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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q92734: Variant p.Arg106Cys

Protein TFG
Gene: TFG
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Variant information Variant position: help 106 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 Arginine (R) to Cysteine (C) at position 106 (R106C, p.Arg106Cys). 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 large size and basic (R) to medium size and polar (C) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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 SPG57; defective self-assembly into an oligomeric complex; impaired interaction with PDCD6; causes mitochondrial fragmentation. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 106 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 400 The length of the canonical sequence.
Location on the sequence: help LTLFVNGQPRPLESSQVKYL R RELIELRNKVNRLLDSLEPP 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                         LTLFVNGQPRPLESSQVKYLRRELIELRNKVNRLLDSLE------------------PP

Caenorhabditis elegans        VTVVVDSRAR----EAVHDVQKQVEQIKLDVGKLLGALSAL
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 – 400 Protein TFG
Coiled coil 97 – 124



Literature citations
Inhibition of TFG function causes hereditary axon degeneration by impairing endoplasmic reticulum structure.
Beetz C.; Johnson A.; Schuh A.L.; Thakur S.; Varga R.E.; Fothergill T.; Hertel N.; Bomba-Warczak E.; Thiele H.; Nurnberg G.; Altmuller J.; Saxena R.; Chapman E.R.; Dent E.W.; Nurnberg P.; Audhya A.;
Proc. Natl. Acad. Sci. U.S.A. 110:5091-5096(2013)
Cited for: FUNCTION; SUBUNIT; VARIANT SPG57 CYS-106; CHARACTERIZATION OF VARIANT SPG57 CYS-106; The calcium-binding protein ALG-2 promotes endoplasmic reticulum exit site localization and polymerization of Trk-fused gene (TFG) protein.
Kanadome T.; Shibata H.; Kuwata K.; Takahara T.; Maki M.;
FEBS J. 284:56-76(2017)
Cited for: FUNCTION; SUBCELLULAR LOCATION; INTERACTION WITH PDCD6; CHARACTERIZATION OF VARIANT SPG57 CYS-106; CHARACTERIZATION OF VARIANT HMSNO LEU-285; Novel genetic, clinical, and pathomechanistic insights into TFG-associated hereditary spastic paraplegia.
Harlalka G.V.; McEntagart M.E.; Gupta N.; Skrzypiec A.E.; Mucha M.W.; Chioza B.A.; Simpson M.A.; Sreekantan-Nair A.; Pereira A.; Guenther S.; Jahic A.; Modarres H.; Moore-Barton H.; Trembath R.C.; Kabra M.; Baple E.L.; Thakur S.; Patton M.A.; Beetz C.; Pawlak R.; Crosby A.H.;
Hum. Mutat. 37:1157-1161(2016)
Cited for: VARIANTS SPG57 CYS-106 AND HIS-106; CHARACTERIZATION OF VARIANTS SPG57 CYS-106 AND HIS-106;
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.