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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q8IUX1: Variant p.Gly212Val

Complex I assembly factor TMEM126B, mitochondrial
Gene: TMEM126B
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Variant information Variant position: help 212 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 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: help 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: 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 MC1DN29; decreased function in complex I assembly. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 212 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 230 The length of the canonical sequence.
Location on the sequence: help 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         TQMKLMAIPLVFQIMFGILNGLYHYAVFEETLEKTIHEE

Mouse                         TGMKAMAIPLFFQIVMGAFTGLHHYNICEKPRARLVPDD

Rat                           TGMKAMAVPLLFQIIFGVFNGLYHYAVCEKAYARIVPDD
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 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.