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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P54577: Variant p.Glu196Lys

Tyrosine--tRNA ligase, cytoplasmic
Gene: YARS1
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Variant information Variant position: help 196 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 Glutamate (E) to Lysine (K) at position 196 (E196K, p.Glu196Lys). 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 acidic (E) to large size and basic (K) 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 CMTDIC; partial loss of activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 196 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 528 The length of the canonical sequence.
Location on the sequence: help YLKVDAQFGGIDQRKIFTFA E KYLPALGYSKRVHLMNPMVP 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                         YLKVDAQFGGIDQRKIFTFAEKYLPALGYSKRVHLMNPMVP

Mouse                         YLKVDAQFGGVDQRKIFTFAEKYLPALGYSKRVHLMNPMVP

Rat                           YLKVDAQFGGIDQRKIFTFAEKYLPTLGYSKRVHLMNPMVP

Bovine                        YLKVDAQFGGVDQRKIFTFAEKYLPALGYSKRIHLMNPMVP

Chicken                       YLKVDAQFGGVDQRKIFTFAEKYLPSLGYAKRIHLMNPMVP

Xenopus laevis                YLKVDAQFGGVDQRKIFTFAEKYLPALGYAKRIHLMNPMVP

Xenopus tropicalis            YLKVDAQFGGVDQRKIFTFAEKYLPALGYAKRIHLMNPMVP

Zebrafish                     YLKVDAQFGGVDQRKIFTLAEKYLPSLGYTKRSHLMNPMVP

Baker's yeast                 FLDVDCQFGGVDQRKIFVLAEENLPSLGYKKRAHLMNPMVP

Fission yeast                 YLGVDVQFGGVDQRKIFVMAEEVLPVLGYKKRGHLMNPMVP
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 – 528 Tyrosine--tRNA ligase, cytoplasmic
Chain 2 – 528 Tyrosine--tRNA ligase, cytoplasmic, N-terminally processed
Binding site 188 – 188
Modified residue 197 – 197 N6-acetyllysine
Modified residue 205 – 205 Phosphoserine
Modified residue 206 – 206 N6-acetyllysine
Helix 189 – 198



Literature citations
Disrupted function and axonal distribution of mutant tyrosyl-tRNA synthetase in dominant intermediate Charcot-Marie-Tooth neuropathy.
Jordanova A.; Irobi J.; Thomas F.P.; Van Dijck P.; Meerschaert K.; Dewil M.; Dierick I.; Jacobs A.; De Vriendt E.; Guergueltcheva V.; Rao C.V.; Tournev I.; Gondim F.A.A.; D'Hooghe M.; Van Gerwen V.; Callaerts P.; Van Den Bosch L.; Timmermans J.-P.; Robberecht W.; Gettemans J.; Thevelein J.M.; De Jonghe P.; Kremensky I.; Timmerman V.;
Nat. Genet. 38:197-202(2006)
Cited for: FUNCTION; CATALYTIC ACTIVITY; SUBCELLULAR LOCATION; VARIANTS CMTDIC 153-VAL--VAL-156 DEL; ARG-41 AND LYS-196; CHARACTERIZATION OF VARIANTS CMTDIC ARG-41 AND LYS-196;
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.