MAP2K2 (MEK2) is a dual-specificity protein kinase in the RAF–MEK–ERK signaling cascade. It phosphorylates the activation-loop threonine and tyrosine residues of ERK MAP kinases, linking upstream signaling to changes in cellular proliferation and differentiation.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000165 MAPK cascade | IBA GO_REF:0000033 | ACCEPT | Summary: MAP2K2 is the MEK2 kinase in the RAF–MEK–ERK cascade. Reason: MAP2K2 is the MEK2 kinase in the RAF–MEK–ERK cascade. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0004672 protein kinase activity | IEA GO_REF:0000002 | MODIFY | Summary: MAP kinase kinase activity specifies the conserved MEK2 substrate class. Reason: MAP kinase kinase activity specifies the conserved MEK2 substrate class. Proposed replacements: MAP kinase kinase activity Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0004674 protein serine/threonine kinase activity | TAS Reactome:R-HSA-109862 | MODIFY | Summary: MEK2 phosphorylates both threonine and tyrosine in ERK activation loops; MAP kinase kinase activity is the informative function. Reason: MEK2 phosphorylates both threonine and tyrosine in ERK activation loops; MAP kinase kinase activity is the informative function. Proposed replacements: MAP kinase kinase activity Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0004708 MAP kinase kinase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Recombinant human MEK2 phosphorylated ERK1 on threonine and tyrosine and activated its kinase activity over100-fold. Supporting Evidence: PMID:8388392 Both MEK1 and MEK2 were expressed in Escherichia coli and shown to be able to activate recombinant human ERK1 in vitro. The purified MEK2 protein stimulated threonine and tyrosine phosphorylation on ERK1 and concomitantly activated ERK1 kinase activity more than 100-fold. |
| GO:0004708 MAP kinase kinase activity | IDA PMID:8388392 Cloning and characterization of two distinct human extracell... | ACCEPT | Summary: Recombinant human MEK2 phosphorylated ERK1 on threonine and tyrosine and activated its kinase activity over100-fold. Supporting Evidence: PMID:8388392 Both MEK1 and MEK2 were expressed in Escherichia coli and shown to be able to activate recombinant human ERK1 in vitro. The purified MEK2 protein stimulated threonine and tyrosine phosphorylation on ERK1 and concomitantly activated ERK1 kinase activity more than 100-fold. |
| GO:0004708 MAP kinase kinase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Recombinant human MEK2 phosphorylated ERK1 on threonine and tyrosine and activated its kinase activity over100-fold. Supporting Evidence: PMID:8388392 Both MEK1 and MEK2 were expressed in Escherichia coli and shown to be able to activate recombinant human ERK1 in vitro. The purified MEK2 protein stimulated threonine and tyrosine phosphorylation on ERK1 and concomitantly activated ERK1 kinase activity more than 100-fold. |
| GO:0004712 protein serine/threonine/tyrosine kinase activity | TAS PMID:19565474 The ERK signaling cascade--views from different subcellular ... | ACCEPT | Summary: Recombinant human MEK2 phosphorylated ERK1 on threonine and tyrosine and activated its kinase activity over100-fold. Supporting Evidence: PMID:8388392 Both MEK1 and MEK2 were expressed in Escherichia coli and shown to be able to activate recombinant human ERK1 in vitro. The purified MEK2 protein stimulated threonine and tyrosine phosphorylation on ERK1 and concomitantly activated ERK1 kinase activity more than 100-fold. |
| GO:0004713 protein tyrosine kinase activity | EXP PMID:10409742 Kinase suppressor of Ras forms a multiprotein signaling comp... | MODIFY | Summary: The established substrate class is MAP kinases; MAP kinase kinase activity describes the dual-specificity reaction more informatively. Reason: The established substrate class is MAP kinases; MAP kinase kinase activity describes the dual-specificity reaction more informatively. Proposed replacements: MAP kinase kinase activity Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0004713 protein tyrosine kinase activity | IEA GO_REF:0000116 | MODIFY | Summary: The established substrate class is MAP kinases; MAP kinase kinase activity describes the dual-specificity reaction more informatively. Reason: The established substrate class is MAP kinases; MAP kinase kinase activity describes the dual-specificity reaction more informatively. Proposed replacements: MAP kinase kinase activity Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005078 MAP kinase scaffold activity | IEA GO_REF:0000117 | UNDECIDED | Summary: MAP2K2 can interact with KSR-family scaffolds, but binding a scaffold does not itself establish MAP kinase scaffold activity. The specific source-side mechanism requires verification. Reason: MAP2K2 can interact with KSR-family scaffolds, but binding a scaffold does not itself establish MAP kinase scaffold activity. The specific source-side mechanism requires verification. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005078 MAP kinase scaffold activity | IMP PMID:29433126 MEK drives BRAF activation through allosteric control of KSR... | UNDECIDED | Summary: MAP2K2 can interact with KSR-family scaffolds, but binding a scaffold does not itself establish MAP kinase scaffold activity. The specific source-side mechanism requires verification. Reason: MAP2K2 can interact with KSR-family scaffolds, but binding a scaffold does not itself establish MAP kinase scaffold activity. The specific source-side mechanism requires verification. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:11909642 Identification of interaction between MEK2 and A-Raf-1. | UNDECIDED | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. The target-specific support in PMID:11909642 still requires detailed assessment of the experimental results. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. The target-specific support in PMID:11909642 still requires detailed assessment of the experimental results. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:11909642 Identification of interaction between MEK2 and A-Raf-1. | UNDECIDED | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. The target-specific support in PMID:11909642 still requires detailed assessment of the experimental results. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. The target-specific support in PMID:11909642 still requires detailed assessment of the experimental results. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:11909642 Identification of interaction between MEK2 and A-Raf-1. | UNDECIDED | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. The target-specific support in PMID:11909642 still requires detailed assessment of the experimental results. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. The target-specific support in PMID:11909642 still requires detailed assessment of the experimental results. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:17979178 A novel tandem affinity purification strategy for the effici... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:21615688 Identification of mitogen-activated protein/extracellular si... | UNDECIDED | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. The target-specific support in PMID:21615688 still requires detailed assessment of the experimental results. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. The target-specific support in PMID:21615688 still requires detailed assessment of the experimental results. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:24746704 Disruption of CRAF-mediated MEK activation is required for e... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:24746704 Disruption of CRAF-mediated MEK activation is required for e... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:24746704 Disruption of CRAF-mediated MEK activation is required for e... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:25600339 Tunable-combinatorial mechanisms of acquired resistance limi... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:25852190 Integrative analysis of kinase networks in TRAIL-induced apo... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:27086506 HiQuant: Rapid Postquantification Analysis of Large-Scale MS... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:29433126 MEK drives BRAF activation through allosteric control of KSR... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:29433126 MEK drives BRAF activation through allosteric control of KSR... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | KEEP AS NON CORE | Summary: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Reason: The observed protein interaction is retained but generic protein binding does not distinguish catalytic signaling from other interactions. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | ACCEPT | Summary: ATP is the phosphate donor for the conserved MAP2K2 reaction. Reason: ATP is the phosphate donor for the conserved MAP2K2 reaction. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005576 extracellular region | NAS PMID:8388392 Cloning and characterization of two distinct human extracell... | UNDECIDED | Summary: An extracellular localization is not explained by the intracellular MEK2 kinase mechanism. The source experiment has not been evaluated at the assay level here, so the assignment is not rejected solely from localization expectations. The target-specific support in PMID:8388392 still requires detailed assessment of the experimental results. Reason: An extracellular localization is not explained by the intracellular MEK2 kinase mechanism. The source experiment has not been evaluated at the assay level here, so the assignment is not rejected solely from localization expectations. The target-specific support in PMID:8388392 still requires detailed assessment of the experimental results. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005634 nucleus | TAS PMID:19565474 The ERK signaling cascade--views from different subcellular ... | KEEP AS NON CORE | Summary: ERK-pathway proteins can redistribute across compartments; a nuclear pool is compatible with signaling but is not the defining MEK2 location. Reason: ERK-pathway proteins can redistribute across compartments; a nuclear pool is compatible with signaling but is not the defining MEK2 location. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005737 cytoplasm | EXP PMID:10409742 Kinase suppressor of Ras forms a multiprotein signaling comp... | ACCEPT | Summary: MEK2 is an intracellular kinase in cytoplasmic RAF–MEK–ERK signaling complexes. Reason: MEK2 is an intracellular kinase in cytoplasmic RAF–MEK–ERK signaling complexes. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: MEK2 is an intracellular kinase in cytoplasmic RAF–MEK–ERK signaling complexes. Reason: MEK2 is an intracellular kinase in cytoplasmic RAF–MEK–ERK signaling complexes. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005739 mitochondrion | IEA GO_REF:0000117 | UNDECIDED | Summary: Mitochondrial localization needs compartment-specific evidence beyond conservation of kinase activity. Reason: Mitochondrial localization needs compartment-specific evidence beyond conservation of kinase activity. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005739 mitochondrion | TAS PMID:19565474 The ERK signaling cascade--views from different subcellular ... | UNDECIDED | Summary: Mitochondrial localization needs compartment-specific evidence beyond conservation of kinase activity. Reason: Mitochondrial localization needs compartment-specific evidence beyond conservation of kinase activity. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005769 early endosome | IEA GO_REF:0000117 | UNDECIDED | Summary: An early-endosome pool is context-specific and cannot be resolved from the conserved kinase sequence alone. Reason: An early-endosome pool is context-specific and cannot be resolved from the conserved kinase sequence alone. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005769 early endosome | TAS PMID:19565474 The ERK signaling cascade--views from different subcellular ... | UNDECIDED | Summary: An early-endosome pool is context-specific and cannot be resolved from the conserved kinase sequence alone. Reason: An early-endosome pool is context-specific and cannot be resolved from the conserved kinase sequence alone. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005770 late endosome | IEA GO_REF:0000117 | UNDECIDED | Summary: A late-endosome pool requires localization evidence; the core MEK2 reaction does not establish it. Reason: A late-endosome pool requires localization evidence; the core MEK2 reaction does not establish it. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005770 late endosome | TAS PMID:19565474 The ERK signaling cascade--views from different subcellular ... | UNDECIDED | Summary: A late-endosome pool requires localization evidence; the core MEK2 reaction does not establish it. Reason: A late-endosome pool requires localization evidence; the core MEK2 reaction does not establish it. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005778 peroxisomal membrane | HDA PMID:21525035 PEX14 is required for microtubule-based peroxisome motility ... | UNDECIDED | Summary: The available PEX14-study abstract does not resolve MEK2-specific peroxisomal membrane association. The full proteomic/experimental material is needed; a different gene in the title is not grounds for removal. Reason: The available PEX14-study abstract does not resolve MEK2-specific peroxisomal membrane association. The full proteomic/experimental material is needed; a different gene in the title is not grounds for removal. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005783 endoplasmic reticulum | IDA PMID:21615688 Identification of mitogen-activated protein/extracellular si... | UNDECIDED | Summary: The specific ER localization requires the original experimental evidence, whose specific experimental results remain to be assessed. The target-specific support in PMID:21615688 still requires detailed assessment of the experimental results. Reason: The specific ER localization requires the original experimental evidence, whose specific experimental results remain to be assessed. The target-specific support in PMID:21615688 still requires detailed assessment of the experimental results. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005794 Golgi apparatus | IDA PMID:21615688 Identification of mitogen-activated protein/extracellular si... | UNDECIDED | Summary: The specific Golgi localization requires the original experimental localization data, rather than transfer from broad ERK-pathway biology. The target-specific support in PMID:21615688 still requires detailed assessment of the experimental results. Reason: The specific Golgi localization requires the original experimental localization data, rather than transfer from broad ERK-pathway biology. The target-specific support in PMID:21615688 still requires detailed assessment of the experimental results. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005794 Golgi apparatus | TAS PMID:19565474 The ERK signaling cascade--views from different subcellular ... | UNDECIDED | Summary: The specific Golgi localization requires the original experimental localization data, rather than transfer from broad ERK-pathway biology. Reason: The specific Golgi localization requires the original experimental localization data, rather than transfer from broad ERK-pathway biology. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | IDA GO_REF:0000052 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS PMID:19565474 The ERK signaling cascade--views from different subcellular ... | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-109858 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-109862 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-109864 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5211356 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5672972 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5672973 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5672978 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5672980 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5674130 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5674132 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5674366 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5674373 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5674496 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6802910 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6802911 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6802912 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6802914 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6802918 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6802919 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6802921 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6802922 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6802925 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6802926 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6802932 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6802933 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6802934 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6802935 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6802942 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6802943 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6803227 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6803230 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6803233 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6803234 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9610152 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9610153 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9610154 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9610156 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9652165 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9656209 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9656211 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9656214 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9656215 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9657599 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9657603 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9657606 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9657608 | ACCEPT | Summary: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Reason: Cytosolic MEK2 is consistent with the characterized intracellular MAPK signaling complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0005874 microtubule | IDA PMID:21615688 Identification of mitogen-activated protein/extracellular si... | UNDECIDED | Summary: The specific microtubule association requires the original localization/interaction evidence, whose target-specific results require assessment. The target-specific support in PMID:21615688 still requires detailed assessment of the experimental results. Reason: The specific microtubule association requires the original localization/interaction evidence, whose target-specific results require assessment. The target-specific support in PMID:21615688 still requires detailed assessment of the experimental results. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005911 cell-cell junction | IDA PMID:21615688 Identification of mitogen-activated protein/extracellular si... | UNDECIDED | Summary: Cell-junction localization is a specific spatial claim not established by core kinase activity. The target-specific support in PMID:21615688 still requires detailed assessment of the experimental results. Reason: Cell-junction localization is a specific spatial claim not established by core kinase activity. The target-specific support in PMID:21615688 still requires detailed assessment of the experimental results. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005925 focal adhesion | IEA GO_REF:0000117 | UNDECIDED | Summary: Focal-adhesion localization requires a distinct cellular experiment or grounded transfer of that observation. Reason: Focal-adhesion localization requires a distinct cellular experiment or grounded transfer of that observation. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0005925 focal adhesion | TAS PMID:19565474 The ERK signaling cascade--views from different subcellular ... | UNDECIDED | Summary: Focal-adhesion localization requires a distinct cellular experiment or grounded transfer of that observation. Reason: Focal-adhesion localization requires a distinct cellular experiment or grounded transfer of that observation. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0009898 cytoplasmic side of plasma membrane | IDA PMID:21615688 Identification of mitogen-activated protein/extracellular si... | UNDECIDED | Summary: KSR–MEK association recruits MEK into membrane-associated fractions on the cytoplasmic side of the signaling membrane. The target-specific support in PMID:21615688 still requires detailed assessment of the experimental results. Reason: KSR–MEK association recruits MEK into membrane-associated fractions on the cytoplasmic side of the signaling membrane. The target-specific support in PMID:21615688 still requires detailed assessment of the experimental results. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0010628 positive regulation of gene expression | IMP PMID:24375836 MiR-92a mediates AZD6244 induced apoptosis and G1-phase arre... | UNDECIDED | Summary: The gene-expression response is stimulus- and assay-dependent; the original experimental reference requires closer evaluation. The target-specific support in PMID:24375836 still requires detailed assessment of the experimental results. Reason: The gene-expression response is stimulus- and assay-dependent; the original experimental reference requires closer evaluation. The target-specific support in PMID:24375836 still requires detailed assessment of the experimental results. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0016020 membrane | EXP PMID:10409742 Kinase suppressor of Ras forms a multiprotein signaling comp... | ACCEPT | Summary: The KSR interaction study detects MEK in membrane-associated fractions, supporting membrane association without a transmembrane protein model. Reason: The KSR interaction study detects MEK in membrane-associated fractions, supporting membrane association without a transmembrane protein model. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0016020 membrane | IEA GO_REF:0000044 | ACCEPT | Summary: The KSR interaction study detects MEK in membrane-associated fractions, supporting membrane association without a transmembrane protein model. Reason: The KSR interaction study detects MEK in membrane-associated fractions, supporting membrane association without a transmembrane protein model. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0030165 PDZ domain binding | IDA PMID:21615688 Identification of mitogen-activated protein/extracellular si... | UNDECIDED | Summary: PDZ-domain binding is a specific interaction claim requiring the original binding assay; a kinase-domain annotation does not establish it. The target-specific support in PMID:21615688 still requires detailed assessment of the experimental results. Reason: PDZ-domain binding is a specific interaction claim requiring the original binding assay; a kinase-domain annotation does not establish it. The target-specific support in PMID:21615688 still requires detailed assessment of the experimental results. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0032872 regulation of stress-activated MAPK cascade | IEA GO_REF:0000117 | UNDECIDED | Summary: Participation in ERK signaling does not by itself establish regulation of a stress-activated MAPK cascade; pathway cross-talk requires evidence. Reason: Participation in ERK signaling does not by itself establish regulation of a stress-activated MAPK cascade; pathway cross-talk requires evidence. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0032872 regulation of stress-activated MAPK cascade | TAS PMID:19565474 The ERK signaling cascade--views from different subcellular ... | UNDECIDED | Summary: Participation in ERK signaling does not by itself establish regulation of a stress-activated MAPK cascade; pathway cross-talk requires evidence. Reason: Participation in ERK signaling does not by itself establish regulation of a stress-activated MAPK cascade; pathway cross-talk requires evidence. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0036289 peptidyl-serine autophosphorylation | IDA PMID:8388392 Cloning and characterization of two distinct human extracell... | UNDECIDED | Summary: MEK2 catalytic activity does not by itself prove serine autophosphorylation. The missing primary experiment is needed to distinguish auto- from trans-phosphorylation. The target-specific support in PMID:8388392 still requires detailed assessment of the experimental results. Reason: MEK2 catalytic activity does not by itself prove serine autophosphorylation. The missing primary experiment is needed to distinguish auto- from trans-phosphorylation. The target-specific support in PMID:8388392 still requires detailed assessment of the experimental results. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0043539 protein serine/threonine kinase activator activity | IDA PMID:8388392 Cloning and characterization of two distinct human extracell... | ACCEPT | Summary: Recombinant human MEK2 phosphorylated ERK1 on threonine and tyrosine and activated its kinase activity over100-fold. Supporting Evidence: PMID:8388392 Both MEK1 and MEK2 were expressed in Escherichia coli and shown to be able to activate recombinant human ERK1 in vitro. The purified MEK2 protein stimulated threonine and tyrosine phosphorylation on ERK1 and concomitantly activated ERK1 kinase activity more than 100-fold. |
| GO:0043539 protein serine/threonine kinase activator activity | IEA GO_REF:0000117 | ACCEPT | Summary: Recombinant human MEK2 phosphorylated ERK1 on threonine and tyrosine and activated its kinase activity over100-fold. Supporting Evidence: PMID:8388392 Both MEK1 and MEK2 were expressed in Escherichia coli and shown to be able to activate recombinant human ERK1 in vitro. The purified MEK2 protein stimulated threonine and tyrosine phosphorylation on ERK1 and concomitantly activated ERK1 kinase activity more than 100-fold. |
| GO:0045893 positive regulation of DNA-templated transcription | IMP PMID:24375836 MiR-92a mediates AZD6244 induced apoptosis and G1-phase arre... | UNDECIDED | Summary: The original transcription-response study requires closer evaluation; generic ERK signaling alone does not establish this specific positive transcriptional response. The target-specific support in PMID:24375836 still requires detailed assessment of the experimental results. Reason: The original transcription-response study requires closer evaluation; generic ERK signaling alone does not establish this specific positive transcriptional response. The target-specific support in PMID:24375836 still requires detailed assessment of the experimental results. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0048471 perinuclear region of cytoplasm | IDA PMID:21615688 Identification of mitogen-activated protein/extracellular si... | UNDECIDED | Summary: The source-specific perinuclear localization requires the original imaging evidence. The target-specific support in PMID:21615688 still requires detailed assessment of the experimental results. Reason: The source-specific perinuclear localization requires the original imaging evidence. The target-specific support in PMID:21615688 still requires detailed assessment of the experimental results. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane CC {ECO:0000269|PubMed:10409742}; Peripheral membrane protein CC {ECO:0000269|PubMed:10409742}. Note=Membrane localization is probably CC regulated by its interaction with KSR1. {ECO:0000269|PubMed:10409742}. |
| GO:0070371 ERK1 and ERK2 cascade | IMP PMID:24375836 MiR-92a mediates AZD6244 induced apoptosis and G1-phase arre... | UNDECIDED | Summary: The ERK1/ERK2 cascade is the defining pathway for MEK2-mediated MAP kinase activation. The target-specific support in PMID:24375836 still requires detailed assessment of the experimental results. Reason: The ERK1/ERK2 cascade is the defining pathway for MEK2-mediated MAP kinase activation. The target-specific support in PMID:24375836 still requires detailed assessment of the experimental results. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0070371 ERK1 and ERK2 cascade | TAS Reactome:R-HSA-112411 | ACCEPT | Summary: The ERK1/ERK2 cascade is the defining pathway for MEK2-mediated MAP kinase activation. Reason: The ERK1/ERK2 cascade is the defining pathway for MEK2-mediated MAP kinase activation. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0071902 positive regulation of protein serine/threonine kinase activity | IDA PMID:8388392 Cloning and characterization of two distinct human extracell... | ACCEPT | Summary: Recombinant human MEK2 phosphorylated ERK1 on threonine and tyrosine and activated its kinase activity over100-fold. Supporting Evidence: PMID:8388392 Both MEK1 and MEK2 were expressed in Escherichia coli and shown to be able to activate recombinant human ERK1 in vitro. The purified MEK2 protein stimulated threonine and tyrosine phosphorylation on ERK1 and concomitantly activated ERK1 kinase activity more than 100-fold. |
| GO:0090170 regulation of Golgi inheritance | IEA GO_REF:0000117 | UNDECIDED | Summary: The specific Golgi-inheritance role requires the relevant cell-cycle experiments. Reason: The specific Golgi-inheritance role requires the relevant cell-cycle experiments. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0090170 regulation of Golgi inheritance | TAS PMID:19565474 The ERK signaling cascade--views from different subcellular ... | UNDECIDED | Summary: The specific Golgi-inheritance role requires the relevant cell-cycle experiments. Reason: The specific Golgi-inheritance role requires the relevant cell-cycle experiments. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0097110 scaffold protein binding | IEA GO_REF:0000117 | ACCEPT | Summary: The KSR interaction study demonstrates MEK association with a Ras–MAPK scaffolding complex. Reason: The KSR interaction study demonstrates MEK association with a Ras–MAPK scaffolding complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0097110 scaffold protein binding | IPI PMID:10409742 Kinase suppressor of Ras forms a multiprotein signaling comp... | ACCEPT | Summary: The KSR interaction study demonstrates MEK association with a Ras–MAPK scaffolding complex. Reason: The KSR interaction study demonstrates MEK association with a Ras–MAPK scaffolding complex. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0097110 scaffold protein binding | IPI PMID:21615688 Identification of mitogen-activated protein/extracellular si... | UNDECIDED | Summary: The KSR interaction study demonstrates MEK association with a Ras–MAPK scaffolding complex. The target-specific support in PMID:21615688 still requires detailed assessment of the experimental results. Reason: The KSR interaction study demonstrates MEK association with a Ras–MAPK scaffolding complex. The target-specific support in PMID:21615688 still requires detailed assessment of the experimental results. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0106310 protein serine kinase activity | EXP PMID:10409742 Kinase suppressor of Ras forms a multiprotein signaling comp... | MODIFY | Summary: The conserved function is activation-loop phosphorylation of MAP kinases; use the substrate-class-specific MAP kinase kinase activity. Reason: The conserved function is activation-loop phosphorylation of MAP kinases; use the substrate-class-specific MAP kinase kinase activity. Proposed replacements: MAP kinase kinase activity Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:0106310 protein serine kinase activity | IEA GO_REF:0000116 | MODIFY | Summary: The conserved function is activation-loop phosphorylation of MAP kinases; use the substrate-class-specific MAP kinase kinase activity. Reason: The conserved function is activation-loop phosphorylation of MAP kinases; use the substrate-class-specific MAP kinase kinase activity. Proposed replacements: MAP kinase kinase activity Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:2000641 regulation of early endosome to late endosome transport | IEA GO_REF:0000117 | UNDECIDED | Summary: Regulation of early-to-late endosome transport is not established merely by the conserved MEK2 catalytic domain. Reason: Regulation of early-to-late endosome transport is not established merely by the conserved MEK2 catalytic domain. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
| GO:2000641 regulation of early endosome to late endosome transport | TAS PMID:19565474 The ERK signaling cascade--views from different subcellular ... | UNDECIDED | Summary: Regulation of early-to-late endosome transport is not established merely by the conserved MEK2 catalytic domain. Reason: Regulation of early-to-late endosome transport is not established merely by the conserved MEK2 catalytic domain. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine and CC a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF CC in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases CC the inhibitory intramolecular interaction between KSR1 or KSR2 protein CC kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF CC dimerization and BRAF activation (PubMed:29433126). CC {ECO:0000250|UniProtKB:Q63932, ECO:0000269|PubMed:29433126}. |
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Download this section (compressed HTML)The human reference supplies mechanistic evidence for the corresponding selected horse protein; the human conclusion alone is not validation of the horse sequence. The exact horse comparison is in genes/HORSE/MAP2K2/MAP2K2-bioinformatics/RESULTS.md. Research reports are source leads; annotation decisions cite the underlying publication or experimentally supported UniProt passages. Unresolved source-specific results retain UNDECIDED.
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