Home  |  Contact

UniProtKB/Swiss-Prot Q8IUX1: Variant p.Gly212Val

Complex I assembly factor TMEM126B, mitochondrial
Gene: TMEM126B
Variant information

Variant position:  212
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Disease [Disclaimer]
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Glycine (G) to Valine (V) at position 212 (G212V, p.Gly212Val).
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 glycine (G) to medium size and hydrophobic (V)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -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:  In MC1DN29; decreased function in complex I assembly.
Any additional useful information about the variant.

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



Sequence information

Variant position:  212
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  230
The length of the canonical sequence.

Location on the sequence:   TQMKLMAIPLVFQIMFGILN  G LYHYAVFEETLEKTIHEE
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                         TQMKLMAIPLVFQIMFGILNGLYHYAVFEETLEKTIHEE

Mouse                         TGMKAMAIPLFFQIVMGAFTGLHHYNICEKPRARLVPDD

Rat                           TGMKAMAVPLLFQIIFGVFNGLYHYAVCEKAYARIVPDD

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 2 – 230 Complex I assembly factor TMEM126B, mitochondrial
Transmembrane 199 – 219 Helical
Alternative sequence 141 – 230 Missing. In isoform 3.
Alternative sequence 171 – 230 Missing. In isoform 4.


Literature citations

Mutations in complex I assembly factor TMEM126B result in muscle weakness and isolated complex I deficiency.
Sanchez-Caballero L.; Ruzzenente B.; Bianchi L.; Assouline Z.; Barcia G.; Metodiev M.D.; Rio M.; Funalot B.; van den Brand M.A.; Guerrero-Castillo S.; Molenaar J.P.; Koolen D.; Brandt U.; Rodenburg R.J.; Nijtmans L.G.; Roetig A.;
Am. J. Hum. Genet. 99:208-216(2016)
Cited for: INVOLVEMENT IN MC1DN29; VARIANTS MC1DN29 70-GLN--GLU-230 DEL AND VAL-212; CHARACTERIZATION OF VARIANTS MC1DN29 70-GLN--GLU-230 DEL AND VAL-212;

Biallelic mutations in TMEM126B cause severe complex I deficiency with a variable clinical phenotype.
Alston C.L.; Compton A.G.; Formosa L.E.; Strecker V.; Olahova M.; Haack T.B.; Smet J.; Stouffs K.; Diakumis P.; Ciara E.; Cassiman D.; Romain N.; Yarham J.W.; He L.; De Paepe B.; Vanlander A.V.; Seneca S.; Feichtinger R.G.; Ploski R.; Rokicki D.; Pronicka E.; Haller R.G.; Van Hove J.L.; Bahlo M.; Mayr J.A.; Van Coster R.; Prokisch H.; Wittig I.; Ryan M.T.; Thorburn D.R.; Taylor R.W.;
Am. J. Hum. Genet. 99:217-227(2016)
Cited for: INVOLVEMENT IN MC1DN29; VARIANT MC1DN29 VAL-212; CHARACTERIZATION OF VARIANT MC1DN29 VAL-212;

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.