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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P55072: Variant p.Arg191Gln

Transitional endoplasmic reticulum ATPase
Gene: VCP
Variant information Variant position: help 191 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 Glutamine (Q) at position 191 (R191Q, p.Arg191Gln). 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 (Q) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 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: help In FTDALS6 and IBMPFD1; abolishes enhancement of K-315 methylation by ASPSCR1. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.

Sequence information Variant position: help 191 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 806 The length of the canonical sequence.
Location on the sequence: help SPYCIVAPDTVIHCEGEPIK R EDEEESLNEVGYDDIGGCRK 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.









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.
Chain 2 – 806 Transitional endoplasmic reticulum ATPase
Mutagenesis 179 – 179 D -> R. No effect on binding to DERL1.
Mutagenesis 183 – 183 H -> W. Severely reduced binding to DERL1.
Helix 191 – 193

Literature citations
A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity.
Cloutier P.; Lavallee-Adam M.; Faubert D.; Blanchette M.; Coulombe B.;
PLoS Genet. 9:E1003210-E1003210(2013)
Cited for: PROTEIN SEQUENCE OF 314-322; IDENTIFICATION BY MASS SPECTROMETRY; METHYLATION AT LYS-315; MUTAGENESIS OF LYS-315; CHARACTERIZATION OF VARIANTS IBMPFD1 HIS-155 AND GLN-191; CHARACTERIZATION OF VARIANT FTDALS6 GLY-159; Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein.
Watts G.D.J.; Wymer J.; Kovach M.J.; Mehta S.G.; Mumm S.; Darvish D.; Pestronk A.; Whyte M.P.; Kimonis V.E.;
Nat. Genet. 36:377-381(2004)
Cited for: VARIANTS IBMPFD1 GLY-95; CYS-155; HIS-155; PRO-155; GLN-191 AND GLU-232; Exome sequencing reveals VCP mutations as a cause of familial ALS.
Johnson J.O.; Mandrioli J.; Benatar M.; Abramzon Y.; Van Deerlin V.M.; Trojanowski J.Q.; Gibbs J.R.; Brunetti M.; Gronka S.; Wuu J.; Ding J.; McCluskey L.; Martinez-Lage M.; Falcone D.; Hernandez D.G.; Arepalli S.; Chong S.; Schymick J.C.; Rothstein J.; Landi F.; Wang Y.D.; Calvo A.; Mora G.; Sabatelli M.; Monsurro M.R.; Battistini S.; Salvi F.; Spataro R.; Sola P.; Borghero G.; Galassi G.; Scholz S.W.; Taylor J.P.; Restagno G.; Chio A.; Traynor B.J.;
Neuron 68:857-864(2010)
Cited for: VARIANTS FTDALS6 HIS-155; GLY-159; GLN-191 AND ASN-592;
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.