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UniProtKB/Swiss-Prot P55072: Variant p.Arg191Gln

Transitional endoplasmic reticulum ATPase
Gene: VCP
Variant information

Variant position:  191
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 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:  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:  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:  In ALS14 and IBMPFD1; abolishes enhancement of K-315 methylation by ASPSCR1.
Any additional useful information about the variant.

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



Sequence information

Variant position:  191
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  806
The length of the canonical sequence.

Location on the sequence:   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: 
The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         SPYCIVAPDTVIHCEGEPIKREDEEESLNEVGYDDIGGCRK

Mouse                         SPYCIVAPDTVIHCEGEPIKREDEEESLNEVGYDDIGGCRK

Rat                           SPYCIVAPDTVIHCEGEPIKREDEEESLNEVGYDDIGGCRK

Pig                           SPYCIVAPDTVIHCEGEPIKREDEEESLNEVGYDDIGGCRK

Bovine                        SPYCIVAPDTVIHCEGEPIKREDEEESLNEVGYDDIGGCRK

Xenopus laevis                SPYCIVAPDTVIHCEGEPIKREDEEESLNEVGYDDIGGCRK

Xenopus tropicalis            SPYCIVAPDTVIHCEGEPIKREDEEESLNEVGYDDIGGCRK

Zebrafish                     SPYCIVAPDTVIHCEGEPIKREDEEESLNEVGYDDIGGVRK

Drosophila                    EPYCIVAPETVIFCDGDPIKREEEEESLNAVGYDDIGGCRK

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 – 806 Transitional endoplasmic reticulum ATPase
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 ALS14 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 ALS14 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.