPLLDDAK	Homo sapiens
pmid	sentence
14988395	Insulin-activated erk-mitogen-activated protein kinases phosphorylate sterol regulatory element-binding protein-2 at serine residues 432 and 455 in vivo.Further characterization by electrophoretic mobility shift assay and promoter reporter gene analyses revealed that phosphorylation does not influence protein/dna interaction, but enhances trans-activity.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-249468	Ser432	SAYGGLTsPGLSYSL
pmid	sentence
16554440	Also, several probable in vivo K8 kinases have been identified including Erk1/2 for K8 Ser431 (Ku and Omary, 1997), and p38 and Jun kinases for K8 Ser73 (Ku et al., 2002a; He et al., 2002).

Identifier	Residue	Sequence	Organism
SIGNOR-196141	Ser432	SAYGGLTsPGLSYSL	Homo sapiens
pmid	sentence
22344252	Our data suggested a close relationship between k8(s431) phosphorylation and keratin reorganization in epithelial tumor cells.

Publications:

2

Organism:

, Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-111515	Ser441	SPRRFIGsPRTPVSP	Rattus norvegicus
pmid	sentence
15774499	Thr 421/Ser 424 have been reported to be targeted by ERK1, 2 (39), JNK or p38 MAPKs (36). Interestingly, with a comparable kinetics, FSH represses ERK1, 2 constitutive phosphorylation in Sertoli cells isolated from 19-d-old rats

Identifier	Residue	Sequence	Organism
SIGNOR-134662	Thr444	RFIGSPRtPVSPVKF	Rattus norvegicus
pmid	sentence
15774499	Thr 421/Ser 424 have been reported to be targeted by ERK1, 2 (39), JNK or p38 MAPKs (36). Interestingly, with a comparable kinetics, FSH represses ERK1, 2 constitutive phosphorylation in Sertoli cells isolated from 19-d-old rats

Identifier	Residue	Organism
SIGNOR-121997		Homo sapiens
pmid	sentence
14967450	Erk phosphorylates multiple cytoplasmatic and cytoskeletal proteins, including mapk-activated protein kinases and the ribosomal p70-s6 kinase

Publications:

3

Organism:

Rattus Norvegicus, Homo Sapiens

Tissue:

Carcinoma Cell

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-195157	Ser454	TGSTPPVsPTPSERS	Homo sapiens	Breast Cancer Cell, Lung Cancer Cell
pmid	sentence
22139079	Serum induces rhoa-dependent translocation of mkl1 from the cytoplasm to the nucleus and also causes a rapid increase in mkl1 phosphorylation. Serum-induced phosphorylation of the serum response factor coactivator mkl1 by the extracellular signal-regulated kinase 1/2 pathway inhibits its nuclear localization.

Identifier	Residue	Sequence	Organism
SIGNOR-179963	Ser454	TGSTPPVsPTPSERS	Homo sapiens
pmid	sentence
18694962	Serum induces rhoa-dependent translocation of mkl1 from the cytoplasm to the nucleus and also causes a rapid increase in mkl1 phosphorylation. Serum-induced phosphorylation of the serum response factor coactivator mkl1 by the extracellular signal-regulated kinase 1/2 pathway inhibits its nuclear localization.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-172642	Ser460	YKACKVDsPTVTTTL	Homo sapiens
pmid	sentence
21385839	Phosphorylation of kinesin light chain 1 at serine 460 modulates binding and trafficking of calsyntenin-1mutation of klc1ser460 to an alanine residue, to preclude phosphorylation, increased the binding of calsyntenin-1, whereas mutation to an aspartate residueklc1ser460 is a predicted mitogen-activated protein kinase (mapk) target site, and we show that extracellular-signal-regulated kinase (erk) phosphorylates this residue in vitro.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-121402	Ser470	PQGQQPLsPQSGSPQ	Homo sapiens
pmid	sentence
14732590	A rare, missense polymorphism, s470n, was identified in the synapsin iii gene and appeared more frequently in individuals with schizophrenia than in controls. Ser470, was determined to be a substrate for mitogen-activated protein kinase, a downstream effector of neurotrophin action.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277584	Ser484	SSCSTPNsPEDYYTS	Homo sapiens	Glioma Stem Cell
pmid	sentence
35191554	The activation of ERK1/2 upon hypoxia promoted HIF-2alpha phosphorylation, enhancing its interaction with USP33.Here, we identified USP33 as essential deubiquitinase that stabilizes HIF-2alpha protein in an ERK1/2-dependent manner to promote hypoxia response in cancer cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-123083	Ser50	GTLFQDPsFPAIPSA	Homo sapiens
pmid	sentence
14993287	Epidermal growth factor activates m-calpain (calpain ii), at least in part, by extracellular signal-regulated kinase-mediated phosphorylation.We now show that erk directly phosphorylates and activates m-calpain both in vitro and in vivo. We identified serine 50 as required for epidermal growth factor (egf)-induced calpain activation in vitro and in vivo.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-38434	Ser505	LNTSYPLsPLSDFAT	Homo sapiens
pmid	sentence
8381049	Activated map kinase phosphorylates cpla2 at ser-505, causing increased enzymatic activity of cpla2, which is only realized upon translocation of cpla2 to the membrane.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-278487	Ser52	MPHTETVsPLPSSMD	Homo sapiens
pmid	sentence
24793005	We found that activation of ERK1 signaling inhibited transactivation activity of Nanog.\|We showed the direct phosphorylation of Nanog by ERK1 and clearly showed that Ser52 is the major phosphorylation site and Ser65 is weakly phosphorylated by ERK1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-146747	Ser523	GVSDVPTsPTLQRPT	Homo sapiens
pmid	sentence
16705159	We hypothesize that phosphorylation of ser523 in jak2 by erks 1 and/or 2 or other as-yet-unidentified kinases acts in a negative feedback manner

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-188143	Ser529	SPMFKFSsPIVKSTE	Homo sapiens
pmid	sentence
19767751	These results indicate that phosphorylation of nup153 and nup214 by erk strongly reduces their affinity for importin-. nup153 depletion caused a strong inhibition of nuclear accumulation of gfp?importin-beta in both erk-inhibited and erk-activated cells (fig. 8b,c), indicating that nup153 is essential for the efficient importin-beta transport.

Identifier	Residue	Sequence	Organism
SIGNOR-188147	Thr388	VYFKPSLtPSGEFRK	Homo sapiens
pmid	sentence
19767751	These results indicate that phosphorylation of nup153 and nup214 by erk strongly reduces their affinity for importin-. nup153 depletion caused a strong inhibition of nuclear accumulation of gfp?importin-beta in both erk-inhibited and erk-activated cells (fig. 8b,c), indicating that nup153 is essential for the efficient importin-beta transport.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-124317	Ser530	DGPPSPRsPVIGSEV	Homo sapiens	Leukemia Cell
pmid	sentence
15093545	Phosphorylation of pml by mitogen-activated protein kinases plays a key role in arsenic trioxide-mediated apoptosis.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-45348	Ser532	KIKQEVEsPTDKSGN	Homo sapiens	JURKAT Cell
pmid	sentence
8960373	Functional analysis of phosphorylation at serine 532 of human c-myb by map kinase. expression of a polypeptide containing the c-myb c-terminal domain stimulated c-myb activity. This effect is reduced upon mapk-dependent phosphorylation of serine 532. Our data suggest that the mapk-dependent state of phosphorylation modifies the cellular function of c-myb by modulating its interaction with a putative inhibitory factor

Identifier	Residue	Sequence	Organism
SIGNOR-43558	Ser532	KIKQEVEsPTDKSGN	Homo sapiens
pmid	sentence
8798443	Here we describe that human c-myb can be phosphorylated by mitogen-activated protein kinases (mapk's) at serine 532 of the carboxy (c-) terminal regulatory domain in vitro. expression of a constitutively active form of ras together with c-myb in transient transfection experiments had no effect on the transcriptional activity of c-myb, while expression of a polypeptide containing the c-myb c-terminal domain stimulated c-myb activity. This effect is reduced upon mapk-dependent phosphorylation of serine 532.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249458	Ser540	KVMARSLsPPPELEE	Mus musculus
pmid	sentence
15851026	Here, we show that Erk may play a critical role in TSC progression through posttranslational inactivation of TSC2. Erk-dependent phosphorylation leads to TSC1-TSC2 dissociation and markedly impairs TSC2 ability to inhibit mTOR signaling, cell proliferation, and oncogenic transformation. \|Serine to alanine substitution at S664 or double S664A/S540A mutagenesis resulted in a marked reduction in TSC2 phosphorylation to a similar extent. In contrast, S540A substitution only moderately impaired TSC2 phosphorylation (Figure 3D), corroborating the notion that in vivo S664 is the most relevant residue for Erk-mediated phosphorylation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249457	Ser664	KKTSGPLsPPTGPPG	Mus musculus	NIH-3T3 Cell
pmid	sentence
15851026	Here, we show that Erk may play a critical role in TSC progression through posttranslational inactivation of TSC2. Erk-dependent phosphorylation leads to TSC1-TSC2 dissociation and markedly impairs TSC2 ability to inhibit mTOR signaling, cell proliferation, and oncogenic transformation. \|Serine to alanine substitution at S664 or double S664A/S540A mutagenesis resulted in a marked reduction in TSC2 phosphorylation to a similar extent. In contrast, S540A substitution only moderately impaired TSC2 phosphorylation (Figure 3D), corroborating the notion that in vivo S664 is the most relevant residue for Erk-mediated phosphorylation.

Identifier	Residue	Organism
SIGNOR-183695		Homo sapiens
pmid	sentence
19188143	Phosphorylation of tsc2 (by akt and erk;refs. 28, 29) and tsc1(by ikkbeta;ref. 30) results in the disruption of the tsc1/2 complex, and thereby activates the oncogenic mtor signaling contributing to tumor progression

Publications:

3

Organism:

Mus Musculus, Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-203290	Ser548	SSPSPPCsPLMADPL	Homo sapiens
pmid	sentence
24269383	We demonstrated that erk1/2 phosphorylate kibra at ser(548) in cells as well as in vitro.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Breast

Identifier	Residue	Sequence	Organism
SIGNOR-248079	Ser59	GGQESQPsPLALLAA	Homo sapiens
pmid	sentence
19318349	PKCalpha, which was activated in senescent cells by ROS strongly activated Erk1/2, and the SA-pErk1/2 in turn phosphorylated Sp1 on Ser(59). Sp1-enhanced transcription of p21(Sdi1) resulted in regulation of cellular senescence in primary human diploid fibroblast cells.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248062	Thr453	SGPIIIRtPTVGPNG	Homo sapiens	HaCaT Cell
pmid	sentence
14744793	We showed that perifosine activates the mitogen-activated protein/extracellular signal-regulated kinase pathway, and this activation promotes the phosphorylation of sp1 in known mitogen-activated protein kinase residues (threonine 453 and 739), thereby leading to increased sp1 binding and enhanced p21(waf1/cip1) transcription.

Identifier	Residue	Sequence	Organism
SIGNOR-248066	Thr453	SGPIIIRtPTVGPNG	Homo sapiens
pmid	sentence
14593115	We showed that perifosine activates the mitogen-activated protein/extracellular signal-regulated kinase pathway, and this activation promotes the phosphorylation of sp1 in known mitogen-activated protein kinase residues (threonine 453 and 739), thereby leading to increased sp1 binding and enhanced p21(waf1/cip1) transcription.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248070	Thr739	SEGSGTAtPSALITT	Homo sapiens	HaCaT Cell
pmid	sentence
14744793	We showed that perifosine activates the mitogen-activated protein/extracellular signal-regulated kinase pathway, and this activation promotes the phosphorylation of sp1 in known mitogen-activated protein kinase residues (threonine 453 and 739), thereby leading to increased sp1 binding and enhanced p21(waf1/cip1) transcription.

Identifier	Residue	Sequence	Organism
SIGNOR-118936	Thr739	SEGSGTAtPSALITT	Homo sapiens
pmid	sentence
14593115	We showed that perifosine activates the mitogen-activated protein/extracellular signal-regulated kinase pathway, and this activation promotes the phosphorylation of sp1 in known mitogen-activated protein kinase residues (threonine 453 and 739), thereby leading to increased sp1 binding and enhanced p21(waf1/cip1) transcription.

Identifier	Residue	Sequence	Organism
SIGNOR-116174	Thr739	SEGSGTAtPSALITT	Homo sapiens
pmid	sentence
11904305	Here we show that p42/p44 mapk directly phosphorylates sp1 on threonines 453 and 739 both in vitro and in vivo. sa-perk1/2 activates the transcription factor, sp1, via ser59 phosphorylation downstream of pkc_, leading to transcription of p21sdi1 and resulting in replicative senescence of hdf cells.

Publications:

6

Organism:

Homo Sapiens

Tissue:

Muscle, Smooth Muscle

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249469	Ser59	EGSNPPAsPLQDNLV	Homo sapiens	HeLa Cell
pmid	sentence
8618896	Phosphorylation at Ser-59 (or alternatively, its mutation to Glu) reverses the inhibition and allows interaction of the p56lck SH2 domain with p62.\|phosphotyrosine-independent binding of p62 to the p56lck SH2 domain appears to provide an alternative pathway for p56lck signaling that is regulated by Ser-59 phosphorylation.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Glucocorticoid receptor Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-123177	Ser616	DDGYMPMsPGVAPVP	Homo sapiens
pmid	sentence
15001544	Rin beta-cells exposed to high glucose exhibited increased c-jun n-terminal kinase (jnk) and erk1/2 activity, which was associated with increased irs-1 phosphorylation at serine (ser)(307) and ser(612), respectively, that inhibits coupling of irs-1 to the insulin receptor and is upstream of the inhibition of irs-1 tyrosine phosphorylation.

Identifier	Residue	Sequence	Organism
SIGNOR-249409	Ser636	SGDYMPMsPKSVSAP	Homo sapiens
pmid	sentence
12510059	Insulin also activates jnk, erk, pkc and mtor, which induce the phosphorylation of irs1 on serine residues 307, 612 and 632 and inhibit its functions. Our results indicate that the insulin-stimulated degradation of irs-1 via the phosphatidylinositol 3-kinase pathway is in part dependent upon the ser(312) phosphorylation of irs-1.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249115	Ser62	ELILKPPsPISEAPR	Rattus norvegicus	Brain
pmid	sentence
9525956	SCG10, a growth cone-enriched MT-destabilizing protein, has been recently characterized as an in vitro substrate for various serine/threonine kinases including PKA, MAP kinase, and CDK (19). We have found that SCG10 is phosphorylated in vivo in developing rat brain.\| The sites for MAP kinase phosphorylation were identified as Ser-62 and Ser-73 of SCG10\|By expressing a series of phosphorylation site mutants, we showed that the MT-destabilizing effect of SCG10 could be modulated. While the nonphosphorylatable mutant showed higher activity than the wild-type protein, the activity of the mutant in which phosphorylation on all four sites was mimicked by an aspartate residue was greatly reduced. These data suggest that the nonphosphorylated state of SCG10 represents the most active form of the protein.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249116	Ser73	EAPRTLAsPKKKDLS	Rattus norvegicus	Brain
pmid	sentence
9525956	SCG10, a growth cone-enriched MT-destabilizing protein, has been recently characterized as an in vitro substrate for various serine/threonine kinases including PKA, MAP kinase, and CDK (19). We have found that SCG10 is phosphorylated in vivo in developing rat brain.\| The sites for MAP kinase phosphorylation were identified as Ser-62 and Ser-73 of SCG10\|By expressing a series of phosphorylation site mutants, we showed that the MT-destabilizing effect of SCG10 could be modulated. While the nonphosphorylatable mutant showed higher activity than the wild-type protein, the activity of the mutant in which phosphorylation on all four sites was mimicked by an aspartate residue was greatly reduced. These data suggest that the nonphosphorylated state of SCG10 represents the most active form of the protein.

Publications:

2

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-236250	Ser62	LLPTPPLsPSRRSGL	in vitro
pmid	sentence
32482868	ERK1 phosphorylates MYC Ser62 resulting in MYC stabilization and activation

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-34678	Ser62	SYTPTPRsPRFIGRR	Homo sapiens
pmid	sentence
7901013	In this paper we have studied the phosphorylation and activation of alternatively spliced forms of human th by mapkap kinase-1 , mapkap kinase-2, map kinase, and cam kinase-11

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-128731	Ser623	ALDFQPSsPSPHRKP	Homo sapiens
pmid	sentence
15356145	Phosphorylation of grb2-associated binder 2 on serine 623 by erk mapk regulates its association with the phosphatase shp-2 and decreases stat5 activation.We and others have demonstrated that il-2-induced tyrosine phosphorylation of gab2 and its interaction with its sh2 domain-containing partners, shp-2, p85 pi3k, and crkl (5, 26, 27). we report that pretreatment of kit 225 cells with the mek inhibitor u0126, strongly decreased the characteristic shift of gab2 in response to il-2 and increased gab2/shp-2 association, an effect that could be ascribed to erk phosphorylation of serine 623.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-263058	Ser625	ADTPPAPsPPPTPAP	in vitro
pmid	sentence
19564905	We further show that the actin barbed-end capping activity of Eps8 is inhibited by brain-derived neurotrophic factor (BDNF) treatment through MAPK-dependent phosphorylation of Eps8 residues S624 and T628. Additionally, an Eps8 mutant, impaired in the MAPK target sites (S624A/T628A), displays increased association to actin-rich structures, is resistant to BDNF-mediated release from microfilaments, and inhibits BDNF-induced filopodia. The opposite is observed for a phosphomimetic Eps8 (S624E/T628E) mutant. Thus, collectively, our data identify Eps8 as a critical capping protein in the regulation of axonal filopodia and delineate a molecular pathway by which BDNF, through MAPK-dependent phosphorylation of Eps8, stimulates axonal filopodia formation, a process with crucial impacts on neuronal development and synapse formation.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-91379	Ser63	KNSDLLTsPDVGLLK	Homo sapiens
pmid	sentence
12169099	Up-regulation of c-jun mrna in cardiac myocytes requires the extracellular signal-regulated kinase cascade, but c-jun n-terminal kinases are required for efficient up-regulation of c-jun protein.

Identifier	Residue	Sequence	Organism
SIGNOR-91383	Ser73	VGLLKLAsPELERLI	Homo sapiens
pmid	sentence
12169099	Up-regulation of c-jun mrna in cardiac myocytes requires the extracellular signal-regulated kinase cascade, but c-jun n-terminal kinases are required for efficient up-regulation of c-jun protein.

Publications:

2

Organism:

Homo Sapiens

Pathways:

Glucocorticoid receptor Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-98980	Ser633	SFDTHFRsPSSSVGS	Homo sapiens
pmid	sentence
12620228	Erk-dependent phosphorylation of the transcription initiation factor tif-ia is required for rna polymerase i transcription and cell growth. phosphopeptide mapping and mutational analysis reveals two serine residues (s633 and s649) that are phosphorylated by erk and rsk kinases. Replacement of s649 by alanine inactivates tif-ia, inhibits pre-rrna synthesis, and retards cell growth.

Identifier	Residue	Sequence	Organism
SIGNOR-98984	Ser649	PVLYMQPsPL	Homo sapiens
pmid	sentence
12620228	Erk-dependent phosphorylation of the transcription initiation factor tif-ia is required for rna polymerase i transcription and cell growth. phosphopeptide mapping and mutational analysis reveals two serine residues (s633 and s649) that are phosphorylated by erk and rsk kinases. Replacement of s649 by alanine inactivates tif-ia, inhibits pre-rrna synthesis, and retards cell growth.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-178731	Ser641	DIKILIAsPSPTHIH	Homo sapiens	HeLa Cell
pmid	sentence
18519666	We show that at least two different nuclear protein kinases, one of them identified as p42/p44 mapk, can modify hif-1_. Analysis of in vitro phosphorylated hif-1_ by mass spectroscopy revealed residues ser-641 and ser-643 as possible mapk phosphorylation sites these data suggest that phosphorylation of ser-641/643 by mapk promotes the nuclear accumulation and transcriptional activity of hif-1_

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-178735	Ser643	KILIASPsPTHIHKE	Homo sapiens	HeLa Cell
pmid	sentence
18519666	We show that at least two different nuclear protein kinases, one of them identified as p42/p44 mapk, can modify hif-1_. Analysis of in vitro phosphorylated hif-1_ by mass spectroscopy revealed residues ser-641 and ser-643 as possible mapk phosphorylation sites these data suggest that phosphorylation of ser-641/643 by mapk promotes the nuclear accumulation and transcriptional activity of hif-1_

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-74304	Ser668	INTKALQsPKRPRSP	Homo sapiens
pmid	sentence
10648599	Tfii-i can be phosphorylated in vitro by erk and mutation of consensus map kinase substrate sites at serines 627 and 633 impairs the phosphorylation of tfii-i by erk and its activity on the c-fos promoter. These results suggest that erk regulates the activity of tfii-i by direct phosphorylation.

Identifier	Residue	Sequence	Organism
SIGNOR-74308	Ser674	QSPKRPRsPGSNSKV	Homo sapiens
pmid	sentence
10648599	Tfii-i can be phosphorylated in vitro by erk and mutation of consensus map kinase substrate sites at serines 627 and 633 impairs the phosphorylation of tfii-i by erk and its activity on the c-fos promoter. These results suggest that erk regulates the activity of tfii-i by direct phosphorylation.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-72582	Ser670	KMKNKPRsPVVELSK	Homo sapiens	HEK-293 Cell
pmid	sentence
10574913	Erk1 phosphorylates grk2 at ser(670). Inhibition of erk activity in hek293 cells potentiates grk2 activity, whereas, conversely, erk activation inhibits grk2 activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-133276	Ser676	SNGRRKRsPTQSFRF	Homo sapiens
pmid	sentence
15657420	The formation of rsk-nfatc4-dna transcription complex is also apparent upon adipogenesis. Bound rsk phosphorylates ser(676) and potentiates nfatc4 dna binding by escalating nfat-dna association. Ser(676) is also targeted by the erk map kinase, which interacts with nfat at a distinct region than rsk. Thus, integration of the erk/rsk signaling pathway provides a mechanism to modulate nfatc4 transcription activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-173413	Ser68	GGGDEPGsPAQGKRG	Homo sapiens	Breast Cancer Cell
pmid	sentence
21502402	Phosphorylation of serine 68 of twist1 by mapks stabilizes twist1 protein and promotes breast cancer cell invasiveness. this ser 68 is phosphorylated by p38, c-jun n-terminal kinases (jnk), and extracellular signal-regulated kinases1/2 in vitro

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-262945	Ser685	PMFSAPSsPMPTSST	in vitro
pmid	sentence
9525907	In vitro, purified mitogen-activated protein (MAP) kinase catalyzed the phosphorylation of Graf on serine 510, suggesting that Graf phosphorylation may be mediated through MAP kinase signaling.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-129878	Ser69	GPLAPPAsPGPFATR	Homo sapiens
pmid	sentence
15486195	In vitro, bimel was phosphorylated by extracellular signal-regulated kinase on ser(69), which resides in the bimel-specific insert region. Using phosphospecific antibody against this site, we show that this residue is actually phosphorylated in cells. We also show that phosphorylation of ser(69) promotes ubiquitination of bimel. We conclude that mek inhibitors sensitize mda-mb231 and hbc4 cells to anoikis by blocking phosphorylation and hence degradation of bimel

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-169526	Ser696	EKNYALPsPATTEGG	Homo sapiens	HEK-293 Cell
pmid	sentence
21071439	We found three proline-directed residues within raptor, ser(8), ser(696), and ser(863), which are directly phosphorylated by erk1/2. Expression of phosphorylation-deficient alleles of raptor revealed that phosphorylation of these sites by erk1/2 normally promotes mtorc1 activity and signaling to downstream substrates, such as 4e-bp1.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-169530	Ser8	MESEMLQsPLLGLGE	Homo sapiens	HEK-293 Cell
pmid	sentence
21071439	We found three proline-directed residues within raptor, ser(8), ser(696), and ser(863), which are directly phosphorylated by erk1/2. Expression of phosphorylation-deficient alleles of raptor revealed that phosphorylation of these sites by erk1/2 normally promotes mtorc1 activity and signaling to downstream substrates, such as 4e-bp1.

Identifier	Residue	Sequence	Organism
SIGNOR-169534	Ser863	LTQSAPAsPTNKGVH	Homo sapiens
pmid	sentence
21071439	We found three proline-directed residues within raptor, ser(8), ser(696), and ser(863), which are directly phosphorylated by erk1/2. Expression of phosphorylation-deficient alleles of raptor revealed that phosphorylation of these sites by erk1/2 normally promotes mtorc1 activity and signaling to downstream substrates, such as 4e-bp1.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-74935	Ser70	RDPVARTsPLQTPAA	Homo sapiens
pmid	sentence
10669763	Erk1 and erk2 directly phosphorylate bcl2 exclusively at ser-70 p44mapk/extracellular signal-regulated kinase 1 (erk1) and p42 mapk/erk2 are activated by il-3, colocalize with mitochondrial bcl2, and can directly phosphorylate bcl2 on ser-70 in a stauro-resistant manner both in vitro and in vivo molecular association.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-77578	Ser715	YQSTIPQsPSPAPDD	Homo sapiens
pmid	sentence
10828059	These straddle the target residue, ser(579), for erk2 phosphorylation of pde4d3. Mutation of either or both of these docking sites prevented erk2 from being co-immunoprecipitated with pde4d3, ablated the ability of epidermal growth factor to inhibit pde4d3 through erk2 action in transfected cos cells, and attenuated the ability of erk2 to phosphorylate pde4d3 in vitro.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-187779	Ser727	NTIDLPMsPRTLDSL	Homo sapiens
pmid	sentence
19723038	The activation of stat-3 is regulated by phosphorylation of tyrosine 705 by receptor and nonreceptor protein tyrosine kinases these include epidermal growth factor receptor (egfr) kinase,92 src,5 janus-activated kinases (jak), and extracellular signal-regulated kinase (erk)a constitutively active galpha16 mutant, galpha16ql, stimulated stat3-dependent luciferase activity as well as the phosphorylation of stat3 at both tyr705 and ser727. Galpha16ql-induced stat3 activation was enhanced by overexpression of extracellular signal-regulated kinase 1 (erk1

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-118596	Ser727	NTIDLPMsPRTLDSL	Homo sapiens	Leukemia Cell
pmid	sentence
14551213	The activation of stat-3 is regulated by phosphorylation of tyrosine 705 by receptor and nonreceptor protein tyrosine kinases these include epidermal growth factor receptor (egfr) kinase,92 src,5 janus-activated kinases (jak), and extracellular signal-regulated kinase (erk)a constitutively active galpha16 mutant, galpha16ql, stimulated stat3-dependent luciferase activity as well as the phosphorylation of stat3 at both tyr705 and ser727. Galpha16ql-induced stat3 activation was enhanced by overexpression of extracellular signal-regulated kinase 1 (erk1

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-118600	Tyr705	DPGSAAPyLKTKFIC	Homo sapiens	Leukemia Cell
pmid	sentence
14551213	The activation of stat-3 is regulated by phosphorylation of tyrosine 705 by receptor and nonreceptor protein tyrosine kinases these include epidermal growth factor receptor (egfr) kinase,92 src,5 janus-activated kinases (jak), and extracellular signal-regulated kinase (erk)a constitutively active galpha16 mutant, galpha16ql, stimulated stat3-dependent luciferase activity as well as the phosphorylation of stat3 at both tyr705 and ser727. Galpha16ql-induced stat3 activation was enhanced by overexpression of extracellular signal-regulated kinase 1 (erk1

Identifier	Residue	Sequence	Organism
SIGNOR-187787	Tyr705	DPGSAAPyLKTKFIC	Homo sapiens
pmid	sentence
19723038	The activation of stat-3 is regulated by phosphorylation of tyrosine 705 by receptor and nonreceptor protein tyrosine kinases these include epidermal growth factor receptor (egfr) kinase,92 src,5 janus-activated kinases (jak), and extracellular signal-regulated kinase (erk)a constitutively active galpha16 mutant, galpha16ql, stimulated stat3-dependent luciferase activity as well as the phosphorylation of stat3 at both tyr705 and ser727. Galpha16ql-induced stat3 activation was enhanced by overexpression of extracellular signal-regulated kinase 1 (erk1

Publications:

4

Organism:

Homo Sapiens

Tissue:

Kidney

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249450	Ser727	NTIDLPMsPRTLDSL	Homo sapiens	HEK-293 Cell
pmid	sentence
14551213	The hematopoietic-specific Galpha16 protein has recently been shown to mediate receptor-induced activation of the signal transducer and activator of transcription 3 (STAT3). In the present study, we have delineated the mechanism by which Galpha16 stimulates STAT3 in human embryonic kidney 293 cells. A constitutively active Galpha16 mutant, Galpha16QL, stimulated STAT3-dependent luciferase activity as well as the phosphorylation of STAT3 at both Tyr705 and Ser727. Galpha16QL-induced STAT3 activation was enhanced by overexpression of extracellular signal-regulated kinase 1 (ERK1),

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-157276	Ser73	CSKIGPPsPGDDEEE	Homo sapiens
pmid	sentence
17685427	Here, we show that sp3, which, as sp1, belongs to the gc-rich binding transcription factor family, is also phosphorylated by erk in vitro on serine 73.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-157711	Ser745	KSRQNLQsPTSSRAT	Homo sapiens	HEK-293 Cell
pmid	sentence
17804409	Erk phosphorylated inos on ser745. Mutation of ser745 to ala did not affect basal inos activity but eliminated inos phosphorylation and activation in response to b1r agonist.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-71041	Ser759	KTPDGNKsPAPKPSD	Homo sapiens
pmid	sentence
10514499	Extracellular signal-regulated kinases (erks) phosphorylate the high molecular mass isoform of the actin-binding protein caldesmon (h-cad) at two sites (ser(759) and ser(789)) during smooth muscle stimulation. Nmr spectroscopy shows that the actin binding properties of the minimal inhibitory region of caldesmon, residues 750-779, alter upon map kinase phosphorylation of ser-759, a residue not involved in actin binding. This phosphorylation leads to markedly diminished actin affinity as a result of the loss of interaction at one of the two sites that bind to f-actin.

Identifier	Residue	Sequence	Organism
SIGNOR-86741	Ser759	KTPDGNKsPAPKPSD	Homo sapiens
pmid	sentence
11983427	The actin binding properties of the minimal inhibitory region of caldesmon, residues 750-779, alter upon map kinase phosphorylation of ser-759. This phosphorylation leads to markedly diminished actin affinity.

Identifier	Residue	Sequence	Organism
SIGNOR-71045	Ser789	QSVDKVTsPTKV	Homo sapiens
pmid	sentence
10514499	Extracellular signal-regulated kinases (erks) phosphorylate the high molecular mass isoform of the actin-binding protein caldesmon (h-cad) at two sites (ser(759) and ser(789)) during smooth muscle stimulation. Nmr spectroscopy shows that the actin binding properties of the minimal inhibitory region of caldesmon, residues 750-779, alter upon map kinase phosphorylation of ser-759, a residue not involved in actin binding. This phosphorylation leads to markedly diminished actin affinity as a result of the loss of interaction at one of the two sites that bind to f-actin.

Publications:

3

Organism:

Homo Sapiens

Tissue:

Smooth Muscle, Muscle, Smooth Muscle

Identifier	Residue	Sequence	Organism
SIGNOR-200884	Ser777	SMPLDQYsPSFPDTR	Homo sapiens
pmid	sentence
23405013	Erk-mediated phosphorylation of fibroblast growth factor receptor 1 on ser777 inhibits signaling

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-66247	Ser780	DSLDSRLsPPAGLFT	Homo sapiens
pmid	sentence
10194762	Serine 780 is the only substrate in full-length stat5a for active erk

Publications:

1

Organism:

Homo Sapiens

Tissue:

Ovary

Pathways:

Glucocorticoid receptor Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-121856	Ser845	SIRQRISsFETFGSS	Homo sapiens
pmid	sentence
14768064	The precursor form of the cytokine il-16 (proil-16) was shown to be phosphorylated on ser144 in antigen receptor-, sdf1alpha- and il-2-activated t cells. Genetic and pharmacological-inhibitor experiments showed that the phosphorylation of proil-16 is dependent on activation of the kinases erk1/2. Il-16 is secreted by mitogen-activated t cells, and the biochemical link between proil-16 and erk1/2, revealed by studies with pap-1, prompted analysis of the role of map kinases in this response.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277854	Ser868	ITRGEWQsEAQDTMK	Homo sapiens	HEK-293 Cell
pmid	sentence
37686242	We found that, in addition to CaMKIIβ, also ERK1/2 is involved in the degradation pathway of GABAB receptors under physiological and ischemic conditions. In contrast to our previous view, CaMKIIβ does not appear to directly phosphorylate S867. Instead, the data support a mechanism in which CaMKIIβ activates ERK1/2, which then phosphorylates S867 and T872 in GABAB1.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277855	Thr873	WQSEAQDtMKTGSST	Homo sapiens	HEK-293 Cell
pmid	sentence
37686242	We found that, in addition to CaMKIIβ, also ERK1/2 is involved in the degradation pathway of GABAB receptors under physiological and ischemic conditions. In contrast to our previous view, CaMKIIβ does not appear to directly phosphorylate S867. Instead, the data support a mechanism in which CaMKIIβ activates ERK1/2, which then phosphorylates S867 and T872 in GABAB1.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262523	Ser9	SGRPRTTsFAESCKP	Mus musculus	MEF Cell
pmid	sentence
28646232	We demonstrate that insulin-mediated activation of ERK1/2 results in phosphorylation of GSK3β at S9 independently of Akt/mTORC1 activity in Tsc2 null mouse embryonic fibroblasts. In addition, we show that inhibition of ERK1/2 rescues GSK3β activity and restores protein synthesis in Tsc2 −/− MEFs to normal levels

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-249475	Ser93	ALQRQPPsPKQLEEE	in vitro
pmid	sentence
16226275	First, Erk phosphorylates HePTP at residues Thr45 and Ser72. Second, HePTP dephosphorylates Erk at PTyr185.\|

Identifier	Residue	Sequence	Organism
SIGNOR-249476	Thr66	EPICSVNtPREVTLH	in vitro
pmid	sentence
16226275	First, Erk phosphorylates HePTP at residues Thr45 and Ser72. Second, HePTP dephosphorylates Erk at PTyr185.\|

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-106565	Ser982	KKKSEPSsPDHGSST	in vitro
pmid	sentence
11287604	Plc beta1 could be efficiently phosphorylated by activated mitogen-activated protein kinase but not by pka. The erk phosphorylation site was mapped to serine 982

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-93989	Thr1032	SSSNRPFtPPTSTGG	Homo sapiens
pmid	sentence
12356758	Phosphorylation of transcriptional coactivator peroxisome proliferator-activated receptor (ppar)-binding protein (pbp). Stimulation of transcriptional regulation by mitogen-activated protein kinase

Identifier	Residue	Sequence	Organism
SIGNOR-93993	Thr1457	HSKSPAYtPQNLDSE	Homo sapiens
pmid	sentence
12356758	Phosphorylation of transcriptional coactivator peroxisome proliferator-activated receptor (ppar)-binding protein (pbp). Stimulation of transcriptional regulation by mitogen-activated protein kinase

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-168248	Thr11	SEAETPStPGEFESK	Homo sapiens	Neuron
pmid	sentence
20920535	The phosphorylation of sult4a1 allows interaction with pin1, which then promotes degradation of the sulfotransferase.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Brain

Identifier	Residue	Sequence	Organism
SIGNOR-112813	Thr117	DFPKKPLtPYFRFFM	Homo sapiens
pmid	sentence
11741541	Erk1/2 was found to phosphorylate the architectural transcription factor ubf at amino acids 117 and 201 within hmg boxes 1 and 2, preventing their interaction with dna

Identifier	Residue	Sequence	Organism
SIGNOR-112817	Thr201	DIPEKPKtPQQLWYT	Homo sapiens
pmid	sentence
11741541	Erk1/2 was found to phosphorylate the architectural transcription factor ubf at amino acids 117 and 201 within hmg boxes 1 and 2, preventing their interaction with dna

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-101548	Thr125	PEVLRPEtPRPVDIG	Homo sapiens
pmid	sentence
12792650	Inhibition of caspase-9 through phosphorylation at thr 125 by erk mapk

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-179812	Thr163	TDGSLPStPPPAEEE	Homo sapiens	Breast Cancer Cell
pmid	sentence
18676833	We then showed that erk could phosphorylate mcl-1 at two consensus residues, thr 92 and 163, which is required for the association of mcl-1 and pin1, resulting in stabilization of mcl-1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-125770	Thr184	PSAPALStPGIRDSA	Homo sapiens
pmid	sentence
15192708	Lat, an adapter protein essential for t-cell signaling, is phosphorylated at its thr 155 by erk in response to t-cell receptor stimulation. Thr 155 phosphorylation reduces the ability of lat to recruit plcgamma1 and slp76, leading to attenuation of subsequent downstream events such as [ca2+]i mobilization and activation of the erk pathway.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-80234	Thr187	NAGSVEQtPKKPGLR	Homo sapiens	Breast Cancer Cell
pmid	sentence
10931950	These data suggest that increased signaling by erbb receptors up-regulates mapk activity, which, in turn, phosphorylates and destabilizes p27, thus contributing to dysregulated cell cycle progression.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248462	Thr202	HDHTGFLtEYVATRW	Rattus norvegicus
pmid	sentence
7535768	We demonstrate that ERK, JNK, and p38 are activated by distinct combinations of stimuli in T cells that simulate full or partial activation through the T cell receptor. These kinases are regulated by reversible phosphorylation on Tyr and Thr, and the dual specific phosphatases PAC1 and MKP-1 previously have been implicated in the in vivo inactivation of ERK or of ERK and JNK, respectively

Identifier	Residue	Sequence	Organism
SIGNOR-248463	Tyr204	HTGFLTEyVATRWYR	Rattus norvegicus
pmid	sentence
7535768	We demonstrate that ERK, JNK, and p38 are activated by distinct combinations of stimuli in T cells that simulate full or partial activation through the T cell receptor. These kinases are regulated by reversible phosphorylation on Tyr and Thr, and the dual specific phosphatases PAC1 and MKP-1 previously have been implicated in the in vivo inactivation of ERK or of ERK and JNK, respectively

Publications:

2

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-59153	Thr202	HDHTGFLtEYVATRW	Homo sapiens
pmid	sentence
9677429	The mek1 proline-rich insert is required for efficient activation of the mitogen-activated protein kinases erk1 and erk2 in mammalian cells.

Identifier	Residue	Sequence	Organism
SIGNOR-59157	Tyr204	HTGFLTEyVATRWYR	Homo sapiens
pmid	sentence
9677429	The mek1 proline-rich insert is required for efficient activation of the mitogen-activated protein kinases erk1 and erk2 in mammalian cells.

Identifier	Residue	Organism
SIGNOR-210176		Homo sapiens
pmid	sentence
12270934	Mek1 as indicated by extensive phosphorylation of erk1 and erk2 during the initial 2 h of adipogenesis.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-244802	Thr202	HDHTGFLtEYVATRW	Homo sapiens
pmid	sentence
9677429	The mek1 proline-rich insert is required for efficient activation of the mitogen-activated protein kinases erk1 and erk2 in mammalian cells.

Identifier	Residue	Sequence	Organism
SIGNOR-244806	Tyr204	HTGFLTEyVATRWYR	Homo sapiens
pmid	sentence
9677429	The mek1 proline-rich insert is required for efficient activation of the mitogen-activated protein kinases erk1 and erk2 in mammalian cells.

Identifier	Residue	Organism
SIGNOR-244798		Homo sapiens
pmid	sentence
12270934	Mek1 as indicated by extensive phosphorylation of erk1 and erk2 during the initial 2 h of adipogenesis.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-144322	Thr202	HDHTGFLtEYVATRW	Homo sapiens
pmid	sentence
16456541	B56-containing pp2a dephosphorylate erk and their activity is controlled by the early gene iex-1 and erk

Identifier	Residue	Organism
SIGNOR-103162		Homo sapiens
pmid	sentence
12840032	P-erk1/2 proteins were efficiently dephosphorylated in vitro by protein phosphatases 1 and 2a (pp1/2a) and mapk phosphatase 3 (mkp3).

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-19240	Thr202	HDHTGFLtEYVATRW	Homo sapiens
pmid	sentence
1411546	The primary structure of mek, a protein kinase that phosphorylates the erk gene product

Identifier	Residue	Sequence	Organism
SIGNOR-19244	Tyr204	HTGFLTEyVATRWYR	Homo sapiens
pmid	sentence
1411546	The primary structure of mek, a protein kinase that phosphorylates the erk gene product

Publications:

2

Organism:

Homo Sapiens

Tissue:

Brain

Identifier	Residue	Sequence	Organism
SIGNOR-248715	Thr202	HDHTGFLtEYVATRW	Rattus norvegicus
pmid	sentence
7535768	Dephosphorylation and Inactivation of ERKs\|ERK1 phosphorylated on either threonine (ERK1Y204F) or tyrosine alone (ERK1T202A) was utilized as a substrate for HVH2. Threonine 202 and tyrosine 204 in ERK1 (53) correspond to threonine 183 and tyrosine 185 in ERK2 which are the activation-phosphorylation sites by MEK(14, 15, 16). ERK1, a kinase-deficient mutant, was phosphorylated on both threonine and tyrosine by MEK2 (Fig. 3B). ERK1T202A, having threonine 202 substituted by an alanine, was phosphorylated only on tyrosine while ERK1Y204F, having tyrosine 204 substituted by a phenylalanine, was phosphorylated only on threonine (Fig. 3B). GST-HVH2 dephosphorylated all three ERK1 mutants (Fig. 3A), suggesting that double phosphorylations of adjacent threonine and tyrosine were not a prerequisite for HVH2 recognition. However, HVH2 dephosphorylated ERK1* and ERK1T202A more efficiently than ERK1Y204F (Fig. 3A), indicating that HVH2 preferred phosphotyrosine over phosphothreonine. Interestingly, MEK also phosphorylated tyrosine residues more efficiently than threonine residues of ERK

Identifier	Residue	Sequence	Organism
SIGNOR-248716	Tyr204	HTGFLTEyVATRWYR	Rattus norvegicus
pmid	sentence
7535768	Dephosphorylation and Inactivation of ERKs\|ERK1 phosphorylated on either threonine (ERK1Y204F) or tyrosine alone (ERK1T202A) was utilized as a substrate for HVH2. Threonine 202 and tyrosine 204 in ERK1 (53) correspond to threonine 183 and tyrosine 185 in ERK2 which are the activation-phosphorylation sites by MEK(14, 15, 16). ERK1, a kinase-deficient mutant, was phosphorylated on both threonine and tyrosine by MEK2 (Fig. 3B). ERK1T202A, having threonine 202 substituted by an alanine, was phosphorylated only on tyrosine while ERK1Y204F, having tyrosine 204 substituted by a phenylalanine, was phosphorylated only on threonine (Fig. 3B). GST-HVH2 dephosphorylated all three ERK1 mutants (Fig. 3A), suggesting that double phosphorylations of adjacent threonine and tyrosine were not a prerequisite for HVH2 recognition. However, HVH2 dephosphorylated ERK1* and ERK1T202A more efficiently than ERK1Y204F (Fig. 3A), indicating that HVH2 preferred phosphotyrosine over phosphothreonine. Interestingly, MEK also phosphorylated tyrosine residues more efficiently than threonine residues of ERK

Publications:

2

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence
SIGNOR-249471	Thr202	HDHTGFLtEYVATRW
pmid	sentence
1712480	Microtubule-associated protein 2 kinases, ERK1 and ERK2, undergo autophosphorylation on both tyrosine and threonine residues: implications for their mechanism of activation.\|

Identifier	Residue	Sequence	Organism
SIGNOR-182628	Thr207	FLTEYVAtRWYRAPE	Homo sapiens
pmid	sentence
19060905	Here we show that autophosphorylation of erk1/2 on thr188 directs erk1/2 to phosphorylate nuclear targets known to cause cardiac hypertrophy.

Identifier	Residue	Sequence
SIGNOR-249472	Tyr204	HTGFLTEyVATRWYR
pmid	sentence
1712480	Microtubule-associated protein 2 kinases, ERK1 and ERK2, undergo autophosphorylation on both tyrosine and threonine residues: implications for their mechanism of activation.\|

Publications:

3

Organism:

, Homo Sapiens

Tissue:

Heart

Pathways:

Glucocorticoid receptor Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-244565	Thr207	FLTEYVAtRWYRAPE	Homo sapiens
pmid	sentence
19060905	Here we show that autophosphorylation of erk1/2 on thr188 directs erk1/2 to phosphorylate nuclear targets known to cause cardiac hypertrophy.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Heart

Identifier	Residue	Sequence	Organism
SIGNOR-143481	Thr232	KNIVTPRtPPPSQGK	Homo sapiens
pmid	sentence
16401070	Phosphorylation decreased the ability of mbp to polymerize actin and to bundle actin filaments but had no effect on the dissociation constant of the mbp-actin complex or on the ability of ca2+-calmodulin to dissociate the complex. The most significant effect of phosphorylation on the mbp-actin complex was a dramatic reduction in its ability to bind to negatively charged lipid bilayers. The identification of myelin basic protein (phosphorylation at -pro-arg-thr-pro-) as a substrate for the erk kinases (fig. 1) demonstrates that there are other determinants important for substrate recognition than those present in the originally identified consensus sequence.

Identifier	Residue	Sequence	Organism
SIGNOR-22424	Thr232	KNIVTPRtPPPSQGK	Homo sapiens
pmid	sentence
1939237	Phosphorylation decreased the ability of mbp to polymerize actin and to bundle actin filaments but had no effect on the dissociation constant of the mbp-actin complex or on the ability of ca2+-calmodulin to dissociate the complex. The most significant effect of phosphorylation on the mbp-actin complex was a dramatic reduction in its ability to bind to negatively charged lipid bilayers. The identification of myelin basic protein (phosphorylation at -pro-arg-thr-pro-) as a substrate for the erk kinases (fig. 1) demonstrates that there are other determinants important for substrate recognition than those present in the originally identified consensus sequence.

Publications:

2

Organism:

Homo Sapiens

Tissue:

Brain

Identifier	Residue	Sequence	Organism
SIGNOR-33909	Thr232	GGLPEVAtPESEEAF	Homo sapiens
pmid	sentence
7816602	Phosphorylation of the c-fos and c-jun hob1 motif stimulates its activation capacity here we show that the hob1-containing activation domain of c-fos is stimulated by ha-ras in vivo and phosphorylated by a map kinase family member in vitro and that mutating t232 to ala abolishes both functions.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-184917	Thr235	SSSSPPGtPSPADAK	Homo sapiens
pmid	sentence
19327116	Thr235 phosphorylation occurs in nuclei of differentiated macrophages, but not in monocytes.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273672	Thr264	EGFYFGEtPLALAAC	Homo sapiens	HaCaT Cell
pmid	sentence
29084846	We observed that ERK-mediated phosphorylation of TRPV3 alters its responsiveness to repeated chemical stimuli. Among several putative ERK phosphorylation sites, we identified threonine 264 in the N-terminal ankyrin repeat domain as the most critical site for the ERK-dependent modulation of TRPV3 channel activity. Of note, Thr264 is in close vicinity to a structurally and functionally important TRPV3 region comprising an atypical finger 3 and oxygen-dependent hydroxylation site. In summary, our findings indicate that Thr264 in TRPV3 is a key ERK phosphorylation site mediating EGFR-induced sensitization of the channel to stimulate signaling pathways involved in regulating skin homeostasis.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-101664	Thr277	GSRTAPYtPNLPHHQ	Homo sapiens
pmid	sentence
12801888	Our results suggest that map kinase can phosphorylate thr276 of smad4 and that phosphorylation can lead to enhanced tgf-beta-induced nuclear accumulation and, as a consequence, enhanced transcriptional activity of smad4.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-123074	Thr292	YTAMDVAtGQEVAIK	Homo sapiens
pmid	sentence
14993270	Activated erk can phosphorylate t292 in the prs, and this blocks the ability of pak to phosphorylate s298 and of rac-pak signaling to enhance mek1-erk complex formation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249117	Thr355	NFSSSPStPVGSPQG	Mus musculus
pmid	sentence
14592976	Notch-induced degradation requires phosphorylation of E47 by p42/p44 MAP kinases. \|Wild_type E47 but not the Mm mutant reacted to the antibodies, suggesting that E47 is at least phosphorylated at the M2 site (Figure 3A)\|anti_phospho_M2 peptide (SSPSpTPVGSPQG)

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence
SIGNOR-249477	Thr361	EPFVSIPtPREKVAM
pmid	sentence
11493009	Specifically, the complex formation between PTP-SL and ERK2 involves an unusual interaction leading to the phosphorylation of PTP-SL by ERK2 at Thr253 and the inactivating dephosphorylation of ERK2 by PTP-SL.

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-116494	Thr38	CADVPLLtPSSKEMM	Homo sapiens
pmid	sentence
11948414	We found that hgf/sf activates the erk1 map kinase, leading to the phosphorylation of the threonine 38 residue of ets1

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-48360	Thr385	APEKGLPtPQVLQRN	Homo sapiens	HeLa Cell
pmid	sentence
9155018	Mnk1 was phosphorylated and activated in vitro by erk1 and p38 map kinasespreliminary results showed that thr344 at least was one of the major sites phosphorylated by erk1

Identifier	Residue	Organism
SIGNOR-48352		Homo sapiens
pmid	sentence
9155017	We have identified a new subfamily of murine serine/threonine kinases, whose members, map kinase-interacting kinase 1 (mnk1) and mnk2, bind tightly to the growth factor-regulated map kinases, erk1 and erk2.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-137175	Thr42	SGVEVRVtPTRTEII	Homo sapiens
pmid	sentence
15950189	Erk phosphorylates threonine 42 residue of ribosomal protein s3.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-137959	Thr42	SGVEVRVtPTRTEII	Homo sapiens
pmid	sentence
15950189	Erk phosphorylates threonine 42 residue of ribosomal protein s3.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-138898	Thr43	KVTTVVAtPGQGPDR	Homo sapiens	Breast Cancer Cell, Kidney Cancer Cell
pmid	sentence
16039586	Erk, which is activated by hbx, associates with gsk-3beta through a docking motif ((291)fkfp) of gsk-3beta and phosphorylates gsk-3beta at the (43)thr residue, which primes gsk-3beta for its subsequent phosphorylation at ser9 by p90rsk, resulting in inactivation of gsk-3beta and upregulation of beta-catenin.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249480	Thr453	SGPIIIRtPTVGPNG	Homo sapiens
pmid	sentence
14744793	Transcriptional activation of p21(waf1/cip1) by alkylphospholipids: role of the mitogen-activated protein kinase pathway in the transactivation of the human p21(waf1/cip1) promoter by Sp1.\|this activation promotes the phosphorylation of Sp1 in known mitogen-activated protein kinase residues (threonine 453 and 739), thereby leading to increased Sp1 binding and enhanced p21(waf1/cip1) transcription.

Identifier	Residue	Sequence	Organism
SIGNOR-249481	Thr739	SEGSGTAtPSALITT	Homo sapiens
pmid	sentence
14744793	Transcriptional activation of p21(waf1/cip1) by alkylphospholipids: role of the mitogen-activated protein kinase pathway in the transactivation of the human p21(waf1/cip1) promoter by Sp1.\|this activation promotes the phosphorylation of Sp1 in known mitogen-activated protein kinase residues (threonine 453 and 739), thereby leading to increased Sp1 binding and enhanced p21(waf1/cip1) transcription.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-137179	Thr456	KVYFLPItPHYVTQV	Homo sapiens
pmid	sentence
15890648	Cad is a multifunctional protein that initiates and regulates mammalian de novo pyrimidine biosynthesis. The activation of the pathway required for cell proliferation is a consequence of the phosphorylation of cad thr-456 by mitogen-activated protein (map) kinase.Activated map kinase (erk1/2), the enzyme responsible for the phosphorylation of thr-456, was also present in larger amounts in the nucleus than the cytosol

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277443	Thr507	GLGENLLtHLPEEIG	Homo sapiens	HEK-293 Cell
pmid	sentence
30865892	Here, we showed that SHOC2, a RAS activator, is a FBXW7 substrate. Growth stimuli trigger SHOC2 phosphorylation on Thr507 by the mitogen-activated protein kinase (MAPK) signal, which facilitates FBXW7 binding for ubiquitylation and degradation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-41800	Thr56	VAPPVPAtPYEAFDP	Homo sapiens	B-lymphocyte
pmid	sentence
8632909	The threonine 56 was defined as the erk1 phosphorylation site by using phosphoamino-acid analyses and a spi-b mutant version

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-74939	Thr56	FSSQPGHtPHPAASR	Homo sapiens
pmid	sentence
10669763	Phosphorylation of the map kinase sites in bcl-2, thr56, thr74, and ser87, is sufficient to inhibit tnf--induced degradation. p44mapk/extracellular signal-regulated kinase 1 (erk1) and p42 mapk/erk2 are activated by il-3, colocalize with mitochondrial bcl2, and can directly phosphorylate bcl2 on ser-70 in a stauro-resistant manner both_ in vitro_ and_ in vivo.

Identifier	Residue	Sequence	Organism
SIGNOR-74943	Thr74	ARTSPLQtPAAPGAA	Homo sapiens
pmid	sentence
10669763	The results of this study reveal the following novel findings: destruction of the three putative MAP kinase sites at positions 56, 74, and 87 results in ubiquitination and subsequent degradation of the protein. Progressive inactivation of these MAP kinase sites revealed that Bcl-2 stability is mainly regulated by phosphorylation at Thr74 and Ser87, with Ser87 phosphorylation playing a predominant role. TNF-Œ± or the MAP kinase-specific inhibitor PD98059 diminishes Ser87 phosphorylation of Bcl-2 in vivo, while activated ERK2 induces phosphorylation of Bcl-2 in vivo and in vitro.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249447	Thr615	QALPIPGtPPPNYDS	in vitro
pmid	sentence
11805112	Using a number of different approaches it was demonstrated that the protein kinase acting on betaThr-613 and gammaThr-623 is the extracellular regulated kinase (ERK). It is suggested that an ERK-mediated phosphorylation of betaThr-613 and gammaThr-623 down-regulates the channel by facilitating its interaction with Nedd4.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-249449	Thr622	LGTQVPGtPPPKYNT	in vitro
pmid	sentence
11805112	Using a number of different approaches it was demonstrated that the protein kinase acting on betaThr-613 and gammaThr-623 is the extracellular regulated kinase (ERK). It is suggested that an ERK-mediated phosphorylation of betaThr-613 and gammaThr-623 down-regulates the channel by facilitating its interaction with Nedd4.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-160420	Thr679	PGVELLLtPREPALP	Homo sapiens	HeLa Cell
pmid	sentence
18211802	Activates rhoa and as a result regulates actin assembly.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-90529	Thr69	SVIVADQtPTPTRFL	Homo sapiens
pmid	sentence
12110590	Here, we show that in fibroblasts, insulin, epidermal growth factor (egf) and serum activate atf2 via a so far unknown two-step mechanism involving two distinct ras effector pathways: the raf-mek-erk pathway induces phosphorylation of atf2 thr71, whereas subsequent atf2 thr69 phosphorylation requires the ral-ralgds-src-p38 pathway.

Identifier	Residue	Sequence	Organism
SIGNOR-163254	Thr69	SVIVADQtPTPTRFL	Homo sapiens
pmid	sentence
20068231	Phosphorylation of thr-69 by mapk14 and mapk11, and at thr-71 by mapk1/erk2, mapk3/erk1, mapk11, mapk12 and mapk14 in response to external stimulus like insulin causes increased transcriptional activity.

Identifier	Residue	Sequence	Organism
SIGNOR-163258	Thr71	IVADQTPtPTRFLKN	Homo sapiens
pmid	sentence
20068231	Phosphorylation of thr-69 by mapk14 and mapk11, and at thr-71 by mapk1/erk2, mapk3/erk1, mapk11, mapk12 and mapk14 in response to external stimulus like insulin causes increased transcriptional activity.

Identifier	Residue	Sequence	Organism
SIGNOR-90533	Thr71	IVADQTPtPTRFLKN	Homo sapiens
pmid	sentence
12110590	Here, we show that in fibroblasts, insulin, epidermal growth factor (egf) and serum activate atf2 via a so far unknown two-step mechanism involving two distinct ras effector pathways: the raf-mek-erk pathway induces phosphorylation of atf2 thr71, whereas subsequent atf2 thr69 phosphorylation requires the ral-ralgds-src-p38 pathway.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-20549	Thr693	RELVEPLtPSGEAPN	Homo sapiens
pmid	sentence
1651322	It is likely that the map2 and ert kinases account for the phosphorylation of the egf receptor at thr669 (egf receptor (krel veplt669psgeapnqallr)) observed in cultured cells.Phosphorylation at ser-695 is partial and occurs only if thr-693 is phosphorylated. Phosphorylation at thr-678 and thr-693 by prkd1 inhibits egf-induced mapk8/jnk1 activation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-114475	Thr72	AAPAPPPtPQAPAAE	Homo sapiens
pmid	sentence
11809795	Together, these results show that activation of saf-1 in response to il-1 and -6 is mediated via map kinase-regulated phosphorylation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-89625	Thr735	KPFPAPQtPGRLQPA	Homo sapiens
pmid	sentence
12058067	Extracellular signal-regulated kinase phosphorylates tumor necrosis factor alpha-converting enzyme at threonine 735: a potential role in regulated sheddingwe show that extracellular signal-regulated kinase (erk) acts as an intermediate in protein kinase c-regulated trka cleavage. We report that the cytosolic tail of the tumor necrosis factor alpha-converting enzyme (tace) is phosphorylated by erk at threonine 735. In addition, we show that erk and tace associate. This association is favored by erk activation and by the presence of threonine 735. In contrast to the erk route, the p38 mapk was able to stimulate trka cleavage in cells devoid of tace activity, indicating that other proteases are also involved in trka shedding.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-161819	Thr753	YACASPKtPIQAGGY	Homo sapiens
pmid	sentence
19933846	Erk-induced phosphorylation of b-raf on t753 promoted the disassembly of raf heterodimers, and the mutation of t753 prolonged growth factor-induced heterodimerization. The b-raf t753a mutant enhanced differentiation of pc12 cells, which was previously shown to be dependent on sustained erk signaling. Site is critical for v-src dependent modulation of slk kinase activity.

Identifier	Residue	Sequence	Organism
SIGNOR-144827	Thr753	YACASPKtPIQAGGY	Homo sapiens
pmid	sentence
16508002	Erk-induced phosphorylation of b-raf on t753 promoted the disassembly of raf heterodimers, and the mutation of t753 prolonged growth factor-induced heterodimerization. The b-raf t753a mutant enhanced differentiation of pc12 cells, which was previously shown to be dependent on sustained erk signaling. Site is critical for v-src dependent modulation of slk kinase activity.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-182782	Thr79	QPPTGYTtPTAPQAY	Homo sapiens
pmid	sentence
19076070	Here we report that ews and ews-fli1 become phosphorylated at thr79 in the n-terminal domain in response to mitogens or dna damage. Mitogen-induced phosphorylation of ews and ews-fli1 was weak and catalysed by erk1 (extracellular signal-regulated kinase 1) and erk2.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-227514	Thr8	MSSILPFtPPVVKRL	Homo sapiens
pmid	sentence
12193595	We show that phosphorylation of Smad2, a mediator of the activin/transforming growth factor-beta signal, by activated extracellular signal-regulated kinase 1 (ERK1) increases the amount of Smad2 protein and leads to enhanced transcriptional activity.[] A site of ERK-dependent phosphorylation on Smad2 was located to Thr8

Identifier	Residue	Organism
SIGNOR-236067		Homo sapiens
pmid	sentence
10197981	These results suggest that oncogenic ras, acting through mek1 and erk kinases, induces the phosphorylation of smad2 and smad3 .we show that phosphorylation of smad2, a mediator of the activin/transforming growth factor-beta signal, by activated extracellular signal-regulated kinase 1 (erk1) increases the amount of smad2 protein and leads to enhanced transcriptional activity

Identifier	Residue	Organism
SIGNOR-217613		Homo sapiens
pmid	sentence
19115199	These results suggest that oncogenic ras, acting through mek1 and erk kinases, induces the phosphorylation of smad2 and smad3 .we show that phosphorylation of smad2, a mediator of the activin/transforming growth factor-beta signal, by activated extracellular signal-regulated kinase 1 (erk1) increases the amount of smad2 protein and leads to enhanced transcriptional activity

Publications:

3

Organism:

Homo Sapiens

Tissue:

Lung, Breast

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249470	Thr891	NSETSSDtPEMSLSA	Mus musculus	NIH-3T3 Cell
pmid	sentence
11581251	Thus, activation of the ERK pathway appears to be able to regulate adipocyte lipolysis by phosphorylating HSL on Ser(600) and increasing the activity of HSL.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277506	Thr906	SLDNNYStPNERGDH	Canis lupus familiaris	MDCK Cell
pmid	sentence
32010791	Upon TGFβ treatment, activated extracellular signal-regulated kinase 1/2 (ERK1/2) phosphorylates T900 of p120-catenin to promote its interaction with Smurf1 and subsequent monoubiquitination. TGFβ promotes monoubiquitination of p120-catenin through Smurf1 to induce junction dissociation.

Publications:

1

Organism:

Canis Lupus Familiaris

Identifier	Residue	Sequence	Organism
SIGNOR-159168	Tyr204	HTGFLTEyVATRWYR	Homo sapiens
pmid	sentence
17998336	The sh3 domain of lck modulates t-cell receptor-dependent activation of extracellular signal-regulated kinase through activation of raf-1.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Glucocorticoid receptor Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-140298	Tyr204	HTGFLTEyVATRWYR	Homo sapiens
pmid	sentence
16153436	We hypothesized that ret could directly phosphorylate fak and erk. erk 2 could be phosphorylated at y187 (y204 in erk1).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248535	Tyr204	HTGFLTEyVATRWYR	Chlorocebus aethiops	COS Cell
pmid	sentence
10224087	Extracellular regulated kinases (ERK) 1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR. A novel role in down-regulating the ERK pathway.\|Catalysis by VHR requires the native structure of ERK and is specific for tyrosine 185 of ERK2

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-103035	Tyr204	HTGFLTEyVATRWYR	Homo sapiens	Dermal Fibroblast
pmid	sentence
12840032	The activation of the mapk activity requires the dual phosphorylation of the ser/thr and tyr residues in the txy kinase activation motif (1113), and deactivation occurs through the action of either ser/thr protein phosphatase (14), protein-tyrosine phosphatase (ptp) (14, 15), or dual specificity phosphatases

Publications:

2

Organism:

Chlorocebus Aethiops, Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248707	Tyr204	HTGFLTEyVATRWYR	in vitro
pmid	sentence
19494114	Tumor suppressor density-enhanced phosphatase-1 (DEP-1) inhibits the RAS pathway by direct dephosphorylation of ERK1/2 kinases\|Pulldown and in vitro dephosphorylation assays confirmed our prediction and demonstrated an overall specificity of DEP-1 in targeting the phosphorylated tyrosine 204 of ERK1/2.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism
SIGNOR-59877		Homo sapiens
pmid	sentence
9733512	A protein called mp1 (mek partner 1) was identified that bound specifically to mek1 and erk1 and facilitated their activation. When overexpressed in cultured cells, mp1 enhanced activation of erk1 and activation of a reporter driven by the transcription factor elk-1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-111502		Homo sapiens
pmid	sentence
11702783	Here, we report that pea-15, a protein variably expressed in multiple cell types, blocks erk-dependent transcription and proliferation by binding erks and preventing their localization in the nucleus._ Pea-15 can redirect the biological outcome of map kinase signaling by regulating the subcellular localization of erk map kinase.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-279070		Homo sapiens
pmid	sentence
28196117	Activation of the ERK1/2 signalling pathway, inducing proliferation and survival, inhibits the expression of HNF4\u03b1.\|Here we have demonstrated that ERK1 is able to phosphorylate HNF4\u03b1 at several serine and threonine residues.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Glucocorticoid receptor Signaling

Identifier	Residue	Organism
SIGNOR-66781		Homo sapiens
pmid	sentence
10197981	These results suggest that oncogenic ras, acting through mek1 and erk kinases, induces the phosphorylation of smad2 and smad3.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Lung, Breast

Identifier	Residue	Organism
SIGNOR-165350		Homo sapiens
pmid	sentence
20457810	We conclude that, by interacting with fibronectin, pref-1 activates integrin downstream signaling to activate mek/erk and to inhibit adipocyte differentiation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-66778		Homo sapiens
pmid	sentence
10197981	These results suggest that oncogenic ras, acting through mek1 and erk kinases, induces the phosphorylation of smad2 and smad3

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-165353		Homo sapiens
pmid	sentence
20457810	Soluble pref-1 inhibits adipocyte differentiation through the activation of extracellular signal-regulated kinase/mitogen-activated protein kinase (erk/mapk) and the subsequent upregulation of sox9 expression.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-168995		Homo sapiens
pmid	sentence
20974802	We show that several proline-directed mitogen-activated protein kinases (mapks), such as p38, erk1/2, and jnk1 are sufficient and required for the phosphorylation of ppps/tp motifs of lrp6. External stimuli, which control the activity of mapks, such as phorbol esters and fibroblast growth factor 2 (fgf2) control the choice of the lrp6-ppps/tp kinase and regulate the amplitude of lrp6 phosphorylation and wnt/beta-catenin-dependent transcription.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-124473		Homo sapiens
pmid	sentence
15118098	Morg1 specifically associates with several components of the erk pathway, including mp1, raf-1, mek, and erk, and stabilizes their assembly into an oligomeric complex.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-198292		Homo sapiens	Breast Cancer Cell
pmid	sentence
22802261	Erk also undergoes rapid translocation into the nucleus, where it phosphorylates and activates a variety of transcription factor targets, including sp1, e2f, elk-1, and ap1

Identifier	Residue	Organism
SIGNOR-121991		Homo sapiens
pmid	sentence
14967450	Erk also undergoes rapid translocation into the nucleus, where it phosphorylates and activates a variety of transcription factor targets, including sp1, e2f, elk-1, and ap1

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-262520		Mus musculus	MEF Cell
pmid	sentence
28646232	We demonstrate that insulin-mediated activation of ERK1/2 results in phosphorylation of GSK3β at S9 independently of Akt/mTORC1 activity in Tsc2 null mouse embryonic fibroblasts. In addition, we show that inhibition of ERK1/2 rescues GSK3β activity and restores protein synthesis in Tsc2 −/− MEFs to normal levels

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Organism
SIGNOR-101282		Homo sapiens
pmid	sentence
12771128	A dominant-negative mutant of high cell densityenhanced ptp 1 (dep-1)//cd148 as well as reduction of its expression by rna interference partially restore vegfr-2 phosphorylation and map kinase activation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-258994		Mus musculus
pmid	sentence
11730323	Raf proteins have been shown to phosphorylate and activate MAPKKs (MAP kinase kinases) called MEKs (MAPK or ERK kinases) which in turn phosphorylate and activate MAPKs (MAP kinases) called ERKs

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Organism
SIGNOR-217559		Homo sapiens
pmid	sentence
19864431	Here we focus primarily although not exclusively on raptor Ser(863) phosphorylation. We report that insulin promotes mTORC1-associated phosphorylation of raptor Ser(863) via the canonical PI3K/TSC/Rheb pathway in a rapamycin-sensitive manner. mTORC1 activation by other stimuli (e.g. amino acids, epidermal growth factor/MAPK signaling, and cellular energy) also promote raptor Ser(863) phosphorylation.

Identifier	Residue	Organism
SIGNOR-217544		Homo sapiens
pmid	sentence
21757713	The phosphorylation of Raptor on these sites enhances mTORC1 activity, and contributes largely to arsenite-induced mTORC1 activation.

Identifier	Residue	Organism
SIGNOR-217556		Homo sapiens
pmid	sentence
19346248	The phosphorylation of raptor is stimulated by insulin and inhibited by rapamycin. Importantly, the site-directed mutation of raptor at one phosphorylation site, Ser(863), reduced mTORC1 activity both in vitro and in vivo.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-67358		Homo sapiens
pmid	sentence
10224087	Extracellular regulated kinases (erk) 1 and erk2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase vhr. A novel role in down-regulating the erk pathway

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-270301		Homo sapiens
pmid	sentence
12809513	We concluded that serine 142 of the tr dbd is the likely site of phosphorylation by t(4)-activated mapk and that the docking site on tr for activated mapk includes residues 128-133 (kgffrr), a basic amino acid-enriched motif novel for mapk substrates. Tr mutations in the proposed mapk docking domain and at residue 142 modulated t(4)-conditioned shedding of co-repressor and recruitment of co-activator proteins by the receptor, and they altered transcriptional activity of tr in a thyroid hormone response element-luciferase reporter assay.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-253012		in vitro
pmid	sentence
9155018	These results indicate that MNK1 is a novel class of protein kinase that is activated through both the ERK and p38 MAP kinase signaling pathways

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism
SIGNOR-48355		Homo sapiens
pmid	sentence
9155017	Erk and p38 phosphorylate mnk1 and mnk2, which stimulates their in vitro kinase activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-103155		Homo sapiens
pmid	sentence
12840032	P-erk1/2 proteins were efficiently dephosphorylated in vitro by protein phosphatases 1 and 2a (pp1/2a) and mapk phosphatase 3 (mkp3). the dual specificity phosphatases that specifically dephosphorylate and inactivate the p-erk1/2 are called mapk phosphatases

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-103165		Homo sapiens
pmid	sentence
12840032	When cells are stimulated with various ligands such as growth factors, hormones, neurotransmitters, or tumor promoters, erk1/2 is activated through dualphosphorylation at the -ptepy-motif. Subsequently, p-erk1/2 translocates into the nucleus and phosphorylates elk-1, thereby acting as a transcription factor for cell proliferationthese data indicate that sa-p-erk1/2 might not only be regulated by mkp such as rvhr, but also by pp1 and ptp as well

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-133392		Homo sapiens	MCF-7 Cell
pmid	sentence
15672448	We found that cdc25a physically interacted with and de-phosphorylated phospho-erk both in vitro and in cell culture.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-209965		Homo sapiens
pmid	sentence
20457810	Soluble pref-1 inhibits adipocyte differentiation through the activation of extracellular signal-regulated kinase/mitogen-activated protein kinase (erk/mapk) and the subsequent upregulation of sox9 expression.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-209859		Homo sapiens
pmid	sentence
19143636	Activation of mTORC1 in two steps: Rheb-GTP activation of catalytic function and increased binding of substrates to raptor.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-83280		Homo sapiens	Breast Cancer Cell
pmid	sentence
11043579	Estrogen rapidly activates the mitogen-activated protein kinases, erk-1 and erk-2, via an as yet unknown mechanism.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-258991		Mus musculus
pmid	sentence
11730323	Raf proteins have been shown to phosphorylate and activate MAPKKs (MAP kinase kinases) called MEKs (MAPK or ERK kinases) which in turn phosphorylate and activate MAPKs (MAP kinases) called ERKs

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Organism
SIGNOR-103149		Homo sapiens
pmid	sentence
12840032	P-erk1/2 proteins were efficiently dephosphorylated in vitro by protein phosphatases 1 and 2a (pp1/2a) and mapk phosphatase 3 (mkp3).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-148002		Homo sapiens	Breast Cancer Cell, Prostate Gland Cancer Cell
pmid	sentence
16854453	Activation of raf/mek/erk cascade can also result in the phosphorylation of the antiapoptotic mcl-1 protein and the pro-apoptotic bim protein.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-262048		Homo sapiens
pmid	sentence
32482868	The MYC stabilizing kinase, ERK1, regulates MYC levels directly and indirectly by inhibiting BRD4 kinase activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-179407		Homo sapiens
pmid	sentence
18596912	The genomic activity of ppargamma is modulated, in addition to ligand binding, by phosphorylation of a serine residue by mapks, such as extracellular signal-regulated protein kinases-1/2 (erk-1/2), or by nucleocytoplasmic compartmentalization through the erk activators mapk kinases-1/2 (mek-1/2). These mapks phosphorylate (in humans) ser 84 in the ppargamma1 and ser 114 in ppargamma2 isoform

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-121994		Homo sapiens
pmid	sentence
14967450	Erk phosphorylates multiple cytoplasmatic and cytoskeletal proteins, including mapk-activated protein kinases and the ribosomal p70-s6 kinase

Identifier	Residue	Organism
SIGNOR-201687		Homo sapiens
pmid	sentence
23583303	Erk phosphorylates multiple cytoplasmatic and cytoskeletal proteins, including mapk-activated protein kinases and the ribosomal p70-s6 kinase

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-44949		Homo sapiens
pmid	sentence
8939914	Several lines of investigation have suggested that rsk is phosphorylated and activated by erk1/2 mapk isoforms

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-60998		Homo sapiens
pmid	sentence
9792677	Rsk-b is a p38alphamapk substrate, and activated by p38alphamapk and, more weakly, by erk1

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-176589		Homo sapiens
pmid	sentence
21908610	Here we demonstrate that inactivation of both erk1/2 and p38_ by dusp9/mkp-4 is mediated by a conserved arginine-rich kinase interaction motif located within the amino-terminal non-catalytic domain of the protein.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-188172		Homo sapiens	HeLa Cell
pmid	sentence
19777442	Erk-1 map kinase prevents tnf-induced apoptosis through bad phosphorylation and inhibition of bax translocation in hela cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-242625		Mus musculus	NIH-3T3 Cell
pmid	sentence
17673906	We report that upon TGF__ stimulation, the activated TGF__ type I receptor (T_RI) recruits and directly phosphorylates ShcA proteins on tyrosine and serine. This dual phosphorylation results from an intrinsic T_RI tyrosine kinase activity that complements its well_defined serine_threonine kinase function. TGF___induced ShcA phosphorylation induces ShcA association with Grb2 and Sos, thereby initiating the well_characterised pathway linking receptor tyrosine kinases with Erk MAP kinases.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Organism
SIGNOR-73617		Homo sapiens
pmid	sentence
10617468	The mitogen-activated protein (map) kinase cascade is inactivated at the level of map kinase by members of the map kinase phosphatase (mkp) family, including mkp-1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-217577		Homo sapiens
pmid	sentence
21071439	We found three proline-directed residues within raptor, ser(8), ser(696), and ser(863), which are directly phosphorylated by erk1/2. Expression of phosphorylation-deficient alleles of raptor revealed that phosphorylation of these sites by erk1/2 normally promotes mtorc1 activity and signaling to downstream substrates, such as 4e-bp1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-258997		Mus musculus
pmid	sentence
11730323	Raf proteins have been shown to phosphorylate and activate MAPKKs (MAP kinase kinases) called MEKs (MAPK or ERK kinases) which in turn phosphorylate and activate MAPKs (MAP kinases) called ERKs

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Organism
SIGNOR-264665		Homo sapiens
pmid	sentence
12840032	P-erk1/2 proteins were efficiently dephosphorylated in vitro by protein phosphatases 1 and 2a (pp1/2a) and mapk phosphatase 3 (mkp3). the dual specificity phosphatases that specifically dephosphorylate and inactivate the p-erk1/2 are called mapk phosphatases

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-118747		Homo sapiens
pmid	sentence
14559906	Spin90 was phosphorylated by erk1, which was, itself, activated by cell adhesion and platelet-derived growth factor. Such phosphorylation of spin90 likely promotes the interaction of the spin90.betapix.wasp complex and nck

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-169004		Homo sapiens
pmid	sentence
20974802	We show that several proline-directed mitogen-activated protein kinases (mapks), such as p38, erk1/2, and jnk1 are sufficient and required for the phosphorylation of ppps/tp motifs of lrp6.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-144328		Homo sapiens
pmid	sentence
16456541	B56-containing pp2a dephosphorylate erk and their activity is controlled by the early gene iex-1 and erk

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-66755		Homo sapiens
pmid	sentence
10197981	Ras signaling was shown previously to induce the phosphorylation of the bmp mediator smad1 at four erk consensus sites in the linker domain (kretzschmar et al. 1997a). Phosphorylation of these four sites inhibits smad1 accumulation in the nucleus

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-277103		Homo sapiens
pmid	sentence
27281782	In particular, DUSP23 can dephosphorylate and inactivate MAPK3 ( xref ).\|In particular, DUSP23 can dephosphorylate and inactivate MAPK3.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-251677		Mus musculus	NIH-3T3 Cell
pmid	sentence
11742987	Both induction of MKP-1 expression and inhibition of its degradation are necessary for glucocorticoid-mediated inhibition of Erk-1/2 activation.

Publications:

1

Organism:

Mus Musculus

Pathways:

Glucocorticoid receptor Signaling

Name	MAPK3 View Modifications
Full Name	Mitogen-activated protein kinase 3
Synonyms	MAP kinase 3, MAPK 3, ERT2, Extracellular signal-regulated kinase 1, ERK-1, Insulin-stimulated MAP2 kinase, MAP kinase isoform p44, p44-MAPK, Microtubule-associated protein 2 kinase, p44-ERK1 \| ERK1, PRKM3
Primary ID	P27361
Links	- -
Type	protein
Relations	423
Pathways	Fructose metabolism, Glucocorticoid receptor Signaling
Function	Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade plays also a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis. The substrates include transcription factors (such as ATF2, BCL6, ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG), regulators of translation (such as EIF4EBP1) and a variety of other signaling-related molecules (like ARHGEF2, FRS2 or GRB10). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK/ERK signal to additional cytosolic and nuclear targets, thereby extending the specificity of the cascade.

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