Go Annotations as Summary Text (Tabular View) (GO Graph)

GO curators for mouse genes have assigned the following annotations to the gene product of Aars. (This text reflects annotations as of Wednesday, January 23, 2013.) MGI curation of this mouse gene is considered complete, including annotations derived from the biomedical literature as of October 16, 2008. If you know of any additional information regarding this mouse gene please let us know. Please supply mouse gene symbol and a PubMed ID.

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Summary from NCBI RefSeq

[Summary is not available for the mouse gene. This summary is for the human ortholog.] The human alanyl-tRNA synthetase (AARS) belongs to a family of tRNA synthases, of the class II enzymes. Class II tRNA synthases evolved early in evolution and are highly conserved. This is reflected by the fact that 498 of the 968-residue polypeptide human AARS shares 41% identity witht the E.coli protein. tRNA synthases are the enzymes that interpret the RNA code and attach specific aminoacids to the tRNAs that contain the cognate trinucleotide anticodons. They consist of a catalytic domain which interacts with the amino acid acceptor-T psi C helix of the tRNA, and a second domain which interacts with the rest of the tRNA structure. [provided by RefSeq, Jul 2008]

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Summary text based on GO annotations supported by experimental evidence in mouse

• Researchers have inferred from direct assay, that the gene product of Aars
  • participates in the following biological processes:
    • regulation of translational fidelity ^[1]
  • performs the following molecular functions:
    • aminoacyl-tRNA editing activity ^[1]
• Researchers have inferred, based on phenotypic analysis of mouse mutants, that the gene product of Aars
  • participates in the following biological processes:
    • alanyl-tRNA aminoacylation ^[2]
    • cellular response to unfolded protein ^[3]
    • cerebellar Purkinje cell layer development ^[2]
    • endoplasmic reticulum unfolded protein response ^[2]
    • hair follicle development ^[4]
    • negative regulation of neuron apoptotic process ^[2]
    • neuromuscular process ^[2]
    • neuromuscular process controlling balance ^[2]
    • protein folding ^[4]
    • response to amino acid stimulus ^[4]
    • skin development ^[4]
    • tRNA modification ^[2]

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Summary text based on GO annotations supported by experimental evidence in other organisms

• From comparative sequence analysis (see table for details), MGI curators have determined that the gene product of Aars:
  • participates in the following biological processes:
    • alanyl-tRNA aminoacylation
  • performs the following molecular functions:
    • alanine-tRNA ligase activity
    • amino acid binding
    • ATP binding
    • tRNA binding
  • is located in the following cellular components:
    • cytoplasm

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Summary text based on GO annotations supported by structural data

• Aars encodes a protein or proteins that contain the following InterPro domains: Alanine-tRNA ligase, class IIc, Alanine-tRNA ligase, class IIc, anti-codon-binding domain, Alanine-tRNA ligase, eukaryota/bacteria, Alanyl-tRNA synthetase, class IIc, core domain, Alanyl-tRNA synthetase, class IIc, N-terminal, Phosphoesterase, DHHA1, Threonyl/alanyl tRNA synthetase, class II-like, putative editing domain, Threonyl/alanyl tRNA synthetase, SAD, indicating that the gene product:
  • participates in the following biological processes:
    • tRNA aminoacylation
  • performs the following molecular functions:
    • ligase activity, forming aminoacyl-tRNA and related compounds
    • nucleic acid binding
    • nucleotide binding

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Summary text for additional MGI annotations

• Automated translation to GO terms of SwissProt keywords that describe Aars indicates that it:
  • participates in the following biological processes:
    • translation
  • performs the following molecular functions:
    • aminoacyl-tRNA ligase activity
    • ligase activity
    • metal ion binding
    • nucleotide binding
    • RNA binding

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References

1. Guo M et al. (2009) Paradox of mistranslation of serine for alanine caused by AlaRS recognition dilemma. Nature, 462:808-12. (PubMed:20010690)
2. Lee JW et al. (2006) Editing-defective tRNA synthetase causes protein misfolding and neurodegeneration Nature, 443:50-5. (PubMed:16906134)
3. Mizoguchi A et al. (2003) Role of the CD5 molecule on TCR gammadelta T cell-mediated immune functions: development of germinal centers and chronic intestinal inflammation. Int Immunol, 15:97-108. (PubMed:12502730)
4. Tsukiyama K et al. (2006) Gastric inhibitory polypeptide as an endogenous factor promoting new bone formation after food ingestion. Mol Endocrinol, 20:1644-51. (PubMed:16469773)

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Gene Ontology Evidence Code Abbreviations:

EXP Inferred from experiment

IC Inferred by curator

IDA Inferred from direct assay

IEA Inferred from electronic annotation

IGI Inferred from genetic interaction

IMP Inferred from mutant phenotype

IPI Inferred from physical interaction

ISS Inferred from sequence or structural similarity

ISO Inferred from sequence orthology

ISA Inferred from sequence alignment

ISM Inferred from sequence model

NAS Non-traceable author statement

ND No biological data available

RCA Reviewed computational analysis

TAS Traceable author statement

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