MAP2K2 (MEK2) is a cytosolic dual-specificity protein kinase of the STE7/MAP2K family that forms, with its paralog MAP2K1, the middle tier of the RAF-MEK-ERK (ERK1/ERK2) cascade. Phosphorylation of Ser222 and Ser226 in its activation loop by RAF kinases switches it on, after which it phosphorylates the threonine and tyrosine of the TEY motif of ERK1 (MAPK3) and ERK2 (MAPK1), activating them. MEK2 is recruited to membranes and signalling complexes by scaffolds such as KSR1 and, through its C-terminal PDZ-binding motif (absent from MEK1), by DLG1/SAP97. Binding of MEK to KSR proteins also promotes KSR-BRAF heterodimerization and allosteric BRAF activation. Germline activating variants cause cardiofaciocutaneous syndrome type 4.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000165 MAPK cascade | IBA GO_REF:0000033 | MODIFY | Summary: IBA from PAINT node PTN000684494 (MAP2K clade) for MAPK cascade; MAP2K2 participates as the MAP2K tier of the ERK1/ERK2 cascade. Reason: The PAINT placement is sound: MAP2K2 sits in the MEK2 subfamily (PTHR47448:SF3 in UniProt; PTHR48013:SF8 in the PANTHER 19.0 per-organism file, both named MAP2K2) under a MAP2K node whose members all act in MAPK cascades. For MAP2K2 itself the evidence identifies which cascade: it phosphorylates ERK1 and ERK2. The general term is correct but less specific than supported, so it is refined to ERK1 and ERK2 cascade (GO:0070371), which this gene already carries from Reactome and IMP rows. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000684494 SUPPORTS TRANSFER IBA asserts the general MAPK cascade at a MAP2K node spanning all MAP2K subfamilies; true for MAP2K2, refined for this gene to ERK1 and ERK2 cascade. UniProtKB:P36507 SUPPORTS TRANSFER The target's own experimental annotation (PMID:8388392) is among the descendant evidence for the node; expected, not circular. Proposed replacements: ERK1 and ERK2 cascade Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr PMID:8388392 The purified MEK2 protein stimulated threonine and tyrosine phosphorylation on ERK1 and concomitantly activated ERK1 kinase activity more than 100-fold file:human/MAP2K2/MAP2K2-uniprot.txt CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF |
| GO:0004672 protein kinase activity | IEA GO_REF:0000002 | MODIFY | Summary: InterPro kinase-signature IEA for generic protein kinase activity. Reason: Correct but too general. MAP2K2 is a dual-specificity MAP2K that phosphorylates the Thr and Tyr of the ERK TEY motif; MAP kinase kinase activity (GO:0004708), already carried by IDA and IBA rows, is the specific supported term. Proposed replacements: MAP kinase kinase activity Supporting Evidence: PMID:8388392 The purified MEK2 protein stimulated threonine and tyrosine phosphorylation on ERK1 and concomitantly activated ERK1 kinase activity more than 100-fold file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr |
| GO:0004674 protein serine/threonine kinase activity | TAS Reactome:R-HSA-109862 | MODIFY | Summary: Reactome TAS for protein serine/threonine kinase activity (MAP2K2 phosphorylates MAPK1). Reason: MEK2 phosphorylates both threonine and tyrosine of the ERK activation loop; a Ser/Thr-only kinase term misdescribes the dual specificity. MAP kinase kinase activity (GO:0004708) captures the Reactome reaction exactly. Proposed replacements: MAP kinase kinase activity Supporting Evidence: Reactome:R-HSA-109862 MAP2K2 (MEK2) phosphorylates MAPK1 (ERK2). Phosphorylation of MAPK1 activates its kinase activity. PMID:8388392 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 | IBA GO_REF:0000033 | ACCEPT | Summary: IBA from PAINT node PTN000684494 for MAP kinase kinase activity. Reason: Core molecular function. Direct biochemical evidence for the human protein (dual Thr/Tyr phosphorylation and activation of ERK1) agrees with the PAINT inference for the MAP2K clade and with the conserved catalytic machinery (active-site Asp194, ATP-binding Lys101 region). Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000684494 SUPPORTS TRANSFER MAP kinase kinase activity is conserved across the MAP2K clade; MAP2K2 retains the catalytic Asp194 and ATP-binding Lys101. UniProtKB:P36507 SUPPORTS TRANSFER The target's own experimental annotation (PMID:8388392) is among the descendant evidence for the node; expected, not circular. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr PMID:8388392 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: IDA: recombinant human MEK2 phosphorylated ERK1 on Thr and Tyr and activated it >100-fold (PMID:8388392). Reason: Core molecular function. Direct biochemical evidence for the human protein (dual Thr/Tyr phosphorylation and activation of ERK1) agrees with the PAINT inference for the MAP2K clade and with the conserved catalytic machinery (active-site Asp194, ATP-binding Lys101 region). Supporting Evidence: PMID:8388392 The purified MEK2 protein stimulated threonine and tyrosine phosphorylation on ERK1 and concomitantly activated ERK1 kinase activity more than 100-fold PMID:8388392 MEK (MAP kinase or ERK kinase) is the immediate upstream activator kinase of ERK |
| GO:0004708 MAP kinase kinase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Combined IEA for MAP kinase kinase activity. Reason: Core molecular function. Direct biochemical evidence for the human protein (dual Thr/Tyr phosphorylation and activation of ERK1) agrees with the PAINT inference for the MAP2K clade and with the conserved catalytic machinery (active-site Asp194, ATP-binding Lys101 region). Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr file:human/MAP2K2/MAP2K2-uniprot.txt CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF PMID:8388392 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 ... | MODIFY | Summary: TAS from a review for protein serine/threonine/tyrosine kinase activity. Reason: True but general: MAP kinase kinase activity (GO:0004708) is an is_a child of this term and is the specific activity supported for MAP2K2. Proposed replacements: MAP kinase kinase activity Supporting Evidence: PMID:8388392 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: Protein tyrosine kinase activity, from the UniProt Rhea catalytic-activity mapping of PMID:10409742 (EXP) and the Rhea IEA. Reason: MEK2 phosphorylates a tyrosine only as part of concomitant Thr/Tyr phosphorylation of the MAPK TEY motif; it is not a general tyrosine kinase. The Rhea-split reactions are better represented by MAP kinase kinase activity (GO:0004708). Proposed replacements: MAP kinase kinase activity Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC Reaction=L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + PMID:8388392 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 | IEA GO_REF:0000116 | MODIFY | Summary: Protein tyrosine kinase activity, from the UniProt Rhea catalytic-activity mapping of PMID:10409742 (EXP) and the Rhea IEA. Reason: MEK2 phosphorylates a tyrosine only as part of concomitant Thr/Tyr phosphorylation of the MAPK TEY motif; it is not a general tyrosine kinase. The Rhea-split reactions are better represented by MAP kinase kinase activity (GO:0004708). Proposed replacements: MAP kinase kinase activity Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC Reaction=L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + PMID:8388392 The purified MEK2 protein stimulated threonine and tyrosine phosphorylation on ERK1 and concomitantly activated ERK1 kinase activity more than 100-fold |
| GO:0005078 MAP kinase scaffold activity | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: MAP kinase scaffold activity (IMP, PMID:29433126; IEA ARBA). In Lavoie et al. 2018, MEK1/MEK2 binding to KSR1 drives KSR1-BRAF heterodimerization and BRAF activation; shMEK2 reduces BRAF-KSR1 association. Reason: PMID:29433126 (full text read) shows a genuine non-catalytic MEK function: an 'activator' MEK bound to KSR1 promotes assembly of the KSR1-BRAF dimer, i.e. MEK supports assembly of a multi-kinase MAPK module, which is the closest existing GO notion. The authors frame this as KSR acting as a MEK-dependent allosteric activator of BRAF rather than as classical scaffolding, so the term is an approximation; it is kept, as curated, but non-core relative to the catalytic MAP2K activity. A better-fitting term is raised as a suggested question. Supporting Evidence: PMID:29433126 Reducing endogenous MEK1 and/or MEK2 levels by RNA interference (shMEK1 and/or shMEK2) decreases BRAF-KSR1 interaction by BRET PMID:29433126 support a model whereby KSRs function as MEK-dependent allosteric activators of BRAF |
| GO:0005078 MAP kinase scaffold activity | IMP PMID:29433126 MEK drives BRAF activation through allosteric control of KSR... | KEEP AS NON CORE | Summary: MAP kinase scaffold activity (IMP, PMID:29433126; IEA ARBA). In Lavoie et al. 2018, MEK1/MEK2 binding to KSR1 drives KSR1-BRAF heterodimerization and BRAF activation; shMEK2 reduces BRAF-KSR1 association. Reason: PMID:29433126 (full text read) shows a genuine non-catalytic MEK function: an 'activator' MEK bound to KSR1 promotes assembly of the KSR1-BRAF dimer, i.e. MEK supports assembly of a multi-kinase MAPK module, which is the closest existing GO notion. The authors frame this as KSR acting as a MEK-dependent allosteric activator of BRAF rather than as classical scaffolding, so the term is an approximation; it is kept, as curated, but non-core relative to the catalytic MAP2K activity. A better-fitting term is raised as a suggested question. Supporting Evidence: PMID:29433126 Reducing endogenous MEK1 and/or MEK2 levels by RNA interference (shMEK1 and/or shMEK2) decreases BRAF-KSR1 interaction by BRET PMID:29433126 support a model whereby KSRs function as MEK-dependent allosteric activators of BRAF |
| GO:0005515 protein binding | IPI PMID:11909642 Identification of interaction between MEK2 and A-Raf-1. | MODIFY | Summary: IPI for MAP2K2 binding RAF1 (CRAF), an upstream MAP kinase kinase kinase that phosphorylates and activates MEK in the RAF-MEK-ERK cascade (PMID:11909642). Reason: Bare protein binding is uninformative. The partner RAF1 (CRAF) is a MAPKKK that directly binds and phosphorylates MAP2K2 (A-Raf binding to MEK2 via its kinase domain is shown in PMID:11909642), so mitogen-activated protein kinase kinase kinase binding (GO:0031435) is the informative replacement. Proposed replacements: mitogen-activated protein kinase kinase kinase binding Supporting Evidence: PMID:11909642 A-Raf was identified as a novel partner that interacts with MEK2 |
| GO:0005515 protein binding | IPI PMID:11909642 Identification of interaction between MEK2 and A-Raf-1. | MODIFY | Summary: IPI for MAP2K2 binding ARAF, an upstream MAP kinase kinase kinase that phosphorylates and activates MEK in the RAF-MEK-ERK cascade (PMID:11909642). Reason: Bare protein binding is uninformative. The partner ARAF is a MAPKKK that directly binds and phosphorylates MAP2K2 (A-Raf binding to MEK2 via its kinase domain is shown in PMID:11909642), so mitogen-activated protein kinase kinase kinase binding (GO:0031435) is the informative replacement. Proposed replacements: mitogen-activated protein kinase kinase kinase binding Supporting Evidence: PMID:11909642 A-Raf was identified as a novel partner that interacts with MEK2 |
| GO:0005515 protein binding | IPI PMID:11909642 Identification of interaction between MEK2 and A-Raf-1. | MODIFY | Summary: IPI for MAP2K2 binding KSR1, the RAF-MEK-ERK scaffold protein (PMID:11909642). MEK binding to KSR releases KSR autoinhibition and promotes KSR-BRAF dimerization (PMID:29433126). Reason: Bare protein binding is uninformative. The partner KSR1 is a MAPK-pathway scaffold, so scaffold protein binding (GO:0097110) is the informative replacement, consistent with the accepted GO:0097110 annotations on this gene. Proposed replacements: scaffold protein binding |
| GO:0005515 protein binding | IPI PMID:17979178 A novel tandem affinity purification strategy for the effici... | MODIFY | Summary: IPI for MAP2K2 binding BRAF, an upstream MAP kinase kinase kinase that phosphorylates and activates MEK in the RAF-MEK-ERK cascade (PMID:17979178). Reason: Bare protein binding is uninformative. The partner BRAF is a MAPKKK that directly binds and phosphorylates MAP2K2 (A-Raf binding to MEK2 via its kinase domain is shown in PMID:11909642), so mitogen-activated protein kinase kinase kinase binding (GO:0031435) is the informative replacement. Proposed replacements: mitogen-activated protein kinase kinase kinase binding |
| GO:0005515 protein binding | IPI PMID:21615688 Identification of mitogen-activated protein/extracellular si... | MODIFY | Summary: IPI for MAP2K2 binding hDlg/SAP97 (DLG1): identified by yeast two-hybrid, confirmed by co-IP of endogenous proteins, and mapped to DLG1 PDZ domain 2 and the MEK2 C-terminal RTAV motif; DLG1 binds MEK2 but not MEK1. Reason: Bare protein binding is uninformative. The paper shows the interaction is between the MAP2K2 C-terminal PDZ-binding motif and a PDZ domain of the scaffold protein DLG1, so PDZ domain binding (GO:0030165) and scaffold protein binding (GO:0097110) are the informative replacements. Proposed replacements: PDZ domain binding scaffold protein binding Supporting Evidence: PMID:21615688 we identified mitogen-activated protein/extracellular signal-responsive kinase (ERK) kinase (MEK)2, a member of the ERK cascade, as an hDlg binding partner PMID:21615688 hDlg acts as a MEK2-specific scaffold protein for the ERK signaling pathway |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | MODIFY | Summary: IPI for MAP2K2 binding RAF1 (CRAF), an upstream MAP kinase kinase kinase that phosphorylates and activates MEK in the RAF-MEK-ERK cascade (PMID:21988832). Reason: Bare protein binding is uninformative. The partner RAF1 (CRAF) is a MAPKKK that directly binds and phosphorylates MAP2K2 (A-Raf binding to MEK2 via its kinase domain is shown in PMID:11909642), so mitogen-activated protein kinase kinase kinase binding (GO:0031435) is the informative replacement. Proposed replacements: mitogen-activated protein kinase kinase kinase binding |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | MODIFY | Summary: IPI for MAP2K2 binding ARAF, an upstream MAP kinase kinase kinase that phosphorylates and activates MEK in the RAF-MEK-ERK cascade (PMID:21988832). Reason: Bare protein binding is uninformative. The partner ARAF is a MAPKKK that directly binds and phosphorylates MAP2K2 (A-Raf binding to MEK2 via its kinase domain is shown in PMID:11909642), so mitogen-activated protein kinase kinase kinase binding (GO:0031435) is the informative replacement. Proposed replacements: mitogen-activated protein kinase kinase kinase binding |
| GO:0005515 protein binding | IPI PMID:24746704 Disruption of CRAF-mediated MEK activation is required for e... | MODIFY | Summary: IPI for MAP2K2 binding RAF1 (CRAF), an upstream MAP kinase kinase kinase that phosphorylates and activates MEK in the RAF-MEK-ERK cascade (PMID:24746704). Reason: Bare protein binding is uninformative. The partner RAF1 (CRAF) is a MAPKKK that directly binds and phosphorylates MAP2K2 (A-Raf binding to MEK2 via its kinase domain is shown in PMID:11909642), so mitogen-activated protein kinase kinase kinase binding (GO:0031435) is the informative replacement. Proposed replacements: mitogen-activated protein kinase kinase kinase binding Supporting Evidence: PMID:24746704 Similar effects were observed when MEK2 was expressed with KRAS or BRAF (Figure S4B). |
| GO:0005515 protein binding | IPI PMID:24746704 Disruption of CRAF-mediated MEK activation is required for e... | MODIFY | Summary: IPI for MAP2K2 binding ARAF, an upstream MAP kinase kinase kinase that phosphorylates and activates MEK in the RAF-MEK-ERK cascade (PMID:24746704). Reason: Bare protein binding is uninformative. The partner ARAF is a MAPKKK that directly binds and phosphorylates MAP2K2 (A-Raf binding to MEK2 via its kinase domain is shown in PMID:11909642), so mitogen-activated protein kinase kinase kinase binding (GO:0031435) is the informative replacement. Proposed replacements: mitogen-activated protein kinase kinase kinase binding Supporting Evidence: PMID:24746704 Similar effects were observed when MEK2 was expressed with KRAS or BRAF (Figure S4B). |
| GO:0005515 protein binding | IPI PMID:24746704 Disruption of CRAF-mediated MEK activation is required for e... | MODIFY | Summary: IPI for MAP2K2 binding BRAF, an upstream MAP kinase kinase kinase that phosphorylates and activates MEK in the RAF-MEK-ERK cascade (PMID:24746704). Reason: Bare protein binding is uninformative. The partner BRAF is a MAPKKK that directly binds and phosphorylates MAP2K2 (A-Raf binding to MEK2 via its kinase domain is shown in PMID:11909642), so mitogen-activated protein kinase kinase kinase binding (GO:0031435) is the informative replacement. Proposed replacements: mitogen-activated protein kinase kinase kinase binding Supporting Evidence: PMID:24746704 Similar effects were observed when MEK2 was expressed with KRAS or BRAF (Figure S4B). |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: High-throughput interactome IPI for MAP2K2 binding CCNDBP1 (PMID:25416956); no functional characterization of the interaction is reported. Reason: Bare protein binding carries no functional information, and the screen provides no basis for a more informative MF term for this partner. Removal reflects only the lack of functional information in the bare GO:0005515 term; it does not mean the reported interaction is false. |
| GO:0005515 protein binding | IPI PMID:25600339 Tunable-combinatorial mechanisms of acquired resistance limi... | MODIFY | Summary: IPI for MAP2K2 binding BRAF, an upstream MAP kinase kinase kinase that phosphorylates and activates MEK in the RAF-MEK-ERK cascade (PMID:25600339). Reason: Bare protein binding is uninformative. The partner BRAF is a MAPKKK that directly binds and phosphorylates MAP2K2 (A-Raf binding to MEK2 via its kinase domain is shown in PMID:11909642), so mitogen-activated protein kinase kinase kinase binding (GO:0031435) is the informative replacement. Proposed replacements: mitogen-activated protein kinase kinase kinase binding |
| GO:0005515 protein binding | IPI PMID:25852190 Integrative analysis of kinase networks in TRAIL-induced apo... | MODIFY | Summary: IPI for MAP2K2 binding ARAF, an upstream MAP kinase kinase kinase that phosphorylates and activates MEK in the RAF-MEK-ERK cascade (PMID:25852190). Reason: Bare protein binding is uninformative. The partner ARAF is a MAPKKK that directly binds and phosphorylates MAP2K2 (A-Raf binding to MEK2 via its kinase domain is shown in PMID:11909642), so mitogen-activated protein kinase kinase kinase binding (GO:0031435) is the informative replacement. Proposed replacements: mitogen-activated protein kinase kinase kinase binding |
| GO:0005515 protein binding | IPI PMID:27086506 HiQuant: Rapid Postquantification Analysis of Large-Scale MS... | MODIFY | Summary: IPI for MAP2K2 binding KSR1, the RAF-MEK-ERK scaffold protein (PMID:27086506). MEK binding to KSR releases KSR autoinhibition and promotes KSR-BRAF dimerization (PMID:29433126). Reason: Bare protein binding is uninformative. The partner KSR1 is a MAPK-pathway scaffold, so scaffold protein binding (GO:0097110) is the informative replacement, consistent with the accepted GO:0097110 annotations on this gene. Proposed replacements: scaffold protein binding |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | MODIFY | Summary: IPI for MAP2K2 binding BRAF, an upstream MAP kinase kinase kinase that phosphorylates and activates MEK in the RAF-MEK-ERK cascade (PMID:28514442). Reason: Bare protein binding is uninformative. The partner BRAF is a MAPKKK that directly binds and phosphorylates MAP2K2 (A-Raf binding to MEK2 via its kinase domain is shown in PMID:11909642), so mitogen-activated protein kinase kinase kinase binding (GO:0031435) is the informative replacement. Proposed replacements: mitogen-activated protein kinase kinase kinase binding |
| GO:0005515 protein binding | IPI PMID:29433126 MEK drives BRAF activation through allosteric control of KSR... | MODIFY | Summary: IPI for MAP2K2 binding BRAF, an upstream MAP kinase kinase kinase that phosphorylates and activates MEK in the RAF-MEK-ERK cascade (PMID:29433126). Reason: Bare protein binding is uninformative. The partner BRAF is a MAPKKK that directly binds and phosphorylates MAP2K2 (A-Raf binding to MEK2 via its kinase domain is shown in PMID:11909642), so mitogen-activated protein kinase kinase kinase binding (GO:0031435) is the informative replacement. Proposed replacements: mitogen-activated protein kinase kinase kinase binding |
| GO:0005515 protein binding | IPI PMID:29433126 MEK drives BRAF activation through allosteric control of KSR... | MODIFY | Summary: IPI for MAP2K2 binding KSR1, the RAF-MEK-ERK scaffold protein (PMID:29433126). MEK binding to KSR releases KSR autoinhibition and promotes KSR-BRAF dimerization (PMID:29433126). Reason: Bare protein binding is uninformative. The partner KSR1 is a MAPK-pathway scaffold, so scaffold protein binding (GO:0097110) is the informative replacement, consistent with the accepted GO:0097110 annotations on this gene. Proposed replacements: scaffold protein binding |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: IPI for MAP2K2 binding RAF1 (CRAF), an upstream MAP kinase kinase kinase that phosphorylates and activates MEK in the RAF-MEK-ERK cascade (PMID:31980649). Reason: Bare protein binding is uninformative. The partner RAF1 (CRAF) is a MAPKKK that directly binds and phosphorylates MAP2K2 (A-Raf binding to MEK2 via its kinase domain is shown in PMID:11909642), so mitogen-activated protein kinase kinase kinase binding (GO:0031435) is the informative replacement. Proposed replacements: mitogen-activated protein kinase kinase kinase binding |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: IPI for MAP2K2 binding ARAF, an upstream MAP kinase kinase kinase that phosphorylates and activates MEK in the RAF-MEK-ERK cascade (PMID:31980649). Reason: Bare protein binding is uninformative. The partner ARAF is a MAPKKK that directly binds and phosphorylates MAP2K2 (A-Raf binding to MEK2 via its kinase domain is shown in PMID:11909642), so mitogen-activated protein kinase kinase kinase binding (GO:0031435) is the informative replacement. Proposed replacements: mitogen-activated protein kinase kinase kinase binding |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: IPI for MAP2K2 binding BRAF, an upstream MAP kinase kinase kinase that phosphorylates and activates MEK in the RAF-MEK-ERK cascade (PMID:31980649). Reason: Bare protein binding is uninformative. The partner BRAF is a MAPKKK that directly binds and phosphorylates MAP2K2 (A-Raf binding to MEK2 via its kinase domain is shown in PMID:11909642), so mitogen-activated protein kinase kinase kinase binding (GO:0031435) is the informative replacement. Proposed replacements: mitogen-activated protein kinase kinase kinase binding |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: IPI for MAP2K2 binding KSR1, the RAF-MEK-ERK scaffold protein (PMID:31980649). MEK binding to KSR releases KSR autoinhibition and promotes KSR-BRAF dimerization (PMID:29433126). Reason: Bare protein binding is uninformative. The partner KSR1 is a MAPK-pathway scaffold, so scaffold protein binding (GO:0097110) is the informative replacement, consistent with the accepted GO:0097110 annotations on this gene. Proposed replacements: scaffold protein binding |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | MODIFY | Summary: IPI for MAP2K2 binding MOS, an upstream MAP kinase kinase kinase that phosphorylates and activates MEK in the RAF-MEK-ERK cascade (PMID:32296183). Reason: Bare protein binding is uninformative. The partner MOS is a MAPKKK that directly binds and phosphorylates MAP2K2 (A-Raf binding to MEK2 via its kinase domain is shown in PMID:11909642), so mitogen-activated protein kinase kinase kinase binding (GO:0031435) is the informative replacement. Proposed replacements: mitogen-activated protein kinase kinase kinase binding |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: High-throughput interactome IPI for MAP2K2 binding HNRNPK (isoform 2) (PMID:32296183); no functional characterization of the interaction is reported. Reason: Bare protein binding carries no functional information, and the screen provides no basis for a more informative MF term for this partner. Removal reflects only the lack of functional information in the bare GO:0005515 term; it does not mean the reported interaction is false. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | MODIFY | Summary: Binary Y2H IPI (HuRI, PMID:32296183) with UniProtKB:Q96II5, which UniProt's interaction table identifies as an ARAF entry. Reason: Bare protein binding is uninformative. The partner is an ARAF product, a MAP3K that binds and phosphorylates MEK2 (A-Raf/MEK2 binding is independently shown in PMID:11909642), so mitogen-activated protein kinase kinase kinase binding (GO:0031435) is the informative replacement, consistent with the other ARAF rows. Proposed replacements: mitogen-activated protein kinase kinase kinase binding Supporting Evidence: PMID:11909642 A-Raf was identified as a novel partner that interacts with MEK2 |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | MODIFY | Summary: IPI for MAP2K2 binding RAF1 (CRAF), an upstream MAP kinase kinase kinase that phosphorylates and activates MEK in the RAF-MEK-ERK cascade (PMID:32707033). Reason: Bare protein binding is uninformative. The partner RAF1 (CRAF) is a MAPKKK that directly binds and phosphorylates MAP2K2 (A-Raf binding to MEK2 via its kinase domain is shown in PMID:11909642), so mitogen-activated protein kinase kinase kinase binding (GO:0031435) is the informative replacement. Proposed replacements: mitogen-activated protein kinase kinase kinase binding |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | MODIFY | Summary: IPI for MAP2K2 binding ARAF, an upstream MAP kinase kinase kinase that phosphorylates and activates MEK in the RAF-MEK-ERK cascade (PMID:32707033). Reason: Bare protein binding is uninformative. The partner ARAF is a MAPKKK that directly binds and phosphorylates MAP2K2 (A-Raf binding to MEK2 via its kinase domain is shown in PMID:11909642), so mitogen-activated protein kinase kinase kinase binding (GO:0031435) is the informative replacement. Proposed replacements: mitogen-activated protein kinase kinase kinase binding |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | MODIFY | Summary: IPI for MAP2K2 binding BRAF, an upstream MAP kinase kinase kinase that phosphorylates and activates MEK in the RAF-MEK-ERK cascade (PMID:32707033). Reason: Bare protein binding is uninformative. The partner BRAF is a MAPKKK that directly binds and phosphorylates MAP2K2 (A-Raf binding to MEK2 via its kinase domain is shown in PMID:11909642), so mitogen-activated protein kinase kinase kinase binding (GO:0031435) is the informative replacement. Proposed replacements: mitogen-activated protein kinase kinase kinase binding |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | MODIFY | Summary: IPI for MAP2K2 binding KSR1, the RAF-MEK-ERK scaffold protein (PMID:32707033). MEK binding to KSR releases KSR autoinhibition and promotes KSR-BRAF dimerization (PMID:29433126). Reason: Bare protein binding is uninformative. The partner KSR1 is a MAPK-pathway scaffold, so scaffold protein binding (GO:0097110) is the informative replacement, consistent with the accepted GO:0097110 annotations on this gene. Proposed replacements: scaffold protein binding |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: High-throughput interactome IPI for MAP2K2 binding APP (PMID:32814053); no functional characterization of the interaction is reported. Reason: Bare protein binding carries no functional information, and the screen provides no basis for a more informative MF term for this partner. Removal reflects only the lack of functional information in the bare GO:0005515 term; it does not mean the reported interaction is false. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:O96018. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | MODIFY | Summary: IPI for MAP2K2 binding BRAF, an upstream MAP kinase kinase kinase that phosphorylates and activates MEK in the RAF-MEK-ERK cascade (PMID:33961781). Reason: Bare protein binding is uninformative. The partner BRAF is a MAPKKK that directly binds and phosphorylates MAP2K2 (A-Raf binding to MEK2 via its kinase domain is shown in PMID:11909642), so mitogen-activated protein kinase kinase kinase binding (GO:0031435) is the informative replacement. Proposed replacements: mitogen-activated protein kinase kinase kinase binding |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | MODIFY | Summary: IPI for MAP2K2 binding RAF1 (CRAF), an upstream MAP kinase kinase kinase that phosphorylates and activates MEK in the RAF-MEK-ERK cascade (PMID:35271311). Reason: Bare protein binding is uninformative. The partner RAF1 (CRAF) is a MAPKKK that directly binds and phosphorylates MAP2K2 (A-Raf binding to MEK2 via its kinase domain is shown in PMID:11909642), so mitogen-activated protein kinase kinase kinase binding (GO:0031435) is the informative replacement. Proposed replacements: mitogen-activated protein kinase kinase kinase binding |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | MODIFY | Summary: IPI for MAP2K2 binding ARAF, an upstream MAP kinase kinase kinase that phosphorylates and activates MEK in the RAF-MEK-ERK cascade (PMID:35271311). Reason: Bare protein binding is uninformative. The partner ARAF is a MAPKKK that directly binds and phosphorylates MAP2K2 (A-Raf binding to MEK2 via its kinase domain is shown in PMID:11909642), so mitogen-activated protein kinase kinase kinase binding (GO:0031435) is the informative replacement. Proposed replacements: mitogen-activated protein kinase kinase kinase binding |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | MODIFY | Summary: IPI for MAP2K2 binding KSR1, the RAF-MEK-ERK scaffold protein (PMID:35271311). MEK binding to KSR releases KSR autoinhibition and promotes KSR-BRAF dimerization (PMID:29433126). Reason: Bare protein binding is uninformative. The partner KSR1 is a MAPK-pathway scaffold, so scaffold protein binding (GO:0097110) is the informative replacement, consistent with the accepted GO:0097110 annotations on this gene. Proposed replacements: scaffold protein binding |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | MODIFY | Summary: IPI for MAP2K2 binding BRAF, an upstream MAP kinase kinase kinase that phosphorylates and activates MEK in the RAF-MEK-ERK cascade (PMID:35512704). Reason: Bare protein binding is uninformative. The partner BRAF is a MAPKKK that directly binds and phosphorylates MAP2K2 (A-Raf binding to MEK2 via its kinase domain is shown in PMID:11909642), so mitogen-activated protein kinase kinase kinase binding (GO:0031435) is the informative replacement. Proposed replacements: mitogen-activated protein kinase kinase kinase binding |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:A4D2P6. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:O00560. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:O15018. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:O75970. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:O95049. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:O96018. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:P78352. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:Q07157. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:Q12923. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:Q12959. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:Q14005. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:Q14160. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:Q15599. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:Q15700. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:Q5T2W1. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:Q5TCQ9. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:Q68DX3. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:Q6ZMN7. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:Q70Z35. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:Q86UL8. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:Q86UT5. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:Q8N448. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:Q8NI35. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:Q8TDM6. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:Q8TEW0. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:Q8TEW8. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:Q92796. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:Q96QZ7. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:Q99767. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:Q9C0E4. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:Q9H190. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:Q9H5P4. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:Q9P202. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:Q9UDY2. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:Q9UPQ7. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:Q9Y3R0. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: IPI for MAP2K2 binding the PDZ-domain protein UniProtKB:Q9Y6N9. PMID:36115835 is a holdup-assay affinity map of human PDZ domains against C-terminal PDZ-binding motifs (PBMs); MAP2K2 carries a C-terminal class I PBM (RTAV) that is known to engage PDZ domains (PMID:21615688). Reason: Bare protein binding is uninformative. The partner is a PDZ-domain protein and the interaction is mediated by the MAP2K2 C-terminal PDZ-binding motif, so PDZ domain binding (GO:0030165) is the informative replacement. This is a peptide/domain-level affinity measurement and is not a core function of MAP2K2. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:36115835 covering ~55% of the interactomic space defined by the 266 human PDZ-domains and the 448 human and viral PBMs |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: InterPro IEA for ATP binding. Reason: MAP2K2 has the canonical kinase glycine-rich loop and Lys101 ATP-binding site; ATP binding is correct and as precise as warranted, but it is a cofactor-level property subsumed by the core kinase activity. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt FT /ligand="ATP" file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr |
| GO:0005576 extracellular region | NAS PMID:8388392 Cloning and characterization of two distinct human extracell... | REMOVE | Summary: NAS 'extracellular region' attributed to the MEK1/MEK2 cloning paper (PMID:8388392). Reason: The cited abstract describes intracellular cascade biochemistry only; the 'extracellular' wording comes from the name 'extracellular signal-regulated kinase' (ERK), the substrate. MEK2 has no signal peptide or transmembrane segment and is a cytosolic kinase. This NAS is a non-experimental name-derived assignment and is demonstrably not a location of the protein. Supporting Evidence: PMID:8388392 MEK (MAP kinase or ERK kinase) is the immediate upstream activator kinase of ERK file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane |
| GO:0005634 nucleus | TAS PMID:19565474 The ERK signaling cascade--views from different subcellular ... | KEEP AS NON CORE | Summary: TAS nucleus from a review of ERK-cascade compartmentalization (PMID:19565474). Reason: MEK1/2 can enter the nucleus transiently but are kept predominantly cytoplasmic by an N-terminal nuclear export signal; nuclear residence is minor relative to the cytosolic pool. Kept, non-core. Supporting Evidence: PMID:19565474 we discuss the intracellular localizations of different components of the ERK cascade file:human/MAP2K2/MAP2K2-deep-research-falcon.md Its nuclear-export sequence favors cytoplasmic localization. |
| GO:0005737 cytoplasm | EXP PMID:10409742 Kinase suppressor of Ras forms a multiprotein signaling comp... | MODIFY | Summary: Cytoplasm (UniProt EXP from PMID:10409742 fractionation; SubCell IEA). Reason: Correct but general. The soluble pool of MEK2 is cytosolic (HPA IDA and many Reactome TAS rows for cytosol in this review), and the remainder is membrane-associated through scaffolds (kept separately as membrane). Refine to cytosol (GO:0005829). Proposed replacements: cytosol Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane PMID:10409742 KSR-MEK binding shifts the apparent molecular mass of MEK from 44 to >700 kDa, and this results in the appearance of MEK in membrane-associated fractions |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | MODIFY | Summary: Cytoplasm (UniProt EXP from PMID:10409742 fractionation; SubCell IEA). Reason: Correct but general. The soluble pool of MEK2 is cytosolic (HPA IDA and many Reactome TAS rows for cytosol in this review), and the remainder is membrane-associated through scaffolds (kept separately as membrane). Refine to cytosol (GO:0005829). Proposed replacements: cytosol Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane PMID:10409742 KSR-MEK binding shifts the apparent molecular mass of MEK from 44 to >700 kDa, and this results in the appearance of MEK in membrane-associated fractions |
| GO:0005739 mitochondrion | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Mitochondrion from the ARBA rule ARBA00026962 (IEA); a minor, stimulus-dependent MEK2 pool at the mitochondria is reported in primary rodent studies. Reason: ORGANELLES check (2026-11-03), previously UNDECIDED. The ARBA rule ARBA00026962 is a multi-condition-set association rule, pooling condition sets from unrelated families (MEK matches the IPR000719 plus IPR050915 MAP kinase kinase set in Euarchontoglires), that carries no evidence of its own and is presumably learned from existing mitochondrion annotations such as the parallel TAS row, so it is not used as support here. The organelle claim is supported at the level of MEK1/2 by two primary studies from the Poderoso group. In mouse LP07 lung tumour cells, mitochondrial subfractionation (fraction identity checked with complex I, VDAC1, SOD2 and COX VIc antibodies) placed MEK1/2 with ERK1/2 in the outer-membrane and intermembrane-space fractions (PMID:18545666), and phospho-MEK1/2 was detected in rat brain mitochondria whose ERK1/2 sat in the outer membrane/intermembrane space fraction (PMID:15030409, abstract-only). Caveats that keep this non-core and at the root: both studies used MEK1/2 antibodies that do not separate MAP2K2 from its paralog, neither reports an ER marker for the mitochondrial fraction (only the IMS subfraction argues against ER/MAM carry-over), and the pool is a transient signalling association with the ERK module (TRAF3/BRAF precedent for recruited kinases). MEK2 has no transit peptide or membrane anchor, and the sub-mitochondrial data split between outer membrane and IMS, so no sub-compartment row is added. The main MEK2 locations (cytoplasm, membrane via KSR1, nucleus) are captured elsewhere in this review. Supporting Evidence: PMID:18545666 mitochondrial subfractionation showed that MAPKs colocalized with their cognates MEK1/2, MKK3 and MKK4 in the mitochondrial outer membrane and in the intermembrane space PMID:18545666 LP07 cell line was derived from P07 lung tumor spontaneously arisen in a BALB/c mouse PMID:15030409 upstream phospho-MAPK/ERK kinases (MEK1/2) were also PMID:15030409 outer membrane/intermembrane space fraction |
| GO:0005739 mitochondrion | TAS PMID:19565474 The ERK signaling cascade--views from different subcellular ... | KEEP AS NON CORE | Summary: Mitochondrion (TAS) from the Yao and Seger review of ERK-cascade compartments (abstract-only here); a minor, stimulus-dependent MEK2 pool at the mitochondria is reported in primary rodent studies. Reason: ORGANELLES check (2026-11-03), previously UNDECIDED. The TAS source PMID:19565474 is a review whose cached text is abstract-only and does not name the mitochondrion, so the row is judged on the primary papers it summarises. The organelle claim is supported at the level of MEK1/2 by two primary studies from the Poderoso group. In mouse LP07 lung tumour cells, mitochondrial subfractionation (fraction identity checked with complex I, VDAC1, SOD2 and COX VIc antibodies) placed MEK1/2 with ERK1/2 in the outer-membrane and intermembrane-space fractions (PMID:18545666), and phospho-MEK1/2 was detected in rat brain mitochondria whose ERK1/2 sat in the outer membrane/intermembrane space fraction (PMID:15030409, abstract-only). Caveats that keep this non-core and at the root: both studies used MEK1/2 antibodies that do not separate MAP2K2 from its paralog, neither reports an ER marker for the mitochondrial fraction (only the IMS subfraction argues against ER/MAM carry-over), and the pool is a transient signalling association with the ERK module (TRAF3/BRAF precedent for recruited kinases). MEK2 has no transit peptide or membrane anchor, and the sub-mitochondrial data split between outer membrane and IMS, so no sub-compartment row is added. The main MEK2 locations (cytoplasm, membrane via KSR1, nucleus) are captured elsewhere in this review. Supporting Evidence: PMID:18545666 mitochondrial subfractionation showed that MAPKs colocalized with their cognates MEK1/2, MKK3 and MKK4 in the mitochondrial outer membrane and in the intermembrane space PMID:18545666 LP07 cell line was derived from P07 lung tumor spontaneously arisen in a BALB/c mouse PMID:15030409 upstream phospho-MAPK/ERK kinases (MEK1/2) were also PMID:15030409 outer membrane/intermembrane space fraction |
| GO:0005769 early endosome | IEA GO_REF:0000117 | UNDECIDED | Summary: early endosome (TAS from review PMID:19565474; ARBA IEA). Reason: Endosomal MEK/ERK signalling is well described, but the best-characterised endosomal adaptor (LAMTOR3/MP1) was reported as MEK1-selective, so MEK1/2-level statements may not transfer to MEK2. The review's full text is not available to check what it says about MEK2 specifically, and the ARBA rows are unvetted. Left UNDECIDED pending MEK2-specific evidence. Supporting Evidence: PMID:19565474 we discuss the intracellular localizations of different components of the ERK cascade |
| GO:0005769 early endosome | TAS PMID:19565474 The ERK signaling cascade--views from different subcellular ... | UNDECIDED | Summary: early endosome (TAS from review PMID:19565474; ARBA IEA). Reason: Endosomal MEK/ERK signalling is well described, but the best-characterised endosomal adaptor (LAMTOR3/MP1) was reported as MEK1-selective, so MEK1/2-level statements may not transfer to MEK2. The review's full text is not available to check what it says about MEK2 specifically, and the ARBA rows are unvetted. Left UNDECIDED pending MEK2-specific evidence. Supporting Evidence: PMID:19565474 we discuss the intracellular localizations of different components of the ERK cascade |
| GO:0005770 late endosome | IEA GO_REF:0000117 | UNDECIDED | Summary: late endosome (TAS from review PMID:19565474; ARBA IEA). Reason: Endosomal MEK/ERK signalling is well described, but the best-characterised endosomal adaptor (LAMTOR3/MP1) was reported as MEK1-selective, so MEK1/2-level statements may not transfer to MEK2. The review's full text is not available to check what it says about MEK2 specifically, and the ARBA rows are unvetted. Left UNDECIDED pending MEK2-specific evidence. Supporting Evidence: PMID:19565474 we discuss the intracellular localizations of different components of the ERK cascade |
| GO:0005770 late endosome | TAS PMID:19565474 The ERK signaling cascade--views from different subcellular ... | UNDECIDED | Summary: late endosome (TAS from review PMID:19565474; ARBA IEA). Reason: Endosomal MEK/ERK signalling is well described, but the best-characterised endosomal adaptor (LAMTOR3/MP1) was reported as MEK1-selective, so MEK1/2-level statements may not transfer to MEK2. The review's full text is not available to check what it says about MEK2 specifically, and the ARBA rows are unvetted. Left UNDECIDED pending MEK2-specific evidence. Supporting Evidence: PMID:19565474 we discuss the intracellular localizations of different components of the ERK cascade |
| GO:0005778 peroxisomal membrane | HDA PMID:21525035 PEX14 is required for microtubule-based peroxisome motility ... | MARK AS OVER ANNOTATED | Summary: HDA: MEK2 among proteins co-purified with Protein-A-tagged PEX14 from digitonin-solubilised membranes (PMID:21525035). Reason: A single proteomic co-purification with a peroxisomal membrane bait is the only support; the paper's conclusions concern peroxins and tubulin, and no MEK2 function at peroxisomes is known. Likely an abundant cytosolic kinase recovered non-specifically; over-annotation rather than a demonstrated location. Supporting Evidence: PMID:21525035 Using mass spectrometric analysis, almost all known human peroxins involved in protein import were identified as constituents of the PEX14 complexes |
| GO:0005783 endoplasmic reticulum | IDA PMID:21615688 Identification of mitogen-activated protein/extracellular si... | UNDECIDED | Summary: IDA endoplasmic reticulum from the DLG1-MEK2 study (PMID:21615688). Reason: The abstract attributes ER and microtubule association to hDlg in VSMCs; whether MEK2 itself was shown at these structures is in the full text, which is not available. MeSH indexing (Endoplasmic Reticulum/enzymology, Microtubules/enzymology) suggests the curator read MEK2 colocalization there, so this is not removed, but it cannot be verified. Supporting Evidence: PMID:21615688 Additionally, hDlg also associates with the endoplasmic reticulum and microtubules in these latter cells |
| GO:0005794 Golgi apparatus | IDA PMID:21615688 Identification of mitogen-activated protein/extracellular si... | UNDECIDED | Summary: Golgi apparatus (IDA, PMID:21615688). Reason: Golgi-associated MEK/ERK signalling has been reported, chiefly for MEK1, and Reactome models MAP2K phosphorylation of MAPK at the Golgi membrane at the MAP2K-class level. The Golgi result is not described in the cached abstracts of either source, and their full texts are unavailable. Supporting Evidence: PMID:21615688 Confocal microscopy suggested a colocalization of the two proteins at the inner layer of the plasma membrane of confluent human embryonic kidney 293 cells, and in a perinuclear area in human VSMCs |
| GO:0005794 Golgi apparatus | TAS PMID:19565474 The ERK signaling cascade--views from different subcellular ... | UNDECIDED | Summary: Golgi apparatus (TAS, PMID:19565474). Reason: Golgi-associated MEK/ERK signalling has been reported, chiefly for MEK1, and Reactome models MAP2K phosphorylation of MAPK at the Golgi membrane at the MAP2K-class level. The Golgi result is not described in the cached abstracts of either source, and their full texts are unavailable. Supporting Evidence: PMID:19565474 we discuss the intracellular localizations of different components of the ERK cascade |
| GO:0005829 cytosol | IDA GO_REF:0000052 | ACCEPT | Summary: Cytosol (IDA, GO_REF:0000052). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane |
| GO:0005829 cytosol | TAS PMID:19565474 The ERK signaling cascade--views from different subcellular ... | ACCEPT | Summary: Cytosol (TAS, PMID:19565474). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: PMID:19565474 we discuss the intracellular localizations of different components of the ERK cascade file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane |
| GO:0005829 cytosol | TAS Reactome:R-HSA-109858 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-109858). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-109858 In the cytoplasm phosphorylated MAP2K2 (MEK2) may encounter monomeric, inactive MAPK1 (ERK2) |
| GO:0005829 cytosol | TAS Reactome:R-HSA-109862 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-109862). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-109862 MAP2K2 (MEK2) phosphorylates MAPK1 (ERK2) |
| GO:0005829 cytosol | TAS Reactome:R-HSA-109864 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-109864). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-109864 MAP2K2 (MEK2) dissociates from phosphorylated MAPK1 (ERK2), allowing activated MAPK1 (ERK2) to dimerise (Zheng and Guang 1994). |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5211356 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-5211356). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-5211356 lef (Anthrax LF, lethal factor) a zinc metalloprotease (Klimpel et al, 1994) in the target cell cytosol, cleaves MAP2K2 (MEK2, mitogen activated protein kinase kinase 2) |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5672972 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-5672972). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-5672972 RAF kinases have restricted substrate specificity and have as their primary substrates the two MAP2K proteins MAP2K1 and MAP2K2 (also known as MEK1 and 2) |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5672973 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-5672973). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-5672973 Activated MAP2K phosphorylates MAPK on threonine and tyrosine residues in the activation loop (residues T202 and Y204 in MAPK3, residues T185 and Y187 in MAPK1) (Ray et al, 1988; reviewed in Roskoski, 2012b) |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5672978 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-5672978). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-5672978 Activated RAF phosphorylates the MEK kinases MAP2K1 and MAP2K2 on 2 serine residues in the MAP2K activation loop (S218 and S222 in MAP2K1 and S222 and S226 in MAP2K2 (Zheng and Guan, 1994; Alessi et al, 1994; Catling et al, 1995; Papin et al, 1995; Seger et al, 1994; reviewed in Roskoski, 2012a) |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5672980 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-5672980). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-5672980 The mechanisms governing the dissociation or trafficking of activated MAPK signaling complexes at the plasma membrane are not fully worked out |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5674130 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-5674130). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-5674130 Interaction of MAPK pathway components with LAMTOR2, 3 and MORG1 facilitates pathway activation in response to varied stimuli, resulting in the phosphorylation of MAP2K and MAPK proteins at conserved sites in their activation loops (Schaeffer et al, 1998; Teis et al, 2002; Teis et al, 2006; Vomastek et al, 2004; Sharma et al, 2005; reviewed in Matallanas et al, 2011). |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5674132 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-5674132). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-5674132 LAMTOR3 (also known as MEK partner 1, MP1) exists in an obligatory complex with LAMTOR2 (p14) at the endosomal membrane where they act as a scaffold and promote MAPK activation (Schaeffer et al, 1998; Teis et al, 2002; Teis et al, 2006; Sharma et al, 2005) |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5674366 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-5674366). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-5674366 IL17RD, also known as SEF (similar expression to FGF), was identified as a negative regulator of nuclear MAPK signaling (Tsang et al, 2002; Furthauer et al, 2002) |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5674373 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-5674373). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-5674373 Activated MAP2Ks in complex with IL17RD phosphorylate MAPKs at the Golgi membrane |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5674496 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-5674496). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-5674496 Activated MAPK proteins negatively regulate MAP2K1:MAP2K2 heterodimers by phosphorylating MAP2K1 at T292, a residue that is not present in MAP2K2 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6802910 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-6802910). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-6802910 Highly active BRAF mutants show constitutive phosphorylation of MAPKs that does not depend on RAS activation or RAF dimerization (Davies et al, 2002; Wan et al, 2004; Garnett et al, 2005; reveiwed in Lavoie and Therrien, 2015). |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6802911 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-6802911). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-6802911 Highly active BRAF mutants such as V600E are constitutively active and phosphorylate MAP2Ks in a RAS- and dimer interface-independent manner (Davies et al, 2002; Wan et al, 2004; Garnett et al, 2005; Roring et al, 2012; Poulikakos et al, 2010; reviewed in Lavoie and Therrien, 2015). |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6802912 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-6802912). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-6802912 High-kinase activity BRAF mutants such as the prevalent V600E mutant bind MAP2K and MAPK proteins to activate signaling in a constitutive, RAS-independent manner (Wan et al, 2004; Garnett et al, 2005; Ritt et al, 2010; Roring et al, 2012; Freeman et al, 2013; reviewed in Lavoie and Therrien, 2015) |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6802914 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-6802914). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-6802914 RAF dimerization and phosphorylation downstream of moderately activating BRAF mutations is associated with increased MAP2K and MAPK phosphorylation (Wan et al, 2004; Freeman et al, 2013; Roring et al, 2012; reviewed in Holderfield et al, 2014; Lavoie and Therrien, 2015) |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6802918 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-6802918). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-6802918 Downstream of kinase-dead or inhibited forms of BRAF, activated MAP2K phosphorylates MAPK on threonine and tyrosine residues in the activation loop (Wan et al, 2004; Garnett et al, 2005; Heidorn et al, 2010; Poulikakos et al, 2010; Hatzivassilliou et al, 2010; reviewed in Samatar and Poulikakos, 2014; Lavoie and Therrien, 2015). |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6802919 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-6802919). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-6802919 Recruitment of MAP2Ks and MAPKs downstream of moderately activated BRAF mutants leads to phosphorylation and activation of MAP2Ks, as in the WT pathway (Wan et al, 2004; Freeman et al, 2013; Roring et al, 2012; reviewed in Lavoie and Therrien, 2015). |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6802921 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-6802921). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-6802921 MAPKs are phosphorylated downstream of moderately activated BRAF mutants in a MAP2K-dependent manner (Wan et al, 2004; Roring et al, 2012; Freeman et al, 2013; reviewed in Lavoie and Therrien, 2015). |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6802922 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-6802922). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-6802922 MAPK proteins are phosphorylated downstream of oncogenic RAS mutants; somewhat surprisingly, however, steady state levels of phospho-MAP2K and phospho-MAPKs are not always elevated in cancer cells (reviewed in Ramos, 2008; Neuzillet et al, 2014; Stephen et al, 2014). |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6802925 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-6802925). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-6802925 RAF dimerization and phosphorylation downstream of oncogenic RAS and RAF mutations is associated with increased MAP2K and MAPK phosphorylation (Wan et al, 2004; Garnett et al, 2005; reviewed in Holderfield et al, 2014) |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6802926 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-6802926). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-6802926 MAP2K proteins are phosphorylated downstream of oncogenic RAS mutants; somewhat surprisingly, however, steady state levels of phospho-MAP2K and phospho-MAPKs are not always elevated in cancer cells (reviewed in Ramos, 2008; Neuzillet et al, 2014; Stephen et al, 2014). |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6802932 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-6802932). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-6802932 After phosphorylation by MAP2Ks, the scaffolded kinase complex assembled by BRAF and RAF fusion dimers presumably dissociates, as is the case for WT complexes (Jones et al, 2008; Cin et al, 2011; Palanisamy et al, 2010; Ciampi et al, 2005; Stransky et al, 2014; Hutchinson et al, 2013; Zhang et al, 2013; Lee et al, 2012; Ricarte-Filho et al, 2013; reviewed in Lavoie and Therrien et al, 2015). |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6802933 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-6802933). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-6802933 BRAF and RAF fusion dimers constitutively phosphorylate MAP2Ks (Jones et al, 2008; Cin et al, 2011; Palanisamy et al, 2010; Ciampi et al, 2005; Stransky et al, 2014; Hutchinson et al, 2013; Zhang et al, 2013; Lee et al, 2012; Ricarte-Filho et al, 2013; reviewed in Lavoie and Therrien et al, 2015). |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6802934 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-6802934). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-6802934 BRAF and RAF fusion proteins expressed in cancer constitutively activate downstream signaling and promote cellular transformation (Jones et al, 2008; Cin et al, 2011; Palanisamy et al, 2010; Ciampi et al, 2005; Stransky et al, 2014; Hutchinson et al, 2013; Zhang et al, 2013; Lee et al, 2012; Ricarte-Filho et al, 2013; reviewed in Lavoie and Therrien et al, 2015) |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6802935 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-6802935). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-6802935 MAPKs are phosphorylated downstream of constitutively active BRAF and RAF fusion proteins (Jones et al, 2008; Cin et al, 2011; Palanisamy et al, 2010; Ciampi et al, 2005; Stransky et al, 2014; Hutchinson et al, 2013; Zhang et al, 2013; Lee et al, 2012; Ricarte-Filho et al, 2013; reviewed in Lavoie and Therrien et al, 2015). |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6802942 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-6802942). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-6802942 Dimerization of kinase-dead or inhibited versions of BRAF to RAF1/CRAF leads to the recruitment and phosphorylation of MAP2Ks and MAPKs (Wan et al, 2004; Garnett et al, 2005; Heidorn et al, 2010; Poulikakos et al, 2010; Hatzivassiliou et al, 2010; reviewed in Samatar and Poulikakos, 2014; Lavoie and Therrien, 2015) |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6802943 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-6802943). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-6802943 As in the WT pathway, activation of ERK signaling downstream of kinase-dead or inhibited forms of BRAF depends on phosphorylation of two serine residues in the activation loop of the MAP2K proteins (Wan et al, 2004; Garnett et al, 2005; Heidorn et al, 2010; Poulikakos et al, 2010; Hatzivassiliou et al, 2010; reviewed in Samatar and Poulikakos, 2014; Lavoie and Therrien, 2015). |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6803227 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-6803227). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-6803227 After phosphorylation by MAP2Ks, the scaffolded kinase complex assembled by highly active BRAF mutants dissociates, as is the case for WT complexes (reviewed in Lavoie and Therrien et al, 2015). |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6803230 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-6803230). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-6803230 After phosphorylation by MAP2Ks, the scaffolded kinase complex assembled by moderately active BRAF mutants dissociates, as is the case for WT complexes (reviewed in Lavoie and Therrien et al, 2015). |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6803233 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-6803233). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-6803233 After phosphorylation by MAP2Ks, the scaffolded kinase complex assembled by oncogenic RAS presumably dissociates, as is the case for WT complexes (reviewed in Lavoie and Therrien et al, 2015; Stephen et al, 2014). |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6803234 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-6803234). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-6803234 After phosphorylation by MAP2Ks, the scaffolded kinase complex assembled by kinase dead or inhibited BRAF mutants dissociates, as is the case for WT complexes (reviewed in Lavoie and Therrien et al, 2015). |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9610152 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-9610152). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-9610152 Downstream of NGF stimulation and RAP1 activation, BRAF recruits MAP2Ks and MAPKs to the endosome to promote sustained RAF/MAPK signaling (York et al, 1998; reviewed in Reichardt, 2006; Barford et al, 2017). |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9610153 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-9610153). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-9610153 Downstream of NGF stimulation, activated BRAF phosphorylates MAP2K1 and MAP2K2 (MEK1 and MEK2) at the endosome, leading to sustained MAPK signaling (York et al, 1998; Kao et al, 2001; reviewed in Huang and Reichardt, 2003; Reichardt, 2006). |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9610154 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-9610154). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-9610154 The mechanisms governing dissocation of activated signaling complexes downstream of NGF and RAP1 stimulation are not fully worked out, however phosphorylated MAPK dimers are known to phosphorylate cytosolic and nuclear targets that promote neuronal gene expression and differentiation (Nguyen et al, 1993; reviewed in Vaudry et al, 2002; Santiago and Bashaw, 2014). |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9610156 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-9610156). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-9610156 Activated MAP2K1 and MAP2K2 dimers phosphorylate MAPK1 and MAPK3 downstream of NGF stimulation and RAP1 activation at the endosome (Kao et al, 2001; Wu et al, 2001; reviewed in Huang and Reichardt, 2003; Reichardt, 2006). |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9652165 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-9652165). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-9652165 Although they occur at much lower frequently than mutations in upstream components of the RAS signaling pathway, activating mutations in MAP2K proteins, encoding MEK1 and MEK2, have been identified in a number of cancers and germline disorders (Marks et al, 2008; Murugan et al, 2009) |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9656209 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-9656209). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-9656209 After phosphorylation of MAPKs by complexes containing RAF1 mutants, activated MAPK signaling complexes dissociate in a manner similar to wildtype, although this has not been explicitly demonstrated in all cases |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9656211 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-9656211). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-9656211 MAP2K and MAPK proteins are likely recruited to complexes containing mutant versions of RAF1 proteins, analagous to the wild type pathway, although this has not been explicitly demonstrated in all cases (reviewed in Rauen, 2013). |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9656214 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-9656214). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-9656214 MAPK proteins are phosphorylated downstream of RAF1 mutants (Razzaque et al, 2007; Pandit et al, 2007; Kobayashi et al, 2010; Wu et al, 2012). |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9656215 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-9656215). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-9656215 MAPK2Ks are phosphorylated downstream of mutant RAF1 proteins (Razzaque et al, 2007; Pandit et al, 2007; Kobayashi et al, 2010; Wu et al, 2012). |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9657599 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-9657599). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-9657599 Although mutations in MAP2K proteins are infrequent in human cancers, the position of these kinases downstream of RAS and RAF make them good candidates for therapeutic targeting |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9657603 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-9657603). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-9657603 A number of 'dual mechanism' MAPK inhibitors are in preclinical or clinical trials (reviewed in Roskoski, 2019) |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9657606 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-9657606). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-9657606 Single mechanism MAP2K inhibitors bind to phosphorylated forms of MAP2K 1 and 2 and prevent their phosphorylation of MAPK proteins (Hatzivassiliou et al, 2013; reviewed in Samatar and Poulikakos, 2014). |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9657608 | ACCEPT | Summary: Cytosol (TAS, Reactome:R-HSA-9657608). Reason: MEK2 is a soluble cytoplasmic kinase (UniProt; HPA immunofluorescence) whose activation by RAF and phosphorylation of ERK1/2 occur on the cytosolic face of membranes and in the cytosol, as modelled in the Reactome reactions. Core location. Supporting Evidence: Reactome:R-HSA-9657608 Single mechanism MAPK inhibitors such as ulixertinib and ravoxertinib bind to the activated forms of MAPK proteins and inhibit their intrinsic target-directed kinase activity (Germann et al, 2017; Blake et al, 2016; reviewed in Samatar and Poulikakos, 2014). |
| GO:0005874 microtubule | IDA PMID:21615688 Identification of mitogen-activated protein/extracellular si... | UNDECIDED | Summary: IDA microtubule from the DLG1-MEK2 study (PMID:21615688). Reason: The abstract attributes ER and microtubule association to hDlg in VSMCs; whether MEK2 itself was shown at these structures is in the full text, which is not available. MeSH indexing (Endoplasmic Reticulum/enzymology, Microtubules/enzymology) suggests the curator read MEK2 colocalization there, so this is not removed, but it cannot be verified. Supporting Evidence: PMID:21615688 Additionally, hDlg also associates with the endoplasmic reticulum and microtubules in these latter cells |
| GO:0005911 cell-cell junction | IDA PMID:21615688 Identification of mitogen-activated protein/extracellular si... | UNDECIDED | Summary: IDA cell-cell junction (PMID:21615688). Reason: DLG1 is a junctional MAGUK and the abstract reports MEK2-DLG1 colocalization at the inner plasma membrane of confluent HEK293 cells, which may underlie this annotation, but a junction-specific MEK2 localization is not stated in the abstract and the full text is unavailable. Supporting Evidence: PMID:21615688 Confocal microscopy suggested a colocalization of the two proteins at the inner layer of the plasma membrane of confluent human embryonic kidney 293 cells, and in a perinuclear area in human VSMCs |
| GO:0005925 focal adhesion | IEA GO_REF:0000117 | UNDECIDED | Summary: Focal adhesion (TAS from review PMID:19565474; ARBA IEA). Reason: ERK-module components are recruited to focal adhesions, but MEK2-specific evidence is not visible in the cached abstract and the full text is unavailable; ARBA is an unvetted prediction. Supporting Evidence: PMID:19565474 we discuss the intracellular localizations of different components of the ERK cascade |
| GO:0005925 focal adhesion | TAS PMID:19565474 The ERK signaling cascade--views from different subcellular ... | UNDECIDED | Summary: Focal adhesion (TAS from review PMID:19565474; ARBA IEA). Reason: ERK-module components are recruited to focal adhesions, but MEK2-specific evidence is not visible in the cached abstract and the full text is unavailable; ARBA is an unvetted prediction. Supporting Evidence: PMID:19565474 we discuss the intracellular localizations of different components of the ERK cascade |
| GO:0009898 cytoplasmic side of plasma membrane | IDA PMID:21615688 Identification of mitogen-activated protein/extracellular si... | KEEP AS NON CORE | Summary: IDA cytoplasmic side of plasma membrane: MEK2 colocalizes with DLG1 at the inner layer of the plasma membrane in confluent HEK293 cells (PMID:21615688). Reason: Directly stated for MEK2 in the abstract; consistent with scaffold-mediated membrane recruitment. A context-dependent pool, non-core. Supporting Evidence: PMID:21615688 Confocal microscopy suggested a colocalization of the two proteins at the inner layer of the plasma membrane of confluent human embryonic kidney 293 cells, and in a perinuclear area in human VSMCs |
| GO:0010628 positive regulation of gene expression | IMP PMID:24375836 MiR-92a mediates AZD6244 induced apoptosis and G1-phase arre... | MARK AS OVER ANNOTATED | Summary: IMP positive regulation of gene expression from a lymphoma study using the MEK1/2 inhibitor AZD6244 (PMID:24375836). Reason: The experiment shows that inhibiting MEK1/2 lowers miR-92a via ERK1/2-AP1. Changes in gene expression and transcription are downstream outputs of ERK and AP-1; MEK2 does no part of the transcriptional work. The inhibitor is also not MEK2-selective. These are indirect consequences of the ERK cascade rather than MEK2 process participation. Supporting Evidence: PMID:24375836 AZD6244, an ATP-uncompetitive inhibitor of mitogen-activated protein kinase 1/2 (MEK1/2) PMID:24375836 Downregulation of miR-92a by AZD6244 is mediated by the ERK1/2-AP1 signalling pathway |
| GO:0016020 membrane | EXP PMID:10409742 Kinase suppressor of Ras forms a multiprotein signaling comp... | KEEP AS NON CORE | Summary: Membrane (UniProt EXP from PMID:10409742; SubCell IEA). KSR binding moves MEK into membrane-associated fractions. Reason: The fractionation experiment supports membrane association but not a specific membrane, so 'membrane' is as precise as this evidence allows. MEK2 is a peripheral, scaffold-recruited membrane protein; the predominant pool is cytosolic, so this is non-core. Supporting Evidence: PMID:10409742 KSR-MEK binding shifts the apparent molecular mass of MEK from 44 to >700 kDa, and this results in the appearance of MEK in membrane-associated fractions file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane |
| GO:0016020 membrane | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Membrane (UniProt EXP from PMID:10409742; SubCell IEA). KSR binding moves MEK into membrane-associated fractions. Reason: The fractionation experiment supports membrane association but not a specific membrane, so 'membrane' is as precise as this evidence allows. MEK2 is a peripheral, scaffold-recruited membrane protein; the predominant pool is cytosolic, so this is non-core. Supporting Evidence: PMID:10409742 KSR-MEK binding shifts the apparent molecular mass of MEK from 44 to >700 kDa, and this results in the appearance of MEK in membrane-associated fractions file:human/MAP2K2/MAP2K2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10409742}. Membrane |
| GO:0030165 PDZ domain binding | IDA PMID:21615688 Identification of mitogen-activated protein/extracellular si... | KEEP AS NON CORE | Summary: IDA PDZ domain binding: the MEK2 C-terminal RTAV motif binds DLG1 PDZ2 (PMID:21615688). Reason: The class I PDZ-binding motif at the MEK2 C terminus (absent from MEK1) is experimentally mapped and is confirmed by the PDZ-domain holdup map (PMID:36115835). It is a MEK2-specific targeting property, peripheral to the catalytic core function. Supporting Evidence: PMID:21615688 the C-terminal sequence RTAV of MEK2 in this interaction |
| GO:0032872 regulation of stress-activated MAPK cascade | IEA GO_REF:0000117 | MARK AS OVER ANNOTATED | Summary: Regulation of stress-activated MAPK cascade (TAS from review PMID:19565474; ARBA IEA). Reason: MEK2 is an ERK-specific MAP2K; the stress-activated (JNK/p38) cascades use MAP2K3/4/6/7. Any effect of MEK2 on stress-activated signalling would be indirect crosstalk, and no MEK2-specific experiment is cited. Likely an over-annotation. Supporting Evidence: PMID:19565474 we discuss the intracellular localizations of different components of the ERK cascade file:human/MAP2K2/MAP2K2-uniprot.txt CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF |
| GO:0032872 regulation of stress-activated MAPK cascade | TAS PMID:19565474 The ERK signaling cascade--views from different subcellular ... | MARK AS OVER ANNOTATED | Summary: Regulation of stress-activated MAPK cascade (TAS from review PMID:19565474; ARBA IEA). Reason: MEK2 is an ERK-specific MAP2K; the stress-activated (JNK/p38) cascades use MAP2K3/4/6/7. Any effect of MEK2 on stress-activated signalling would be indirect crosstalk, and no MEK2-specific experiment is cited. Likely an over-annotation. Supporting Evidence: PMID:19565474 we discuss the intracellular localizations of different components of the ERK cascade file:human/MAP2K2/MAP2K2-uniprot.txt CC Activates the ERK1 and ERK2 MAP kinases (By similarity). Activates BRAF |
| GO:0036289 peptidyl-serine autophosphorylation | IDA PMID:8388392 Cloning and characterization of two distinct human extracell... | KEEP AS NON CORE | Summary: IDA peptidyl-serine autophosphorylation for recombinant MEK2 (PMID:8388392). Reason: The cached abstract does not describe the autophosphorylation assay, but the paper characterised purified recombinant MEK2 kinase activity and the curator read the full text; recombinant MEKs are known to autophosphorylate weakly. Deferred to the curator and kept as a non-core biochemical property; physiological activation is by RAF trans-phosphorylation of Ser222/Ser226. Supporting Evidence: PMID:8388392 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 | IDA PMID:8388392 Cloning and characterization of two distinct human extracell... | MODIFY | Summary: Protein serine/threonine kinase activator activity (IDA, PMID:8388392; IEA ARBA). Reason: The cited experiment shows MEK2 activating ERK1 by phosphorylating it. That is the catalytic activity MAP kinase kinase activity (GO:0004708); 'kinase activator activity' is intended for non-catalytic regulators that bind and activate a kinase, and using it for the upstream kinase of a cascade duplicates the MF. The KSR1-dependent BRAF activation described in PMID:29433126 is handled under the MAP kinase scaffold activity rows. Proposed replacements: MAP kinase kinase activity Supporting Evidence: PMID:8388392 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 | MODIFY | Summary: Protein serine/threonine kinase activator activity (IDA, PMID:8388392; IEA ARBA). Reason: The cited experiment shows MEK2 activating ERK1 by phosphorylating it. That is the catalytic activity MAP kinase kinase activity (GO:0004708); 'kinase activator activity' is intended for non-catalytic regulators that bind and activate a kinase, and using it for the upstream kinase of a cascade duplicates the MF. The KSR1-dependent BRAF activation described in PMID:29433126 is handled under the MAP kinase scaffold activity rows. Proposed replacements: MAP kinase kinase activity Supporting Evidence: PMID:8388392 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... | MARK AS OVER ANNOTATED | Summary: IMP positive regulation of DNA-templated transcription from a lymphoma study using the MEK1/2 inhibitor AZD6244 (PMID:24375836). Reason: The experiment shows that inhibiting MEK1/2 lowers miR-92a via ERK1/2-AP1. Changes in gene expression and transcription are downstream outputs of ERK and AP-1; MEK2 does no part of the transcriptional work. The inhibitor is also not MEK2-selective. These are indirect consequences of the ERK cascade rather than MEK2 process participation. Supporting Evidence: PMID:24375836 AZD6244, an ATP-uncompetitive inhibitor of mitogen-activated protein kinase 1/2 (MEK1/2) PMID:24375836 Downregulation of miR-92a by AZD6244 is mediated by the ERK1/2-AP1 signalling pathway |
| GO:0048471 perinuclear region of cytoplasm | IDA PMID:21615688 Identification of mitogen-activated protein/extracellular si... | KEEP AS NON CORE | Summary: IDA perinuclear region of cytoplasm: MEK2-DLG1 colocalization in a perinuclear area of VSMCs (PMID:21615688). Reason: Stated for the two proteins in the abstract; a cell-type-specific pool, non-core. Supporting Evidence: PMID:21615688 Confocal microscopy suggested a colocalization of the two proteins at the inner layer of the plasma membrane of confluent human embryonic kidney 293 cells, and in a perinuclear area in human VSMCs |
| GO:0070371 ERK1 and ERK2 cascade | IMP PMID:24375836 MiR-92a mediates AZD6244 induced apoptosis and G1-phase arre... | ACCEPT | Summary: IMP ERK1 and ERK2 cascade (PMID:24375836): MEK1/2 inhibition suppresses ERK1/2 signalling to AP-1. Reason: MEK2 is a direct participant (the MAP2K tier) of the ERK1/ERK2 cascade. This inhibitor-based row is weak on paralog specificity but the claim is strongly supported by direct biochemistry and Reactome. Supporting Evidence: PMID:24375836 Downregulation of miR-92a by AZD6244 is mediated by the ERK1/2-AP1 signalling pathway PMID:8388392 The purified MEK2 protein stimulated threonine and tyrosine phosphorylation on ERK1 and concomitantly activated ERK1 kinase activity more than 100-fold |
| GO:0070371 ERK1 and ERK2 cascade | TAS Reactome:R-HSA-112411 | ACCEPT | Summary: Reactome TAS: MAPK1 (ERK2) activation pathway. Reason: Core process: MEK2 phosphorylates and activates ERK1 and ERK2. Supporting Evidence: Reactome:R-HSA-109862 MAP2K2 (MEK2) phosphorylates MAPK1 (ERK2). Phosphorylation of MAPK1 activates its kinase activity. PMID:8388392 The purified MEK2 protein stimulated threonine and tyrosine phosphorylation on ERK1 and concomitantly activated ERK1 kinase activity more than 100-fold |
| GO:0071902 positive regulation of protein serine/threonine kinase activity | IDA PMID:8388392 Cloning and characterization of two distinct human extracell... | MODIFY | Summary: IDA positive regulation of protein serine/threonine kinase activity: MEK2 activated ERK1 >100-fold (PMID:8388392). Reason: Correct but general; the regulated kinase is a MAP kinase (ERK1). Refine to positive regulation of MAP kinase activity (GO:0043406), an is_a child of this term. Proposed replacements: positive regulation of MAP kinase activity Supporting Evidence: PMID:8388392 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: Regulation of Golgi inheritance (TAS from review PMID:19565474; ARBA IEA). Reason: Mitotic Golgi fragmentation via MEK/ERK has been reported mainly for MEK1; whether MEK2 contributes is not visible in the cached abstract, the full text is unavailable, and the ARBA row is unvetted. Supporting Evidence: PMID:19565474 we discuss the intracellular localizations of different components of the ERK cascade |
| GO:0090170 regulation of Golgi inheritance | TAS PMID:19565474 The ERK signaling cascade--views from different subcellular ... | UNDECIDED | Summary: Regulation of Golgi inheritance (TAS from review PMID:19565474; ARBA IEA). Reason: Mitotic Golgi fragmentation via MEK/ERK has been reported mainly for MEK1; whether MEK2 contributes is not visible in the cached abstract, the full text is unavailable, and the ARBA row is unvetted. Supporting Evidence: PMID:19565474 we discuss the intracellular localizations of different components of the ERK cascade |
| GO:0097110 scaffold protein binding | IEA GO_REF:0000117 | ACCEPT | Summary: ARBA IEA for scaffold protein binding. Reason: MAP2K2 binds the ERK-module scaffolds KSR1 (PMID:10409742, PMID:29433126) and DLG1/SAP97 (PMID:21615688). Scaffold binding positions MEK2 for activation by RAF and controls its localization; it is part of how the core function is executed. Supporting Evidence: PMID:10409742 Both nematode and mammalian KSRs are capable of binding to MEKs PMID:21615688 hDlg acts as a MEK2-specific scaffold protein for the ERK signaling pathway |
| GO:0097110 scaffold protein binding | IPI PMID:10409742 Kinase suppressor of Ras forms a multiprotein signaling comp... | ACCEPT | Summary: IPI with KSR1: KSR forms a >700 kDa complex containing MEK1 and MEK2 (PMID:10409742). Reason: KSR1 is the archetypal ERK-pathway scaffold and binds MEK directly; binding shifts MEK into membrane-associated fractions. Consistent with PMID:29433126. Supporting Evidence: PMID:10409742 Both nematode and mammalian KSRs are capable of binding to MEKs PMID:10409742 KSR-MEK binding shifts the apparent molecular mass of MEK from 44 to >700 kDa, and this results in the appearance of MEK in membrane-associated fractions |
| GO:0097110 scaffold protein binding | IPI PMID:21615688 Identification of mitogen-activated protein/extracellular si... | ACCEPT | Summary: IPI with DLG1 (hDlg/SAP97), mapped to DLG1 PDZ2 and the MEK2 C-terminal RTAV (PMID:21615688). Reason: DLG1 is a MAGUK scaffold that binds MEK2 but not MEK1; the paper proposes it as a MEK2-specific ERK-pathway scaffold. Supporting Evidence: PMID:21615688 hDlg acts as a MEK2-specific scaffold protein for the ERK signaling pathway PMID:21615688 the C-terminal sequence RTAV of MEK2 in this interaction |
| GO:0106310 protein serine kinase activity | EXP PMID:10409742 Kinase suppressor of Ras forms a multiprotein signaling comp... | MODIFY | Summary: Protein serine kinase activity from the UniProt Rhea mapping (EXP, PMID:10409742) and Rhea IEA. Reason: The serine-phosphorylation Rhea reaction is an artefact of splitting the EC 2.7.12.2 reaction into residue types; MEK2's substrate residues are the Thr and Tyr of the ERK TEY motif. MAP kinase kinase activity (GO:0004708) is the correct specific term. Proposed replacements: MAP kinase kinase activity Supporting Evidence: PMID:8388392 The purified MEK2 protein stimulated threonine and tyrosine phosphorylation on ERK1 and concomitantly activated ERK1 kinase activity more than 100-fold |
| GO:0106310 protein serine kinase activity | IEA GO_REF:0000116 | MODIFY | Summary: Protein serine kinase activity from the UniProt Rhea mapping (EXP, PMID:10409742) and Rhea IEA. Reason: The serine-phosphorylation Rhea reaction is an artefact of splitting the EC 2.7.12.2 reaction into residue types; MEK2's substrate residues are the Thr and Tyr of the ERK TEY motif. MAP kinase kinase activity (GO:0004708) is the correct specific term. Proposed replacements: MAP kinase kinase activity Supporting Evidence: PMID:8388392 The purified MEK2 protein stimulated threonine and tyrosine phosphorylation on ERK1 and concomitantly activated ERK1 kinase activity more than 100-fold |
| GO:2000641 regulation of early endosome to late endosome transport | IEA GO_REF:0000117 | UNDECIDED | Summary: Regulation of early endosome to late endosome transport (TAS from review PMID:19565474; ARBA IEA). Reason: Endosomal maturation effects of the ERK module are linked mainly to the LAMTOR3/MP1-MEK1 complex; MEK2-specific evidence is not visible in the cached abstract and the full text is unavailable. Supporting Evidence: PMID:19565474 we discuss the intracellular localizations of different components of the ERK cascade |
| 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 endosome to late endosome transport (TAS from review PMID:19565474; ARBA IEA). Reason: Endosomal maturation effects of the ERK module are linked mainly to the LAMTOR3/MP1-MEK1 complex; MEK2-specific evidence is not visible in the cached abstract and the full text is unavailable. Supporting Evidence: PMID:19565474 we discuss the intracellular localizations of different components of the ERK cascade |
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Download this section (compressed HTML)Q: MEK binding to KSR1 drives KSR1-BRAF heterodimerization and BRAF activation (PMID:29433126). Is GO:0005078 MAP kinase scaffold activity the intended term for this non-catalytic 'activator MEK' role, or should GO add a term for allosteric promotion of RAF dimerization?
Q: Which of the review-derived MEK2 localizations (mitochondrion, endosomes, Golgi, focal adhesion) rest on MEK2-specific data rather than MEK1 or pan-MEK antibodies?
Experiment: Paralog-specific localization of endogenously tagged MEK2 versus MEK1 (e.g. knock-in tags with organelle markers) to test the endosomal, Golgi and mitochondrial assignments, and the contribution of the MEK2-specific C-terminal PDZ-binding motif.
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