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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P41091: Variant p.Ile259Met

Eukaryotic translation initiation factor 2 subunit 3
Gene: EIF2S3
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Variant information Variant position: help 259 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 Isoleucine (I) to Methionine (M) at position 259 (I259M, p.Ile259Met). 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 Similar physico-chemical property. Both residues are medium size and hydrophobic. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 1 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 MEHMO; impairs eIF2 complex function.. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 259 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 472 The length of the canonical sequence.
Location on the sequence: help IVKKIPVPPRDFTSEPRLIV I RSFDVNKPGCEVDDLKGGVA 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                         IVKKIPVPPRDFTSEPRLIVIRSFDVNKPGCEVDDLKGGVA

Mouse                         IVKKIPVPPRDFTSEPRLIVIRSFDVNKPGCEVDDLKGGVA

Rat                           IVKKIPVPPRDFTSEPRLIVIRSFDVNKPGCEVDDLKGGVA

Pig                           IVKKIPVPPRDFTSEPRLIVIRSFDVNKPGCEVDDLKGGVA

Bovine                        IVKKIPVPPRDFTSEPRLIVIRSFDVNKPGCEVDDLKGGVA

Chicken                       IVKKIPVPLRDFTSEPRLIVIRSFDVNKPGCEVDDLKGGVA

Zebrafish                     IVNKIPVPVRDFTSEPRLIVIRSFDVNKPGCEVDDLKGGVA

Drosophila                    IVNKIPVPPRDFNAPPRLIVIRSFDVNKPGCEVADLKGGVA

Slime mold                    IVKKIPIPVRDFTSDPRMIVIRSFDVNKPGSRVDEIKGGVA

Baker's yeast                 IVKTIPVPPRDFMISPRLIVIRSFDVNKPGAEIEDLKGGVA

Fission yeast                 IVKKIPIPVRDFTTAPRLIVIRSFDVNKPGAEVDDLKGGVA

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 2 – 472 Eukaryotic translation initiation factor 2 subunit 3
Beta strand 256 – 259



Literature citations
Two novel EIF2S3 mutations associated with syndromic intellectual disability with severe microcephaly, growth retardation, and epilepsy.
Moortgat S.; Desir J.; Benoit V.; Boulanger S.; Pendeville H.; Nassogne M.C.; Lederer D.; Maystadt I.;
Am. J. Med. Genet. A 170:2927-2933(2016)
Cited for: INVOLVEMENT IN MEHMO; VARIANT MEHMO MET-259; MEHMO syndrome mutation EIF2S3-I259M impairs initiator Met-tRNAiMet binding to eukaryotic translation initiation factor eIF2.
Young-Baird S.K.; Shin B.S.; Dever T.E.;
Nucleic Acids Res. 47:855-867(2019)
Cited for: CHARACTERIZATION OF VARIANT MEHMO MET-259; INVOLVEMENT IN MEHMO;
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.