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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P07814: Variant p.Pro1115Arg

Bifunctional glutamate/proline--tRNA ligase
Gene: EPRS1
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Variant information Variant position: help 1115 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] 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: help From Proline (P) to Arginine (R) at position 1115 (P1115R, p.Pro1115Arg). 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: help Change from medium size and hydrophobic (P) to large size and basic (R) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 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: help In HLD15; slightly decreased protein level; does not affect multisynthetase complex assembly. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 1115 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 1512 The length of the canonical sequence.
Location on the sequence: help ADFAPEVAWVTRSGKTELAE P IAIRPTSETVMYPAYAKWVQ 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         ADFAPEVAWVTRSGKTELAEPIAIRPTSETVMYPAYAKWVQ

Mouse                         EDFAPEVAWVTRSGKTELAEPIAIRPTSETVMYPAYAKWVQ

Drosophila                    ADFAPEVAWVTKSGDSDLAEPIAVRPTSETVMYPAYAKWVQ
Sequence annotation in neighborhood: help 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 – 1512 Bifunctional glutamate/proline--tRNA ligase
Region 1007 – 1512 Proline--tRNA ligase
Mutagenesis 1097 – 1097 F -> A. Almost complete loss of prolyl-tRNA ligase activity.
Mutagenesis 1097 – 1097 F -> W. No effect on prolyl-tRNA ligase activity. Decreases inhibition by halofuginone.
Beta strand 1110 – 1118



Literature citations
Bi-allelic Mutations in EPRS, Encoding the Glutamyl-Prolyl-Aminoacyl-tRNA Synthetase, Cause a Hypomyelinating Leukodystrophy.
Mendes M.I.; Gutierrez Salazar M.; Guerrero K.; Thiffault I.; Salomons G.S.; Gauquelin L.; Tran L.T.; Forget D.; Gauthier M.S.; Waisfisz Q.; Smith D.E.C.; Simons C.; van der Knaap M.S.; Marquardt I.; Lemes A.; Mierzewska H.; Weschke B.; Koehler W.; Coulombe B.; Wolf N.I.; Bernard G.;
Am. J. Hum. Genet. 102:676-684(2018)
Cited for: INVOLVEMENT IN HLD15; VARIANTS HLD15 339-ARG--TYR-1512 DEL; ARG-1115; THR-1126 AND SER-1160; CHARACTERIZATION OF VARIANTS HLD15 ARG-1115 AND THR-1126; FUNCTION; CATALYTIC ACTIVITY;
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.