Search results for MAPK3

Showing 30 results out of 111

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Species

Types

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Protein (6 results from a total of 7)

Identifier: R-HSA-59284
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: MAPK3: P27361
Identifier: R-HSA-73724
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: MAPK3: P27361
Identifier: R-HSA-9636295
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen
Primary external reference: UniProt: MAPK3: P27361
Identifier: R-HSA-9635775
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: MAPK3: P27361
Identifier: R-HSA-2422448
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: MAPK3: P27361
Identifier: R-HSA-112359
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: MAPK3: P27361

Complex (6 results from a total of 8)

Identifier: R-HSA-5675359
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-5675357
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-9635770
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-109844
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-109845
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-2422444
Species: Homo sapiens
Compartment: cytosol

Reaction (6 results from a total of 70)

Identifier: R-HSA-109860
Species: Homo sapiens
Compartment: cytosol
MAP2K1 (also known as MEK1) phosphorylates the critical Thr202 and Tyr204 on MAPK3 (ERK1), converting two ATP to ADP. Phosphorylation of MAPK3 activates its kinase activity.

MAP2K1 activation requires the phosphorylation of two serine residues (S218 and S222) in the activation loop.

Identifier: R-HSA-9636304
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen
Mtb Mce-family lipoprotein Mce3E (Mce3E) translocates to the phagocyte's endoplasmic reticulum (ER) and binds to newly produced human mitogen activated protein kinase 3 (MAPK3), inhibiting its transport out of the ER (Li et al. 2015).
Identifier: R-HSA-109857
Species: Homo sapiens
Compartment: cytosol
In the cytoplasm phosphorylated MAP2K1 (MEK1) may encounter monomeric, inactive MAPK3 (ERK1).
IL-6-type receptor activation leads to induction of the MAPK cascade. Experiments using gp130 identified that the gp130 SHP2 (SH2-domain-containing tyrosine phosphatase)-binding site Tyr-759 (Stahl et al. 1995) is required for this activation. Mutation of gp130 Tyr-759 impairs IL-6 induced activation of the MAPK cascade (Kim et al. 1998). While there is a consensus that SHP2 is involved in IL-6-induced activation of the MAPK pathway, the molecular details are uncertain. One proposed mechanism suggests SHP2 acts as an adaptor for Grb2-Sos recruitment (Fukada et al. 1996, Kim & Baumann 1999). IL-6 induced SHP2 recruitment to p-Tyr-759 of gp130 was demonstrated but relatively little of the SHP2 remained associated with gp130, suggesting that SHP2 dissociates from the receptor when phosphorylated. This seems inconsistent with a Grb2-Sos recruitment role for SHP2, though it is possible that only low levels or transient recruitment are required. IL-6 induced ERK activation was not inhibited in cells transfected with a phosphatase inactive mutant of SHP2, whereas an SHP2 mutant missing the Grb2 interaction region significantly suppressed ERK activation. This suggests phosphatase activity is not required for ERK activation while SHP-2 interaction with Grb2 is important. However, overexpression studies can generate artefactual interactions and this interpretation has been questioned (Dance et al. 2008). An alternative proposal suggests that SHP2 and the adaptor protein Gab1 couple gp130 signalling to Erk activation. In this proposal phosphorylated SHP2 dissociates from gp130 and becomes associated with membrane associated Gab1 in a complex with PI3-kinase (Takahashi-Tezuka et al. 1998, Eulenfeld & Schaper 2009). SHP2 interaction is suggested to induce a conformational change in Gab1 that permits Gab1-PI3-kinase activation and enhancement of IL-6-induced Erk pathway activation. However this is speculative, the role of SHP2 phosphatase activity is unclear. Other possible mechanisms are outlined by Dance et al. (2008), extrapolated from growth factor receptor mechanisms but with unknown relevance to IL-6/gp130.
Identifier: R-HSA-9731111
Species: Homo sapiens
Compartment: nucleoplasm
MAPK1 (ERK2) and MAPK3 (ERK1) phosphorylate SMAD2 and SMAD3 on conserved residues in the linker region, which connects the DNA-binding domain and the transcriptional activation domain. ERK-mediated phosphorylation leads to cytosolic retention of SMAD2 and SMAD3 and inhibits TGF-beta signaling (Kretzschmar et al. 1999). Potential ERK phosphorylation residues in SMAD2 are T220, S245, S250 and S255, and in SMAD3 they are T179, S213, S204 and S208 (Kretzschmar et al. 1999). The residue S250 in SMAD2 was shown to be phosphorylated by ERKs in several studies (Rostam et al. 2016, Talati et al. 2018). The corresponding site in SMAD3 is residue S208, and it was shown to be the most prominent ERK phosphorylation site (Matsuura et al. 2005). Only these two sites have been annotated as targets of ERK-mediated phosphorylation. Additional sites will be annotated as more information becomes available.

In addition to inhibitory phosphorylation of SMAD2 and SMAD3 by ERKs, an activating phosphorylation of SMAD2 on S8 by MAPK3 has also been reported (Funaba et al. 2002).
Identifier: R-HSA-9626832
Species: Homo sapiens
Compartment: cytosol
In resting cells, the NADPH oxidase components, NCF1 (p47phox), NCF2 (p67phox), and NCF4 (p40phox) are located in the cytosol where they associate in a trimer complex with a 1:1:1 stoichiometry through specific domains (Groemping Y & Rittinger K 2005; El-Benna J et al. 2005; Park JW et al. 1994; Lapouge K et al. 2002; El-Benna J et al. 2016). However, NCF1 may also exist separately from the trimer (El-Benna J et al. 2016). In the resting state, two SH3 domains of NCF1 (p47phox) bind the auto‐inhibitory region (AIR; amino acids 292‐340) to keep NCF1 in a closed auto‐inhibited state, preventing its binding to p22phox and therefore NOX2 activation (Groemping Y et al. 2003; Yuzawa S et al. 2004; El-Benna J et al. 2016). Priming of neutrophils by several agents such as GM‐CSF, TNFα, PAF, LPS and CL097, a TLR7/8 agonist, induces partial phosphorylation of NCF1 (Makni-Maalej K et al. 2015; Dang PM et al. 1999; Dewas C et al. 2003; DeLeo FR et al. 1998). Mass spectrometry analysis of NCF1 identified Ser345 as the phosphorylated site in neutrophils primed by TNFα and GM‐CSF, and site‐directed mutagenesis of Ser345 and use of a competitive inhibitory peptide containing the Ser345 sequence have demonstrated that this step is critical for the priming of ROS production in human neutrophils (Dang PMC et al. 2006). Further, inhibitors of the MAPK1 and MAPK3 (ERK1/2) pathway abrogated GM-CSF-induced phosphorylation of Ser345 (Dang PMC et al. 2006).
Identifier: R-HSA-9845033
Species: Homo sapiens
Compartment: cytosol
The CLIP1-LTK fusion promotes phosphorylation of MAPK1 and MAPK3 (ERK1 and ERK2) as assessed by Western blot (Izumi et al, 2021). The mechanism by which the signal is transmitted from the activated receptor to induce MAPK phosphorylation has not yet been elucidated.

Pathway (6 results from a total of 18)

Identifier: R-HSA-110056
Species: Homo sapiens
Compartment: cytosol, nucleoplasm
Mitogen-activated protein kinase kinase MAP2K1 (also known as MEK1) is a dual threonine and tyrosine recognition kinase that phosphorylates and activates MAPK3 (ERK1) (Ohren et al. 2004; Roskoski 2012a).
Identifier: R-HSA-5684996
Species: Homo sapiens
The extracellular signal regulated kinases (ERKs) 1 and 2, also known as MAPK3 and MAPK1, are phosphorylated by the MAP2Ks 1 and 2 in response to a wide range of extracellular stimuli to promote differentiation, proliferation, cell motility, cell survivial, metabolism and transcription, among others (reviewed in Roskoski, 2012b; McKay and Morrison, 2007; Raman et al, 2007). In the classical pathway, MAPK1/3 activation is triggered by the GEF-mediated activation of RAS at the plasma membrane, leading to the activation of the RAF MAP3Ks (reviewed in McKay and Morrison, 2007; Matallanas et al, 2011; Wellbrock et al, 2004). However, many physiological and pathological stimuli have been found to activate MAPK1/3 independently of RAF and RAS, acting instead through MAP3Ks such as MOS, TPL2 and AMPK (Dawson et al, 2008; Wang et al, 2009; Kuriakose et al, 2014; Awane et al, 1999). Activated MAPK1/3 phosphorylate numerous targets in both the nucleus and cytoplasm (reviewed in Yoon and Seger, 2006; Roskoski 2012b).
Identifier: R-HSA-5674135
Species: Homo sapiens
Activated RAF proteins are restricted substrate kinases whose primary downstream targets are the two MAP2K proteins, MAPK2K1 and MAP2K2 (also known as MEK1 and MEK2) (reviewed in Roskoski, 2010, Roskoski, 2012a). Phosphorylation of the MAPK2K activation loop primes them to phosphorylate the primary effector of the activated MAPK pathway, the two MAPK proteins MAPK3 and MAPK1 (also known as ERK1 and 2). Unlike their upstream counterparts, MAPK3 and MAPK1 catalyze the phosphorylation of hundreds of cytoplasmic and nuclear targets including transcription factors and regulatory molecules (reviewed in Roskoski, 2012b). Activation of MAP2K and MAPK proteins downstream of activated RAF generally occurs in the context of a higher order scaffolding complex that regulates the specificity and localization of the pathway (reviewed in Brown and Sacks, 2009; Matallanas et al, 2011).
Identifier: R-HSA-9732724
Species: Homo sapiens
Interferon-gamma (IFNG) signaling results in transient activation of MAPK1 (ERK2) and MAPK3 (ERK1) (Sakatsume et al. 1998, Ulloa et al. 1999). IFNG-mediated MAPK (ERK) activation is JAK1-dependent and RAS-independent (Sakatsume et al. 1998). It is thought to occur through JAK1-meidated phosphorylation of RAF1 (Sakatsume et al. 1998).
Identifier: R-HSA-8865999
Species: Homo sapiens
PTPN11 (SHP2), recruited to activated MET receptor through GAB1, is phosphorylated in response to HGF treatment, although phosphorylation sites and direct MET involvement have not been examined (Schaeper et al. 2000, Duan et al. 2006). Phosphorylation of PTPN11 in response to HGF treatment is required for the recruitment and activation of sphingosine kinase SPHK1, which may play a role in HGF-induced cell scattering (Duan et al. 2006). While PTPN11 promotes MAPK3/1 (ERK1/2) signaling downstream of MET, it can also dephosphorylate MET on unidentified tyrosine residues (Furcht et al. 2014).
Identifier: R-HSA-8875656
Species: Homo sapiens
Activated MET receptor is subject to recycling from the plasma membrane through the endosomal compartment and back to the plasma membrane (Peschard et al. 2001, Hammond et al. 2001, Petrelli et al. 2002). In the recycling process, activated MET receptor is endocytosed, and the GGA3 protein directs it, via a largely unknown mechanism, through the RAB4 positive endosomal compartments back to the plasma membrane (Parachoniak et al. 2011). Endosomal signaling by MET during the recycling process appears to play an important role in sustained activation of ERK1/ERK2 (MAPK3/MAPK1) and STAT3 downstream of MET (Kermorgant and Parker 2008).

Set (6 results from a total of 8)

Identifier: R-HSA-3656389
Species: Homo sapiens
Compartment: cytosol
This CandidateSet contains sequences identified by William Pearson's analysis of Reactome catalyst entities. Catalyst entity sequences were used to identify analagous sequences that shared overall homology and active site homology. Sequences in this Candidate set were identified in an April 24, 2012 analysis. Further candidates were identified by Ralf Stephan in a July 15, 2023 analysis.
Identifier: R-HSA-9769857
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-9769851
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-9769858
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-199878
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-199955
Species: Homo sapiens
Compartment: nucleoplasm
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