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UniProtKB/Swiss-Prot Q13155: Variant p.Gly209Ser

Aminoacyl tRNA synthase complex-interacting multifunctional protein 2
Gene: AIMP2
Variant information

Variant position:  209
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  US
The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance

Residue change:  From Glycine (G) to Serine (S) at position 209 (G209S, p.Gly209Ser).
Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.

Physico-chemical properties:  Change from glycine (G) to small size and polar (S)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  0
The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page

Variant description:  In a lung cancer cell line; no effect on proapoptotic activity.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  209
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  320
The length of the canonical sequence.

Location on the sequence:   WKNVPKTQMKFSIQTMCPIE  G EGNIARFLFSLFGQKHNAVN
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.

Residue conservation: 
The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         WKNVPKTQMKFSIQTMCPIEGEGNIARFLFSLFGQKHNAVN

Mouse                         WKNVPKTQMKFSVQTMCPIEGEGNIARFLFSLFGQKHNAVT

Rat                           WKNVPKTQMKFSVQTMCPIEGEGNIARFLFSLFGQKHNAVH

Bovine                        WKDVPKTQMKFSVQTMCPIEGEGNIARFLFSLFGQKQDAVN

Drosophila                    WKNCEHTEMISSPTMYVPIYGEVNIIRYLGRVGPAEYRYEG

Sequence annotation in neighborhood:  
The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
  • Type: the type of sequence feature.
  • Positions: endpoints of the sequence feature.
  • Description: contains additional information about the feature.

TypePositionsDescription
Chain 1 – 320 Aminoacyl tRNA synthase complex-interacting multifunctional protein 2
Region 162 – 225 Interaction with TP53
Mutagenesis 215 – 215 R -> A. Nearly abolishes interaction with EPRS1.
Beta strand 207 – 209


Literature citations

AIMP2/p38, the scaffold for the multi-tRNA synthetase complex, responds to genotoxic stresses via p53.
Han J.M.; Park B.-J.; Park S.G.; Oh Y.S.; Choi S.J.; Lee S.W.; Hwang S.-K.; Chang S.-H.; Cho M.-H.; Kim S.;
Proc. Natl. Acad. Sci. U.S.A. 105:11206-11211(2008)
Cited for: INTERACTION WITH TP53; VARIANTS VAL-92; 97-ASP--SER-99 AND SER-209; MUTAGENESIS OF 163-GLU-ASN-164 AND 172-GLN-ASN-173;

Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.