Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Automatic Gene Ontology annotation based on Rhea mapping
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Kinase suppressor of Ras forms a multiprotein signaling complex and modulates MEK localization.
Identification of interaction between MEK2 and A-Raf-1.
A novel tandem affinity purification strategy for the efficient isolation and characterisation of native protein complexes.
The ERK signaling cascade--views from different subcellular compartments.
PEX14 is required for microtubule-based peroxisome motility in human cells.
Identification of mitogen-activated protein/extracellular signal-responsive kinase kinase 2 as a novel partner of the scaffolding protein human homolog of disc-large.
Toward an understanding of the protein interaction network of the human liver.
MiR-92a mediates AZD6244 induced apoptosis and G1-phase arrest of lymphoma cells by targeting Bim.
Disruption of CRAF-mediated MEK activation is required for effective MEK inhibition in KRAS mutant tumors.
A proteome-scale map of the human interactome network.
Tunable-combinatorial mechanisms of acquired resistance limit the efficacy of BRAF/MEK cotargeting but result in melanoma drug addiction.
Integrative analysis of kinase networks in TRAIL-induced apoptosis provides a source of potential targets for combination therapy.
HiQuant: Rapid Postquantification Analysis of Large-Scale MS-Generated Proteomics Data.
Architecture of the human interactome defines protein communities and disease networks.
MEK drives BRAF activation through allosteric control of KSR proteins.
Extensive rewiring of the EGFR network in colorectal cancer cells expressing transforming levels of KRAS(G13D).
A reference map of the human binary protein interactome.
Kinase Interaction Network Expands Functional and Disease Roles of Human Kinases.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
OpenCell: Endogenous tagging for the cartography of human cellular organization.
Systematic discovery of mutation-directed neo-protein-protein interactions in cancer.
Quantitative fragmentomics allow affinity mapping of interactomes.
Cloning and characterization of two distinct human extracellular signal-regulated kinase activator kinases, MEK1 and MEK2.
MAP2K2 phosphorylates MAPK1
Dissociation of p-T,Y-MAPK1:p-S,T-MAP2K2
Anthrax lef cleaves target cell MAP2K2 (MEK2)
MAP2Ks and MAPKs bind to the activated RAF complex
MAP2Ks phosphorylate MAPKs
RAF phosphorylates MAP2K dimer
Dissociation of RAS:RAF complex
MAP2Ks and MAPKs are phosphorylated at the endosome membrane
WDR83:LAMTOR2:LAMTOR3 binds MAPK components
IL17RD binds p-2S MAP2Ks and MAPKs
MAP2Ks phosphorylate MAPK at the Golgi membrane
Activated MAPKs phosphorylate MAP2K1
Activated MAP2Ks phosphorylate MAPKs downstream of high kinase activity BRAF mutants
High kinase activity BRAF complexes phosphorylate MAP2Ks
High kinase activity BRAF mutants bind MAP2Ks and MAPKs
RAS:GTP:moderate kinase activity p-RAF complexes bind MAP2Ks and MAPKs
Activated MAP2Ks phosphorylate MAPKs downstream of inactive BRAF mutants
RAS:GTP:moderate kinase activity p-RAF complexes phosphorylate MAP2Ks
Activated MAP2Ks phosphorylate MAPKs downstream of moderate kinase activity BRAF mutants
Activated MAP2Ks phosphorylate MAPKs downstream of oncogenic RAS
Mutant RAS:p-RAF complexes bind MAP2Ks and MAPKs
Mutant RAS:p-RAF complexes phosphorylate MAP2Ks
Dissociation of BRAF/RAF fusion complex
p-BRAF and RAF fusion dimers phosphorylate MAP2Ks
p-BRAF and RAF fusion dimers bind MAP2Ks and MAPKs
MAPKs are phosphorylated downstream of BRAF and RAF fusion dimers
RAS:GTP:p-RAF complexes paradoxically bind MAP2Ks and MAPKs
RAS:GTP:inactive p-RAF complexes phosphorylate MAP2Ks
Dissociation of high activity BRAF complexes
Dissociation of moderate activity BRAF complexes
Dissociation of oncogenic RAS:RAF complex
Dissociation of paradoxically activated RAS:BRAF complexes
Activated BRAF recruits MAP2Ks and MAPKs to the endosome
Activated BRAF phosphorylates MAP2K dimers downstream of RAP1 and NGF
Dissociation of phosphorylated MAP2Ks and MAPKs
MAP2Ks phosphorylate MAPKs downstream of BRAF and NGF
MAP2K mutants constitutively phosphorylate MAPKs
Dissociation of RAS:RAF1 mutant complex
MAP2Ks and MAPKs bind to the activated mutant RAF1 complex
MAP2Ks phosphorylate MAPKs downstream of RAF1 mutants
RAF1 mutant complexes phosphorylate MAP2K dimer
Dual mechanism MAP2K inhibitors bind MAP2Ks
Dual mechanism MAPK inhibitors bind MAPKs
Single mechanism MAP2K inhibitors bind phosphorylated MAP2Ks
Single mechanism MAPK inhibitors bind phosphorylated MAPK
UniProt record for human MAP2K2