AIMP2

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0017101 aminoacyl-tRNA synthetase multienzyme complex	IBA GO_REF:0000033	ACCEPT	Summary: AIMP2 is an integral structural component of the cytosolic multisynthetase complex. Reason: The cached PTHR13438 PAINT record places the MSC IBD at PTN001412300 and includes human Q13155 in the family. The target experimental evidence legitimately contributes to that ancestral assertion. Human purification and component-depletion experiments independently show p38 joining MSC subassemblies. PMID:32644155 supplies cross-linking mass spectrometry and modeling, not a complete cryo-EM structure. No target-specific loss contradicts the inherited complex membership. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN001412300 SUPPORTS TRANSFER The cached PTHR13438 PAINT IBD assigns GO:0017101 at this node; the family member record includes Q13155. Human descendant evidence is legitimate experimental grounding, not circular support. The entire tree/MSA was not reconstructed. Supporting Evidence: PMID:19131329 with p38 connecting two subcomplexes that may form in the absence of p38
GO:0005634 nucleus	IEA GO_REF:0000120	KEEP AS NON CORE	Summary: AIMP2 can move from the cytoplasmic complex to the nucleus during stress responses. Reason: The combined automatic source includes mouse Q8R010/ENSMUSP00000031613 and the UniProt nuclear-location vocabulary. Independent human-cell studies support nuclear AIMP2 in genotoxic and oxidative stress responses (PMID:18695251; PMID:21285945). Retain the compartment as a conditional signaling location; the evidence does not imply constitutive nuclear residency or identify a direct JNK phosphorylation step. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:Q8R010 UNRESOLVED Mouse donor identity is established; its exact nuclear experimental chain was not recovered. Independent human stress-response studies support the target compartment. ensembl:ENSMUSP00000031613 UNRESOLVED This mouse protein is the Compara-linked donor record; source-level assay provenance is unresolved. UniProtKB-SubCell:SL-0191 SUPPORTS TRANSFER The nuclear-location mapping agrees with human AIMP2 stress-induced translocation. Supporting Evidence: PMID:18695251 Upon DNA damage, AIMP2 was phosphorylated, dissociated from the multi-tRNA synthetase complex, and translocated into the nuclei of cells PMID:21285945 translocates to the nucleus, associates with FBP and co-activates the transcription of a new FBP target, ubiquitin-specific peptidase 29 (USP29)
GO:0005829 cytosol	IEA GO_REF:0000044	ACCEPT	Summary: Cytosol is a principal compartment of the AIMP2-containing synthetase complex. Reason: The SL-0091 mapping agrees with the human-cell IDA assignment in PMID:19289464 and the cytosolic MSC reactions. Retain this broad source-level compartment without excluding the independently demonstrated nuclear pool. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB-SubCell:SL-0091 SUPPORTS TRANSFER The cytosol mapping agrees with human MSC localization and the source IDA assertion.
GO:0006412 translation	IEA GO_REF:0000043	ACCEPT	Summary: AIMP2 contributes structure to the aminoacylation machinery used in protein translation. Reason: The translation keyword mapping is consistent with structural participation: AIMP2 connects synthetase subassemblies and retains KARS1 in the MSC. GO:0006418 tRNA aminoacylation for protein translation is part_of GO:0006412 in the live ontology. A structural participant can therefore carry the broader process without itself catalyzing tRNA charging. Human complex dissection (PMID:19131329) and the KARS1 anchoring structure (PMID:23159739) support this role; neither asserts that AIMP2 is a ribosomal catalyst or universally required for growth in every culture condition. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB-KW:KW-0648 SUPPORTS TRANSFER The translation keyword is consistent with structural participation in tRNA aminoacylation, a part_of descendant of translation. Supporting Evidence: PMID:19131329 with p38 connecting two subcomplexes that may form in the absence of p38 PMID:23159739 The crystal structure of an MSC subcomplex established that LysRS is held in the MSC by binding to the N terminus of the scaffold protein p38/AIMP2
GO:0006915 apoptotic process	IEA GO_REF:0000043	MODIFY	Summary: AIMP2 promotes apoptosis through defined signaling mechanisms. Reason: The keyword-derived process is better represented by positive regulation of apoptotic process. Direct AIMP2–p53 binding prevents MDM2-mediated p53 degradation, and AIMP2 loss/rescue changes damage-induced apoptosis (PMID:18695251). A distinct TNF pathway study reports facilitation of TRAF2 association with c-IAP1 (PMID:19584093). These mechanisms support positive regulation without assigning AIMP2 caspase or ubiquitin-ligase catalysis. This is a contextual signaling function. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB-KW:KW-0053 SUPPORTS TRANSFER The apoptosis keyword captures a real positive signaling role; the human p53 and TRAF2 mechanisms justify the proposed regulatory refinement. Proposed replacements: positive regulation of apoptotic process Supporting Evidence: PMID:18695251 AIMP2 directly interacts with p53, thereby preventing MDM2-mediated ubiquitination and degradation of p53 PMID:18695251 Depletion of AIMP2 increased resistance to DNA damage-induced apoptosis, and introduction of AIMP2 into AIMP2-deficient cells restored the susceptibility to apoptosis
GO:0017101 aminoacyl-tRNA synthetase multienzyme complex	IEA GO_REF:0000120	ACCEPT	Summary: The combined automated sources assign AIMP2 to the multisynthetase complex. Reason: The aggregate source comprises an ARBA rule, rodent orthology records and the AIMP2 domain mapping. Human purification and knockdown experiments directly establish complex membership, so the target assertion is supported even though the internal evidence for every automated source has not been reconstructed. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00027195 UNRESOLVED The exact ARBA rule conditions and evidence internals were not retrieved; human MSC membership is independently established. UniProtKB:Q32PX2 UNRESOLVED Rat orthology source for MSC membership; the precise donor experiment was not reconstructed. ensembl:ENSRNOP00000001379 UNRESOLVED Rat Compara-linked protein source; donor experimental provenance unresolved. UniProtKB:Q8R010 UNRESOLVED Mouse orthology source; mouse knockout literature supports conserved MSC assembly, without reconstructing this exact annotation chain. ensembl:ENSMUSP00000031613 UNRESOLVED Mouse Compara-linked protein source; target support comes independently from human experiments. InterPro:IPR042360 SUPPORTS TRANSFER The AIMP2 domain/family mapping agrees with the human structural MSC role; it does not independently establish every signaling function. Supporting Evidence: PMID:19131329 with p38 connecting two subcomplexes that may form in the absence of p38
GO:0030154 cell differentiation	IEA GO_REF:0000043	KEEP AS NON CORE	Summary: AIMP2 contributes to differentiation in defined developmental and cellular contexts. Reason: The keyword annotation agrees with the mouse p38-null lung phenotype and FBP/c-MYC mechanism in PMID:12819782. Human-cell TGF-beta experiments separately support AIMP2-dependent FUBP1 regulation (PMID:27197155). These data support contextual differentiation participation, not a universal differentiation program or a direct human type II pneumocyte assay. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB-KW:KW-0221 SUPPORTS TRANSFER The differentiation keyword reflects context-dependent developmental evidence, including the mouse lung phenotype. No universal human differentiation mechanism is inferred. Supporting Evidence: PMID:12819782 Binding of p38 stimulated ubiquitination and degradation of FBP, leading to downregulation of c-myc
GO:0005515 protein binding	IPI PMID:16189514 Towards a proteome-scale map of the human protein-protein in...	REMOVE	Summary: The source records an interaction, but generic protein binding does not specify an AIMP2 function. Reason: The source is a proteome-scale human interaction map based on binary interaction screening. Remove the uninformative GO:0005515 term under the binding-curation policy. The available source does not resolve a more specific AIMP2 activity for this particular assertion. This judgment does not deny the interaction or infer nonbinding from an unrecovered pair-level supplementary record.
GO:0005515 protein binding	IPI PMID:18695251 AIMP2/p38, the scaffold for the multi-tRNA synthetase comple...	MODIFY	Summary: AIMP2 binds p53 and protects it from MDM2-dependent degradation. Reason: PMID:18695251 directly establishes a functionally consequential AIMP2–p53 contact during genotoxic stress. The specific p53-binding term captures that interaction. Competitive exclusion of MDM2 is not evidence that AIMP2 bridges p53 to MDM2, and the observed outcome is p53 stabilization and activation. Proposed replacements: p53 binding Supporting Evidence: PMID:18695251 AIMP2 directly interacts with p53, thereby preventing MDM2-mediated ubiquitination and degradation of p53
GO:0005515 protein binding	IPI PMID:19060904 An empirical framework for binary interactome mapping.	REMOVE	Summary: The source records an interaction, but generic protein binding does not specify an AIMP2 function. Reason: The study develops an empirical framework for binary interactome mapping and orthogonal assay assessment. Remove the uninformative GO:0005515 term under the binding-curation policy. The available source does not resolve a more specific AIMP2 activity for this particular assertion. This judgment does not deny the interaction or infer nonbinding from an unrecovered pair-level supplementary record.
GO:0005515 protein binding	IPI PMID:21044950 Genome-wide YFP fluorescence complementation screen identifi...	REMOVE	Summary: The source records an interaction, but generic protein binding does not specify an AIMP2 function. Reason: The source uses YFP complementation around telomere-signaling proteins; a detected pair is not itself an AIMP2 telomere mechanism. Remove the uninformative GO:0005515 term under the binding-curation policy. The available source does not resolve a more specific AIMP2 activity for this particular assertion. This judgment does not deny the interaction or infer nonbinding from an unrecovered pair-level supplementary record.
GO:0005515 protein binding	IPI PMID:21285945 JTV1 co-activates FBP to induce USP29 transcription and stab...	MODIFY	Summary: AIMP2/JTV1 coactivates FBP-dependent USP29 transcription in the oxidative-stress response. Reason: The cached abstract explicitly identifies coactivation of USP29 transcription. The externally read primary PMC3049210 Results/Figure 1 and ChIP methods show promoter recruitment of GFP-JTV1 constructs with endogenous FBP and FBP-dependent transcriptional activation. GO:0003713 describes this protein-mediated coactivation. USP29 performs the downstream deubiquitination of p53; this paper does not establish FUBP1 degradation as the mechanism. Human-cell/stress and expression-construct scope are retained. Proposed replacements: transcription coactivator activity Supporting Evidence: PMID:21285945 translocates to the nucleus, associates with FBP and co-activates the transcription of a new FBP target, ubiquitin-specific peptidase 29 (USP29)
GO:0005515 protein binding	IPI PMID:21516116 Next-generation sequencing to generate interactome datasets.	REMOVE	Summary: The source records an interaction, but generic protein binding does not specify an AIMP2 function. Reason: The source develops Stitch-seq for sequencing interaction-screen outputs. Remove the uninformative GO:0005515 term under the binding-curation policy. The available source does not resolve a more specific AIMP2 activity for this particular assertion. This judgment does not deny the interaction or infer nonbinding from an unrecovered pair-level supplementary record.
GO:0005515 protein binding	IPI PMID:21536907 Structural context for mobilization of a human tRNA syntheta...	MODIFY	Summary: The AIMP2 N terminus structurally anchors KARS1 to the multisynthetase complex. Reason: PMID:21536907 uses solution scattering and hydrogen-deuterium exchange to define the LysRS–p38 subcomplex. AIMP2 supplies an integral scaffold rather than an unspecified binding function. The reported dimeric arrangement belongs to the studied subcomplex and does not settle the stoichiometry of every native MSC assembly. Proposed replacements: protein complex scaffold activity Supporting Evidence: PMID:21536907 Each of the N-terminal 48 residues of p38 binds one LysRS dimer
GO:0005515 protein binding	IPI PMID:21900206 A directed protein interaction network for investigating int...	REMOVE	Summary: The source records an interaction, but generic protein binding does not specify an AIMP2 function. Reason: The source assembles a directed interaction network around intracellular signaling proteins. Remove the uninformative GO:0005515 term under the binding-curation policy. The available source does not resolve a more specific AIMP2 activity for this particular assertion. This judgment does not deny the interaction or infer nonbinding from an unrecovered pair-level supplementary record.
GO:0005515 protein binding	IPI PMID:21988832 Toward an understanding of the protein interaction network o...	REMOVE	Summary: The source records an interaction, but generic protein binding does not specify an AIMP2 function. Reason: The source maps the human liver protein interaction network. Remove the uninformative GO:0005515 term under the binding-curation policy. The available source does not resolve a more specific AIMP2 activity for this particular assertion. This judgment does not deny the interaction or infer nonbinding from an unrecovered pair-level supplementary record.
GO:0005515 protein binding	IPI PMID:22190034 Global landscape of HIV-human protein complexes.	REMOVE	Summary: The source records an interaction, but generic protein binding does not specify an AIMP2 function. Reason: The source uses affinity purification to map HIV–human protein complexes in HEK293 and Jurkat contexts. Remove the uninformative GO:0005515 term under the binding-curation policy. The available source does not resolve a more specific AIMP2 activity for this particular assertion. This judgment does not deny the interaction or infer nonbinding from an unrecovered pair-level supplementary record.
GO:0005515 protein binding	IPI PMID:24212136 Chemical inhibition of prometastatic lysyl-tRNA synthetase-l...	REMOVE	Summary: The source records an interaction, but generic protein binding does not specify an AIMP2 function. Reason: The paper studies inhibition of the KARS1–laminin-receptor interaction; the seeded AIMP2 interaction does not assign KARS1 enzymatic or prometastatic activity to AIMP2. Remove the uninformative GO:0005515 term under the binding-curation policy. The available source does not resolve a more specific AIMP2 activity for this particular assertion. This judgment does not deny the interaction or infer nonbinding from an unrecovered pair-level supplementary record.
GO:0005515 protein binding	IPI PMID:25416956 A proteome-scale map of the human interactome network.	REMOVE	Summary: The source records an interaction, but generic protein binding does not specify an AIMP2 function. Reason: The source is a large-scale map of human binary protein interactions. Remove the uninformative GO:0005515 term under the binding-curation policy. The available source does not resolve a more specific AIMP2 activity for this particular assertion. This judgment does not deny the interaction or infer nonbinding from an unrecovered pair-level supplementary record.
GO:0005515 protein binding	IPI PMID:26496610 A human interactome in three quantitative dimensions organiz...	REMOVE	Summary: The source records an interaction, but generic protein binding does not specify an AIMP2 function. Reason: The source measures affinity-purified complexes and their abundance/stoichiometry in HeLa cells. Remove the uninformative GO:0005515 term under the binding-curation policy. The available source does not resolve a more specific AIMP2 activity for this particular assertion. This judgment does not deny the interaction or infer nonbinding from an unrecovered pair-level supplementary record.
GO:0005515 protein binding	IPI PMID:26871637 Widespread Expansion of Protein Interaction Capabilities by ...	REMOVE	Summary: The source records an interaction, but generic protein binding does not specify an AIMP2 function. Reason: The source tests interaction changes across alternative splice isoforms; construct identity matters for transferring a particular pair to full-length AIMP2. Remove the uninformative GO:0005515 term under the binding-curation policy. The available source does not resolve a more specific AIMP2 activity for this particular assertion. This judgment does not deny the interaction or infer nonbinding from an unrecovered pair-level supplementary record.
GO:0005515 protein binding	IPI PMID:27107012 Pooled-matrix protein interaction screens using Barcode Fusi...	REMOVE	Summary: The source records an interaction, but generic protein binding does not specify an AIMP2 function. Reason: The source describes pooled barcode-fusion interaction screening. Remove the uninformative GO:0005515 term under the binding-curation policy. The available source does not resolve a more specific AIMP2 activity for this particular assertion. This judgment does not deny the interaction or infer nonbinding from an unrecovered pair-level supplementary record.
GO:0005515 protein binding	IPI PMID:27107014 An inter-species protein-protein interaction network across ...	REMOVE	Summary: The source records an interaction, but generic protein binding does not specify an AIMP2 function. Reason: The source is a human–yeast interspecies interaction network; the source partners include yeast accessions, so an interaction need not be a native human cellular complex. Remove the uninformative GO:0005515 term under the binding-curation policy. The available source does not resolve a more specific AIMP2 activity for this particular assertion. This judgment does not deny the interaction or infer nonbinding from an unrecovered pair-level supplementary record.
GO:0005515 protein binding	IPI PMID:28514442 Architecture of the human interactome defines protein commun...	REMOVE	Summary: The source records an interaction, but generic protein binding does not specify an AIMP2 function. Reason: The source is the BioPlex affinity-purification interaction network and its protein communities. Remove the uninformative GO:0005515 term under the binding-curation policy. The available source does not resolve a more specific AIMP2 activity for this particular assertion. This judgment does not deny the interaction or infer nonbinding from an unrecovered pair-level supplementary record.
GO:0005515 protein binding	IPI PMID:29892012 An interactome perturbation framework prioritizes damaging m...	REMOVE	Summary: The source records an interaction, but generic protein binding does not specify an AIMP2 function. Reason: The source measures variant-induced interaction perturbations relevant to developmental disorders. Remove the uninformative GO:0005515 term under the binding-curation policy. The available source does not resolve a more specific AIMP2 activity for this particular assertion. This judgment does not deny the interaction or infer nonbinding from an unrecovered pair-level supplementary record.
GO:0005515 protein binding	IPI PMID:29997244 LuTHy: a double-readout bioluminescence-based two-hybrid tec...	REMOVE	Summary: The source records an interaction, but generic protein binding does not specify an AIMP2 function. Reason: The LuTHy platform combines proximity and coprecipitation readouts; these do not by themselves define the biochemical work of an AIMP2 pair. Remove the uninformative GO:0005515 term under the binding-curation policy. The available source does not resolve a more specific AIMP2 activity for this particular assertion. This judgment does not deny the interaction or infer nonbinding from an unrecovered pair-level supplementary record.
GO:0005515 protein binding	IPI PMID:31116475 Mutations in KARS cause a severe neurological and neurosenso...	REMOVE	Summary: The source records an interaction, but generic protein binding does not specify an AIMP2 function. Reason: The paper concerns KARS disease variants and associated interactions. The seeded KARS1-isoform pair is relevant to MSC contacts, but the abstract does not resolve how each tested variant affects AIMP2 scaffolding. Remove the uninformative GO:0005515 term under the binding-curation policy. The available source does not resolve a more specific AIMP2 activity for this particular assertion. Partner identity alone does not transfer the scaffold mechanism measured in PMID:21536907 and PMID:23159739 to this variant-specific experiment. This judgment does not deny the interaction or infer nonbinding from an unrecovered pair-level supplementary record.
GO:0005515 protein binding	IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari...	REMOVE	Summary: The source records an interaction, but generic protein binding does not specify an AIMP2 function. Reason: The source screens effects of population variants on protein interactions. Remove the uninformative GO:0005515 term under the binding-curation policy. The available source does not resolve a more specific AIMP2 activity for this particular assertion. This judgment does not deny the interaction or infer nonbinding from an unrecovered pair-level supplementary record.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	REMOVE	Summary: The source records an interaction, but generic protein binding does not specify an AIMP2 function. Reason: The source is the HuRI reference map of binary protein interactions. Remove the uninformative GO:0005515 term under the binding-curation policy. The available source does not resolve a more specific AIMP2 activity for this particular assertion. This judgment does not deny the interaction or infer nonbinding from an unrecovered pair-level supplementary record.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	REMOVE	Summary: The source records an interaction, but generic protein binding does not specify an AIMP2 function. Reason: The source maps neurodegeneration-related interactions and aggregation; its AIMP2 entry is not a direct PARP1 activation or parkin-substrate assay. Remove the uninformative GO:0005515 term under the binding-curation policy. The available source does not resolve a more specific AIMP2 activity for this particular assertion. This judgment does not deny the interaction or infer nonbinding from an unrecovered pair-level supplementary record.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	REMOVE	Summary: The source records an interaction, but generic protein binding does not specify an AIMP2 function. Reason: The source compares BioPlex networks in HEK293T and HCT116 cells; cell-specific associations do not alone establish an AIMP2 molecular mechanism. Remove the uninformative GO:0005515 term under the binding-curation policy. The available source does not resolve a more specific AIMP2 activity for this particular assertion. This judgment does not deny the interaction or infer nonbinding from an unrecovered pair-level supplementary record.
GO:0060090 molecular adaptor activity	IEA GO_REF:0000107	MODIFY	Summary: The orthology-derived adaptor assertion corresponds to integral MSC scaffolding. Reason: The proximate source is mouse Q8R010/ENSMUSP00000031613. Independent human dissection establishes AIMP2 as a structural MSC component. The live GO:0030674 comment redirects integral complex scaffolds to GO:0140378; that specific structural activity better describes this conserved MSC role. The donor experimental chain was not independently reconstructed, and this refinement does not assign a signaling adaptor mechanism to the MSC contact. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:Q8R010 UNRESOLVED Mouse Aimp2 is the donor. The exact experimental donor assertion was not independently retrieved; direct human MSC dissection supports the target structural function. ensembl:ENSMUSP00000031613 UNRESOLVED Compara links this mouse protein to human AIMP2; this is not an independent experiment. Proposed replacements: protein complex scaffold activity Supporting Evidence: PMID:19131329 with p38 connecting two subcomplexes that may form in the absence of p38
GO:0065003 protein-containing complex assembly	IEA GO_REF:0000107	ACCEPT	Summary: AIMP2 contributes the physical connections required to assemble MSC submodules. Reason: The mouse orthology transfer is independently supported by human purification and stable knockdown experiments in PMID:19131329. AIMP2 performs assembly work through its structural contacts; this is more than a loss-of-function phenotype. Exact donor experiment provenance remains unresolved, but the human target process is well established. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:Q8R010 UNRESOLVED Mouse Aimp2 is the donor. The exact experimental donor assertion was not independently retrieved; direct human MSC dissection supports the target structural function. ensembl:ENSMUSP00000031613 UNRESOLVED Compara links this mouse protein to human AIMP2; this is not an independent experiment. Supporting Evidence: PMID:19131329 with p38 connecting two subcomplexes that may form in the absence of p38
GO:0005737 cytoplasm	NAS PMID:32644155 3-Dimensional architecture of the human multi-tRNA synthetas...	ACCEPT	Summary: Cytoplasm is the source-level compartment of the human complex analyzed by cross-linking mass spectrometry. Reason: PMID:32644155 analyzes the cytoplasmic human multisynthetase complex by cross-linking mass spectrometry and integrative modeling. Retain the source-level cytoplasm assertion; finer cytosolic annotations provide additional precision without replacing this correct broader location.
GO:0006418 tRNA aminoacylation for protein translation	NAS PMID:32644155 3-Dimensional architecture of the human multi-tRNA synthetas...	ACCEPT	Summary: AIMP2 supplies structural support to the tRNA-aminoacylation complex. Reason: The NAS source describes the human MSC and models its connected synthetase/scaffold architecture. Independent human MSC dissection and KARS1 anchoring experiments show that AIMP2 performs structural work in this machinery (PMID:19131329; PMID:23159739). Aminoacyl-transfer chemistry belongs to the synthetases. The annotation does not imply that AIMP2 is an enzyme or that proposed tRNA channeling has been directly demonstrated. Supporting Evidence: PMID:19131329 with p38 connecting two subcomplexes that may form in the absence of p38 PMID:23159739 The crystal structure of an MSC subcomplex established that LysRS is held in the MSC by binding to the N terminus of the scaffold protein p38/AIMP2
GO:0030674 protein-macromolecule adaptor activity	IDA PMID:19131329 Dissection of the structural organization of the aminoacyl-t...	MODIFY	Summary: Human MSC dissection identifies p38/AIMP2 as an integral complex scaffold. Reason: The original IDA source recovers subassemblies following depletion of auxiliary proteins and specifically places p38 between two subcomplexes. The live ontology distinguishes integral protein-complex scaffolding (GO:0140378) from protein-macromolecule adaptor activity and explicitly directs scaffolds to the former. Preserve the original source and IDA evidence while refining the molecular function. Proposed replacements: protein complex scaffold activity Supporting Evidence: PMID:19131329 with p38 connecting two subcomplexes that may form in the absence of p38
GO:0005515 protein binding	IPI PMID:24312579 Reinvestigation of aminoacyl-tRNA synthetase core complex by...	REMOVE	Summary: The source records an interaction, but generic protein binding does not specify an AIMP2 function. Reason: The cached full paper uses AIMP1, AIMP2 and KARS baits to recover MSC partners and reports TARSL2 as a potential member. Co-complex recovery is informative association evidence but does not establish the mechanistic role of every AIMP2–TARSL2 contact. Remove the uninformative GO:0005515 term under the binding-curation policy. The available source does not resolve a more specific AIMP2 activity for this particular assertion. This judgment does not deny the interaction or infer nonbinding from an unrecovered pair-level supplementary record.
GO:0005515 protein binding	IPI PMID:23159739 Structural switch of lysyl-tRNA synthetase between translati...	MODIFY	Summary: AIMP2 holds KARS1 in the cytoplasmic complex through an N-terminal structural contact. Reason: The crystal structure described in PMID:23159739 establishes how AIMP2 anchors LysRS. This supports protein complex scaffold activity rather than generic binding. Ser207 phosphorylation, nuclear translocation and Ap4A production in that study are properties of KARS1; they are not catalytic functions of AIMP2. Proposed replacements: protein complex scaffold activity Supporting Evidence: PMID:23159739 The crystal structure of an MSC subcomplex established that LysRS is held in the MSC by binding to the N terminus of the scaffold protein p38/AIMP2
GO:0005829 cytosol	IDA PMID:19289464 Dynamic Organization of Aminoacyl-tRNA Synthetase Complexes ...	ACCEPT	Summary: The human-cell study supports cytosolic AIMP2 as a component of dynamically organized MSC assemblies. Reason: Retain the curated IDA compartment. The cached abstract describes synthetase complexes in human-cell cytoplasm and their dynamic organization, while the precise AIMP2 imaging experiment is not reproduced in the abstract-only cache. Independent human MSC purification and cytosolic pathway context support the compartment; no evidence contradicts the curator assignment.
GO:0017101 aminoacyl-tRNA synthetase multienzyme complex	IDA PMID:19131329 Dissection of the structural organization of the aminoacyl-t...	ACCEPT	Summary: Human tandem-affinity purification identifies AIMP2 in the multisynthetase complex. Reason: The original study isolates complexes from human cells and analyzes the consequences of auxiliary-component depletion. This directly supports complex membership independently of the IBA and electronic assertions. Supporting Evidence: PMID:19131329 with p38 connecting two subcomplexes that may form in the absence of p38
GO:0016020 membrane	HDA PMID:19946888 Defining the membrane proteome of NK cells.	UNDECIDED	Summary: The exact AIMP2 detection and membrane-association scope in the NK-cell proteomics dataset remain unresolved. Reason: PMID:19946888 describes membrane-enriched NK-cell proteomics, including nonintegral proteins that may associate transiently. The cached abstract does not expose the AIMP2 peptide row, fraction controls or target-specific validation, and the relevant supplementary record was not recovered. Cytosolic abundance is not evidence of contamination. Preserve the experimental HDA source and leave the membrane assignment open rather than declaring it false or nonfunctional.
GO:0005829 cytosol	TAS Reactome:R-HSA-379861	ACCEPT	Summary: The Reactome event supports the cytosolic compartment of the AIMP2-containing complex. Reason: The cached Reactome:R-HSA-379861 event places an MSC-mediated amino acid–tRNA ligation in the cytosol. AIMP2 is a structural component of the cytosolic complex; the named synthetase performs the corresponding ligation. Retain the compartment at the resolution asserted by this source.
GO:0005829 cytosol	TAS Reactome:R-HSA-379865	ACCEPT	Summary: The Reactome event supports the cytosolic compartment of the AIMP2-containing complex. Reason: The cached Reactome:R-HSA-379865 event places an MSC-mediated amino acid–tRNA ligation in the cytosol. AIMP2 is a structural component of the cytosolic complex; the named synthetase performs the corresponding ligation. Retain the compartment at the resolution asserted by this source.
GO:0005829 cytosol	TAS Reactome:R-HSA-379867	ACCEPT	Summary: The Reactome event supports the cytosolic compartment of the AIMP2-containing complex. Reason: The cached Reactome:R-HSA-379867 event places an MSC-mediated amino acid–tRNA ligation in the cytosol. AIMP2 is a structural component of the cytosolic complex; the named synthetase performs the corresponding ligation. Retain the compartment at the resolution asserted by this source.
GO:0005829 cytosol	TAS Reactome:R-HSA-379893	ACCEPT	Summary: The Reactome event supports the cytosolic compartment of the AIMP2-containing complex. Reason: The cached Reactome:R-HSA-379893 event places an MSC-mediated amino acid–tRNA ligation in the cytosol. AIMP2 is a structural component of the cytosolic complex; the named synthetase performs the corresponding ligation. Retain the compartment at the resolution asserted by this source.
GO:0005829 cytosol	TAS Reactome:R-HSA-379974	ACCEPT	Summary: The Reactome event supports the cytosolic compartment of the AIMP2-containing complex. Reason: The cached Reactome:R-HSA-379974 event places an MSC-mediated amino acid–tRNA ligation in the cytosol. AIMP2 is a structural component of the cytosolic complex; the named synthetase performs the corresponding ligation. Retain the compartment at the resolution asserted by this source.
GO:0005829 cytosol	TAS Reactome:R-HSA-379982	ACCEPT	Summary: The Reactome event supports the cytosolic compartment of the AIMP2-containing complex. Reason: The cached Reactome:R-HSA-379982 event places an MSC-mediated amino acid–tRNA ligation in the cytosol. AIMP2 is a structural component of the cytosolic complex; the named synthetase performs the corresponding ligation. Retain the compartment at the resolution asserted by this source.
GO:0005829 cytosol	TAS Reactome:R-HSA-379993	ACCEPT	Summary: The Reactome event supports the cytosolic compartment of the AIMP2-containing complex. Reason: The cached Reactome:R-HSA-379993 event places an MSC-mediated amino acid–tRNA ligation in the cytosol. AIMP2 is a structural component of the cytosolic complex; the named synthetase performs the corresponding ligation. Retain the compartment at the resolution asserted by this source.
GO:0005829 cytosol	TAS Reactome:R-HSA-379994	ACCEPT	Summary: The Reactome event supports the cytosolic compartment of the AIMP2-containing complex. Reason: The cached Reactome:R-HSA-379994 event places an MSC-mediated amino acid–tRNA ligation in the cytosol. AIMP2 is a structural component of the cytosolic complex; the named synthetase performs the corresponding ligation. Retain the compartment at the resolution asserted by this source.
GO:0005829 cytosol	TAS Reactome:R-HSA-380008	ACCEPT	Summary: The Reactome event supports the cytosolic compartment of the AIMP2-containing complex. Reason: The cached Reactome:R-HSA-380008 event places an MSC-mediated amino acid–tRNA ligation in the cytosol. AIMP2 is a structural component of the cytosolic complex; the named synthetase performs the corresponding ligation. Retain the compartment at the resolution asserted by this source.
GO:0005829 cytosol	TAS Reactome:R-HSA-9825759	ACCEPT	Summary: The Reactome event supports the cytosolic compartment of the AIMP2-containing complex. Reason: The cached event describes MAPK-dependent phosphorylation and release of KARS from the MSC. It supports the cytosolic location of the complex context, not AIMP2 kinase activity or an AIMP2 phosphorylation event. Retain the compartment at the resolution asserted by this source.

Gene Description

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