Relation Results

Identifier	Residue	Sequence	Organism
SIGNOR-77651	Ser10	NVRVSNGsPSLERMD	Homo sapiens
pmid	sentence
10831586	Phosphorylation on ser-10 of kip1 is the major site of phosphorylation in resting cells, takes place at the g(0)-g1 phase and leads to protein stability.

Identifier	Residue	Sequence	Organism
SIGNOR-77655	Ser178	EENVSDGsPNAGSVE	Homo sapiens
pmid	sentence
10831586	Indeed, p27kip1 was phosphorylated by p42 mapk (erk2) in vitrothese results suggest that ser(10) is the major site of phosphorylation of p27(kip1) and that phosphorylation at this site, like that at thr(187), contributes to regulation of p27(kip1) stability.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-196030	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-262770	Ser101	RELPDGPsPLLKNAI	Mus musculus
pmid	sentence
22028470	We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5'-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. This approach identified 80 proteins phosphorylated by ERK2, 13 of which are known ERK2 substrates. With this improved methodology, we detected 98 sites directly phosphorylated by ERK2 on 80 proteins from NIH 3T3-L1 fibroblasts. Thirteen of these proteins are known substrates and the rest represent previously unknown kinase/substrate interactions. (table1)

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-277601	Ser102	LQTVIRTsPSSLVAF	in vitro
pmid	sentence
35831023	We conclude that multisite phosphorylation of GLI1 by ERK2 or other MAP kinases weakens GLI1-SUFU binding, thereby facilitating GLI1 activation and contributing to both physiological and pathological crosstalk.

Identifier	Residue	Sequence	Organism
SIGNOR-277602	Ser116	FINSRCTsPGGSYGH	in vitro
pmid	sentence
35831023	We conclude that multisite phosphorylation of GLI1 by ERK2 or other MAP kinases weakens GLI1-SUFU binding, thereby facilitating GLI1 activation and contributing to both physiological and pathological crosstalk.

Identifier	Residue	Sequence	Organism
SIGNOR-277600	Ser130	HLSIGTMsPSLGFPA	in vitro
pmid	sentence
35831023	We conclude that multisite phosphorylation of GLI1 by ERK2 or other MAP kinases weakens GLI1-SUFU binding, thereby facilitating GLI1 activation and contributing to both physiological and pathological crosstalk.

Publications:

3

Organism:

In Vitro

Pathways:

Glucocorticoid receptor Signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262776	Ser104	LKHTGPNsPDTANDG	Mus musculus	NIH-3T3 Cell
pmid	sentence
22028470	We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5'-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. This approach identified 80 proteins phosphorylated by ERK2, 13 of which are known ERK2 substrates. With this improved methodology, we detected 98 sites directly phosphorylated by ERK2 on 80 proteins from NIH 3T3-L1 fibroblasts. Thirteen of these proteins are known substrates and the rest represent previously unknown kinase/substrate interactions. (table1)

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-178133	Ser104	FPPLNSVsPSPLMLL	Homo sapiens	Breast Cancer Cell
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-156848	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	Cell Line
SIGNOR-156852	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-178137	Ser106	PLNSVSPsPLMLLHP	Homo sapiens	Breast Cancer Cell
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
SIGNOR-156856	Ser118	LHPPPQLsPFLQPHG	Homo sapiens
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.

Identifier	Residue	Sequence	Organism
SIGNOR-96072	Ser118	LHPPPQLsPFLQPHG	Homo sapiens
pmid	sentence
12466266	Phosphorylation at serines 104 and 106 by erk1/2 mapk is important for estrogen receptor-alpha activity;ser118 is phosphorylated by mitogen-activated protein kinase (mapk) in vitro and in cells treated with epidermal growth factor (egf) and insulin-like growth factor (igf) in vivo.

Publications:

6

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-32753	Ser1044	WNLVSPDsPRSIDSN	Homo sapiens
pmid	sentence
7777512	Indeed, phosphorylation of the cytoplasmic domain of the low-affinity lif receptor alpha-subunit (lifr) in mono q-fractionated, lif-stimulated 3t3-l1 extracts occurred only in those fractions containing activated mapk;ser-1044 served as the major phosphorylation site in the human lifr for mapk both in agonist-stimulated 3t3-l1 lysates and by recombinant extracellular signal-regulated kinase 2 in vitro

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-192097	Ser111	ESNSDGAsPEPCTVT	Homo sapiens
pmid	sentence
23024368	We demonstrate that oct4a interacts with erk1/2 by using both in vitro gst pulldown and in vivo co-immunoprecipitation assays. Ms analysis identified phosphorylation of oct4a at ser-111. / serine 111 phosphorylation regulates oct4a protein subcellular distribution and degradation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-112544	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-113130	Ser1126	IAPSTNSsPVLKTKP	Homo sapiens
pmid	sentence
11747808	Both cdc2/cyclinb1 and mapk (erk2) efficiently phosphorylate separase at its major inhibitory site in vitro

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262765	Ser113	SPAPPAIsPIIKNAI	Mus musculus	NIH-3T3 Cell
pmid	sentence
22028470	We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5'-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. This approach identified 80 proteins phosphorylated by ERK2, 13 of which are known ERK2 substrates. With this improved methodology, we detected 98 sites directly phosphorylated by ERK2 on 80 proteins from NIH 3T3-L1 fibroblasts. Thirteen of these proteins are known substrates and the rest represent previously unknown kinase/substrate interactions. (table1)

Identifier	Residue	Sequence	Organism
SIGNOR-262766	Ser195	RRSDSLLsFRLDLDL	Mus musculus
pmid	sentence
22028470	We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5'-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. This approach identified 80 proteins phosphorylated by ERK2, 13 of which are known ERK2 substrates. With this improved methodology, we detected 98 sites directly phosphorylated by ERK2 on 80 proteins from NIH 3T3-L1 fibroblasts. Thirteen of these proteins are known substrates and the rest represent previously unknown kinase/substrate interactions. (table1)

Publications:

2

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-235742	Ser1132	TLPHGPRsASVSSIS	Chlorocebus aethiops
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 hsos1Replacing the MAP kinase phosphorylation sites with alanine residues results in an increase in the binding affinity of Grb2 to hSos1

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-235933	Ser1167	ESAPAESsPSKIMSK	Chlorocebus aethiops	COS Cell
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 hsos1Replacing the MAP kinase phosphorylation sites with alanine residues results in an increase in the binding affinity of Grb2 to hSos1

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-235925	Ser1178	IMSKHLDsPPAIPPR	Chlorocebus aethiops	COS Cell
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 hsos1Replacing the MAP kinase phosphorylation sites with alanine residues results in an increase in the binding affinity of Grb2 to hSos1

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236440	Ser1193	QPTSKAYsPRYSISD	Chlorocebus aethiops	COS Cell
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 hsos1Replacing 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-235929	Ser1197	KAYSPRYsISDRTSI	Chlorocebus aethiops
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 hsos1Replacing the MAP kinase phosphorylation sites with alanine residues results in an increase in the binding affinity of Grb2 to hSos1

Identifier	Residue	Organism
SIGNOR-236242		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:

6

Organism:

Chlorocebus Aethiops, Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-80092	Ser117	YPSMPAFsPGPGIKE	Homo sapiens
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
SIGNOR-74872	Ser1185	GTPPASTsPFSQLAA	Homo sapiens
pmid	sentence
10660621	Furthermore, erk-2 phosphorylated threonine 1179 and serine 1185 (and to a lesser extent, serine 395) in vitro, suggesting the importance of this pathway for src-1 regulation. Treatment of cells expressing src-1 with epidermal growth factor enhanced the ligand-dependent, progesterone receptor-mediated activation of a target reporter gene.

Identifier	Residue	Sequence	Organism
SIGNOR-74876	Ser395	PSVNPSIsPAHGVAR	Homo sapiens
pmid	sentence
10660621	Furthermore, erk-2 phosphorylated threonine 1179 and serine 1185 (and to a lesser extent, serine 395) in vitro, suggesting the importance of this pathway for src-1 regulation. Treatment of cells expressing src-1 with epidermal growth factor enhanced the ligand-dependent, progesterone receptor-mediated activation of a target reporter gene.

Identifier	Residue	Sequence	Organism
SIGNOR-74880	Thr1179	NYGTNPGtPPASTSP	Homo sapiens
pmid	sentence
10660621	Furthermore, erk-2 phosphorylated threonine 1179 and serine 1185 (and to a lesser extent, serine 395) in vitro, suggesting the importance of this pathway for src-1 regulation. Treatment of cells expressing src-1 with epidermal growth factor enhanced the ligand-dependent, progesterone receptor-mediated activation of a target reporter gene.

Publications:

3

Organism:

Homo Sapiens

Pathways:

Glucocorticoid receptor Signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249433	Ser12	ESPLCPLsPLEAGDL	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.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249434	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-277360	Ser122	CPMEHPLsADIAMAT	in vitro
pmid	sentence
28689659	Here we show that Akt, Erk2, and IKK1/2 phosphorylate Bcl3. Phosphorylation of Ser33 by Akt induces switching of K48 ubiquitination to K63 ubiquitination and thus promotes nuclear localization and stabilization of Bcl3. Phosphorylation by Erk2 and IKK1/2 of Ser114 and Ser446 converts Bcl3 into a transcriptional coregulator by facilitating its recruitment to DNA.

Identifier	Residue	Sequence	Organism
SIGNOR-277361	Ser454	PSPAPGGs	in vitro
pmid	sentence
28689659	Here we show that Akt, Erk2, and IKK1/2 phosphorylate Bcl3. Phosphorylation of Ser33 by Akt induces switching of K48 ubiquitination to K63 ubiquitination and thus promotes nuclear localization and stabilization of Bcl3. Phosphorylation by Erk2 and IKK1/2 of Ser114 and Ser446 converts Bcl3 into a transcriptional coregulator by facilitating its recruitment to DNA.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-157167	Ser126	SVYYKPSsPPTPTTP	Homo sapiens	Neuron
pmid	sentence
17681692	We have shown that erk2 is a kinase to phosphorylate nurr1 on multiple sites. S126 and t132, which are located near af1 core of nurr1, are dominant sites phosphorylated by erk2. reporter gene assays show that nurr1delta124-133/t185a, an erk2 phospho-site mutant form, could not further increase its transcriptional activity on th promoter, suggesting that nurr1 phosphorylation by erk2 may regulate its transcriptional activity on th promoter.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-157171	Thr132	SSPPTPTtPGFQVQH	Homo sapiens	Neuron
pmid	sentence
17681692	We have shown that erk2 is a kinase to phosphorylate nurr1 on multiple sites. S126 and t132, which are located near af1 core of nurr1, are dominant sites phosphorylated by erk2. reporter gene assays show that nurr1delta124-133/t185a, an erk2 phospho-site mutant form, could not further increase its transcriptional activity on th promoter, suggesting that nurr1 phosphorylation by erk2 may regulate its transcriptional activity on th promoter.

Publications:

2

Organism:

Homo Sapiens

Tissue:

Brain

Identifier	Residue	Sequence	Organism
SIGNOR-185215	Ser130	SGEQAEGsPGGPGDS	Homo sapiens
pmid	sentence
19364816	Extracellular signal-regulated kinase 2-dependent phosphorylation induces cytoplasmic localization and degradation of p21cip1.\|Phosphopeptide analysis of in vitro ERK2-phosphorylated p21(Cip1) revealed two phosphorylation sites, Thr57 and Ser130.

Identifier	Residue	Sequence	Organism
SIGNOR-185219	Thr57	NFDFVTEtPLEGDFA	Homo sapiens
pmid	sentence
19364816	We have shown that erk2 interacts with and phosphorylates p21cip1, promoting p21cip1_ubiquitination. We identified two erk2 phosphorylation sites, thr57 and ser130, in p21cip1_and showed that phosphorylation of these residues increases p21cip1_cytoplasmic distribution and proteasome-dependent degradation.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-262758	Ser139	SSGVVPQsAPPVPTA	Mus musculus
pmid	sentence
22028470	We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5'-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. This approach identified 80 proteins phosphorylated by ERK2, 13 of which are known ERK2 substrates. With this improved methodology, we detected 98 sites directly phosphorylated by ERK2 on 80 proteins from NIH 3T3-L1 fibroblasts. Thirteen of these proteins are known substrates and the rest represent previously unknown kinase/substrate interactions. Among the ERK2 substrates, we identified the E-twenty six (ETS) domain-containing protein ETV3. We determined that phosphorylation of this protein by ERK2 was functionally relevant, abrogating the DNA-binding activity of ETV3 at thousands of targets across the genome, thereby providing an additional mechanism for transcriptional regulation downstream of ERK2 activation.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-108560	Ser14	MGAELPSsPLAIEYV	Homo sapiens	HeLa Cell
pmid	sentence
11416124	These residues are phosphorylated by erk2 but not by p38, jnk, and erk5 in vitro. However, the contribution of the mek/erk pathway to mafa phosphorylation in vivo appears to be moderate, implicating another kinase. The integrity of serine 14 and serine 65 residues is required for transcriptional activity, since their mutation into alanine severely impairs mafa capacity to activate transcription.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275976	Ser14	MGAELPSsPLAIEYV	Homo sapiens	HeLa Cell
pmid	sentence
11416124	In the present study, we provide the first evidence that MafA is phosphorylated and that its biological properties strongly rely upon phosphorylation of serines 14 and 65, two residues located in the transcriptional activating domain within a consensus for phosphorylation by mitogen-activated protein kinases and which are conserved among Maf proteins. These residues are phosphorylated by ERK2 but not by p38, JNK, and ERK5 in vitro.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-108564	Ser65	PCSSVPSsPSFCAPS	Homo sapiens	HeLa Cell
pmid	sentence
11416124	These residues are phosphorylated by erk2 but not by p38, jnk, and erk5 in vitro. However, the contribution of the mek/erk pathway to mafa phosphorylation in vivo appears to be moderate, implicating another kinase. The integrity of serine 14 and serine 65 residues is required for transcriptional activity, since their mutation into alanine severely impairs mafa capacity to activate transcription.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275977	Ser65	PCSSVPSsPSFCAPS	Homo sapiens	HeLa Cell
pmid	sentence
11416124	In the present study, we provide the first evidence that MafA is phosphorylated and that its biological properties strongly rely upon phosphorylation of serines 14 and 65, two residues located in the transcriptional activating domain within a consensus for phosphorylation by mitogen-activated protein kinases and which are conserved among Maf proteins. These residues are phosphorylated by ERK2 but not by p38, JNK, and ERK5 in vitro.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-169875	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-102216	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	Cell Line
SIGNOR-248279	Ser142	AGNSAPNsPMAMLHI	Homo sapiens	HeLa Cell
pmid	sentence
21617040	Evidence for ERK2-mediated TFEB phosphorylation came from ERK2-TFEB coimmuno-precipitation (fig. S12C) in normal but not in starved medium and from a peptide-based kinase assay showing that mutation of Ser142 to alanine abolished ERK2-mediated phosphorylation (

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-265221	Ser145	ARDDGLFsGDPNWFP	Homo sapiens	SW-1990 Cell
pmid	sentence
30041673	ERK2 interacted with 29-31 amino acids of transgelin-2 and subsequently phosphorylated the S145 residue of transgelin-2. S145 phosphorylation of transgelin-2 played important roles in cell proliferation and tumorigenesis of PDAC.\| We found that the protein stability of transgelin-2 was regulated by KRAS. ERK-mediated phosphorylation resulted in accumulation of transgelin-2 protein.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249435	Ser15	GPGGPLRsASPHRSA	Homo sapiens
pmid	sentence
15728359	We have identified three sites phosphorylated by ERK2 (Ser-15 and Ser-205) and cyclin-dependent PK 5 (Cdk5) (Ser-17), within the actin-binding domain of spinophilin.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-138163	Ser150	PELCGPGsPPVLTPG	Homo sapiens
pmid	sentence
15952796	We show that grb10 is a direct substrate of the p42/44 mitogen-activated protein kinase (mapk)we identified ser(150), ser(418), and ser(476) of human grb10zeta as mapk-mediated in vitro phosphorylation sites. Replacing ser(150) and ser(476) with alanines reduced the inhibitory effect of human grb10zeta on insulin-stimulated irs1 tyrosine phosphorylation. Taken together, our findings suggest that phosphorylation of the adaptor protein may provide a feedback inhibitory mechanism by which grb10 regulates insulin signaling.

Identifier	Residue	Sequence	Organism
SIGNOR-138167	Ser476	MNILGSQsPLHPSTL	Homo sapiens
pmid	sentence
15952796	We show that grb10 is a direct substrate of the p42/44 mitogen-activated protein kinase (mapk)we identified ser(150), ser(418), and ser(476) of human grb10zeta as mapk-mediated in vitro phosphorylation sites. Replacing ser(150) and ser(476) with alanines reduced the inhibitory effect of human grb10zeta on insulin-stimulated irs1 tyrosine phosphorylation. Taken together, our findings suggest that phosphorylation of the adaptor protein may provide a feedback inhibitory mechanism by which grb10 regulates insulin signaling.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-129883	Ser151	EDYVSILsPKEVSLD	Homo sapiens
pmid	sentence
15488168	Phosphorylation of gaip by erk2 were abrogated when serine at position 151 in the rgs domain was substituted by an alanine residue using site-directed mutagenesis. Furthermore, the lysosomal-autophagic pathway was not stimulated in s151a-gaip mutant-expressing cells when compared with wild-type gaip-expressing cells. These results demonstrate that the gtpase-activating protein activity of gaip is stimulated by erk2 phosphorylation.

Identifier	Residue	Sequence	Organism
SIGNOR-82083	Ser151	EDYVSILsPKEVSLD	Homo sapiens
pmid	sentence
10993892	Phosphorylation of gaip by erk2 were abrogated when serine at position 151 in the rgs domain was substituted by an alanine residue using site-directed mutagenesis. Furthermore, the lysosomal-autophagic pathway was not stimulated in s151a-gaip mutant-expressing cells when compared with wild-type gaip-expressing cells. These results demonstrate that the gtpase-activating protein activity of gaip is stimulated by erk2 phosphorylation.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-259920	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236388	Thr753	YACASPKtPIQAGGY	Rattus norvegicus	PC-12 Cell
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, Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-88716	Ser152	PASSVSSsPSPPFGH	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
SIGNOR-88720	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
SIGNOR-88724	Ser164	FGHSAAVsPTFMPRS	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.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-132967	Ser159	DGSCSSSsPPLPVLG	Homo sapiens
pmid	sentence
15632084	In vitro phosphorylation assays using glutathione S-transferase (GST)-MKP-3 fusion proteins indicated that ERK2 could phosphorylate MKP-3 on serines 159 and 197Double serine mutants of MKP-3 or MKP-3-GFP were more efficiently protected from degradation than single mutants or wild-type MKP-3, indicating that phosphorylation of either serine by ERK1/2 enhances proteasomal degradation of MKP-3.

Identifier	Residue	Sequence	Organism
SIGNOR-132971	Ser197	SATDSDGsPLSNSQP	Homo sapiens
pmid	sentence
15632084	In vitro phosphorylation assays using glutathione S-transferase (GST)-MKP-3 fusion proteins indicated that ERK2 could phosphorylate MKP-3 on serines 159 and 197Double serine mutants of MKP-3 or MKP-3-GFP were more efficiently protected from degradation than single mutants or wild-type MKP-3, indicating that phosphorylation of either serine by ERK1/2 enhances proteasomal degradation of MKP-3.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262940	Ser16	KYEPAAVsEQGDKKG	Mycolicibacterium chitae	OK Cell
pmid	sentence
14976217	Parathyroid hormone (PTH) inhibits Na+,K+-ATPase activity through protein kinase C- (PKC) and extracellular signal-regulated kinase- (ERK) dependent pathways and increases serine phosphorylation of the α1-subunit. These results suggest that PTH regulates Na(+),K(+)-ATPase by PKC and ERK-dependent alpha(1)-subunit phosphorylation and that the phosphorylation requires the expression of a serine at the 11 position of the Na(+),K(+)-ATPase alpha(1)-subunit.

Publications:

1

Organism:

Mycolicibacterium Chitae

Identifier	Residue	Sequence	Organism
SIGNOR-262928	Ser160	GVTKAISsPTVSRLT	in vitro
pmid	sentence
17693641	Here we show that TPPP induces tubulin self-assembly into intact frequently bundled microtubules, and that the phosphorylation of specific sites distinctly affects the function of TPPP. The phosphorylation sites Thr(14), Ser(18), Ser(160) for Cdk5; Ser(18), Ser(160) for ERK2, and Ser(32) for PKA were identified by mass spectrometry. The phosphorylation by ERK2 or Cdk5 resulted in the loss of microtubule-assembling activity of TPPP.

Identifier	Residue	Sequence	Organism
SIGNOR-262929	Ser18	ANRTPPKsPGDPSKD	in vitro
pmid	sentence
17693641	Here we show that TPPP induces tubulin self-assembly into intact frequently bundled microtubules, and that the phosphorylation of specific sites distinctly affects the function of TPPP. The phosphorylation sites Thr(14), Ser(18), Ser(160) for Cdk5; Ser(18), Ser(160) for ERK2, and Ser(32) for PKA were identified by mass spectrometry. The phosphorylation by ERK2 or Cdk5 resulted in the loss of microtubule-assembling activity of TPPP.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-67520	Ser161	SPTEDPRsPPACSSS	Homo sapiens
pmid	sentence
10330152	The experiments presented here indicate that erf is regulated during nuclear import and/or export and that this process depends on its phosphorylation by erks our analysis indicates that in addition to t526 (position 7), s161 (position 2), s246 (position 3), and s251 (position 4) are also phosphorylated in vitro by erk2 and in vivo after mitogenic stimulation (fig. 3a).

Identifier	Residue	Sequence	Organism
SIGNOR-67524	Ser246	RGGPEPLsPFPVSPL	Homo sapiens
pmid	sentence
10330152	The experiments presented here indicate that erf is regulated during nuclear import and/or export and that this process depends on its phosphorylation by erks our analysis indicates that in addition to t526 (position 7), s161 (position 2), s246 (position 3), and s251 (position 4) are also phosphorylated in vitro by erk2 and in vivo after mitogenic stimulation (fig. 3a).

Identifier	Residue	Sequence	Organism
SIGNOR-67528	Ser251	PLSPFPVsPLAGPGS	Homo sapiens
pmid	sentence
10330152	The experiments presented here indicate that erf is regulated during nuclear import and/or export and that this process depends on its phosphorylation by erks our analysis indicates that in addition to t526 (position 7), s161 (position 2), s246 (position 3), and s251 (position 4) are also phosphorylated in vitro by erk2 and in vivo after mitogenic stimulation (fig. 3a).

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-120084	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-120088	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-120092	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-119366	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-120096	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-120100	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-120104	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-120108	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-120112	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-120116	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-120120	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-120124	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-120128	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-120132	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-120136	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-120140	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-120144	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-120148	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-120152	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-120156	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-120160	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-120164	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-120168	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-79515	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-249198	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-262910	Ser173	MLETLSQsPPKGVTI	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-262911	Ser189	YRPKPSSsPVIFAGG	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	Cell Line
SIGNOR-262912	Ser272	FSGIESSsPEVKGYW	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	Cell Line
SIGNOR-262913	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
SIGNOR-120451	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-120455	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-120459	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-120463	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	Organism
SIGNOR-75030	Ser180	PGSSAPNsPMAMLTL	Homo sapiens
pmid	sentence
10673502	The current study reveals that c-kit signaling triggers two phosphorylation events on mi, which up-regulate transactivation potential yet simultaneously target mi for ubiquitin-dependent proteolysis. The specific activation/degradation signals derive from mapk/erk targeting of serine 73the results suggested that s1p reduced melanin synthesis via s1p(3) receptor-mediated erk and rsk-1 activation, and subsequent mitf dual phosphorylation and degradation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-172869	Ser183	PPTQKPPsPPMSGRG	Homo sapiens
pmid	sentence
21419341	Our mass spectrometry also identified abi1 s183 and s225 on abi1 (numbering corresponds to abi1 isoform 1) as sites phosphorylated on endogenous protein and in the wildtype erk-dependent in vitro phosphorylated sample. these data indicate erk phosphorylation of abi1 is required for basal and egf-induced wrc interaction with the wrp2/3 complex.

Identifier	Residue	Sequence	Organism
SIGNOR-172873	Ser222	TSPARLGsQHSPGRT	Homo sapiens
pmid	sentence
21419341	Our mass spectrometry also identified abi1 s183 and s225 on abi1 (numbering corresponds to abi1 isoform 1) as sites phosphorylated on endogenous protein and in the wildtype erk-dependent in vitro phosphorylated sample. these data indicate erk phosphorylation of abi1 is required for basal and egf-induced wrc interaction with the wrp2/3 complex.

Identifier	Residue	Sequence	Organism
SIGNOR-172877	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:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-161593	Ser187	NSHPFPHsPNSSYPN	Homo sapiens
pmid	sentence
19914161	Phosphorylation of the linker region of smads mediated by erk2, gsk3?, And cdk2/4 negatively regulates smad activity by preventing their relocation to the nucleus, by inhibiting their interactions with coactivators, or by accelerating their degradation;in contrast, erk2 phosphorylated all four smad1 residues almost evenly, while showing a preference for s204 over s208 and s213 in smad3

Identifier	Residue	Sequence	Organism
SIGNOR-52674	Ser187	NSHPFPHsPNSSYPN	Homo sapiens
pmid	sentence
9335504	In contrast to the bmp-stimulated phosphorylation of smad1, which affects carboxy-terminal serines and induces nuclear accumulation of smad1, erk-mediated phosphorylation specifically inhibits the nuclear accumulation of smad1. phosphorylation occurs at specific serines within the region linking the inhibitory and effector domains of smad1

Identifier	Residue	Sequence	Organism
SIGNOR-161597	Ser195	PNSSYPNsPGSSSST	Homo sapiens
pmid	sentence
19914161	Phosphorylation of the linker region of smads mediated by erk2, gsk3?, And cdk2/4 negatively regulates smad activity by preventing their relocation to the nucleus, by inhibiting their interactions with coactivators, or by accelerating their degradation;in contrast, erk2 phosphorylated all four smad1 residues almost evenly, while showing a preference for s204 over s208 and s213 in smad3

Identifier	Residue	Sequence	Organism
SIGNOR-161686	Ser195	PNSSYPNsPGSSSST	Homo sapiens
pmid	sentence
19914168	Phosphorylation of the linker region of smads mediated by erk2, gsk3?, And cdk2/4 negatively regulates smad activity by preventing their relocation to the nucleus, by inhibiting their interactions with coactivators, or by accelerating their degradation;in contrast, erk2 phosphorylated all four smad1 residues almost evenly, while showing a preference for s204 over s208 and s213 in smad3

Identifier	Residue	Sequence	Organism
SIGNOR-52678	Ser195	PNSSYPNsPGSSSST	Homo sapiens
pmid	sentence
9335504	In contrast to the bmp-stimulated phosphorylation of smad1, which affects carboxy-terminal serines and induces nuclear accumulation of smad1, erk-mediated phosphorylation specifically inhibits the nuclear accumulation of smad1. phosphorylation occurs at specific serines within the region linking the inhibitory and effector domains of smad1

Identifier	Residue	Sequence	Organism
SIGNOR-52691	Ser214	PTSSDPGsPFQMPAD	Homo sapiens
pmid	sentence
9335504	In contrast to the bmp-stimulated phosphorylation of smad1, which affects carboxy-terminal serines and induces nuclear accumulation of smad1, erk-mediated phosphorylation specifically inhibits the nuclear accumulation of smad1. phosphorylation occurs at specific serines within the region linking the inhibitory and effector domains of smad1

Identifier	Residue	Sequence	Organism
SIGNOR-161605	Ser214	PTSSDPGsPFQMPAD	Homo sapiens
pmid	sentence
19914161	Phosphorylation of the linker region of smads mediated by erk2, gsk3?, And cdk2/4 negatively regulates smad activity by preventing their relocation to the nucleus, by inhibiting their interactions with coactivators, or by accelerating their degradation;in contrast, erk2 phosphorylated all four smad1 residues almost evenly, while showing a preference for s204 over s208 and s213 in smad3

Identifier	Residue	Sequence	Organism
SIGNOR-161694	Ser214	PTSSDPGsPFQMPAD	Homo sapiens
pmid	sentence
19914168	Phosphorylation of the linker region of smads mediated by erk2, gsk3?, And cdk2/4 negatively regulates smad activity by preventing their relocation to the nucleus, by inhibiting their interactions with coactivators, or by accelerating their degradation;in contrast, erk2 phosphorylated all four smad1 residues almost evenly, while showing a preference for s204 over s208 and s213 in smad3

Publications:

8

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-269087	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-276107	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-276103	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-276101	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-276105	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-276104	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-276109	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-277338	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	Cell Line
SIGNOR-249431	Ser203	EYPEPYAsPPQPGLP	Chlorocebus aethiops	COS Cell
pmid	sentence
10230405	Here we show that maximal SF-1-mediated transcription and interaction with general nuclear receptor cofactors depends on phosphorylation of a single serine residue (Ser-203) located in a major activation domain (AF-1) of the protein. Moreover, phosphorylation-dependent SF-1 activation is likely mediated by the mitogen-activated protein kinase (MAPK) signaling pathway.

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-161609	Ser204	NHSMDAGsPNLSPNP	Homo sapiens
pmid	sentence
19914161	Phosphorylation of the linker region of Smads mediated by ERK2, GSK3β, and CDK2/4 negatively regulates Smad activity

Identifier	Residue	Sequence	Organism
SIGNOR-161613	Ser208	DAGSPNLsPNPMSPA	Homo sapiens
pmid	sentence
19914161	Phosphorylation of the linker region of smads mediated by erk2, gsk3?, And cdk2/4 negatively regulates smad activity by preventing their relocation to the nucleus, by inhibiting their interactions with coactivators, or by accelerating their degradation;in contrast, erk2 phosphorylated all four smad1 residues almost evenly, while showing a preference for s204 over s208 and s213 in smad3

Identifier	Residue	Sequence	Organism
SIGNOR-66746	Thr179	PQSNIPEtPPPGYLS	Homo sapiens
pmid	sentence
10197981	Oncogenically activated ras inhibits the tgfbeta-induced nuclear accumulation of smad2 and smad3 and smad-dependent transcription. Ras acting via erk map kinases causes phosphorylation of smad2 and smad3 at specific sites in the region linking the dna-binding domain and the transcriptional activation domain.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-161698	Ser204	NHSMDAGsPNLSPNP	Homo sapiens
pmid	sentence
19914168	In contrast, ERK2 phosphorylated all four Smad1 residues almost evenly, while showing a preference for S204 over S208 and S213 in Smad3

Identifier	Residue	Sequence	Organism
SIGNOR-126744	Ser204	NHSMDAGsPNLSPNP	Homo sapiens
pmid	sentence
15241418	We found that ser 203 and ser 207 were phosphorylated by map kinase and that thr 178 was phosphorylated mostly by cdk and to a lesser extent by map kinase

Identifier	Residue	Sequence	Organism
SIGNOR-126748	Ser208	DAGSPNLsPNPMSPA	Homo sapiens
pmid	sentence
15241418	We found that ser 203 and ser 207 were phosphorylated by map kinase and that thr 178 was phosphorylated mostly by cdk and to a lesser extent by map kinase

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-161601	Ser206	SSSTYPHsPTSSDPG	Homo sapiens
pmid	sentence
19914161	Phosphorylation of the linker region of smads mediated by erk2, gsk3?, And cdk2/4 negatively regulates smad activity by preventing their relocation to the nucleus, by inhibiting their interactions with coactivators, or by accelerating their degradation;in contrast, erk2 phosphorylated all four smad1 residues almost evenly, while showing a preference for s204 over s208 and s213 in smad3

Identifier	Residue	Sequence	Organism
SIGNOR-52687	Ser206	SSSTYPHsPTSSDPG	Homo sapiens
pmid	sentence
9335504	In contrast to the bmp-stimulated phosphorylation of smad1, which affects carboxy-terminal serines and induces nuclear accumulation of smad1, erk-mediated phosphorylation specifically inhibits the nuclear accumulation of smad1. phosphorylation occurs at specific serines within the region linking the inhibitory and effector domains of smad1

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-120566	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-264775	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-264774	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	Cell Line
SIGNOR-260086	Ser213	DNMIRRLsPAERAQG	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.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-260087	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
SIGNOR-161617	Ser213	NLSPNPMsPAHNNLD	Homo sapiens
pmid	sentence
19914161	Phosphorylation of the linker region of smads mediated by erk2, gsk3?, And cdk2/4 negatively regulates smad activity by preventing their relocation to the nucleus, by inhibiting their interactions with coactivators, or by accelerating their degradation;in contrast, erk2 phosphorylated all four smad1 residues almost evenly, while showing a preference for s204 over s208 and s213 in smad3

Identifier	Residue	Sequence	Organism
SIGNOR-161706	Ser213	NLSPNPMsPAHNNLD	Homo sapiens
pmid	sentence
19914168	Phosphorylation of the linker region of smads mediated by erk2, gsk3?, And cdk2/4 negatively regulates smad activity by preventing their relocation to the nucleus, by inhibiting their interactions with coactivators, or by accelerating their degradation;in contrast, erk2 phosphorylated all four smad1 residues almost evenly, while showing a preference for s204 over s208 and s213 in smad3

Identifier	Residue	Sequence	Organism
SIGNOR-66742	Ser213	NLSPNPMsPAHNNLD	Homo sapiens
pmid	sentence
10197981	Oncogenically activated ras inhibits the tgfbeta-induced nuclear accumulation of smad2 and smad3 and smad-dependent transcription. Ras acting via erk map kinases causes phosphorylation of smad2 and smad3 at specific sites in the region linking the dna-binding domain and the transcriptional activation domain.

Identifier	Residue	Organism
SIGNOR-66749		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:

4

Organism:

Homo Sapiens

Tissue:

Lung, Breast

Identifier	Residue	Sequence	Organism
SIGNOR-181014	Ser2155	GFAEAIHsPQVAGVP	Homo sapiens
pmid	sentence
18794356	Tpr is phosphorylated by erk2 at four different sites. / because phosphorylation of tpr by activated erk stabilizes their interaction, we hypothesize that this phosphorylation is not part of a signal amplification cascade but rather positions activated erk to perform a continuing function in the nuclear pore.

Identifier	Residue	Sequence	Organism
SIGNOR-181018	Thr2116	VGRGLQLtPGIGGMQ	Homo sapiens
pmid	sentence
18794356	Tpr is phosphorylated by erk2 at four different sites. / because phosphorylation of tpr by activated erk stabilizes their interaction, we hypothesize that this phosphorylation is not part of a signal amplification cascade but rather positions activated erk to perform a continuing function in the nuclear pore.

Identifier	Residue	Sequence	Organism
SIGNOR-181022	Thr2137	EDRTVPStPTLVVPH	Homo sapiens
pmid	sentence
18794356	Tpr is phosphorylated by erk2 at four different sites. / because phosphorylation of tpr by activated erk stabilizes their interaction, we hypothesize that this phosphorylation is not part of a signal amplification cascade but rather positions activated erk to perform a continuing function in the nuclear pore.

Identifier	Residue	Sequence	Organism
SIGNOR-181026	Thr2214	GGRSVPTtPLQVAAP	Homo sapiens
pmid	sentence
18794356	Tpr is phosphorylated by erk2 at four different sites. / because phosphorylation of tpr by activated erk stabilizes their interaction, we hypothesize that this phosphorylation is not part of a signal amplification cascade but rather positions activated erk to perform a continuing function in the nuclear pore.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262762	Ser216	PSGSGAAsPTGSAVD	Mus musculus	NIH-3T3 Cell
pmid	sentence
22028470	We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5'-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. This approach identified 80 proteins phosphorylated by ERK2, 13 of which are known ERK2 substrates. With this improved methodology, we detected 98 sites directly phosphorylated by ERK2 on 80 proteins from NIH 3T3-L1 fibroblasts. Thirteen of these proteins are known substrates and the rest represent previously unknown kinase/substrate interactions. (table1)

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262763	Ser5099	DVEFDIKsPKFKAEA	Mus musculus	NIH-3T3 Cell
pmid	sentence
22028470	We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5'-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. This approach identified 80 proteins phosphorylated by ERK2, 13 of which are known ERK2 substrates. With this improved methodology, we detected 98 sites directly phosphorylated by ERK2 on 80 proteins from NIH 3T3-L1 fibroblasts. Thirteen of these proteins are known substrates and the rest represent previously unknown kinase/substrate interactions. (table1)

Identifier	Residue	Sequence	Organism
SIGNOR-262764	Ser5110	KAEAPLPsPKLEGEL	Mus musculus
pmid	sentence
22028470	We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5'-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. This approach identified 80 proteins phosphorylated by ERK2, 13 of which are known ERK2 substrates. With this improved methodology, we detected 98 sites directly phosphorylated by ERK2 on 80 proteins from NIH 3T3-L1 fibroblasts. Thirteen of these proteins are known substrates and the rest represent previously unknown kinase/substrate interactions. (table1)

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262767	Thr5794	REFSGPStPTGTLEF	Mus musculus	NIH-3T3 Cell
pmid	sentence
22028470	We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5'-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. This approach identified 80 proteins phosphorylated by ERK2, 13 of which are known ERK2 substrates. With this improved methodology, we detected 98 sites directly phosphorylated by ERK2 on 80 proteins from NIH 3T3-L1 fibroblasts. Thirteen of these proteins are known substrates and the rest represent previously unknown kinase/substrate interactions. (table1)

Identifier	Residue	Sequence	Organism
SIGNOR-262768	Thr694	LPDMSVKtPKISMPD	Mus musculus
pmid	sentence
22028470	We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5'-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. This approach identified 80 proteins phosphorylated by ERK2, 13 of which are known ERK2 substrates. With this improved methodology, we detected 98 sites directly phosphorylated by ERK2 on 80 proteins from NIH 3T3-L1 fibroblasts. Thirteen of these proteins are known substrates and the rest represent previously unknown kinase/substrate interactions. (table1)

Publications:

5

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-188139	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.

Identifier	Residue	Sequence	Organism
SIGNOR-188135	Ser315	TQSKPVSsPFPTKPL	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:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-219308	Ser221	DHEKKAYsFCGTVEY	Chlorocebus aethiops	COS Cell
pmid	sentence
9430688	Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-219312	Ser363	TSRTPKDsPGIPPSA	Chlorocebus aethiops	COS Cell
pmid	sentence
9430688	Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-219316	Ser380	HQLFRGFsFVATGLM	Chlorocebus aethiops	COS Cell
pmid	sentence
9430688	Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733.

Identifier	Residue	Sequence	Organism
SIGNOR-219320	Ser732	RRVRKLPsTTL	Chlorocebus aethiops
pmid	sentence
9430688	Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-219324	Thr359	DTEFTSRtPKDSPGI	Chlorocebus aethiops	COS Cell
pmid	sentence
9430688	Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-59363	Thr573	AENGLLMtPCYTANF	Homo sapiens	HeLa Cell
pmid	sentence
9687510	Thus, MAPK1/ERK1 and MAPK2/ERK2 activate three closely related protein kinases known as MAPK_activated protein kinases_1a, _1b and _1c (MAPKAP_K1a/b/c; also known as RSK1/2/3)

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-219328	Thr573	AENGLLMtPCYTANF	Chlorocebus aethiops	COS Cell
pmid	sentence
9430688	Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733.

Identifier	Residue	Organism
SIGNOR-102645		Homo sapiens
pmid	sentence
12832467	Efficient rsk activation by erk requires its interaction through a docking site located near the c terminus of rsk

Publications:

8

Organism:

Chlorocebus Aethiops, Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252750	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-252754	Ser363	TSRTPKDsPGIPPSA	Chlorocebus aethiops	COS Cell
pmid	sentence
9430688	Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252748	Ser380	HQLFRGFsFVATGLM	Chlorocebus aethiops	COS Cell
pmid	sentence
9430688	Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252747	Ser732	RRVRKLPsTTL	Chlorocebus aethiops	COS Cell
pmid	sentence
9430688	Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252751	Thr359	DTEFTSRtPKDSPGI	Chlorocebus aethiops	COS Cell
pmid	sentence
9430688	Several lines of evidence indicate that the mapkap-k1 isoforms are also activated by mapks in vivo via the ras-dependent protein kinase cascade that is triggered by growth factors or tumor-promoting phorbol esters, such as phorbol 12-myristate 13-acetate (pma). here we identify six sites in mapkap-k1a that become phosphorylated in transfected cos-1 cells. The inactive form of mapkap-k1a in unstimulated cells is partially phosphorylated at ser222 and ser733. Stimulation with phorbol 12-myristate 13-acetate induces the phosphorylation of thr360, ser364, thr574, and ser381 and increases the phosphorylation of ser222 and ser733.

Identifier	Residue	Sequence	Organism
SIGNOR-252753	Thr573	AENGLLMtPCYTANF	Homo sapiens
pmid	sentence
9687510	Thus, MAPK1/ERK1 and MAPK2/ERK2 activate three closely related protein kinases known as MAPK_activated protein kinases_1a, _1b and _1c (MAPKAP_K1a/b/c; also known as RSK1/2/3)

Identifier	Residue	Sequence	Organism
SIGNOR-252752	Thr573	AENGLLMtPCYTANF	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	Organism
SIGNOR-252749		Homo sapiens
pmid	sentence
12832467	Efficient rsk activation by erk requires its interaction through a docking site located near the c terminus of rsk

Publications:

8

Organism:

Chlorocebus Aethiops, Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-118546	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-249428	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-156887	Ser2279	PVQPNPMsPQQHMLP	Homo sapiens
pmid	sentence
17623675	Serine residues (ser-2279, ser-2315, and ser-2366) on the c terminus of p300 were the major signaling targets of egf. Furthermore, the c-terminal serine phosphorylation of p300 stimulated its histone acetyltransferase activity these results also constituted the first report identifying the unique p300 phosphorylation sites induced by erk2 in vivo.

Identifier	Residue	Sequence	Organism
SIGNOR-156891	Ser2315	RSPQPVPsPRPQSQP	Homo sapiens
pmid	sentence
17623675	Erk2-mediated c-terminal serine phosphorylation of p300 (ser-2279, ser-2315, and ser-2366) is vital to the regulation of epidermal growth factor-induced keratin 16 gene expression.

Identifier	Residue	Sequence	Organism
SIGNOR-156895	Ser2366	MEQGHFAsPDQNSML	Homo sapiens
pmid	sentence
17623675	Serine residues (ser-2279, ser-2315, and ser-2366) on the c terminus of p300 were the major signaling targets of egf. Furthermore, the c-terminal serine phosphorylation of p300 stimulated its histone acetyltransferase activity these results also constituted the first report identifying the unique p300 phosphorylation sites induced by erk2 in vivo.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249456	Ser228	PPGDLPLsPSAFSAA	Mus musculus	NIH-3T3 Cell
pmid	sentence
7768935	By a combination of protease digestion experiments and site-directed mutagenesis strategies, we found that serine 220 was phosphorylated by p42 MAP kinase in vitro. Expression of mutant TTP in fibroblasts confirmed that serine 220 was one of the major, mitogen-stimulated phosphorylation sites on the protein in intact cells. \|It is not obvious how phosphorylation of TTP at serine 220 would alter DNA binding, since this residue lies well outside of the putative zinc finger region, which is between amino acids 95 to 159 in the mouse protein

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249421	Ser239	FRRGLDDsTGGTPLT	Homo sapiens	HEK-293 Cell
pmid	sentence
12556484	Moreover, both proteins were phosphorylated by Cdc2 and Erk2 in vitro. In the case of Nudel, the phosphorylation sites were also located in the S/TP motifs. Detailed mutagenesis study indicated that T219, S242, and T245 were phosphorylated by Cdc2, while T219 and T245 were phosphorylated by Erk2.\|Phosphorylation of Nudel in M phase appears to positively modulate dynein motor activity. Both phosphorylated and unphosphorylated forms of Nudel were transported by dynein (Fig. 7 and 9 and data not shown), indicating that neither of them inactivated the dynein motor. On the other hand, both phospho-Nudel and Nudelpmt5 bound Lis1 more strongly than Nudel or Nudelmt5 did

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249422	Thr215	ATGSVPStPIAHRGP	Homo sapiens	HEK-293 Cell
pmid	sentence
12556484	Moreover, both proteins were phosphorylated by Cdc2 and Erk2 in vitro. In the case of Nudel, the phosphorylation sites were also located in the S/TP motifs. Detailed mutagenesis study indicated that T219, S242, and T245 were phosphorylated by Cdc2, while T219 and T245 were phosphorylated by Erk2.\|Phosphorylation of Nudel in M phase appears to positively modulate dynein motor activity. Both phosphorylated and unphosphorylated forms of Nudel were transported by dynein (Fig. 7 and 9 and data not shown), indicating that neither of them inactivated the dynein motor. On the other hand, both phospho-Nudel and Nudelpmt5 bound Lis1 more strongly than Nudel or Nudelmt5 did

Identifier	Residue	Organism
SIGNOR-274078		in vitro
pmid	sentence
12556484	We found that Nudel and NudE were also phosphorylated in M phase (Fig. (Fig.22 and and3).3). First, Nudel and NudE were specifically phosphorylated in M phase. Moreover, both proteins were phosphorylated by Cdc2 and Erk2 in vitro.Due to conservation of the S/TP motifs, NudE may also be phosphorylated at similar sites by these kinases, though it contains an additional potential Cdk site at S282 (SPNR).

Publications:

3

Organism:

Homo Sapiens, In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-91714	Ser245	NQSMDTGsPAELSPT	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.

Identifier	Residue	Sequence	Organism
SIGNOR-91718	Ser250	TGSPAELsPTTLSPV	Homo sapiens
pmid	sentence
12193595	Phosphorylation of smad2 by erk increases its transcriptional activity /thr220 and ser245, ser250, and ser255 were possible phosphorylation sites. The phosphorylation of peak a peptide by erk1 is consistent with that prediction.

Identifier	Residue	Sequence	Organism
SIGNOR-91722	Ser255	ELSPTTLsPVNHSLD	Homo sapiens
pmid	sentence
12193595	Phosphorylation of smad2 by erk increases its transcriptional activity /thr220 and ser245, ser250, and ser255 were possible phosphorylation sites. The phosphorylation of peak a peptide by erk1 is consistent with that prediction.

Identifier	Residue	Sequence	Organism
SIGNOR-91726	Thr220	QSNYIPEtPPPGYIS	Homo sapiens
pmid	sentence
12193595	Phosphorylation of smad2 by erk increases its transcriptional activity /thr220 and ser245, ser250, and ser255 were possible phosphorylation sites. The phosphorylation of peak a peptide by erk1 is consistent with that prediction.

Publications:

4

Organism:

Homo Sapiens

Tissue:

Lung

Identifier	Residue	Sequence	Organism
SIGNOR-138969	Ser249	DTRQIQPsPPWSYDQ	Homo sapiens
pmid	sentence
16046550	We have identified four phosphorylation sites on AML1c that are necessary for transcriptional activity of AML1c in K562 and 293T cells (27).4 Mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. The presence of these mutations results in an increase in the amount of ubiquitinated AML1c in the matrix, and increases the half-life of this insoluble AML1c. One possible model to explain these observations is that phosphorylation might be necessary for the normal process of both proteasome degradation and transcriptional activation.

Identifier	Residue	Sequence	Organism
SIGNOR-138973	Ser266	QYLGSIAsPSVHPAT	Homo sapiens
pmid	sentence
16046550	We have identified four phosphorylation sites on AML1c that are necessary for transcriptional activity of AML1c in K562 and 293T cells (27).4 Mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. The presence of these mutations results in an increase in the amount of ubiquitinated AML1c in the matrix, and increases the half-life of this insoluble AML1c. One possible model to explain these observations is that phosphorylation might be necessary for the normal process of both proteasome degradation and transcriptional activation.

Identifier	Residue	Sequence	Organism
SIGNOR-138985	Ser276	VHPATPIsPGRASGM	Homo sapiens
pmid	sentence
16046550	We have identified four phosphorylation sites on AML1c that are necessary for transcriptional activity of AML1c in K562 and 293T cells (27).4 Mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. The presence of these mutations results in an increase in the amount of ubiquitinated AML1c in the matrix, and increases the half-life of this insoluble AML1c. One possible model to explain these observations is that phosphorylation might be necessary for the normal process of both proteasome degradation and transcriptional activation.

Identifier	Residue	Sequence	Organism
SIGNOR-138981	Thr273	SPSVHPAtPISPGRA	Homo sapiens
pmid	sentence
16046550	We have identified four phosphorylation sites on AML1c that are necessary for transcriptional activity of AML1c in K562 and 293T cells (27).4 Mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. The presence of these mutations results in an increase in the amount of ubiquitinated AML1c in the matrix, and increases the half-life of this insoluble AML1c. One possible model to explain these observations is that phosphorylation might be necessary for the normal process of both proteasome degradation and transcriptional activation.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-268218	Ser249	DTRQIQPsPPWSYDQ	Homo sapiens	HEK-293T Cell
pmid	sentence
16046550	We have identified four phosphorylation sites on AML1c that are necessary for transcriptional activity of AML1c in K562 and 293T cells (27).4 Mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. The presence of these mutations results in an increase in the amount of ubiquitinated AML1c in the matrix, and increases the half-life of this insoluble AML1c. One possible model to explain these observations is that phosphorylation might be necessary for the normal process of both proteasome degradation and transcriptional activation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-268219	Ser266	QYLGSIAsPSVHPAT	Homo sapiens	HEK-293T Cell
pmid	sentence
16046550	We have identified four phosphorylation sites on AML1c that are necessary for transcriptional activity of AML1c in K562 and 293T cells (27).4 Mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. The presence of these mutations results in an increase in the amount of ubiquitinated AML1c in the matrix, and increases the half-life of this insoluble AML1c. One possible model to explain these observations is that phosphorylation might be necessary for the normal process of both proteasome degradation and transcriptional activation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-268221	Ser276	VHPATPIsPGRASGM	Homo sapiens	HEK-293T Cell
pmid	sentence
16046550	We have identified four phosphorylation sites on AML1c that are necessary for transcriptional activity of AML1c in K562 and 293T cells (27).4 Mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. The presence of these mutations results in an increase in the amount of ubiquitinated AML1c in the matrix, and increases the half-life of this insoluble AML1c. One possible model to explain these observations is that phosphorylation might be necessary for the normal process of both proteasome degradation and transcriptional activation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-268220	Thr273	SPSVHPAtPISPGRA	Homo sapiens	HEK-293T Cell
pmid	sentence
16046550	We have identified four phosphorylation sites on AML1c that are necessary for transcriptional activity of AML1c in K562 and 293T cells (27).4 Mutation of these four sites (serine 276, serine 293, serine 303, and threonine 300) to alanine abolishes transcriptional activation, whereas mutation of these sites to aspartic acid (which mimics phosphorylation) results in a hyperactive protein. The presence of these mutations results in an increase in the amount of ubiquitinated AML1c in the matrix, and increases the half-life of this insoluble AML1c. One possible model to explain these observations is that phosphorylation might be necessary for the normal process of both proteasome degradation and transcriptional activation.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-197543	Ser250	SSSGVPYsPAIPNKR	Homo sapiens
pmid	sentence
22595671	Erk1/2 phosphorylation enhances the binding of exo70 to other exocyst components and promotes the assembly of the exocyst complex in response to epidermal growth factor (egf) signaling.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249401	Ser255	HATSGALsPAKDCGS	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.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249402	Ser279	SSPTAPLsPMSPPGY	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.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249403	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-88658	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-262958	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-44339	Ser272	SNHGLAIsPGMKTRI	Homo sapiens
pmid	sentence
8846784	Using novel methodology we demonstrate that activation of mapkap kinase-2 requires the phosphorylation of any two of the three residues thr222, ser272 and thr334. gst-mapkap kinase-2 lacking the n-terminal domain was inactive, but activated fully when phosphorylated at thr222, ser272 and thr334 by p42 mapk or rk.

Identifier	Residue	Sequence	Organism
SIGNOR-44343	Thr222	TSHNSLTtPCYTPYY	Homo sapiens
pmid	sentence
8846784	Using novel methodology we demonstrate that activation of mapkap kinase-2 requires the phosphorylation of any two of the three residues thr222, ser272 and thr334. gst-mapkap kinase-2 lacking the n-terminal domain was inactive, but activated fully when phosphorylated at thr222, ser272 and thr334 by p42 mapk or rk.

Identifier	Residue	Sequence	Organism
SIGNOR-44347	Thr334	QSTKVPQtPLHTSRV	Homo sapiens
pmid	sentence
8846784	Using novel methodology we demonstrate that activation of mapkap kinase-2 requires the phosphorylation of any two of the three residues thr222, ser272 and thr334. gst-mapkap kinase-2 lacking the n-terminal domain was inactive, but activated fully when phosphorylated at thr222, ser272 and thr334 by p42 mapk or rk.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264439	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-264409	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-262841	Ser274	DPLPGPGsPSHSAPD	Rattus norvegicus	NRK Cell
pmid	sentence
15834132	Here we show that GRASP65 is phosphorylated on serine 277 in interphase cells, and this is strongly enhanced in response to the addition of serum or epidermal growth factor. This is directly mediated by ERK suggesting that GRASP65 has some role in growth factor signal transduction. These results argue against Ser-277 phosphorylation alone causing the dissolution of GRASP65 oligomers and cisternal unstacking, although it may make a significant contribution to these events.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-249452	Ser274	LAPNPSFsPTPGFTP	in vitro
pmid	sentence
11606045	Phosphorylation of murine CD120a by p42(mapk/erk2) has been shown to inhibit its ability to initiate apoptosis while preserving signaling events such as NF-kappaB activation.\|Additionally, we demonstrated that (i) the p42(mapk/erk2)-dependent phosphorylation of CD120a and DR3 occurred on Ser and Thr residues, (ii) p42(mapk/erk2) phosphorylated residues located in the membrane proximal regions but not the death domains of CD120a and DR3, (iii) Ser 253 is a preferred site of phosphorylation on CD120a

Identifier	Residue	Sequence	Organism
SIGNOR-249453	Thr280	FSPTPGFtPTLGFSP	in vitro
pmid	sentence
11606045	Phosphorylation of murine CD120a by p42(mapk/erk2) has been shown to inhibit its ability to initiate apoptosis while preserving signaling events such as NF-kappaB activation.\|Additionally, we demonstrated that (i) the p42(mapk/erk2)-dependent phosphorylation of CD120a and DR3 occurred on Ser and Thr residues, (ii) p42(mapk/erk2) phosphorylated residues located in the membrane proximal regions but not the death domains of CD120a and DR3, (iii) Ser 253 is a preferred site of phosphorylation on CD120a

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-126250	Ser280	TVHGLPTsPDRPGST	Homo sapiens
pmid	sentence
15210796	We show in this study that the nuclear localized form of ciita is a predominantly phosphorylated form of the protein, whereas cytoplasmic ciita is predominantly unphosphorylated. Novel phosphorylation sites were determined to be located within a region that contains serine residues 286, 288, and 293. Double mutations of these residues increased nuclear ciita, indicating that these sites are not required for nuclear import. 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.

Identifier	Residue	Sequence	Organism
SIGNOR-160609	Ser280	TVHGLPTsPDRPGST	Homo sapiens
pmid	sentence
18245089	We show in this study that the nuclear localized form of ciita is a predominantly phosphorylated form of the protein, whereas cytoplasmic ciita is predominantly unphosphorylated. Novel phosphorylation sites were determined to be located within a region that contains serine residues 286, 288, and 293. Double mutations of these residues increased nuclear ciita, indicating that these sites are not required for nuclear import. 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:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-164227	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-163659	Ser282	VGKQAPLsPGLPAMG	Homo sapiens	HEK-293 Cell
pmid	sentence
20110267	These results demonstrated a critical role of noxa1 phosphorylation on ser-282 and ser-172 in preventing nox1 hyperactivation through the decrease of noxa1 interaction to nox1 and rac1.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-126254	Ser288	PDRPGSTsPFAPSAT	Homo sapiens
pmid	sentence
15210796	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.

Identifier	Residue	Sequence	Organism
SIGNOR-160613	Ser288	PDRPGSTsPFAPSAT	Homo sapiens
pmid	sentence
18245089	Novel phosphorylation sites were determined to be located within a region that contains serine residues 286, 288, and 293. ... 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:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249440	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	Cell Line
SIGNOR-249441	Ser29	FDGSSCIsPTIVQQF	Mus musculus	NIH-3T3 Cell
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-249442	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249443	Ser301	SSSPNNLsPTGWSQP	Mus musculus	NIH-3T3 Cell
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	Cell Line
SIGNOR-249439	Ser43	FGYQRRAsDDGKLTD	Mus musculus	NIH-3T3 Cell
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	Cell Line
SIGNOR-249444	Ser642	NACTLTTsPRLPVF	Mus musculus	NIH-3T3 Cell
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:

6

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276223	Ser29	GPRYTNLsYIGEGAY	Homo sapiens	Hep-G2 Cell
pmid	sentence
19447520	SGK1 was found to physically interact with ERK1/2 as well as MEK1/2. Furthermore, SGK1 mediated the phosphorylation of ERK2 on Ser(29) in a serum-dependent manner. Replacement of Ser(29) to aspartic acid, which mimics the phosphorylation of Ser(29), enhanced the ERK2 activity as well as the MEK/ERK complexes formation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-184168	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-184172	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-126859	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-252957	Ser294	QLSKWPGsPTSRSSD	Homo sapiens
pmid	sentence
18204439	Here, we show that erk downregulates forkhead box o 3a (foxo3a) by directly interacting with and phosphorylating foxo3a at ser 294, ser 344 and ser 425, which consequently promotes cell proliferation and tumorigenesisMDM2 is required for ERk-mediated FOXO3a degradation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252958	Ser344	QDDDAPLsPMLYSSS	Homo sapiens	HEK-293 Cell
pmid	sentence
18204439	Here, we show that erk downregulates forkhead box o 3a (foxo3a) by directly interacting with and phosphorylating foxo3a at ser 294, ser 344 and ser 425, which consequently promotes cell proliferation and tumorigenesisMDM2 is required for ERk-mediated FOXO3a degradation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252959	Ser425	TKGSGLGsPTSSFNS	Homo sapiens	HEK-293 Cell
pmid	sentence
18204439	Here, we show that erk downregulates forkhead box o 3a (foxo3a) by directly interacting with and phosphorylating foxo3a at ser 294, ser 344 and ser 425, which consequently promotes cell proliferation and tumorigenesisMDM2 is required for ERk-mediated FOXO3a degradation.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-160407	Ser294	QLSKWPGsPTSRSSD	Homo sapiens
pmid	sentence
18204439	Here, we show that erk downregulates forkhead box o 3a (foxo3a) by directly interacting with and phosphorylating foxo3a at ser 294, ser 344 and ser 425, which consequently promotes cell proliferation and tumorigenesisMDM2 is required for ERk-mediated FOXO3a degradation.

Identifier	Residue	Sequence	Organism
SIGNOR-160411	Ser344	QDDDAPLsPMLYSSS	Homo sapiens
pmid	sentence
18204439	Here, we show that erk downregulates forkhead box o 3a (foxo3a) by directly interacting with and phosphorylating foxo3a at ser 294, ser 344 and ser 425, which consequently promotes cell proliferation and tumorigenesisMDM2 is required for ERk-mediated FOXO3a degradation.

Identifier	Residue	Sequence	Organism
SIGNOR-160415	Ser425	TKGSGLGsPTSSFNS	Homo sapiens
pmid	sentence
18204439	Here, we show that erk downregulates forkhead box o 3a (foxo3a) by directly interacting with and phosphorylating foxo3a at ser 294, ser 344 and ser 425, which consequently promotes cell proliferation and tumorigenesisMDM2 is required for ERk-mediated FOXO3a degradation.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-74712	Ser294	APMAPGRsPLATTVM	Homo sapiens	Breast Cancer Cell
pmid	sentence
10655479	Phosphorylation of human progesterone receptors at serine-294 by mitogen-activated protein kinase signals their degradation by the 26s proteasome

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-126863	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-141593	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-141601	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-262775	Ser30	SITSPPLsPALPKYK	Mus musculus
pmid	sentence
22028470	We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5'-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. This approach identified 80 proteins phosphorylated by ERK2, 13 of which are known ERK2 substrates. With this improved methodology, we detected 98 sites directly phosphorylated by ERK2 on 80 proteins from NIH 3T3-L1 fibroblasts. Thirteen of these proteins are known substrates and the rest represent previously unknown kinase/substrate interactions. (table1)

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-152418	Ser312	TESITATsPASMVGG	Homo sapiens	Uveal Melanoma Cell
pmid	sentence
17242212	Our data suggest that il-6 impairs the vasodilator effects of insulin that are mediated by the irs-1/pi3-kinase/akt/enos pathway through activation of jnk and erk1/2.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-134837	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	Cell Line
SIGNOR-235459	Ser324	RDLELPLsPSLLGGP	Mus musculus	NIH-3T3 Cell
pmid	sentence
7889942	We demonstrate that elk-1, a protein closely related to p62tcf in function, is a nuclear target of two members of the map kinase family, erk1 and erk2, erk1 phosphorylates five c-terminal sites in elk-1 (s324,t336, s383, s389 and s422) with varying degrees of efficiency.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-235455	Ser383	IHFWSTLsPIAPRSP	Mus musculus	NIH-3T3 Cell
pmid	sentence
7889942	We demonstrate that elk-1, a protein closely related to p62tcf in function, is a nuclear target of two members of the map kinase family, erk1 and erk2, erk1 phosphorylates five c-terminal sites in elk-1 (s324,t336, s383, s389 and s422) with varying degrees of efficiency.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-235471	Ser389	LSPIAPRsPAKLSFQ	Mus musculus	NIH-3T3 Cell
pmid	sentence
7889942	We demonstrate that elk-1, a protein closely related to p62tcf in function, is a nuclear target of two members of the map kinase family, erk1 and erk2, erki phosphorylates five c-terminal sites in elk-i (s324,t336, s383, s389 and s422) with varying degrees of efficiency.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-235463	Ser422	LSTPVVLsPGPQKP	Mus musculus	NIH-3T3 Cell
pmid	sentence
7889942	We demonstrate that elk-1, a protein closely related to p62tcf in function, is a nuclear target of two members of the map kinase family, erk1 and erk2, erki phosphorylates five c-terminal sites in elk-i (s324,t336, s383, s389 and s422) with varying degrees of efficiency.

Publications:

4

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-58481	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-58485	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	Cell Line
SIGNOR-262771	Ser333	YSVPSVLsPRRAATE	Mus musculus	NIH-3T3 Cell
pmid	sentence
22028470	We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5'-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. This approach identified 80 proteins phosphorylated by ERK2, 13 of which are known ERK2 substrates. With this improved methodology, we detected 98 sites directly phosphorylated by ERK2 on 80 proteins from NIH 3T3-L1 fibroblasts. Thirteen of these proteins are known substrates and the rest represent previously unknown kinase/substrate interactions. (table1)

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-144313	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	Cell Line
SIGNOR-147170	Ser345	QARPGPQsPGSPLEE	Homo sapiens	Neutrophil
pmid	sentence
16778989	Erk1/2 are the kinases involved in p47phox_ phosphorylation on ser345 in gm-csfprimed human neutrophils._ Phosphorylation of ser345 is required for the priming of nadph oxidase activity in neutrophil-like cells

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276743	Ser352	TRPTALTsPELSSWS	Homo sapiens	HCT-116 Cell
pmid	sentence
28945223	In addition, the phosphorylation of JMJD2B via p-ERK at Thr305, Ser352, Ser566 and Thr1065 contribute to JMJD2B stability. p-ERK stabilizes the JMJD2B protein level by protecting JMJD2B from ubiquitination and proteasome degradation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276742	Ser566	PTWKEPVsPMELTGP	Homo sapiens	HCT-116 Cell
pmid	sentence
28945223	In addition, the phosphorylation of JMJD2B via p-ERK at Thr305, Ser352, Ser566 and Thr1065 contribute to JMJD2B stability. p-ERK stabilizes the JMJD2B protein level by protecting JMJD2B from ubiquitination and proteasome degradation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276744	Thr1065	AKRPRVGtPLATEDS	Homo sapiens	HCT-116 Cell
pmid	sentence
28945223	In addition, the phosphorylation of JMJD2B via p-ERK at Thr305, Ser352, Ser566 and Thr1065 contribute to JMJD2B stability. p-ERK stabilizes the JMJD2B protein level by protecting JMJD2B from ubiquitination and proteasome degradation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276741	Thr305	IDYGKVAtQCTCRKD	Homo sapiens	HCT-116 Cell
pmid	sentence
28945223	In addition, the phosphorylation of JMJD2B via p-ERK at Thr305, Ser352, Ser566 and Thr1065 contribute to JMJD2B stability. p-ERK stabilizes the JMJD2B protein level by protecting JMJD2B from ubiquitination and proteasome degradation.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-73621	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-73625	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	Cell Line
SIGNOR-124240	Ser36	PSEGRQPsPSPSPTE	Homo sapiens	Leukemia Cell
pmid	sentence
15093545	We conclude that phosphorylation by map kinase cascades potentiates the antiproliferative functions of pml and helps mediate the proapoptotic effects of as(2)o(3).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-124244	Ser38	EGRQPSPsPSPTERA	Homo sapiens	Leukemia Cell
pmid	sentence
15093545	We conclude that phosphorylation by map kinase cascades potentiates the antiproliferative functions of pml and helps mediate the proapoptotic effects of as(2)o(3).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-124248	Ser40	RQPSPSPsPTERAPA	Homo sapiens	Leukemia Cell
pmid	sentence
15093545	We report here that as(2)o(3) treatment induces phosphorylation of the pml protein through a mitogen-activated protein (map) kinase pathway. Increased pml phosphorylation is associated with increased sumoylation of pml and increased pml-mediated apoptosis.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-124252	Ser527	PHLDGPPsPRSPVIG	Homo sapiens	Leukemia Cell
pmid	sentence
15093545	We conclude that phosphorylation by map kinase cascades potentiates the antiproliferative functions of pml and helps mediate the proapoptotic effects of as(2)o(3).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-124056	Ser530	DGPPSPRsPVIGSEV	Homo sapiens	Leukemia Cell
pmid	sentence
15093545	We conclude that phosphorylation by map kinase cascades potentiates the antiproliferative functions of pml and helps mediate the proapoptotic effects of as(2)o(3).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-124313	Thr28	PTMPPPEtPSEGRQP	Homo sapiens	Leukemia Cell
pmid	sentence
15093545	We conclude that phosphorylation by map kinase cascades potentiates the antiproliferative functions of pml and helps mediate the proapoptotic effects of as(2)o(3).

Publications:

6

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-116485	Ser360	TEMDPTYsPAALPQS	Homo sapiens
pmid	sentence
11940578	Together, our in vivo and in vitro studies indicate that the pkc/c-raf/mek/erk pathway plays a major role in the s6k1 activation in hypertrophic cardiac growth.

Identifier	Residue	Sequence	Organism
SIGNOR-59435	Ser360	TEMDPTYsPAALPQS	Homo sapiens
pmid	sentence
9687510	Together, our in vivo and in vitro studies indicate that the pkc/c-raf/mek/erk pathway plays a major role in the s6k1 activation in hypertrophic cardiac growth.

Identifier	Residue	Sequence	Organism
SIGNOR-131311	Ser360	TEMDPTYsPAALPQS	Homo sapiens
pmid	sentence
15568999	Together, our in vivo and in vitro studies indicate that the pkc/c-raf/mek/erk pathway plays a major role in the s6k1 activation in hypertrophic cardiac growth.

Identifier	Residue	Sequence	Organism
SIGNOR-116489	Thr581	PDNQPLKtPCFTLHY	Homo sapiens
pmid	sentence
11940578	Together, our in vivo and in vitro studies indicate that the pkc/c-raf/mek/erk pathway plays a major role in the s6k1 activation in hypertrophic cardiac growth.

Identifier	Residue	Sequence	Organism
SIGNOR-160787	Thr581	PDNQPLKtPCFTLHY	Homo sapiens
pmid	sentence
18267068	Together, our in vivo and in vitro studies indicate that the pkc/c-raf/mek/erk pathway plays a major role in the s6k1 activation in hypertrophic cardiac growth.

Publications:

5

Organism:

Homo Sapiens

Tissue:

Muscle

Identifier	Residue	Sequence
SIGNOR-262996	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-235671	Ser374	PSSDSLSsPTLLAL	Homo sapiens
pmid	sentence
12972619	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. ERK2 phosphorylated c-Fos TADs that included Thr- 325, Thr-331, or Ser-374 as unique phospho-acceptor sites, thus indicating that these residues can serve as in vitro targets for the enzymatic activity of ERK2.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-235877	Thr232	GGLPEVAtPESEEAF	Homo sapiens	1BR3.G Cell
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.

Identifier	Residue	Sequence
SIGNOR-263011	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-236010	Thr325	TELEPLCtPVVTCTP	Homo sapiens
pmid	sentence
12972619	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. ERK2 phosphorylated c-Fos TADs that included Thr- 325, Thr-331, or Ser-374 as unique phospho-acceptor sites, thus indicating that these residues can serve as in vitro targets for the enzymatic activity of ERK2.

Identifier	Residue	Sequence
SIGNOR-263007	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-236014	Thr331	CTPVVTCtPSCTAYT	Homo sapiens
pmid	sentence
12972619	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. ERK2 phosphorylated c-Fos TADs that included Thr- 325, Thr-331, or Ser-374 as unique phospho-acceptor sites, thus indicating that these residues can serve as in vitro targets for the enzymatic activity of ERK2.

Publications:

7

Organism:

, Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-263054	Ser362	PVHPKPLsPDSRASS	Homo sapiens	Prostate Cancer Cell Line
pmid	sentence
23188829	Mechanistic study revealed that EGF could activate the phosphorylation, ubiquitination, and degradation of EPLIN through an extracellular signal-regulated kinase 1/2 (ERK1/2)-dependent signaling cascade. Pharmacological inhibition of the ERK1/2 pathway effectively antagonized EGF-induced EPLIN degradation. Two serine residues, i.e. serine 362 and serine 604, were identified as putative ERK1/2 phosphorylation sites in human EPLIN, whose point mutation rendered resistance to EGF-induced protein turnover.

Identifier	Residue	Sequence	Organism
SIGNOR-263055	Ser604	FQSTSVKsPKTVSPP	Homo sapiens
pmid	sentence
23188829	Mechanistic study revealed that EGF could activate the phosphorylation, ubiquitination, and degradation of EPLIN through an extracellular signal-regulated kinase 1/2 (ERK1/2)-dependent signaling cascade. Pharmacological inhibition of the ERK1/2 pathway effectively antagonized EGF-induced EPLIN degradation. Two serine residues, i.e. serine 362 and serine 604, were identified as putative ERK1/2 phosphorylation sites in human EPLIN, whose point mutation rendered resistance to EGF-induced protein turnover.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-161851	Ser362	ISSVPTPsPLGPLAG	Homo sapiens	Glioblastoma Cell
pmid	sentence
19941816	Erk2, which is activated by egfr signaling, directly binds to ck2alpha via the erk2 docking groove and phosphorylates ck2alpha primarily at t360/s362, subsequently enhancing ck2alpha activity

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-161855	Thr360	SGISSVPtPSPLGPL	Homo sapiens	Glioblastoma Cell
pmid	sentence
19941816	Erk2, which is activated by egfr signaling, directly binds to ck2alpha via the erk2 docking groove and phosphorylates ck2alpha primarily at t360/s362, subsequently enhancing ck2alpha activity

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-272240	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	Organism	Cell Line
SIGNOR-146220	Ser372	VAATPPPsTASAPAA	Homo sapiens	Neuron
pmid	sentence
16627622	Parp1 phosphorylation by erk1/2 is required for maximal parp-1 activation after dna damage. S372a and t373a mutations impaired parp-1 activation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-146224	Thr373	AATPPPStASAPAAV	Homo sapiens	Neuron
pmid	sentence
16627622	Parp1 phosphorylation by erk1/2 is required for maximal parp-1 activation after dna damage. S372a and t373a mutations impaired parp-1 activation.

Publications:

2

Organism:

Homo Sapiens

Tissue:

Brain

Identifier	Residue	Sequence
SIGNOR-249445	Ser376	EKLFQGYsFVAPSIL
pmid	sentence
15568999	In the present study, we show that, in addition to being phosphorylated on Thr-581 and Ser-360 by ERK1/2 or p38, MSK1 can autophosphorylate on at least six sites: Ser-212, Ser-376, Ser-381, Ser-750, Ser-752 and Ser-758. Of these sites, the N-terminal T-loop residue Ser-212 and the 'hydrophobic motif' Ser-376 are phosphorylated by the C-terminal kinase domain of MSK1, and their phosphorylation is essential for the catalytic activity of the N-terminal kinase domain of MSK1

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-166686	Ser38	SVPEFPLsPPKKKDL	Homo sapiens
pmid	sentence
20630875	Involved in the regulation of the microtubule (mt) filament system by destabilizing microtubules. Prevents assembly and promotes disassembly of microtubules. The kinases involved in phosphorylating stmn ser-16 and ser-63 include camp-dependent protein kinase (pka) and pak1, whereas stmn ser-25 and ser-38 have been shown to be targets for proline-directed serine/threonine kinases such as cyclin-dependent kinases, erk1/2, and members of the p38 mapk subfamily.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249395	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
SIGNOR-249396	Ser454	YVPMNPNsPPRQHSS	Cricetulus griseus
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-249397	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-249398	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-249399	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-249400	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
SIGNOR-153379	Ser387	PATVEPAsPTPAHSL	Homo sapiens
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
SIGNOR-153383	Thr614	AFRLEPLtPRGVLTV	Homo sapiens
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-203473	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
SIGNOR-279537	Ser394	RSKSSPTsPTSCTPP	Homo sapiens
pmid	sentence
27107697	ERK2 phosphorylates RasGRP2 at Ser394 located in the linker region implicated in its autoinhibition.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-265760	Ser4	sPQKSPSV	Homo sapiens
pmid	sentence
22955285	Actopaxin (alpha-parvin) is a paxillin, integrin-linked kinase, and F-actin binding focal adhesion protein with several serine phosphorylation sites in the amino terminus that contribute to the regulation of cell spreading and migration.\|Actopaxin phosphorylation of Ser4/8 enhances cell migration whereas a nonphosphorylatable (Quint) mutant suppresses migration in U2OS osteosarcoma cells (7).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-265759	Ser8	MATSPQKsPSVPKSP	Homo sapiens	U2-OS Cell
pmid	sentence
22955285	Actopaxin (alpha-parvin) is a paxillin, integrin-linked kinase, and F-actin binding focal adhesion protein with several serine phosphorylation sites in the amino terminus that contribute to the regulation of cell spreading and migration.\|Actopaxin phosphorylation of Ser4/8 enhances cell migration whereas a nonphosphorylatable (Quint) mutant suppresses migration in U2OS osteosarcoma cells (7).

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-169674	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	Cell Line
SIGNOR-165200	Ser405	KTQTPPVsPAPQPTE	Homo sapiens	Neuron
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-169678	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.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-165204	Ser418	TEERLPSsPVYEDAA	Homo sapiens	Neuron
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.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-67630	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-183480	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-129585	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-262978	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	Cell Line
SIGNOR-262981	Ser497	GSLCSVFsPSFVQWE	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	Cell Line
SIGNOR-262984	Thr345	GADSDVEtPSNFGKY	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.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249405	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-276937	Ser421	YEPAARIsPLGALQH	in vitro
pmid	sentence
26346493	S421 resides within a Ser-Pro phosphoacceptor motif that is typical for ERK1/2 and recombinant ERK2 phosphorylated DYRK1B at S421 in vitro.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-140890	Ser425	NREKVAAsPKSPTAA	Homo sapiens
pmid	sentence
16198290	Upon mitotic entry, centrosome dissociation of cep55 is triggered by erk2/cdk1-dependent phosphorylation at s425 and s428. S425/428 phosphorylation is required for interaction with plk1, enabling phosphorylation of cep55 at s436. enabling it to relocate to the midbody to function in mitotic exit and cytokinesis.

Identifier	Residue	Sequence	Organism
SIGNOR-140894	Ser428	KVAASPKsPTAALNE	Homo sapiens
pmid	sentence
16198290	Upon mitotic entry, centrosome dissociation of cep55 is triggered by erk2/cdk1-dependent phosphorylation at s425 and s428. S425/428 phosphorylation is required for interaction with plk1, enabling phosphorylation of cep55 at s436. enabling it to relocate to the midbody to function in mitotic exit and cytokinesis.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-209876	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-265950	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-265946	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-265948	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-123041	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-123045	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-249411	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).

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-169150	Ser434	SFEPKIRsPRRFIGS	Homo sapiens
pmid	sentence
21035469	Erk phosphorylates multiple cytoplasmatic and cytoskeletal proteins, including mapk-activated protein kinases and the ribosomal p70-s6 kinase

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-182804	Ser434	SFEPKIRsPRRFIGS	Homo sapiens	Breast Cancer Cell
pmid	sentence
19085255	Erk phosphorylates multiple cytoplasmatic and cytoskeletal proteins, including mapk-activated protein kinases and the ribosomal p70-s6 kinase.

Identifier	Residue	Sequence	Organism
SIGNOR-121984	Ser434	SFEPKIRsPRRFIGS	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	Sequence	Organism
SIGNOR-28796	Ser434	SFEPKIRsPRRFIGS	Homo sapiens
pmid	sentence
7545671	Erk phosphorylates multiple cytoplasmatic and cytoskeletal proteins, including mapk-activated protein kinases and the ribosomal p70-s6 kinase

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-182808	Ser447	GSPRTPVsPVKFSPG	Homo sapiens	Breast Cancer Cell
pmid	sentence
19085255	Erk phosphorylates multiple cytoplasmatic and cytoskeletal proteins, including mapk-activated protein kinases and the ribosomal p70-s6 kinase.

Identifier	Residue	Sequence	Organism
SIGNOR-121988	Ser447	GSPRTPVsPVKFSPG	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	Sequence	Organism
SIGNOR-169154	Ser447	GSPRTPVsPVKFSPG	Homo sapiens
pmid	sentence
21035469	Erk phosphorylates multiple cytoplasmatic and cytoskeletal proteins, including mapk-activated protein kinases and the ribosomal p70-s6 kinase

Identifier	Residue	Sequence	Organism
SIGNOR-28800	Ser447	GSPRTPVsPVKFSPG	Homo sapiens
pmid	sentence
7545671	Erk phosphorylates multiple cytoplasmatic and cytoskeletal proteins, including mapk-activated protein kinases and the ribosomal p70-s6 kinase

Identifier	Residue	Sequence	Organism
SIGNOR-111511	Thr444	RFIGSPRtPVSPVKF	Homo sapiens
pmid	sentence
11705993	The principal target of rapamycin-induced p70s6k inactivation is a novel phosphorylation site within a conserved hydrophobic domain.

Identifier	Residue	Sequence	Organism
SIGNOR-134658	Thr444	RFIGSPRtPVSPVKF	Homo sapiens
pmid	sentence
15774499	The principal target of rapamycin-induced p70s6k inactivation is a novel phosphorylation site within a conserved hydrophobic domain.

Publications:

10

Organism:

Homo Sapiens

Tissue:

Muscle, Skeletal Muscle

Pathways:

Nucleotide Biosynthesis

Identifier	Residue	Sequence	Organism
SIGNOR-262748	Ser434	LTLASERsSPQRKSQ	in vitro
pmid	sentence
12175859	Here, we have identified phosphorylation sites on the human ρ1 GABA receptor for six protein kinases widely expressed in the brain: protein kinase C (PKC); cAMP‐dependent protein kinase (PKA); calmodulin‐dependent kinase (CaMKII); casein kinase (CKII); mitogen‐activated protein kinase (MAPK); and cGMP‐dependent protein kinase (PKG). From these data we conclude that T373 is the predominant site of phosphorylation, with a low level of phosphorylation at S413 and/or S414.An extensive functional analysis comparing wild type 1 receptors and receptors with select or multiple phosphorylation sites removed as well as pharmacological manipulation of five kinase pathways failed to reveal any functional effects of phosphorylation

Identifier	Residue	Sequence	Organism
SIGNOR-262747	Ser435	TLASERSsPQRKSQR	in vitro
pmid	sentence
12175859	Here, we have identified phosphorylation sites on the human ρ1 GABA receptor for six protein kinases widely expressed in the brain: protein kinase C (PKC); cAMP‐dependent protein kinase (PKA); calmodulin‐dependent kinase (CaMKII); casein kinase (CKII); mitogen‐activated protein kinase (MAPK); and cGMP‐dependent protein kinase (PKG). From these data we conclude that T373 is the predominant site of phosphorylation, with a low level of phosphorylation at S413 and/or S414. An extensive functional analysis comparing wild type 1 receptors and receptors with select or multiple phosphorylation sites removed as well as pharmacological manipulation of five kinase pathways failed to reveal any functional effects of phosphorylation

Identifier	Residue	Sequence	Organism
SIGNOR-262749	Thr394	SGLPPPRtAMLDGNY	in vitro
pmid	sentence
12175859	Here, we have identified phosphorylation sites on the human ρ1 GABA receptor for six protein kinases widely expressed in the brain: protein kinase C (PKC); cAMP‐dependent protein kinase (PKA); calmodulin‐dependent kinase (CaMKII); casein kinase (CKII); mitogen‐activated protein kinase (MAPK); and cGMP‐dependent protein kinase (PKG). From these data we conclude that T373 is the predominant site of phosphorylation, with a low level of phosphorylation at S413 and/or S414.An extensive functional analysis comparing wild type 1 receptors and receptors with select or multiple phosphorylation sites removed as well as pharmacological manipulation of five kinase pathways failed to reveal any functional effects of phosphorylation

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-249389	Ser446	TNKLCQFsPVQELSE	Chlorocebus aethiops
pmid	sentence
15689616	Phosphorylation of Ser-446 determines stability of MKP-7.\|We also determined that MKP-7 phosphorylated at Ser-446 has a longer half-life than unphosphorylated form of the wild type protein, as does a phospho-mimic mutant of MKP-7. These results indicate that activation of the ERK pathway strongly blocks JNK activation through stabilization of MKP-7 mediated by phosphorylation.

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-195153	Ser454	TGSTPPVsPTPSERS	Homo sapiens
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-179959	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-263052	Ser46	SASGSAFsPYPGSAA	in vitro
pmid	sentence
15133517	We tested the transcriptional properties of Irx2 by dividing it into amino- and carboxy terminal parts and found that Mek1-mediated phosphorylation activates and derepresses the amino and carboxyl parts, respectively. When Ser46 and Ser65 were mutated to alanine (S46A and S65A), phosphorylation was reduced, whereas substitution of Ser83 and Ser103 (S83A and S103A) did not affect phosphorylation.

Identifier	Residue	Sequence	Organism
SIGNOR-263053	Ser64	QAATGFGsPLQYSAD	in vitro
pmid	sentence
15133517	We tested the transcriptional properties of Irx2 by dividing it into amino- and carboxy terminal parts and found that Mek1-mediated phosphorylation activates and derepresses the amino and carboxyl parts, respectively. When Ser46 and Ser65 were mutated to alanine (S46A and S65A), phosphorylation was reduced, whereas substitution of Ser83 and Ser103 (S83A and S103A) did not affect phosphorylation.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-172638	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	Cell Line
SIGNOR-277585	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-275971	Ser487	YQSMIPQsPSPPLDE	in vitro
pmid	sentence
11030732	The short-form PDE4B2 isoenzyme was activated by Erk2 phosphorylation. These functional changes in PDE activity were mimicked by mutation of the target serine for Erk2 phosphorylation to the negatively charged amino acid, aspartic acid.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-123079	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	Cell Line
SIGNOR-55706	Ser505	LNTSYPLsPLSDFAT	Homo sapiens	HeLa Cell
pmid	sentence
9468497	The inhibitor of the 38-kda stress-activated protein kinase (p38(mapk)), sb 203580, reduced phosphorylation of both ser-505 and ser-727 by 50 and 60%, respectively, in thrombin-stimulated platelets.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-178718	Ser516	VSRVPYPsPTCVKSE	Homo sapiens	Prostate Gland Cancer Cell
pmid	sentence
18511414	Map kinase-dependent phosphorylation at ar ser-515 was supported by the decrease in intensity of the slower migrating 23-kda band after treatment with both egf and increasing concentrations of the map kinase inhibitor, u0126

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262773	Ser516	VSPTTPTsPTEGEAS	Mus musculus	NIH-3T3 Cell
pmid	sentence
22028470	We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5'-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. This approach identified 80 proteins phosphorylated by ERK2, 13 of which are known ERK2 substrates. With this improved methodology, we detected 98 sites directly phosphorylated by ERK2 on 80 proteins from NIH 3T3-L1 fibroblasts. Thirteen of these proteins are known substrates and the rest represent previously unknown kinase/substrate interactions. (table1)

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249423	Ser518	SPEKEAKsPVKEEAK	Rattus norvegicus	Neuron
pmid	sentence
9592082	The fraction containing Erk2, as well as bacterially expressed Erk1 and Erk2, phosphorylated all types of KSP motifs in peptides (KSPXK, KSPXXK, KSPXXXK, and KSPXXXXK) derived from NF-M and NF-H. They also phosphorylated an expressed 24 KSPXXXK repeat NF-H polypeptide, an expressed NF-H as well as dephosphorylated native rat NF-H, and NF-M proteins with accompanying decreases in their respective electrophoretic mobilities. \|Our data on primary hippocampal cells also showed an inhibition of neurite outgrowth by the drug that was accompanied by inhibition of MAP, NF-H, and NF-M phosphorylation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249424	Ser526	PVKEEAKsPAEAKSP	Rattus norvegicus	Neuron
pmid	sentence
9592082	The fraction containing Erk2, as well as bacterially expressed Erk1 and Erk2, phosphorylated all types of KSP motifs in peptides (KSPXK, KSPXXK, KSPXXXK, and KSPXXXXK) derived from NF-M and NF-H. They also phosphorylated an expressed 24 KSPXXXK repeat NF-H polypeptide, an expressed NF-H as well as dephosphorylated native rat NF-H, and NF-M proteins with accompanying decreases in their respective electrophoretic mobilities. \|Our data on primary hippocampal cells also showed an inhibition of neurite outgrowth by the drug that was accompanied by inhibition of MAP, NF-H, and NF-M phosphorylation.

Identifier	Residue	Sequence	Organism
SIGNOR-249425	Ser532	KSPAEAKsPEKEEAK	Rattus norvegicus
pmid	sentence
9592082	The fraction containing Erk2, as well as bacterially expressed Erk1 and Erk2, phosphorylated all types of KSP motifs in peptides (KSPXK, KSPXXK, KSPXXXK, and KSPXXXXK) derived from NF-M and NF-H. They also phosphorylated an expressed 24 KSPXXXK repeat NF-H polypeptide, an expressed NF-H as well as dephosphorylated native rat NF-H, and NF-M proteins with accompanying decreases in their respective electrophoretic mobilities. \|Our data on primary hippocampal cells also showed an inhibition of neurite outgrowth by the drug that was accompanied by inhibition of MAP, NF-H, and NF-M phosphorylation.

Publications:

3

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249416	Ser519	SGYSSPGsPGTPGSR	Homo sapiens	Alzheimer Disease Specific Cell Type
pmid	sentence
10737616	Using nanoelectrospray mass spectrometry, we have undertaken an extensive comparison of phosphorylation in vitro by several candidate tau kinases, namely, JNK, p38, ERK2, and glycogen synthase kinase 3beta (GSK3beta). Between 10 and 15 sites were identified for each kinase. The three MAP kinases phosphorylated Ser202 and Thr205 but not detectably Ser199, whereas conversely GSK3beta phosphorylated Ser199 but not detectably Ser202 or Thr205. Phosphorylated Ser404 was found with all of these kinases except JNK. The MAP kinases may not be strictly proline specific: p38 phosphorylated the nonproline sites Ser185, Thr245, Ser305, and Ser356, whereas ERK2 was the most strict. All of the sites detected except Thr245 and Ser305 are known or suspected phosphorylation sites in paired helical filament-tau extracted from Alzheimer brains. Thus, the three MAP kinases and GSK3beta are importantly all strong candidates as tau kinases that may be involved in the pathogenic hyperphosphorylation of tau in Alzheimer's disease.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249418	Ser721	PVVSGDTsPRHLSNV	Homo sapiens	Alzheimer Disease Specific Cell Type
pmid	sentence
10737616	Using nanoelectrospray mass spectrometry, we have undertaken an extensive comparison of phosphorylation in vitro by several candidate tau kinases, namely, JNK, p38, ERK2, and glycogen synthase kinase 3beta (GSK3beta). Between 10 and 15 sites were identified for each kinase. The three MAP kinases phosphorylated Ser202 and Thr205 but not detectably Ser199, whereas conversely GSK3beta phosphorylated Ser199 but not detectably Ser202 or Thr205. Phosphorylated Ser404 was found with all of these kinases except JNK. The MAP kinases may not be strictly proline specific: p38 phosphorylated the nonproline sites Ser185, Thr245, Ser305, and Ser356, whereas ERK2 was the most strict. All of the sites detected except Thr245 and Ser305 are known or suspected phosphorylation sites in paired helical filament-tau extracted from Alzheimer brains. Thus, the three MAP kinases and GSK3beta are importantly all strong candidates as tau kinases that may be involved in the pathogenic hyperphosphorylation of tau in Alzheimer's disease.

Identifier	Residue	Sequence	Organism
SIGNOR-249417	Thr522	SSPGSPGtPGSRSRT	Homo sapiens
pmid	sentence
10737616	Using nanoelectrospray mass spectrometry, we have undertaken an extensive comparison of phosphorylation in vitro by several candidate tau kinases, namely, JNK, p38, ERK2, and glycogen synthase kinase 3beta (GSK3beta). Between 10 and 15 sites were identified for each kinase. The three MAP kinases phosphorylated Ser202 and Thr205 but not detectably Ser199, whereas conversely GSK3beta phosphorylated Ser199 but not detectably Ser202 or Thr205. Phosphorylated Ser404 was found with all of these kinases except JNK. The MAP kinases may not be strictly proline specific: p38 phosphorylated the nonproline sites Ser185, Thr245, Ser305, and Ser356, whereas ERK2 was the most strict. All of the sites detected except Thr245 and Ser305 are known or suspected phosphorylation sites in paired helical filament-tau extracted from Alzheimer brains. Thus, the three MAP kinases and GSK3beta are importantly all strong candidates as tau kinases that may be involved in the pathogenic hyperphosphorylation of tau in Alzheimer's disease.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236331	Ser523	GVSDVPTsPTLQRPT	Chlorocebus aethiops	COS Cell
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:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-188123	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-188127	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
SIGNOR-125221	Ser530	DGPQLPTsPRLTAAA	Homo sapiens
pmid	sentence
15184391	Vinexin was directly phosphorylated by erk2 upon stimulation with egf at the serine 189 of vinexin _.

Identifier	Residue	Organism
SIGNOR-125224		Homo sapiens
pmid	sentence
15184391	Vinexin was directly phosphorylated by erk2 upon stimulation with egf at the serine 189 of vinexin _.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249420	Ser532	KIKQEVEsPTDKSGN	in vitro
pmid	sentence
8960373	Functional analysis of phosphorylation at serine 532 of human c-Myb by MAP kinase\| 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:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249454	Ser540	KVMARSLsPPPELEE	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.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-171847	Ser544	RSVTMRKsQRSSKGS	Homo sapiens
pmid	sentence
21297032	These results suggest that the mek/erk1/2 pathway is necessary but not sufficient to regulate the pma-dependent activation of nox5.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-203286	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	Cell Line
SIGNOR-192788	Ser575	LVEKLPDsPALAKKA	Homo sapiens	Myoblast
pmid	sentence
22298426	The netrin-2-mediated nfatc3 activation was coincident with robust interactions between cdo and stim1 in myoblasts and the erk-mediated stim1 phosphorylation at serine 575

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-77563	Ser579	YQSTIPQsPSPAPDD	Homo sapiens
pmid	sentence
10828059	The pde4d2 isoform is inhibited by erk2 phosphorylation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-96410	Ser58	SRGGARAsPATQPPP	Homo sapiens
pmid	sentence
12478298	In support of this assumption, purified gst_sam68 protein was phosphorylated by recombinant erk2we found that sam68 mutated in ser 58, thr 71 and thr 84 showed the same extent of impairment in induced exon inclusion as did sam68 mutated in all s/tp sites

Identifier	Residue	Sequence	Organism
SIGNOR-96414	Thr72	PLLPPSAtGPDATVG	Homo sapiens
pmid	sentence
12478298	In support of this assumption, purified gst_sam68 protein was phosphorylated by recombinant erk2we found that sam68 mutated in ser 58, thr 71 and thr 84 showed the same extent of impairment in induced exon inclusion as did sam68 mutated in all s/tp sites

Identifier	Residue	Sequence	Organism
SIGNOR-96418	Thr84	TVGGPAPtPLLPPSA	Homo sapiens
pmid	sentence
12478298	In support of this assumption, purified gst_sam68 protein was phosphorylated by recombinant erk2we found that sam68 mutated in ser 58, thr 71 and thr 84 showed the same extent of impairment in induced exon inclusion as did sam68 mutated in all s/tp sites

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248075	Ser59	GGQESQPsPLALLAA	Homo sapiens	Fibroblast
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
SIGNOR-116158	Ser59	GGQESQPsPLALLAA	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. Mutation of these sites to alanines decreases by half the mapk-dependent transcriptional activity of sp1. Phosphorylated extracellular signal-regulated protein kinases 1 and 2 phosphorylate sp1 on serine 59 and regulate cellular senescence via transcription of p21sdi1/cip1/waf1.

Identifier	Residue	Sequence	Organism
SIGNOR-116162	Thr453	SGPIIIRtPTVGPNG	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. Mutation of these sites to alanines decreases by half the mapk-dependent transcriptional activity of sp1. Phosphorylated extracellular signal-regulated protein kinases 1 and 2 phosphorylate sp1 on serine 59 and regulate cellular senescence via transcription of p21sdi1/cip1/waf1.

Identifier	Residue	Sequence	Organism
SIGNOR-116166	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. Mutation of these sites to alanines decreases by half the mapk-dependent transcriptional activity of sp1. Phosphorylated extracellular signal-regulated protein kinases 1 and 2 phosphorylate sp1 on serine 59 and regulate cellular senescence via transcription of p21sdi1/cip1/waf1.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249412	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	Cell Line
SIGNOR-262934	Ser616	EGDDRPEsPEYSGGN	Rattus norvegicus	Hippocampus
pmid	sentence
11080179	We determined that the Kv4.2 C-terminal cytoplasmic domain is an effective ERK2 substrate, and that it is phosphorylated at three sites: Thr(602), Thr(607), and Ser(616). Phosphorylation of the Kv4.2 channel by ERK during LTP induction may lead to increased excitability and membrane depolarization of neurons, which would increase the magnitude of the calcium influx and the probability of triggering LTP.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262935	Thr602	TAIISIPtPPVTTPE	Rattus norvegicus	Hippocampus
pmid	sentence
11080179	We determined that the Kv4.2 C-terminal cytoplasmic domain is an effective ERK2 substrate, and that it is phosphorylated at three sites: Thr(602), Thr(607), and Ser(616). Phosphorylation of the Kv4.2 channel by ERK during LTP induction may lead to increased excitability and membrane depolarization of neurons, which would increase the magnitude of the calcium influx and the probability of triggering LTP.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262936	Thr607	IPTPPVTtPEGDDRP	Rattus norvegicus	Hippocampus
pmid	sentence
11080179	We determined that the Kv4.2 C-terminal cytoplasmic domain is an effective ERK2 substrate, and that it is phosphorylated at three sites: Thr(602), Thr(607), and Ser(616). Phosphorylation of the Kv4.2 channel by ERK during LTP induction may lead to increased excitability and membrane depolarization of neurons, which would increase the magnitude of the calcium influx and the probability of triggering LTP.

Publications:

3

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-123173	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-249407	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
SIGNOR-34674	Ser62	SYTPTPRsPRFIGRR	Homo sapiens
pmid	sentence
7901013	Mitogen-activated protein-kinase (map) kinase-activated protein kinases 1 and 2 (mapkap kinase-1, mapkap kinase-2), were found to phosphorylate bacterially expressed human tyrosine hydroxylase in vitro at comparable rates to other proteins thought to be physiological substrates of these protein kinases.The effect on activity of phosphorylating both ser31 and ser40 was not additive. The possible roles of mapkap kinase-1, mapkap kinase-2 and map kinase in the regulation of tyrosine hydroxylase in vivo are discussed.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-235700	Ser62	LLPTPPLsPSRRSGL	Chlorocebus aethiops	COS Cell
pmid	sentence
8386367	Transactivation of gene expression by myc is inhibited by mutation at the phosphorylation sites thr-58 and ser-62.

Publications:

1

Organism:

Chlorocebus Aethiops

Pathways:

Nucleotide Biosynthesis

Identifier	Residue	Sequence	Organism
SIGNOR-128727	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	Cell Line
SIGNOR-178723	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-178727	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-83187	Ser641	YQSKIPRsPSDLTNP	Homo sapiens
pmid	sentence
11030732	The short-form pde4b2 isoenzyme was activated by erk2 phosphorylation. sub-family selective actions in the ability of erk2 map kinase to phosphorylate and regulate the activity of pde4 cyclic amp-specific phosphodiesterases

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249390	Ser65	FLMECRNsPVTKTPP	Homo sapiens	HEK-293 Cell
pmid	sentence
11691836	The 4E-BPs inhibit translation in a reversible manner. Hypophosphorylated 4E-BPs interact avidly with eIF4E, whereas 4E-BP hyperphosphorylation, elicited by stimulation of cells with hormones, cytokines, or growth factors, results in an abrogation of eIF4E-binding activity.\|These results are at variance with reports that have characterized the 4E-BP1/eIF4E interaction utilizing recombinant 4E-BP1 proteins phosphorylated in vitro with ERK, and harboring alanine substitutions at Thr 37, Thr 46, Thr 70, and Ser 83 \|phosphorylation of either Thr 46 or Ser 65 was reported to result in a decrease in eIF4E binding

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249391	Ser83	PTIPGVTsPSSDEPP	Homo sapiens	HEK-293 Cell
pmid	sentence
11691836	The 4E-BPs inhibit translation in a reversible manner. Hypophosphorylated 4E-BPs interact avidly with eIF4E, whereas 4E-BP hyperphosphorylation, elicited by stimulation of cells with hormones, cytokines, or growth factors, results in an abrogation of eIF4E-binding activity.\|These results are at variance with reports that have characterized the 4E-BP1/eIF4E interaction utilizing recombinant 4E-BP1 proteins phosphorylated in vitro with ERK, and harboring alanine substitutions at Thr 37, Thr 46, Thr 70, and Ser 83 \|phosphorylation of either Thr 46 or Ser 65 was reported to result in a decrease in eIF4E binding

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249392	Thr37	PPGDYSTtPGGTLFS	Homo sapiens	HEK-293 Cell
pmid	sentence
11691836	The 4E-BPs inhibit translation in a reversible manner. Hypophosphorylated 4E-BPs interact avidly with eIF4E, whereas 4E-BP hyperphosphorylation, elicited by stimulation of cells with hormones, cytokines, or growth factors, results in an abrogation of eIF4E-binding activity.\|These results are at variance with reports that have characterized the 4E-BP1/eIF4E interaction utilizing recombinant 4E-BP1 proteins phosphorylated in vitro with ERK, and harboring alanine substitutions at Thr 37, Thr 46, Thr 70, and Ser 83 \|phosphorylation of either Thr 46 or Ser 65 was reported to result in a decrease in eIF4E binding

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249393	Thr46	GGTLFSTtPGGTRII	Homo sapiens	HEK-293 Cell
pmid	sentence
11691836	The 4E-BPs inhibit translation in a reversible manner. Hypophosphorylated 4E-BPs interact avidly with eIF4E, whereas 4E-BP hyperphosphorylation, elicited by stimulation of cells with hormones, cytokines, or growth factors, results in an abrogation of eIF4E-binding activity.\|These results are at variance with reports that have characterized the 4E-BP1/eIF4E interaction utilizing recombinant 4E-BP1 proteins phosphorylated in vitro with ERK, and harboring alanine substitutions at Thr 37, Thr 46, Thr 70, and Ser 83 \|phosphorylation of either Thr 46 or Ser 65 was reported to result in a decrease in eIF4E binding

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249394	Thr70	RNSPVTKtPPRDLPT	Homo sapiens	HEK-293 Cell
pmid	sentence
11691836	The 4E-BPs inhibit translation in a reversible manner. Hypophosphorylated 4E-BPs interact avidly with eIF4E, whereas 4E-BP hyperphosphorylation, elicited by stimulation of cells with hormones, cytokines, or growth factors, results in an abrogation of eIF4E-binding activity.\|These results are at variance with reports that have characterized the 4E-BP1/eIF4E interaction utilizing recombinant 4E-BP1 proteins phosphorylated in vitro with ERK, and harboring alanine substitutions at Thr 37, Thr 46, Thr 70, and Ser 83 \|phosphorylation of either Thr 46 or Ser 65 was reported to result in a decrease in eIF4E binding

Publications:

5

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-275970	Ser659	YQSMIPQsPSPPLDE	in vitro
pmid	sentence
11030732	The short-form PDE4B2 isoenzyme was activated by Erk2 phosphorylation. These functional changes in PDE activity were mimicked by mutation of the target serine for Erk2 phosphorylation to the negatively charged amino acid, aspartic acid.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-135696	Ser664	KKTSGPLsPPTGPPG	Homo sapiens
pmid	sentence
15851026	Here, we show that erk may play a critical role in tsc progression through posttranslational inactivation of tsc2. s664 is the primary erk phosphorylation site on tsc2 in vitro and in vivo

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-74296	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-74300	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
SIGNOR-133272	Ser676	SNGRRKRsPTQSFRF	Homo sapiens
pmid	sentence
15657420	We demonstrate that p90 ribosomal s6 kinase (rsk) is recruited to the nfat-dna transcription complex upon activation.Bound Rsk phosphorylates ser(676) and potentiates nfatc4 dna binding. Ser(676) is also targeted by the erk map kinase.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-264895	Ser68	PSDLSPEsPMLSSPP	in vitro
pmid	sentence
22577147	Altogether, these results indicate that CDK5 phosphorylates similarly serines 68 and 73, whereas ERK2 targets mostly serine 68 and GSK-3beta mostly serine 60.\|This observation may support the hypothesis of a specific localization of stathmin 3 depending on its phosphorylation by GSK-3beta

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-173401	Ser68	GGGDEPGsPAQGKRG	Homo sapiens	HEK-293 Cell, Breast Cancer Cell
pmid	sentence
21502402	We identified the serine 68 (s68) as a major phosphorylation site of twist1 by mass spectrometry and with specific antibodies. This s68 is phosphorylated by p38, jnk and erk1/2 in vitro, and its phosphorylation levels positively correlate with twist1 protein levels in hek293 and breast cancer cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-262944	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-129874	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

Identifier	Residue	Organism
SIGNOR-141584		Homo sapiens
pmid	sentence
16282323	Erk phosphorylation serves as a signal for bim ubiquitination and proteasomal degradation

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-169514	Ser696	EKNYALPsPATTEGG	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.

Identifier	Residue	Sequence	Organism
SIGNOR-169518	Ser8	MESEMLQsPLLGLGE	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.

Identifier	Residue	Sequence	Organism
SIGNOR-169522	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	Cell Line
SIGNOR-74919	Ser70	RDPVARTsPLQTPAA	Homo sapiens	HeLa Cell
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	Cell Line
SIGNOR-219217	Ser70	RDPVARTsPLQTPAA	Chlorocebus aethiops	COS Cell
pmid	sentence
10677502	Erk1 and erk2 directly phosphorylate bcl2 exclusively at ser-70.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-74931	Ser87	AAAGPALsPVPPVVH	Homo sapiens	HeLa Cell
pmid	sentence
10669763	Phosphorylation of the map kinase sites in bcl-2, thr56, thr74, and ser87, is sufficient to inhibit tnf--induced degradation.

Identifier	Residue	Sequence	Organism
SIGNOR-74923	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	Cell Line
SIGNOR-74927	Thr74	ARTSPLQtPAAPGAA	Homo sapiens	HeLa Cell
pmid	sentence
10669763	In endothelial cells, tumor necrosis factor alpha (tnf-alpha) induces dephosphorylation and subsequent ubiquitin-dependent degradation of the antiapoptotic protein bcl-2. Here, we investigate the role of different putative phosphorylation sites to facilitate bcl-2 degradation

Publications:

5

Organism:

Homo Sapiens, Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-149570	Ser715	YQSTIPQsPSPAPDD	Homo sapiens	Macrophage
pmid	sentence
16973330	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.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-64326	Ser715	YQSTIPQsPSPAPDD	Homo sapiens	HEK-293 Cell
pmid	sentence
10022832	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.

Identifier	Residue	Sequence	Organism
SIGNOR-77571	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.

Identifier	Residue	Organism
SIGNOR-77574		Homo sapiens
pmid	sentence
10828059	Long pde4d forms are inhibited by erk2 phosphorylation

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-262972	Ser727	TIPSPVTsPVLSRRH	in vitro
pmid	sentence
11328814	Here we incubated a recombinant preparation of the phospholipase in vitro with several enzymes including protein kinase CK2 (CK2), extracellular signal-regulated kinase 2 (ERK2), and protein phosphatase 2A (PP2A) to identify effects that might be of regulatory importance in vivo.Major findings were that 1) CK2 phosphorylated the phospholipase on serines 93, 105, and 716; 2) ERK2 phosphorylated the enzyme on serine 730; 3) there was cross-antagonism between the reactions that phosphorylated serines 716 and 730; 4) PP2A selectively hydrolyzed phosphate groups that were esterified to serines 716 and 730. The results of two independent experiments with each type of assay indicated that the incubation caused a 50% loss of phospholipase activity (TableV). These results differed from those of corresponding incubation experiments with PA-PLA1α plus ERK2 and MgATP (see “Experimental Procedures”), which provided no evidence for complex formation or phosphorylation-dependent loss of phospholipase activity

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-157272	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. in the inducible cell lines, expression of wild-type form of sp3 increases vegf production whereas the s73a form has a reduced potential reflecting its lower transcriptional activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-132614	Ser734	NSSRFPPsPLASKPT	Homo sapiens
pmid	sentence
15616583	Dapk interacts with erk through a docking sequence within its death domain and is a substrate of erk. Phosphorylation of dapk at ser 735 by erk increases the catalytic activity of dapk both in vitro and in vivo

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-195471	Ser74	DKATQTLsPASPSQG	Homo sapiens	Lymphoma Cell
pmid	sentence
22258404	Phosphomimetic mutation of this site (s74d) moderately enhanced bmf apoptotic activity in vivo.22 here, we demonstrate a previously unrecognized mode of regulation of bmf. We show that b-raf-mek-erk2 signaling regulates bmf phosphorylation at serine 74 and serine 77. Phosphorylation of serine 77 downregulates the pro-apoptotic activity of bmf.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-195475	Ser77	TQTLSPAsPSQGVML	Homo sapiens	Lymphoma Cell
pmid	sentence
22258404	Phosphomimetic mutation of this site (s74d) moderately enhanced bmf apoptotic activity in vivo.22 here, we demonstrate a previously unrecognized mode of regulation of bmf. We show that b-raf-mek-erk2 signaling regulates bmf phosphorylation at serine 74 and serine 77. Phosphorylation of serine 77 downregulates the pro-apoptotic activity of bmf.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-71033	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-71037	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:

2

Organism:

Homo Sapiens

Tissue:

Smooth Muscle

Identifier	Residue	Sequence	Organism
SIGNOR-151925	Ser770	MMRSKETsSPGTDDV	Homo sapiens
pmid	sentence
17209041	We have demonstrated that the map kinases extracellular signal-regulated kinases 1 and 2 (erk1/2) are implicated in growth factor activation of nhe1. / our results suggest that amino acids ser770 and ser771 mediate erk-dependent activation of the na+/h+ exchanger in vivo.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-200880	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-66239	Ser780	DSLDSRLsPPAGLFT	Homo sapiens
pmid	sentence
10194762	Gh treatment of chinese hamster ovary cells stably transfected with the gh receptor (choa cells) led to rapid and transient activation of both stat5a and erk1 and erk2. these observations show, for the first time, direct physical interaction between erk and stat5a and also clearly identify serine 780 as a target for erk.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Ovary

Pathways:

Glucocorticoid receptor Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-264414	Ser827	NSDMPAPsPGLDYEP	in vitro
pmid	sentence
24312625	Hence ASPP2 can be phosphorylated at serine 827 by MAPK1 in vitro.\|Phosphorylation of ASPP2 by MAPK is required for RAS-induced increased binding to p53 and increased transactivation of pro-apoptotic genes.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-121852	Ser845	SIRQRISsFETFGSS	Homo sapiens
pmid	sentence
14768064	The precursor form of the cytokine il-16 (proil-16) was shown to be phosphorylated on ser144 . 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
SIGNOR-278409	Ser85	VNGGHPPsALAPAAR	Homo sapiens
pmid	sentence
23082118	CITED2 coactivation is enhanced by activation of MAPK1 and requires T166.\|CITED2 is phosphorylated by MAPK1 at S85, T166 and T175.

Identifier	Residue	Sequence	Organism
SIGNOR-278410	Thr166	KHSGGSStPGGSGGS	Homo sapiens
pmid	sentence
23082118	CITED2 coactivation is enhanced by activation of MAPK1 and requires T166.\|CITED2 is phosphorylated by MAPK1 at S85, T166 and T175.

Identifier	Residue	Sequence	Organism
SIGNOR-278408	Thr175	GGSGGSStPGGSGSS	Homo sapiens
pmid	sentence
23082118	CITED2 coactivation is enhanced by activation of MAPK1 and requires T166.\|CITED2 is phosphorylated by MAPK1 at S85, T166 and T175.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-188916	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:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277856	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-277857	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
SIGNOR-262772	Ser87	YWVPPPMsPSSKSVS	Mus musculus
pmid	sentence
22028470	We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5'-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. This approach identified 80 proteins phosphorylated by ERK2, 13 of which are known ERK2 substrates. With this improved methodology, we detected 98 sites directly phosphorylated by ERK2 on 80 proteins from NIH 3T3-L1 fibroblasts. Thirteen of these proteins are known substrates and the rest represent previously unknown kinase/substrate interactions. (table1)

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-265882	Ser884	NKDVTLTsPLLVNLL	in vitro
pmid	sentence
11773444	In vitro phosphorylation studies with His-tagged TRBP (795–931) suggested that S884 can be phosphorylated by MAPK (ERK2) in vitro (Fig. 10A).Analysis of in vitro and in vivo receptor interactions with TRBP suggested that S884 allowed selective interactions for ERβ, TR, and RXR vs. ERα.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262524	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-249436	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-249437	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-106561	Ser982	KKKSEPSsPDHGSST	in vitro
pmid	sentence
11287604	coimmunoprecipitation detected a specific association between the activated erk and plc beta1 within the nucleus. In vitro studies revealed that recombinant 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 this result suggests that erk-evoked phosphorylation of plc beta1 at serine 982 plays a critical role in the activation of the nuclear pi cycle and is also crucial to the mitogenic action of igf-i.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262781	Thr1032	GGLFSPStAHVPDGA	Mus musculus	NIH-3T3 Cell
pmid	sentence
22028470	We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5'-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. This approach identified 80 proteins phosphorylated by ERK2, 13 of which are known ERK2 substrates. With this improved methodology, we detected 98 sites directly phosphorylated by ERK2 on 80 proteins from NIH 3T3-L1 fibroblasts. Thirteen of these proteins are known substrates and the rest represent previously unknown kinase/substrate interactions. (table1)

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262782	Thr131	KEEPPPLtPPARCAA	Mus musculus	NIH-3T3 Cell
pmid	sentence
22028470	We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5'-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. This approach identified 80 proteins phosphorylated by ERK2, 13 of which are known ERK2 substrates. With this improved methodology, we detected 98 sites directly phosphorylated by ERK2 on 80 proteins from NIH 3T3-L1 fibroblasts. Thirteen of these proteins are known substrates and the rest represent previously unknown kinase/substrate interactions. (table1)

Publications:

2

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-142458	Thr1032	SSSNRPFtPPTSTGG	Homo sapiens
pmid	sentence
16314496	We demonstrate that erk phosphorylates trap220/med1 in vivo at two specific sites: threonine 1032 and threonine 1457. importantly, we found that erk phosphorylation significantly increases the stability and half-life of trap220/med1 in vivo and correlates with increased thyroid hormone receptor-dependent transcription.

Identifier	Residue	Sequence	Organism
SIGNOR-142462	Thr1457	HSKSPAYtPQNLDSE	Homo sapiens
pmid	sentence
16314496	We demonstrate that erk phosphorylates trap220/med1 in vivo at two specific sites: threonine 1032 and threonine 1457. importantly, we found that erk phosphorylation significantly increases the stability and half-life of trap220/med1 in vivo and correlates with increased thyroid hormone receptor-dependent transcription.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-112805	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-112809	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-124646	Thr1223	AEREGPGtPPTTLAR	Homo sapiens
pmid	sentence
15125835	Both cdk1 and erk2 induced phosphorylation of the wild-type nir2. Substitution of t794 by alanine reduced the phosphorylation by erk2, whereas the double mutations t794/1223a completely abolished it. The requirement of multiple nir2 phosphorylation sites for plk1 binding may provide a mechanism that sets a threshold for the nir2-plk1 interaction during mitosis.

Identifier	Residue	Sequence	Organism
SIGNOR-124650	Thr794	LEMLVPStPTSTSGA	Homo sapiens
pmid	sentence
15125835	Both cdk1 and erk2 induced phosphorylation of the wild-type nir2. Substitution of t794 by alanine reduced the phosphorylation by erk2, whereas the double mutations t794/1223a completely abolished it. The requirement of multiple nir2 phosphorylation sites for plk1 binding may provide a mechanism that sets a threshold for the nir2-plk1 interaction during mitosis.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-101544	Thr125	PEVLRPEtPRPVDIG	Homo sapiens
pmid	sentence
12792650	Inhibition of caspase-9 through phosphorylation at Thr 125 by ERK MAPK

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-148616	Thr125	PEVLRPEtPRPVDIG	Mus musculus	T-lymphocyte
pmid	sentence
16888006	ERK/MAPK phosphorylates caspase-9 at Thr(125), and this phosphorylation is crucial for caspase-9 inhibition

Publications:

2

Organism:

Homo Sapiens, Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262777	Thr1346	RATGAALtPTEERRT	Mus musculus	NIH-3T3 Cell
pmid	sentence
22028470	We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5'-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. This approach identified 80 proteins phosphorylated by ERK2, 13 of which are known ERK2 substrates. With this improved methodology, we detected 98 sites directly phosphorylated by ERK2 on 80 proteins from NIH 3T3-L1 fibroblasts. Thirteen of these proteins are known substrates and the rest represent previously unknown kinase/substrate interactions. (table1)

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249430	Thr143	CSAPSPStPSFQPPQ	Rattus norvegicus	PC-12 Cell
pmid	sentence
11883936	NGFI-B is an inducible orphan nuclear receptor that initiates apoptosis. Growth factors such as EGF activate the MAP kinase ERK, whose activity may determine if a cell survives or undergoes apoptosis. EGF stimulation of cells leads to phosphorylation of threonine in NGFI-B. Thr-142 of NGFI-B is comprised in a consensus MAP kinase site and was identified as a preferred substrate for ERK2 (but not ERK1) in vitro.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-94003	Thr160	GVPVRTYtHEVVTLW	Homo sapiens
pmid	sentence
12359725	In addition to its role in stimulating cyclin d1 expression and nuclear translocation of cdk2, erk regulates thr-160 phosphorylation of cdk2-cyclin e.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-179808	Thr163	TDGSLPStPPPAEEE	Homo sapiens
pmid	sentence
18676833	We found that jnk phosphorylated ser-121 and thr-163 of mcl-1 in response to stimulation with h(2)o(2) and that transfection of unphosphorylatable mcl-1 resulted in an enhanced anti-apoptotic activity in response to stimulation with h(2)o(2). Jnk-dependent phosphorylation and thus inactivation of mcl-1 may be one of the mechanisms through which oxidative stress induces cellular damage.

Identifier	Residue	Sequence	Organism
SIGNOR-92593	Thr163	TDGSLPStPPPAEEE	Homo sapiens
pmid	sentence
12223490	We found that jnk phosphorylated ser-121 and thr-163 of mcl-1 in response to stimulation with h(2)o(2) and that transfection of unphosphorylatable mcl-1 resulted in an enhanced anti-apoptotic activity in response to stimulation with h(2)o(2). Jnk-dependent phosphorylation and thus inactivation of mcl-1 may be one of the mechanisms through which oxidative stress induces cellular damage.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-183379	Thr177	TAEKRVAtPVDWKDG	Homo sapiens
pmid	sentence
19140803	These results show that the mapks can mediate phosphorylation of prdx6 at thr-177 with a consequent marked increase in its aipla(2) activity.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Lung

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262769	Thr1772	QQTPPPVtPRAKLSF	Mus musculus	NIH-3T3 Cell
pmid	sentence
22028470	We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5'-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. This approach identified 80 proteins phosphorylated by ERK2, 13 of which are known ERK2 substrates. With this improved methodology, we detected 98 sites directly phosphorylated by ERK2 on 80 proteins from NIH 3T3-L1 fibroblasts. Thirteen of these proteins are known substrates and the rest represent previously unknown kinase/substrate interactions. (table1)

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-93740	Thr18	MTILQAPtPAPSTIP	Homo sapiens
pmid	sentence
12356731	Upon phosphorylation by erks, iex-1 acquires the ability to inhibit cell death induced by various stimuli. In turn, iex-1 potentiates erk activation in response to various growth factors.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-174076	Thr182	IDQGDLMtPQFTPYY	Homo sapiens
pmid	sentence
21666810	Like mk2, mk5 could be phosphorylated and activated by p38mapk and erk2 in vitro, but not by sapk?/Jnk3

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-58127	Thr182	IDQGDLMtPQFTPYY	Homo sapiens	HeLa Cell
pmid	sentence
9628874	Activated following phosphorylation at thr-182 by p38-alpha/mapk14, p38-beta/mapk11, erk2/mapk1, erk3/mapk6, and erk4/mapk4.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-154914	Thr183	PGEAEPLtPTYNISA	Homo sapiens
pmid	sentence
17512500	We identified the extracellular signal-regulated kinase 2 (erk-2) as roralpha4 phosphorylating kinase in vitro. The primary sequence of roralpha4 contains an erk-2 recognition motif (p-l-t(128)-p) within the hinge domain, and mutation of thr-128 to ala prevents roralpha4 phosphorylation by erk. The roralpha4-t128a mutant exhibits an increased dna-binding affinity, an increased transcriptional activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-103159	Thr185	HDHTGFLtEYVATRW	Homo sapiens	Dermal Fibroblast
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).Mapk activity is tightly regulated by phosphorylation and dephosphorylation. 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

Identifier	Residue	Sequence	Organism
SIGNOR-248625	Thr185	HDHTGFLtEYVATRW	Rattus norvegicus
pmid	sentence
7780739	Inactivation of p42 MAP kinase by protein phosphatase 2A and a protein tyrosine phosphatase, but not CL100, in various cell lines\|Protein phosphatase-2A was the only vanadate-insensitive phosphatase acting on Thr 183 of p42mapk or on MAPKK to be detected in PC12 cell extracts.

Publications:

2

Organism:

Homo Sapiens, Rattus Norvegicus

Identifier	Residue	Sequence
SIGNOR-249414	Thr185	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
SIGNOR-249415	Tyr187	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:

2

Pathways:

Glucocorticoid receptor Signaling, Nucleotide Biosynthesis

Identifier	Residue	Sequence	Organism
SIGNOR-248464	Thr185	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-248465	Tyr187	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-248590	Thr185	HDHTGFLtEYVATRW	Rattus norvegicus
pmid	sentence
7780739	Inactivation of p42 MAP kinase by protein phosphatase 2A and a protein tyrosine phosphatase, but not CL100, in various cell lines\|Protein phosphatase-2A was the only vanadate-insensitive phosphatase acting on Thr 183 of p42mapk or on MAPKK to be detected in PC12 cell extracts.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-248449	Thr185	HDHTGFLtEYVATRW	Homo sapiens
pmid	sentence
12754301	The effect of PTP epsilon on ERKs is at least in part indirect because phosphorylation of the threonine residue in the ERK activation loop is reduced in the presence of PTP epsilon. Nonetheless, PTP epsilon is present in a molecular complex with ERK, providing PTP epsilon with opportunity to act on ERK proteins also directly. We conclude that PTP epsilon is a physiological inhibitor of ERK signaling\|These enzymes are joined by the large family of dual-specificity phosphatases, which are structurally similar to tyrosine phosphatases but which can dephosphorylate both residues of the activation loop

Identifier	Residue	Sequence	Organism
SIGNOR-248448	Tyr187	HTGFLTEyVATRWYR	Homo sapiens
pmid	sentence
12754301	The effect of PTP epsilon on ERKs is at least in part indirect because phosphorylation of the threonine residue in the ERK activation loop is reduced in the presence of PTP epsilon. Nonetheless, PTP epsilon is present in a molecular complex with ERK, providing PTP epsilon with opportunity to act on ERK proteins also directly. We conclude that PTP epsilon is a physiological inhibitor of ERK signaling\|These enzymes are joined by the large family of dual-specificity phosphatases, which are structurally similar to tyrosine phosphatases but which can dephosphorylate both residues of the activation loop

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-143052	Thr185	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-166655		Homo sapiens
pmid	sentence
20626350	In particular, p38 mapk activity stimulates the physical association between ppa2 and mkk1/2- erk1/2 complex, leading to mkk1/2 dephosphorilation by pp2a . p38 mapks activity stimulates the physical association between pp2a and erk complex, leading to mkk1/2 dephosphorylation by pp2a.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236447	Thr185	HDHTGFLtEYVATRW	Homo sapiens	BJ Cell
pmid	sentence
11971971	Mapk1 is phosphorylated by map2k1/mek1 and map2k2/mek2 on thr-185 and tyr-187 in response to external stimuli like insulin or ngf. Both phosphorylations are required for activity.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-235937	Tyr187	HTGFLTEyVATRWYR	Homo sapiens	BJ Cell
pmid	sentence
11971971	Mapk1 is phosphorylated by map2k1/mek1 and map2k2/mek2 on thr-185 and tyr-187 in response to external stimuli like insulin or ngf. Both phosphorylations are required for activity.

Identifier	Residue	Organism
SIGNOR-235940		Homo sapiens
pmid	sentence
12270934	Mek1 as indicated by extensive phosphorylation of erk1 and erk2 during the initial 2 h of adipogenesis.

Identifier	Residue	Organism
SIGNOR-258993		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:

4

Organism:

Homo Sapiens, Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-248717	Thr185	HDHTGFLtEYVATRW	Rattus norvegicus
pmid	sentence
7535768	Dephosphorylation and Inactivation of ERKs\|A single protein kinase, MEK, activates ERK2 by phosphorylating threonine 183 and tyrosine 185

Identifier	Residue	Sequence	Organism
SIGNOR-248718	Tyr187	HTGFLTEyVATRWYR	Rattus norvegicus
pmid	sentence
7535768	Dephosphorylation and Inactivation of ERKs\|A single protein kinase, MEK, activates ERK2 by phosphorylating threonine 183 and tyrosine 185

Publications:

2

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-86709	Thr185	HDHTGFLtEYVATRW	Homo sapiens
pmid	sentence
11971971	Mapk1 is phosphorylated by map2k1/mek1 and map2k2/mek2 on thr-185 and tyr-187 in response to external stimuli like insulin or ngf. Both phosphorylations are required for activity.

Identifier	Residue	Sequence	Organism
SIGNOR-86713	Tyr187	HTGFLTEyVATRWYR	Homo sapiens
pmid	sentence
11971971	Mapk1 is phosphorylated by map2k1/mek1 and map2k2/mek2 on thr-185 and tyr-187 in response to external stimuli like insulin or ngf. Both phosphorylations are required for activity.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-244792	Thr185	HDHTGFLtEYVATRW	Homo sapiens	BJ Cell
pmid	sentence
11971971	Mapk1 is phosphorylated by map2k1/mek1 and map2k2/mek2 on thr-185 and tyr-187 in response to external stimuli like insulin or ngf. Both phosphorylations are required for activity.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-244788	Tyr187	HTGFLTEyVATRWYR	Homo sapiens	BJ Cell
pmid	sentence
11971971	Mapk1 is phosphorylated by map2k1/mek1 and map2k2/mek2 on thr-185 and tyr-187 in response to external stimuli like insulin or ngf. Both phosphorylations are required for activity.

Identifier	Residue	Organism
SIGNOR-258990		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

Identifier	Residue	Organism	Cell Line
SIGNOR-244795		Homo sapiens	Adipocyte
pmid	sentence
12270934	Mek1 as indicated by extensive phosphorylation of erk1 and erk2 during the initial 2 h of adipogenesis.

Publications:

4

Organism:

Homo Sapiens, Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249432	Thr212	VIEPLPVtPTRDVAT	Rattus norvegicus	Smooth Muscle
pmid	sentence
15542607	We also show that ERK2 phosphorylates PAK1 on Thr(212) in vitro and that Thr(212) is phosphorylated in smooth muscle cells following PDGF-BB treatment in an adhesion- and MEK/ERK-dependent fashion. Expression of a phosphomimic variant, PAK-T212E, does not alter ERK association, but markedly attenuates downstream ERK signaling. Taken together, these data suggest that PAK1 may facilitate ERK signaling by serving as a scaffold to recruit Raf, MEK, and ERK to adhesion complexes, and that subsequent growth factor-stimulated phosphorylation of PAK-Thr(212) by ERK may serve to provide a negative feedback signal

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-274076	Thr219	ASLSLPAtPVGKGTE	in vitro
pmid	sentence
12556484	In this case, only NudelS2 and NudelS5 were phosphorylated. Therefore, T219, S242, and T245 of Nudel were phosphorylation sites of Cdc2 in vitro. In contrast, Erk2 only phosphorylated T219 and T245. These two sites, with surrounding sequences such as PATP from residues 217 to 220 and PLTP from 243 to 246, respectively, are indeed typical MAPK sites

Identifier	Residue	Sequence	Organism
SIGNOR-274075	Thr245	GFGTSPLtPSARISA	in vitro
pmid	sentence
12556484	In this case, only NudelS2 and NudelS5 were phosphorylated. Therefore, T219, S242, and T245 of Nudel were phosphorylation sites of Cdc2 in vitro. In contrast, Erk2 only phosphorylated T219 and T245. These two sites, with surrounding sequences such as PATP from residues 217 to 220 and PLTP from 243 to 246, respectively, are indeed typical MAPK sites

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249404	Thr225	QMAGTPItPLKDGFT	Homo sapiens	HeLa Cell
pmid	sentence
11408587	Furthermore, ERK2 directly phosphorylated GRASP55 on the same residues that generated the MPM2 phospho-epitope.\|The obvious next challenge is to demonstrate the precise role of these phosphorylation events.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249419	Thr229	HFFKNIVtPRTPPPS	Homo sapiens	JURKAT Cell
pmid	sentence
12760422	Thr94 in bovine myelin basic protein is a second phosphorylation site for 42-kDa mitogen-activated protein kinase (ERK2).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-143477	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-22420	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-187798	Thr235	SSSSPPGtPSPADAK	Homo sapiens
pmid	sentence
19723873	Phosphorylation of cebpb at thr(235) peaked at 16 hours in il-1beta-stimulated cells. The mek inhibitor u0126 inhibited this phosphorylation and reduced mmp-1 gene induction.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-262839	Thr243	QEQLRPQtPEPVEGR	Homo sapiens
pmid	sentence
19684019	ERK1/2 phosphorylate RSPH3. the extent of radiolabeled phosphate incorporation into RSPH3 T286A was much less than that into wild-type RSPH3, suggesting that threonine 286 is the major ERK1/2 phosphorylation site in cells. ERK2 also phosphorylates RSPH3 on threonine 243 to a lesser extent. Phosphorylation of the double mutant T243V/T286A RSPH3 was no more than 20% that of wild-type RSPH3 (Fig. 4, C and D). inhibiting ERK1/2 activity appears to negatively regulate the AKAP function of RSPH3.

Identifier	Residue	Sequence	Organism
SIGNOR-262838	Thr286	AFLDRPPtPLFIPAK	Homo sapiens
pmid	sentence
19684019	ERK1/2 phosphorylate RSPH3. the extent of radiolabeled phosphate incorporation into RSPH3 T286A was much less than that into wild-type RSPH3, suggesting that threonine 286 is the major ERK1/2 phosphorylation site in cells. ERK2 also phosphorylates RSPH3 on threonine 243 to a lesser extent. Phosphorylation of the double mutant T243V/T286A RSPH3 was no more than 20% that of wild-type RSPH3 (Fig. 4, C and D).

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262760	Thr249	SQDADLKtPTKPKQH	Mus musculus	NIH-3T3 Cell
pmid	sentence
22028470	We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5'-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. This approach identified 80 proteins phosphorylated by ERK2, 13 of which are known ERK2 substrates. With this improved methodology, we detected 98 sites directly phosphorylated by ERK2 on 80 proteins from NIH 3T3-L1 fibroblasts. Thirteen of these proteins are known substrates and the rest represent previously unknown kinase/substrate interactions. (table1)

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-271861	Thr265	KERISPRtPASKIAS	Homo sapiens	Spermatozoon
pmid	sentence
27901058	Here we demonstrate that ERK1/2 phosphorylates proAKAP4 on Thr265 in human spermatozoa in vitro and in vivo

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262970	Thr269	FTSYIVStPPGGFPP	Homo sapiens	HEK-293 Cell
pmid	sentence
16848763	Further experiments showed that DAZAP1 was phosphorylated stoichiometrically in vitro by ERK2 (extracellular-signal-regulated protein kinase 2) at two Thr-Pro sequences (Thr269 and Thr315), and that both sites became phosphorylated in HEK-293 (human embryonic kidney 293) cells in response to PMA or EGF (epidermal growth factor), or RAW 264.7 macrophages in response to LPS. Phosphorylation of the ARE-binding protein DAZAP1 by ERK2 induces its dissociation from DAZ

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262971	Thr315	GVPPPPAtPGAAPLA	Homo sapiens	HEK-293 Cell
pmid	sentence
16848763	Further experiments showed that DAZAP1 was phosphorylated stoichiometrically in vitro by ERK2 (extracellular-signal-regulated protein kinase 2) at two Thr-Pro sequences (Thr269 and Thr315), and that both sites became phosphorylated in HEK-293 (human embryonic kidney 293) cells in response to PMA or EGF (epidermal growth factor), or RAW 264.7 macrophages in response to LPS. Phosphorylation of the ARE-binding protein DAZAP1 by ERK2 induces its dissociation from DAZ

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-101660	Thr277	GSRTAPYtPNLPHHQ	Homo sapiens
pmid	sentence
12801888	Phosphorylation of thr276 is shown to be important for tgf-?-Induced nuclear accumulation and, as a consequence, transcriptional activity of smad4. these results suggest that smad4 can be phosphorylated by erk2 at thr276.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236335	Thr292	ETPPRPRtPGRPLSS	Chlorocebus aethiops	COS Cell
pmid	sentence
14993270	We propose that activation of erk during adhesion creates a feedback system in which erk phosphorylates mek1 on t292, and this in turn blocks additional s298 phosphorylation in response to integrin signaling.

Identifier	Residue	Sequence	Organism
SIGNOR-236498	Thr386	IGLNQPStPTHAAGV	Homo sapiens
pmid	sentence
10567369	An ERK2-binding site at the N terminus of MEK1 was reported to mediate their stable association. We examined the importance of this binding site in the feedback phosphorylation of mek1 on thr(292) and thr(386) by erk2

Publications:

2

Organism:

Chlorocebus Aethiops, Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-235467	Thr336	GGPGPERtPGSGSGS	Mus musculus	NIH-3T3 Cell
pmid	sentence
7889942	We demonstrate that elk-1, a protein closely related to p62tcf in function, is a nuclear target of two members of the map kinase family, erk1 and erk2, erki phosphorylates five c-terminal sites in elk-i (s324,t336, s383, s389 and s422) with varying degrees of efficiency.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277468	Thr349	HRLESPTtPLLDDMD	Homo sapiens	A-549 Cell
pmid	sentence
31320475	ERK-dependent Txnip ubiquitination and proteasome degradation depended upon phosphorylation of a PXTP motif threonine (Thr349) located within the C-terminal α-arrestin domain and proximal to a previously characterized E3 ubiquitin ligase-binding site.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249451	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-249438	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-137955	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-136075	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-138894	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-113563	Thr45	PGGTLFStTPGGTRI	Homo sapiens
pmid	sentence
11777913	Phosphorylation of 4e-bp1 is mediated by the p38/msk1 pathway in response to uvb irradiation. In the present study we demonstrated that uvb induced 4e-bp1 phosphorylation at multiple sites, thr-36, thr-45, ser-64, and thr-69, leading to dissociation of 4e-bp1 from eif-4e. Uvb-induced phosphorylation of 4e-bp1 was blocked by p38 kinase inhibitors, pd169316 and sb202190, and msk1 inhibitor, h89, but not by mitogen-activated protein kinase kinase inhibitors, pd98059 or u0126.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-56337	Thr451	KRTRSKGtLRYMSPE	Homo sapiens
pmid	sentence
9528799	Our results provide strong evidence that dsrna binding is required for dimerization of full-length pkr molecules in vivo, leading to autophosphorylation in the activation loop and stimulation of the eif2alpha kinase function of pkr.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-137171	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

Pathways:

Nucleotide Biosynthesis

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277442	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
SIGNOR-29505	Thr526	GEAGGPLtPRRVSSD	Homo sapiens
pmid	sentence
7588608	Consistent with the in vivo phosphorylation and inactivation by ras, erf is efficiently phosphorylated in vitro by erk2 and cdc2/cyclin b kinases, at sites similar to those detected in vivo. Furthermore, a single mutation at position 526 results in the loss of a specific phosphopeptide both in in vivo and in vitro (by erk2) labeling. Substitution of thr526 for glutamic acid also decreases the repression ability of erf

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-279068	Thr55	DDIEQWFtEDPGPDE	Homo sapiens
pmid	sentence
15116093	In summary, our results suggest that phosphorylation of p53Thr55 by ERK2 is important for doxorubicin-induced p53 activation and cell death.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249446	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-267306	Thr619	GQGDAPPtPLPTPVD	Homo sapiens
pmid	sentence
32485148	T619 in PFAS is required to mediate ERK2-dependent purine synthesis stimulation. We demonstrate that ERK2, but not ERK1, phosphorylates the purine synthesis enzyme PFAS (phosphoribosylformylglycinamidine synthase) at T619 in cells to stimulate de novo purine synthesis. The expression of nonphosphorylatable PFAS (T619A) decreases purine synthesis, RAS-dependent cancer cell-colony formation, and tumor growth. Thus, ERK2-mediated PFAS phosphorylation facilitates the increase in nucleic acid synthesis required for anabolic cell growth and proliferation.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Nucleotide Biosynthesis

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262897	Thr621	GEPEFRYtAGIHGNE	Mus musculus	NIH-3T3 Cell
pmid	sentence
15654748	We show that DNA binding by AEBP1 requires both the N- and C-terminal domains of AEBP1, and MAPK interaction with AEBP1 (through its N terminus) results in enhanced DNA binding. A threonine at position 623 within the C-terminal domain of AEBP1 plays an important role in DNA binding by AEBP1, because the mutation results in decreased DNA binding by AEBP1, which leads to a decrease in the transcriptional repression ability of AEBP1. We also show that in vitro phosphorylation of AEBP1 by MAPK is greatly reduced upon mutation of T623. These results suggest that MAPK regulates the transcriptional activity of AEBP1 by a novel dual mechanism, in which MAPK interaction enhances and subsequent phosphorylation decreases the DNA-binding ability of AEBP1.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-249448	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
SIGNOR-184469	Thr679	PGVELLLtPREPALP	Homo sapiens
pmid	sentence
19261619	Importantly tnf-alpha enhanced the erk pathway-dependent phosphorylation of thr-678 of gef-h1 that was key for activation.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Kidney

Identifier	Residue	Sequence	Organism
SIGNOR-163242	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-90517	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:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262759	Thr691	AGVTLPPtPSGSRTK	Mus musculus	NIH-3T3 Cell
pmid	sentence
22028470	We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5'-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. This approach identified 80 proteins phosphorylated by ERK2, 13 of which are known ERK2 substrates. With this improved methodology, we detected 98 sites directly phosphorylated by ERK2 on 80 proteins from NIH 3T3-L1 fibroblasts. Thirteen of these proteins are known substrates and the rest represent previously unknown kinase/substrate interactions. (table1)

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-20545	Thr693	RELVEPLtPSGEAPN	in vitro
pmid	sentence
1651322	A growth factor-stimulated protein kinase activity that phosphorylates the epidermal growth factor (EGF) receptor at Thr669 has been described Anion-exchange chromatography demonstrated that this protein kinase activity was accounted for by two enzymes. The first peak of activity eluted from the column corresponded to the microtubule-associated protein 2 (MAP2) kinase

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-262761	Thr7	tPGYHGFP	Mus musculus
pmid	sentence
22028470	We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5'-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. This approach identified 80 proteins phosphorylated by ERK2, 13 of which are known ERK2 substrates. With this improved methodology, we detected 98 sites directly phosphorylated by ERK2 on 80 proteins from NIH 3T3-L1 fibroblasts. Thirteen of these proteins are known substrates and the rest represent previously unknown kinase/substrate interactions. (table1)

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-182770	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-262774	Thr844	IPFPTPTtPLTGRDG	Mus musculus
pmid	sentence
22028470	We have optimized a chemical genetic system using analog-sensitive ERK2, a form of ERK2 engineered to use an analog of adenosine 5'-triphosphate (ATP), to tag and isolate ERK2 substrates in vitro. This approach identified 80 proteins phosphorylated by ERK2, 13 of which are known ERK2 substrates. With this improved methodology, we detected 98 sites directly phosphorylated by ERK2 on 80 proteins from NIH 3T3-L1 fibroblasts. Thirteen of these proteins are known substrates and the rest represent previously unknown kinase/substrate interactions. (table1)

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249413	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-277505	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-248484	Tyr187	HTGFLTEyVATRWYR	Homo sapiens
pmid	sentence
10702794	HePTP efficiently dephosphorylated active ERK2 on the tyrosine residue in the activation loop in vitro. Together, these data identify ERK2 as a specific and direct target of HePTP and are consistent with a model in which HePTP negatively regulates ERK2 activity as part of a feedback mechanism

Identifier	Residue	Sequence	Organism
SIGNOR-248483	Tyr187	HTGFLTEyVATRWYR	Homo sapiens
pmid	sentence
16226275	First, Erk phosphorylates HePTP at residues Thr45 and Ser72. Second, HePTP dephosphorylates Erk at PTyr185

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248536	Tyr187	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

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248840	Tyr187	HTGFLTEyVATRWYR	Chlorocebus aethiops	COS Cell
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.\|PTP-SL dephosphorylates the regulatory phosphotyrosine on the active loop of ERK1/2. Tyrosine dephosphorylation of ERK1/2 causes the inactivation of ERK1/2 and its retention in the cytoplasm

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-248708	Tyr187	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.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-101276	Tyr205	IMLNSKGyTKSIDIW	Homo sapiens	HEK-293 Cell
pmid	sentence
19494114	In this study we show that one of these potential targets, the erk1/2, is indeed a direct dep-1 substrate in vivo.

Publications:

2

Organism:

In Vitro, Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-140294	Tyr187	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
SIGNOR-161536	Tyr205	IMLNSKGyTKSIDIW	Homo sapiens
pmid	sentence
19494114	In this study we show that one of these potential targets, the erk1/2, is indeed a direct dep-1 substrate in vivo.

Identifier	Residue	Organism
SIGNOR-101279		Homo sapiens
pmid	sentence
12771128	A dominant-negative mutant of high cell density-enhanced 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:

2

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-261910		Homo sapiens	MCF-7 Cell
pmid	sentence
28939105	Protein kinase C-eta regulates Mcl-1 level via ERK1. knockdown of PKCη but not PKCα, -δ or -ε caused a significant decrease in ERK (extracellular signal-regulated kinase) phosphorylation. Knockdown of ERK1 but not ERK2 decreased Mcl-1 level, and the decrease in Mcl-1 caused by PKCη knockdown was restored by ERK1 overexpression. These results suggest that PKCη utilizes the ERK signaling pathway to protect against ubiquitin-mediated proteasomal degradation of Mcl-1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-179400		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

Identifier	Residue	Organism
SIGNOR-210182		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:

2

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-67355		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

Identifier	Residue	Organism
SIGNOR-134049		Homo sapiens
pmid	sentence
15713638	Here we demonstrate that dusp5, an inducible nuclear phosphatase, interacts specifically with erk2 via a kinase interaction motif (kim) within its amino-terminal noncatalytic domain. This binding determines the substrate specificity of dusp5 in vivo, as it inactivates erk2 but not jun n-terminal protein kinase or p38 map kinase.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-244916		Chlorocebus aethiops	COS Cell
pmid	sentence
14993270	We propose that activation of erk during adhesion creates a feedback system in which erk phosphorylates mek1 on t292, and this in turn blocks additional s298 phosphorylation in response to integrin signaling.

Identifier	Residue	Organism	Cell Line
SIGNOR-244912		Homo sapiens	HEK-293 Cell
pmid	sentence
10567369	An ERK2-binding site at the N terminus of MEK1 was reported to mediate their stable association. We examined the importance of this binding site in the feedback phosphorylation of mek1 on thr(292) and thr(386) by erk2

Publications:

2

Organism:

Chlorocebus Aethiops, Homo Sapiens

Identifier	Residue	Organism
SIGNOR-279636		Homo sapiens
pmid	sentence
26682816	ERK2 phosphorylates three serines in titin\u2019s N2B-Us: S3918, S3960, and S4010 (the latter of which is well conserved) ().

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-103152		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
SIGNOR-159164		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	Organism
SIGNOR-168989		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-217499		Homo sapiens
pmid	sentence
12359725	In addition to its role in stimulating cyclin d1 expression and nuclear translocation of cdk2, erk regulates thr-160 phosphorylation of cdk2-cyclin e.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-249609		Homo sapiens
pmid	sentence
10706702	CD19 is a coreceptor on B cells that enhances the increase in cytoplasmic calcium and ERK2 activation when coligated with the B cell Ag receptor.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-201943		Homo sapiens
pmid	sentence
23616010	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:

1

Organism:

Homo Sapiens

Pathways:

Glucocorticoid receptor Signaling

Identifier	Residue	Organism
SIGNOR-161515		Homo sapiens
pmid	sentence
19282669	Erk-activates the rsk family of serine/threonine kinases,rsk1, rsk2, and rsk3.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-157162		Homo sapiens	Breast Cancer Cell, Brain Cancer Cell
pmid	sentence
17671177	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 signalin.

Identifier	Residue	Organism
SIGNOR-135692		Homo sapiens
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 signalin.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-279635		Homo sapiens
pmid	sentence
9872331	ERK2 phosphorylates Stat3 on three serine-containing peptides and decreases its tyrosine phosphorylation induced by EGF treatment.\|Here, we report that ERK2 activated by its upstream kinase, MEK1, represses Stat3 transcriptional activity induced by Src or Jak-2.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-66738		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-279745		Homo sapiens
pmid	sentence
28100697	Upon IFNgamma treatment, PHF8 is phosphorylated by ERK2 and evicted from the promoters, which correlates with an increase in H4K20me1 and H3K4me3 levels.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-217574		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	Cell Line
SIGNOR-60871		Homo sapiens	Breast Cancer Cell
pmid	sentence
9788880	Pyst2 preferentially dephosphorylates and inactivates p42 map kinase in vitro and in vivo

Publications:

1

Organism:

Homo Sapiens

Tissue:

Skin

Identifier	Residue	Organism
SIGNOR-279136		Homo sapiens
pmid	sentence
20693286	AKT1 stimulated PLD activity via activation of ERK.\|AKT1 actually phosphorylated ERK2 as a substrate (K(m) 1 \u03bcm).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-77559		Homo sapiens
pmid	sentence
10828059	The short pde4d1 isoenzyme is activated by erk2 phosphorylation this signifies that erk2 phosphorylated pde4d1 at a single site, ser491, that is cognate to the single erk2 phosphorylation site (ser579) found in pde4d3.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-280021		Homo sapiens
pmid	sentence
27802129	Our results indicate that CPEB4 activation is driven by ERK2- and Cdk1 mediated hyperphosphorylation of at least 12 residues in the intrinsically disordered NTD.\|We concluded that, in interphase, unphosphorylated CPEB4 phase separates into liquid like droplets that recruit mRNAs but are inactive for cytoplasmic polyadenylation and translation, whereas in M-phase, CPEB4 is phosphorylated by ERK2 and Cdk1 and recovers its monomeric form, which can drive the cytoplasmic polyadenylation of target mRNAs.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-280022		Homo sapiens
pmid	sentence
20548102	Recombinant active ERK2 also phosphorylated Sec16 (XREF_FIG).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-144325		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-264664		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
SIGNOR-103146		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
SIGNOR-40926		Homo sapiens
pmid	sentence
8626452	Here we characterize a new map kinase phosphatase, mkp-2, that is induced in human peripheral blood t cells with phorbol 12-myristate 13-acetate and is expressed in a variety of nonhematopoietic tissues as well. We show that the in vivo substrate specificities of individual phosphatases are unique. Pac1, mkp-2, and mkp-1 recognize erk and p38, erk and jnk, and erk, p38, and jnk, respectively.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-164289		Homo sapiens
pmid	sentence
20231899	In addition, extracellular signal-regulated kinase (erk) is stimulated by ampk-induced pld1 activation through the formation of phosphatidic acid (pa), which is a product of pld

Publications:

1

Organism:

Homo Sapiens

Tissue:

Muscle, Skeletal Muscle

Identifier	Residue	Organism
SIGNOR-176586		Homo sapiens
pmid	sentence
21908610	In addition, although mutation of ser-58 to either alanine or glutamic acid does not affect the intrinsic catalytic activity of dusp9/mkp-4, phospho-mimetic (ser-58 to glu) substitution inhibits both the interaction of dusp9/mkp-4 with erk2 and p38? In vivo and its ability to dephosphorylate and inactivate these map kinases.

Identifier	Residue	Organism
SIGNOR-176583		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:

2

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-262244		Homo sapiens	Leukemia Cell
pmid	sentence
31482470	In the present study, we have shown that ERK2 inhibitor VX-11e demonstrates a potent synergy with voreloxin in leukemia cell lines and that this effect is associated with the inhibition of proliferation, cell cycle arrest and induction of apoptosis.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-44858		in vitro
pmid	sentence
8929531	The rapid phosphorylation of bad following il-3 connects a proximal survival signal with the bcl-2 family, modulating this checkpoint for apoptosis.phosphorylatedBAD is bound to 14-3-3 within the cytosol, while only nonphosphorylated BAD is heterodimerized with membrane-bound BCL-XL.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism
SIGNOR-40915		Homo sapiens
pmid	sentence
8626452	Pac1 and mkp-1 previously have been implicated in the in vivo inactivation of erk or of erk and jnk, respectively.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-278957		Homo sapiens
pmid	sentence
19204783	We also reported that ERK2-phosphorylated TR2 is recruited to PML nuclear bodies (PML NBs) for its subsequent small ubiquitin-like modification (SUMOylation) and function as a potent transcriptional repressor xref , xref .

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-48338		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 erk2erk and p38 phosphorylate mnk1 and mnk2, which stimulates their in vitro kinase activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-279227		Homo sapiens
pmid	sentence
19036157	ERK2 may also directly phosphorylate YB-1 and therefore promotes its ability to transactivate target genes.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-161518		Homo sapiens
pmid	sentence
19282669	Erk-activates the rsk family of serine/threonine kinases,rsk1, rsk2, and rsk3.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-279106		Homo sapiens
pmid	sentence
10559258	RIP2 directly phosphorylates and activates ERK2 in vivo and in vitro.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-114771		Homo sapiens	Macrophage
pmid	sentence
11842088	In addition, immunoblot and immunostaining analysis revealed that phosphorylation of erk was increased by treatment with sb203580;whereas pd98059 increased the phosphorylation of p38, which implies a seesaw-like balance between erk and p38 phosphorylation.

Identifier	Residue	Organism
SIGNOR-178639		Homo sapiens
pmid	sentence
18481201	In addition, immunoblot and immunostaining analysis revealed that phosphorylation of erk was increased by treatment with sb203580;whereas pd98059 increased the phosphorylation of p38, which implies a seesaw-like balance between erk and p38 phosphorylation.

Publications:

2

Organism:

Homo Sapiens

Pathways:

Glucocorticoid receptor Signaling

Identifier	Residue	Organism	Cell Line
SIGNOR-69448		Homo sapiens	HEK-293 Cell
pmid	sentence
10415025	Lc-ptp dephosphorylated erk2 in vitro. the complex formation of lc-ptp with erk is the essential mechanism for the suppression. Taken collectively, these results indicate that lc-ptp suppresses mitogen-activated protein kinase directly in vivo.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-111499		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-278417		Homo sapiens
pmid	sentence
17631144	Phosphorylation of ELK1 or ERK2 increased dramatically compared with controls and suggested that TOPK or ERK2 could enhance ERK2 or TOPK kinase activity by respective and mutual phosphorylation of each other.\|The results indicated that active TOPK could strongly phosphorylate ERK2 and very weakly phosphorylate ERK1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-173000		Homo sapiens
pmid	sentence
21454675	Expression of rptp-beta inhibits both mek1/2 and erk1/2 phosphorylation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-73614		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-48298		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 erk2erk and p38 phosphorylate mnk1 and mnk2, which stimulates their in vitro kinase activity toward a substrate, eukaryotic initiation factor-4e (eif-4e).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-169001		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-258996		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	Cell Line
SIGNOR-146751		Homo sapiens	Neutrophil
pmid	sentence
16709866	The role of members of the arrestin family to mediate kinase activation is also a well-established phenomenon, including activation of members of the src family, erk1/2, and jnk3. Activation often includes the recruitment and interaction of arrestins with upstream mapks (ask1, mek3, mkk3, and mek kinase-2).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-46064		Homo sapiens
pmid	sentence
9013873	Vav may link gp130 activation to downstream mapk activation in hematopoietic cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-279538		Homo sapiens
pmid	sentence
30696942	Interestingly, we discovered that several kinases in the MEK and ERK2 pathway destabilize Shank3 and that genetic deletion and pharmacological inhibition of ERK2 increases Shank3 abundance in vivo.\|We also determined that phosphorylation of Shank3 by ERK2 at selective residues promotes its ubiquitination and degradation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-270303		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-279226		Homo sapiens
pmid	sentence
24116218	Inhibition of ERK2 impaired phosphorylation of MLCK and insulin stimulated glucose uptake.\|These findings suggest that ERK2 activates MLCK which then mediates the phosphorylation of RLC of MyoIIA.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-132610		Homo sapiens
pmid	sentence
15616583	Conversely, dapk promotes the cytoplasmic retention of erk, thereby inhibiting erk signaling in the nucleus.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-279351		Homo sapiens
pmid	sentence
30760631	In vitro kinase assay results indicated that STK33 can phosphorylate ERK2.\|STK33 phosphorylated ERK2 and increased the activity of ERK2 and promote the tumorigenesis of colorectal cancer HCT15 cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-277006		Homo sapiens
pmid	sentence
20638106	Dual-specificity phosphatase six (DUSP6, MKP3, or PYST1) dephosphorylates phosphotyrosine and phosphothreonine residues on ERK-2 (MAPK1) to inactivate the ERK-2 kinase.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-164286		Homo sapiens
pmid	sentence
20231899	An erk pharmacological inhibitor, pd98059, and the pld inhibitor, 1-btoh, both attenuate (14)c-glucose uptake in muscle cells. Finally, the extracellular stresses caused by glucose deprivation or aminoimidazole carboxamide ribonucleotide (aicar;ampk activator) regulate (14)c-glucose uptake and cell surface glucose transport (glut) 4 through erk stimulation by ampk-mediated pld1 activation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-242622		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	Cell Line
SIGNOR-262521		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-64169		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

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-251678		Mus musculus	NIH-3T3 Cell
pmid	sentence
11742987	Glucocorticoids inhibit MAP kinase via increased expression and decreased degradation of MKP-1\|Both induction of MKP-1 expression and inhibition of its degradation are necessary for glucocorticoid-mediated inhibition of Erk-1/2 activation. In NIH-3T3 fibroblasts, although glucocorticoids up-regulate the MKP-1 level, they do not attenuate the proteasomal degradation of this protein and consequently they are unable to inhibit Erk-1/2 activity.

Publications:

1

Organism:

Mus Musculus

Pathways:

Glucocorticoid receptor Signaling

Identifier	Residue	Organism
SIGNOR-279744		Homo sapiens
pmid	sentence
35546143	In the present study, Ser32 was revealed to be a novel phosphorylated site on TOPK that could be activated by ERK2.\|TOPK/PBK is phosphorylated by ERK2 at serine 32, promotes tumorigenesis and is involved in sorafenib resistance in RCC.

Publications:

1

Organism:

Homo Sapiens

Name	MAPK1 View Modifications
Full Name	Mitogen-activated protein kinase 1
Synonyms	MAP kinase 1, MAPK 1, ERT1, Extracellular signal-regulated kinase 2, ERK-2, MAP kinase isoform p42, p42-MAPK, Mitogen-activated protein kinase 2, MAP kinase 2, MAPK 2 \| ERK2, PRKM1, PRKM2
Primary ID	P28482
Links	- -
Type	protein
Relations	576
Pathways	Glucocorticoid receptor Signaling, Nucleotide Biosynthesis
Inhibitors	4-[2-(2-chloro-4-fluoroanilino)-5-methyl-4-pyrimidinyl]-N-[(1S)-1-(3-chlorophenyl)-2-hydroxyethyl]-1H-pyrrole-2-carboxamide
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, DCC, 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. Mediates phosphorylation of TPR in respons to EGF stimulation. May play a role in the spindle assembly checkpoint. Phosphorylates PML and promotes its interaction with PIN1, leading to PML degradation. Phosphorylates CDK2AP2 (By similarity).

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