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UniProtKB/Swiss-Prot P38919: Variant p.Asp270Gly

Eukaryotic initiation factor 4A-III
Gene: EIF4A3
Variant information

Variant position:  270
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  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:  From Aspartate (D) to Glycine (G) at position 270 (D270G, p.Asp270Gly).
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 medium size and acidic (D) to glycine (G)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -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:  In RCPS.
Any additional useful information about the variant.

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



Sequence information

Variant position:  270
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  411
The length of the canonical sequence.

Location on the sequence:   GIKQFFVAVEREEWKFDTLC  D LYDTLTITQAVIFCNTKRKV
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                         GIKQFFVAVEREEWKFDTLCDLYDTLTITQAVIFCNTKRKV

Mouse                         GIKQFFVAVEREEWKFDTLCDLYDTLTITQAVIFCNTKRKV

Rat                           GIKQFFVAVEREEWKFDTLCDLYDTLTITQAVIFCNTKRKV

Pig                           GIKQFFVAVEREEWKFDTLCDLYDTLTITQAVIFCNTKRKV

Bovine                        GIKQFFVAVEREEWKFDTLCDLYDTLTITQAVIFCNTKRKV

Chicken                       GIKQFFVAVEREEWKFDTLCDLYDTLTITQAVIFCNTKRKV

Xenopus tropicalis            GIKQFFVAVEREEWKFDTLCDLYDTLTITQAVIFCNTKRKV

Zebrafish                     GIKQFFVAVEREEWKFDTLCDLYDTLTITQAVIFCNTKRKV

Drosophila                    GIKQFFVAVEREEWKFDTLCDLYDTLTITQAVIFCNTKRKV

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 – 411 Eukaryotic initiation factor 4A-III
Chain 2 – 411 Eukaryotic initiation factor 4A-III, N-terminally processed
Domain 250 – 411 Helicase C-terminal
Mutagenesis 270 – 270 D -> K. Loss of CWC22-binding and loss of incorporation into EJCs; when associated with K-273.
Mutagenesis 273 – 273 D -> K. Loss of CWC22-binding and loss of incorporation into EJCs; when associated with K-270.
Helix 264 – 274


Literature citations

A noncoding expansion in EIF4A3 causes Richieri-Costa-Pereira syndrome, a craniofacial disorder associated with limb defects.
Favaro F.P.; Alvizi L.; Zechi-Ceide R.M.; Bertola D.; Felix T.M.; de Souza J.; Raskin S.; Twigg S.R.; Weiner A.M.; Armas P.; Margarit E.; Calcaterra N.B.; Andersen G.R.; McGowan S.J.; Wilkie A.O.; Richieri-Costa A.; de Almeida M.L.; Passos-Bueno M.R.;
Am. J. Hum. Genet. 94:120-128(2014)
Cited for: FUNCTION; VARIANT RCPS GLY-270;

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.