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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O75962: Variant p.Glu1299Lys

Triple functional domain protein
Gene: TRIO
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Variant information Variant position: help 1299 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 1299 (E1299K, p.Glu1299Lys). 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 MRD44; severely decreased activation of RAC1-mediated signaling; severely decreased neurite outgrowth. Any additional useful information about the variant.


Sequence information Variant position: help 1299 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 3097 The length of the canonical sequence.
Location on the sequence: help AHELNEEKRKSARRKEFIMA E LIQTEKAYVRDLRECMDTYL 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                         AHELNEEKRKSARRKEFIMAELIQTEKAYVRDLRECMDTYL

Mouse                         AHELNEEKRKSARRKEFIMAELIQTEKAYVRDLRECMDTYL

Rat                           AHELNEEKRKSARRKEFIMAELIQTEKAYVRDLRECMDTYL

Zebrafish                     AHELNEEKRKSARRKDFIMAELIQTEKAYVRDLRECMDTYL
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 – 3097 Triple functional domain protein
Domain 1292 – 1467 DH 1
Alternative sequence 1 – 2501 Missing. In isoform 3.
Mutagenesis 1299 – 1299 E -> A. 50% decrease in nucleotide exchange activity.
Mutagenesis 1303 – 1303 T -> A. 40% decrease in nucleotide exchange activity.
Helix 1291 – 1316



Literature citations
Opposite modulation of RAC1 by mutations in TRIO is associated with distinct, domain-specific neurodevelopmental disorders.
Barbosa S.; Greville-Heygate S.; Bonnet M.; Godwin A.; Fagotto-Kaufmann C.; Kajava A.V.; Laouteouet D.; Mawby R.; Wai H.A.; Dingemans A.J.M.; Hehir-Kwa J.; Willems M.; Capri Y.; Mehta S.G.; Cox H.; Goudie D.; Vansenne F.; Turnpenny P.; Vincent M.; Cogne B.; Lesca G.; Hertecant J.; Rodriguez D.; Keren B.; Burglen L.; Gerard M.; Putoux A.; Cantagrel V.; Siquier-Pernet K.; Rio M.; Banka S.; Sarkar A.; Steeves M.; Parker M.; Clement E.; Moutton S.; Tran Mau-Them F.; Piton A.; de Vries B.B.A.; Guille M.; Debant A.; Schmidt S.; Baralle D.;
Am. J. Hum. Genet. 106:338-355(2020)
Cited for: VARIANTS MRD44 768-GLN--VAL-3097 DEL; LYS-1299; GLN-1428; THR-1461 AND ARG-1469; VARIANTS MRD63 ILE-1075; GLN-1078; GLY-1078; TRP-1078; ILE-1080 AND LEU-1461; INVOLVEMENT IN MRD63; FUNCTION; CHARACTERIZATION OF VARIANTS MRD63 ILE-1075; GLN-1078; GLY-1078; TRP-1078; ILE-1080 AND LEU-1461; CHARACTERIZATION OF VARIANTS MRD44 LYS-1299; GLN-1428 AND ARG-1469;
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.