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UniProtKB/Swiss-Prot P13804: Variant p.Thr171Ile

Electron transfer flavoprotein subunit alpha, mitochondrial
Gene: ETFA
Variant information

Variant position:  171
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  LB/B
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 Threonine (T) to Isoleucine (I) at position 171 (T171I, p.Thr171Ile).
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 polar (T) to medium size and hydrophobic (I)
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:  Decreased protein stability.
Any additional useful information about the variant.

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



Sequence information

Variant position:  171
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  333
The length of the canonical sequence.

Location on the sequence:   GNALCTVKCDEKVKVFSVRG  T SFDAAATSGGSASSEKASST
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                         GNALCTVKCDEKVKVFSVRGTSFDAAATSGGSASSEKASST

Mouse                         GNALCTVKCDEKVKVFSVRGTSFEAAATSGGSASSEKAPSS

Rat                           GNALCTVKCDEKVKVFSVRGTSFEAAAASGGSASSEKAPSS

Bovine                        GNAICTVKCDEKVKVFSVRGTSFEAAAASGGSASSEKASST

Caenorhabditis elegans        GNAVKKVKSTAPIKLLTFRGTSFE-PAKEGGSGAVENAPSA

Slime mold                    GNAIATVKSTDKCKVGTVRTTAFDKAPTSGGSAKVVSANDW

Baker's yeast                 GNIISTIECQAEKKLLIIRASAFP-PIAEGSMDSVTIEKRT

Fission yeast                 GNVNVTVSTKDPIKIVTVRASAFDAAPSSGEGAATVVEGID

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 20 – 333 Electron transfer flavoprotein subunit alpha, mitochondrial
Region 20 – 204 Domain I
Modified residue 158 – 158 N6-acetyllysine; alternate
Modified residue 158 – 158 N6-succinyllysine; alternate
Modified residue 164 – 164 N6-acetyllysine
Modified residue 187 – 187 N6-succinyllysine
Helix 170 – 172


Literature citations

A polymorphic variant in the human electron transfer flavoprotein alpha-chain (alpha-T171) displays decreased thermal stability and is overrepresented in very-long-chain acyl-CoA dehydrogenase-deficient patients with mild childhood presentation.
Bross P.; Pedersen P.; Winter V.; Nyholm M.; Johansen B.N.; Olsen R.K.; Corydon M.J.; Andresen B.S.; Eiberg H.; Kolvraa S.; Gregersen N.;
Mol. Genet. Metab. 67:138-147(1999)
Cited for: VARIANT ILE-171; CHARACTERIZATION OF VARIANT ILE-171; FUNCTION;

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.