A database built with INDRA combining content from numerous readers and databases. This page allows you to curate the loaded statements. For more information please see the manual.

IndraLab

Statements

databases
phosphosite cbn pc11 biopax bel_lc signor biogrid tas lincs_drug hprd trrust | geneways tees isi trips rlimsp medscan sparser reach
reading

MAP2K1 is active
34 22 |
MAP2K1 phosphorylated on S222 and S218 is active. 10 / 33
33 |
biopax:pid
No evidence text available
biopax:pid
No evidence text available
biopax:pid
No evidence text available
biopax:pid
No evidence text available
biopax:pid
No evidence text available
biopax:pid
No evidence text available
biopax:pid
No evidence text available
biopax:pid
No evidence text available
biopax:pid
No evidence text available
biopax:pid
No evidence text available
MAP2K1 phosphorylated on S222 is active. 6 / 6
6 |
signor
"In vitro kinase assay revealed that the direct targets of pdk1 in the mapk pathway were the upstream mapk kinases mek1 and mek2. The identified pdk1 phosphorylation sites in mek1 and mek2 are ser222 and ser226, respectively, and are known to be essential for full activation"
signor
"Phosphorylation at ser-218 and ser-222 by map kinase kinase kinases (raf or mekk1) positively regulates mek1 kinase activity."
signor
"Raf-1 phosphorylation of MEK activated it, as judged by its ability to stimulate the phosphorylation of myelin basic protein by glutathione S-transferase-ERK1."
signor
"Among other effectors, active ras binds and activates the raf kinase, iniziating a kinase cascade involving serine phosporylation of mek1/2 (mapkk) and tyrosine and threonine phosphorylation of erk1/2 ras activation leads to raf and subsequently mek activation. Phospholipide analysis demostrated that serine residues 218 and 222 of human mek1 are the primary sites for phosphorylation by c-raf."
signor
"Activation of mek family kinases requires phosphorylation of two conserved ser/thr residues.Phosphopeptide analysis demonstrated that serine residues 218 and 222 of human mek1 are the primary sites for phosphorylation by c-raf"
signor
"Our data demonstrated that a-raf is, indeed, a mek1 activator and may play a role in growth factor signaling|The immunoprecipitates were assayed for GST-MEK1 activation. D, activation of MEK1 by A-Raf requires the presence of serine residue 218 and 222."
MAP2K1 phosphorylated on S218 is active. 5 / 5
5 |
signor
"Cot proteins were used in an in vitro kinase assay using mek as a substrate. Samples were analyzed by western blotting. As seen in the cascade activity assay only wild-type cot was active against mekregulation of cot is of great interest to the signaling field since the cot/mek/erk pathway potentially plays a role in the etiology of inflammatory autoimmune diseases."
signor
"Among other effectors, active ras binds and activates the raf kinase, iniziating a kinase cascade involving serine phosporylation of mek1/2 (mapkk) and tyrosine and threonine phosphorylation of erk1/2 active raf phosphorylates mek phospholpeptide analysis demostrated that serine residues 218 and 222 of human mek1 are the primary sites for phosphorylation by c-raf."
signor
"Our data demonstrated that a-raf is, indeed, a mek1 activator and may play a role in growth factor signaling|The immunoprecipitates were assayed for GST-MEK1 activation. D, activation of MEK1 by A-Raf requires the presence of serine residue 218 and 222."
signor
"Activation of mek family kinases requires phosphorylation of two conserved ser/thr residueserine residues 218 and 222 of human mek1 are the primary sites for phosphorylation by c-raf."
signor
"Phosphorylation at ser-218 and ser-222 by map kinase kinase kinases (raf or mekk1) positively regulates mek1 kinase activity."
Phosphorylated MAP2K1 is active. 2 / 2
2 |
signor
"In particular, p38 mapk activity stimulates the physical association between ppa2 and mkk1/2- erk1/2 complex, leading to mkk1/2 dephosphorilation by pp2a."
signor
"Both mekk2 and mekk3 are able to activate the jun kinase pathway in vivo. However, following routine immunoprecipitation in triton x-100, mekk2 but not mekk3 is able to effectively phosphorylate both sek-1 and mek-1 and to undergo autophosphorylation"
MAP2K1 phosphorylated on S248 is active. 2 / 2
2 |
signor
"Activation of mek family kinases requires phosphorylation of two conserved ser/thr residues.Phosphopeptide analysis demonstrated that serine residues 218 and 222 of human mek1 are the primary sites for phosphorylation by c-raf"
signor
"Raf-1 phosphorylation of MEK activated it, as judged by its ability to stimulate the phosphorylation of myelin basic protein by glutathione S-transferase-ERK1."
MAP2K1 phosphorylated on S298 is active. 2 / 2
2 |
signor
"We find that adhesion to fibronectin induces pak1-dependent phosphorylation of mek1 on s298 and that this phosphorylation is necessary for efficient activation of mek1 and subsequent mapk activation."
signor
"Inhibition of pak kinase activity dramatically decreased phosphorylation of mek1 at ser(298) in response to either pdgf or egf."
MAP2K1 bound to LAMTOR3 is active. 1 / 1
1 |
signor
"We analyzed the ability of mp1 to bind to mek1, erk1, and to itself, and the regulation of these interactions. Gel filtration of cell lysates revealed two major mp1 peaks: a broad high molecular weight peak and a 28 kda complex. An mp1 mutant that lost mek1 binding no longer enhanced rasv12-stimulated erk1 activity, and functioned as a dominant negative, consistent with the concept that mp1 function depends on facilitating these oligomerizations."
MAP2K1 bound to WDR83 is active. 1 / 1
1 |
signor
"Morg1 specifically associates with several components of the erk pathway, including mp1, raf-1, mek, and erk, and stabilizes their assembly into an oligomeric complex."
MAP2K1 phosphorylated on T286, S222, T386, T292, and S218 is active. 1 / 1
1 |
biopax:pid
No evidence text available
MAP2K1 phosphorylated on S304 is active. 1 / 1
1 |
signor
"MEK1 and MEK2 can also be activated by autophosphorylation. Tyrosine 304 may be a candidate for the autophosphorylation site in MEK1."
MAP2K1 phosphorylated on S252 is active. 1 / 1
1 |
signor
"Raf-1 phosphorylation of MEK activated it, as judged by its ability to stimulate the phosphorylation of myelin basic protein by glutathione S-transferase-ERK1."
MAP2K1 phosphorylated on S244 is active. 1 / 1
1 |
signor
"Activation of mek family kinases requires phosphorylation of two conserved ser/thr residues.Phosphopeptide analysis demonstrated that serine residues 218 and 222 of human mek1 are the primary sites for phosphorylation by c-raf"
MAP2K1 affects kinase, and True
8 |
MAP2K1 phosphorylated on S218 is kinase-active. 3 / 3
3 |
bel
"Activation of MEK1 and MEK2 involves phosphorylation upon conserved serine residues (Ser-218 and Ser-222 on MEK1, Ser-222 and Ser-226 on MEK2"
bel
"Activation of MEK1 requires the phosphorylation of serine residues 218 and 222."
bel
"Raf-1 activity, measured by the abundance of phosphorylated S217/221 MEK1 2, a direct target of Raf-1 (30) , was consistently elevated in Cdc37 overexpressing cells, whereas total MEK1 2 levels were unchanged."
MAP2K1 phosphorylated on S222 is kinase-active. 3 / 3
3 |
bel
"Activation of MEK1 requires the phosphorylation of serine residues 218 and 222."
bel
"Raf-1 activity, measured by the abundance of phosphorylated S217/221 MEK1 2, a direct target of Raf-1 (30) , was consistently elevated in Cdc37 overexpressing cells, whereas total MEK1 2 levels were unchanged."
bel
"Activation of MEK1 and MEK2 involves phosphorylation upon conserved serine residues (Ser-218 and Ser-222 on MEK1, Ser-222 and Ser-226 on MEK2"
Serine-phosphorylated MAP2K1 is kinase-active. 2 / 2
2 |
bel
"Despite remarkable progress in dissecting the signaling pathways that are crucial for the metabolic effects of insulin, the molecular basis for the specificity of its cellular actions is not fully understood. One clue might lie in the spatial and temporal aspects of signaling. Recent evidence suggests that signaling molecules and pathways are localized to discrete compartments in cells by specific protein interactions. Also, the rapid termination of tyrosine or lipid phosphorylation by phosphatases or serine kinases might tightly control the strength of a signaling pathway, thus determining its effect on growth, differentiation and metabolism. Insulin is the most potent anabolic hormone known, promoting the synthesis and storage of carbohydrates, lipids and proteins and inhibiting their degradation and release back into the circulation. Decreased secretion of insulin, coupled with resistance to its actions, results in type 2 diabetes, a devastating disease that is reaching epidemic proportions [1]. Even in the absence of diabetes, insulin resistance is often associated with central obesity, hypertension, polycystic ovarian syndrome, dyslipidemia and atherosclerosis. At the cellular level, insulin action is characterized by diverse effects, including changes in vesicle trafficking, stimulation of protein kinases and phosphatases, promotion of cellular growth and differentiation and activation or repression of transcription. This complexity suggests that insulin action must involve multiple signaling pathways that diverge at or near the activation of its tyrosine kinase receptor. In fact, it is likely that even individual effects of the hormone require multiple signaling inputs. Evidence is emerging that the coordination of these pathways might be governed by their intracellular compartmentalization or duration of action. Here, we consider how temporal and spatial aspects of signal transduction play a crucial role in determining the specificity of insulin action, focusing on signal initiation from the receptor that is spatially segregated into discrete domains of the plasma membrane, as well as the mechanisms that determine the duration of individual signaling pathways. Together, these factors help to differentiate insulin from other hormones that share some of the same overall signaling properties. Divergent signaling pathways are initiated by insulin receptor substrates. The insulin receptor is a tyrosine kinase that catalyzes the phosphorylation of several intracellular substrates, including the insulin receptor substrate (IRS) proteins [2], GAB-1 [3], Shc [4], APS [5], p60DOK [6], SIRPS [7] and c-Cbl [8] (Fig. 1). Each of these substrates recruits a distinct subset of signaling proteins containing Src homology 2 (SH2) domains, which interact specifically with sequences surrounding the phosphotyrosine residue. Moreover, each of these substrates can be confined to distinct locations in the cell by specific sequences that direct interactions with other proteins or lipids. Most attention in the field of insulin receptor substrates has focused on the IRS family of proteins. Mice lacking the IRS-1 protein are insulin resistant but do not develop overt diabetes [9,10]. By contrast, animals lacking IRS-2 exhibit both impaired glucose tolerance and diabetes [11], which appears to result from a defect in insulin secretion as well as insulin resistance, presumably owing to decreased b-cell proliferation in the pancreas in the face of increased demand for insulin. Despite the similarity in structure and function, the apparent differences in phenotype between IRS1 and IRS2 knockout mice underscore a specific signaling specificity that probably results from their tissue distribution, subcellular location, activation–inactivation kinetics and combinatorial interactions with downstream effectors [12]. The tyrosine phosphorylation of IRS family members generates docking sites for sev..."
bel
"Raf-1 phosphorylates and activates MEK-1, a kinase that activates the extracellular signal regulated kinases (ERK)"
MAP2K1 is not active
7 |
MAP2K1 phosphorylated on T292 is inactive. 3 / 3
3 |
signor
"P34cdc2 catalyzes the in vitro phosphorylation of mkk1 on both of these threonine residues and inactivates mkk1 enzymatic activity. Both sites are phosphorylated in vivo as well"
signor
"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."
signor
"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."
MAP2K1 phosphorylated on T286 is inactive. 2 / 2
2 |
signor
"P34cdc2 catalyzes the in vitro phosphorylation of mkk1 on both of these threonine residues and inactivates mkk1 enzymatic activity. Both sites are phosphorylated in vivo as well"
signor
"Phosphorylation of MEK1 by cdk5/p35 down-regulates the mitogen-activated protein kinase pathway. | suggesting that Thr286 in MEK1 is a site of cdk5/p35 phosphorylation that inhibits MEK1 activity."
MAP2K1 phosphorylated on T386 is inactive. 2 / 2
2 |
signor
"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"
signor
"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"