Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Combined Automated Annotation using Multiple IEA Methods
Dissection of the structural organization of the aminoacyl-tRNA synthetase complex.
AIMP2/p38, the scaffold for the multi-tRNA synthetase complex, responds to genotoxic stresses via p53.
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AIMP2 dissociates from MSC upon DNA damage and translocates to nucleus
"Upon DNA damage, AIMP2 was phosphorylated, dissociated from the multi-tRNA synthetase complex, and translocated into the nuclei of cells"
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AIMP2 directly binds p53 and prevents MDM2-mediated ubiquitination
"AIMP2 directly interacts with p53, thereby preventing MDM2-mediated ubiquitination and degradation of p53"
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AIMP2 is a proapoptotic factor via p53 in response to DNA damage
"Depletion of AIMP2 increased resistance to DNA damage-induced apoptosis"
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Mutations affecting p53 interaction impair proapoptotic function
"Mutations in AIMP2, affecting its interaction with p53, hampered its ability to activate p53"
3-Dimensional architecture of the human multi-tRNA synthetase complex.
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Human MSC architecture was modeled using cross-linking mass spectrometry and structural information.
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AIMP2 contributes structural contacts within the complex; exact native oligomer stoichiometry is not settled by the model.
Dynamic Organization of Aminoacyl-tRNA Synthetase Complexes in the Cytoplasm of Human Cells.
Structural switch of lysyl-tRNA synthetase between translation and transcription.
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The LysRS subcomplex structure identifies the AIMP2 N terminus as its MSC anchor.
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Ser207 phosphorylation changes LysRS conformation and mobilization; the kinase substrate and Ap4A-producing enzyme are LysRS.
Assembly of Multi-tRNA Synthetase Complex via Heterotetrameric Glutathione Transferase-homology Domains.
Reinvestigation of aminoacyl-tRNA synthetase core complex by affinity purification-mass spectrometry reveals TARSL2 as a potential member of the complex.
Defining the membrane proteome of NK cells.
Towards a proteome-scale map of the human protein-protein interaction network.
An empirical framework for binary interactome mapping.
Genome-wide YFP fluorescence complementation screen identifies new regulators for telomere signaling in human cells.
JTV1 co-activates FBP to induce USP29 transcription and stabilize p53 in response to oxidative stress.
Next-generation sequencing to generate interactome datasets.
Structural context for mobilization of a human tRNA synthetase from its cytoplasmic complex.
A directed protein interaction network for investigating intracellular signal transduction.
Toward an understanding of the protein interaction network of the human liver.
Global landscape of HIV-human protein complexes.
Chemical inhibition of prometastatic lysyl-tRNA synthetase-laminin receptor interaction.
A proteome-scale map of the human interactome network.
A human interactome in three quantitative dimensions organized by stoichiometries and abundances.
Widespread Expansion of Protein Interaction Capabilities by Alternative Splicing.
Pooled-matrix protein interaction screens using Barcode Fusion Genetics.
An inter-species protein-protein interaction network across vast evolutionary distance.
Architecture of the human interactome defines protein communities and disease networks.
An interactome perturbation framework prioritizes damaging missense mutations for developmental disorders.
LuTHy: a double-readout bioluminescence-based two-hybrid technology for quantitative mapping of protein-protein interactions in mammalian cells.
Mutations in KARS cause a severe neurological and neurosensory disease with optic neuropathy.
Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.
A reference map of the human binary protein interactome.
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.
MAPK-dependent phosphorylation of KARS
Cyberian deep research on AIMP2
Falcon deep research on AIMP2
OpenAI deep research on AIMP2
Perplexity deep research on AIMP2
Analysis of the 5' region of PMS2 reveals heterogeneous transcripts and a novel overlapping gene.
p38 is essential for the assembly and stability of macromolecular tRNA synthetase complex: implications for its physiological significance.
Downregulation of FUSE-binding protein and c-myc by tRNA synthetase cofactor p38 is required for lung cell differentiation
The p38 subunit of the aminoacyl-tRNA synthetase complex is a Parkin substrate: linking protein biosynthesis and neurodegeneration.
AIMP2 promotes TNFalpha-dependent apoptosis via ubiquitin-mediated degradation of TRAF2
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AIMP2 binds TRAF2 and augments its association with c-IAP1
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AIMP2 promotes ubiquitin-dependent TRAF2 degradation
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TNF-alpha-induced cell death is compromised in AIMP2-deficient cells
Aminoacyl-tRNA synthetase-interacting multifunctional proteins (AIMPs) - A triad for cellular homeostasis
Cancer-associated splicing variant of tumor suppressor AIMP2/p38: pathological implication in tumorigenesis.
Parthanatos Mediates AIMP2-Activated Age-Dependent Dopaminergic Neuronal Loss
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AIMP2 overexpression causes dopaminergic-neuron loss in mouse models.
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AIMP2 directly interacts with and stimulates PARP1 in the reported biochemical experiments.
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PARP1 deletion or inhibition protects in the tested AIMP2-dependent neurotoxicity models.
Oncogenic Mutation of AIMP2/p38 Inhibits Its Tumor-Suppressive Interaction with Smurf2.
AIMP2 Controls Intestinal Stem Cell Compartments and Tumorigenesis by Modulating Wnt/β-Catenin Signaling.
Dynamic landscape and regulation of RNA editing in mammals
The DRS-AIMP2-EPRS subcomplex acts as a pivot in the multi-tRNA synthetase complex
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The 3.6-angstrom DRS–AIMP2–EPRS structure uses a truncated DX2-derived AIMP2 construct.
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Substitutions at AIMP2 Ser156 impair DRS association, including both alanine and phosphomimetic substitutions.
Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer
Homozygosity for a nonsense variant in AIMP2 is associated with a progressive neurodevelopmental disorder with microcephaly, seizures, and spastic quadriparesis.
Human lysyl-tRNA synthetase evolves a dynamic structure that can be stabilized by forming complex.
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AIMP2 stabilizes human LysRS and protects its aminoacylation activity under the tested stress conditions.
"The interaction with AIMP2 stabilizes the closed conformation of LysRS, thereby protects the essential aminoacylation activity under stressed conditions."
Newly identified human aminoacyl-tRNA synthetase complex interacting multifunctional protein 2 (AIMP2) loss-of-function mutations cause neurodevelopmental defects linked to cell death in a zebrafish model.
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Patient-derived fibroblast AIMP2 mutations affect protein expression and synthesis; zebrafish disruption supplies separate developmental evidence.
"We show patient-derived fibroblast AIMP2 mutations cause decreased protein expression, attenuation of protein synthesis, and dysregulation of the MSC component, methionyl-tRNA synthetase (MARS1). CRISPR-mediated disruption of aimp2 in zebrafish led to increased cell death and atrophy in the developing brain, further supporting a link between AIMP2 dysfunction and neurodevelopmental defects."
Assembly of the Human Multi-tRNA Synthetase Complex Through Leucine Zipper Motifs.
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AIMP2 participates in a structurally characterized leucine-zipper assembly with AIMP1 and RARS1.
"Here, we determined a crystal structure of the LZ complex of AIMP1 and AIMP2 and revealed the interaction mode of a heterotrimeric complex of RARS1, AIMP1, and AIMP2."
AIMP2-DX2 provides therapeutic interface to control KRAS-driven tumorigenesis.
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In the tested CCD18CO expression comparison, DX2 increases KRAS protein abundance while full-length AIMP2 does not.
"The cells expressing DX2, but not AIMP2, increased the levels of both the wild-type (WT) and mutant forms of the KRAS, but not the N and H isoforms"
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The cellular stabilization difference does not establish that full-length AIMP2 cannot bind KRAS in vitro.
"AIMP2 showed similar binding ability to KRAS4B as DX2 in in vitro binding assays because it also contains the GST domain"
Knockdown of Golgi Stress-Responsive Caspase-2 Ameliorates HLD17-Associated AIMP2 Mutant-Mediated Inhibition of Oligodendroglial Cell Morphological Differentiation.
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The expressed Tyr35Ter mutant aggregates in Golgi bodies in a mouse oligodendroglial cell model.
"the HLD17-associated nonsense mutation (Tyr35-to-Ter [Y35X]) of AIMP2 localizes AIMP2 proteins as aggregates into the Golgi bodies in mouse oligodendroglial FBD-102b cells."
Interaction of NS2 with AIMP2 facilitates the switch from ubiquitination to SUMOylation of M1 in influenza A virus-infected cells.
Stepping Out of the Cytosol: AIMp1/p43 Potentiates the Link Between Innate and Adaptive Immunity.
Human lysyl-tRNA synthetase phosphorylation promotes HIV-1 proviral DNA transcription.
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An expressed, tagged AIMP2-N36 peptide suppresses HIV-1 replication in SupT1 cells; this is a peptide intervention rather than an assay of an endogenous full-length antiviral role.
"HIV-1 replication was suppressed in cells expressing the AIMP2-N36 peptide, compared with the EGFP control cells, as indicated by reduced Gag expression (Figure 3B)."
Bi-directional regulation of AIMP2 and its splice variant on PARP-1-dependent neuronal cell death; Therapeutic implication for Parkinson's disease.
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In the oxidative-stress human neuroblastoma comparison, full-length AIMP2 enhances PARylation whereas exon-2-skipped DX2 does not; this distinguishes regulation of PARP1 from AIMP2 catalytic activity.
"AIMP2 enhanced PARylation in the presence of H2O2, whereas DX2 had no effect (Fig. 2d)."
Identification and structure of AIMP2-DX2 for therapeutic perspectives.
AIMP2 restricts EV71 replication by recruiting SMURF2 to promote the degradation of 3D polymerase.
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In the transfected HEK293T ubiquitination assays, AIMP2 increases EV71 3D-polymerase ubiquitination through the reported K63 linkage rather than K48.
"The results suggest that AIMP2 can increase the ubiquitination of 3D polymerase via the K63 ubiquitin linkage but not the K48 ubiquitin linkage."
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AIMP2 supports recruitment of SMURF2 for EV71 3D-polymerase turnover; SMURF2 supplies the ligase activity. Pairwise interaction and reciprocal knockdown experiments support this context-specific mechanism.
"Taken together, these results demonstrate that AIMP2 recruits the E3 ligase SMURF2 to promote the degradation of 3D polymerase."