AIMP2

AIMP2 is part of the aminoacyl-tRNA synthetase complex, which contains nine different aminoacyl-tRNA synthetases and three non-enzymatic factors. The encoded protein is one of the non-enzymatic factors and is required for assembly and stability of the com

Full Name

Aminoacyl TRNA Synthetase Complex Interacting Multifunctional Protein 2

Function

Required for assembly and stability of the aminoacyl-tRNA synthase complex (PubMed:19131329). Mediates ubiquitination and degradation of FUBP1, a transcriptional activator of MYC, leading to MYC down-regulation which is required for aveolar type II cell differentiation. Blocks MDM2-mediated ubiquitination and degradation of p53/TP53. Functions as a proapoptotic factor.

Biological Process

Apoptotic process Source: UniProtKB-KW
Negative regulation of cell population proliferation Source: Ensembl
Positive regulation of aminoacyl-tRNA ligase activity Source: GO_Central
Positive regulation of neuron death Source: Ensembl
Positive regulation of protein ubiquitination Source: Ensembl
Protein-containing complex assembly Source: Ensembl
tRNA aminoacylation for protein translation Source: Reactome
Type II pneumocyte differentiation Source: Ensembl

Cellular Location

Cytosol; Nucleus. Following DNA damage, dissociates from the aminoacyl-tRNA synthase complex and translocates from the cytoplasm to the nucleus.

Involvement in disease

Leukodystrophy, hypomyelinating, 17 (HLD17): An autosomal recessive neurodevelopmental disorder characterized by atrophy of cerebral cortex, spinal cord and cerebellum, thin corpus callosum, abnormal signals in the basal ganglia, and features suggesting hypo- or demyelination observed on brain imaging. Clinical manifestations include lack of development, absent speech, microcephaly, spasticity, seizures, and contractures.

PTM

Phosphorylated on serine residues in response to UV irradiation.
Ubiquitinated by PRKN, leading to its degradation by the proteasome. Mutant PRKN fails to ubiquitinate AIMP2 efficiently, allowing its accumulation which may contribute to neurodegeneration associated with Parkinson disease.