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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O75197: Variant p.Gly171Val

Low-density lipoprotein receptor-related protein 5
Gene: LRP5
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Variant information Variant position: help 171 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 171 (G171V, p.Gly171Val). 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 HBM; also in HBM individuals with enlarged mandible and torus palatinus; abolishes interaction with MESD; impairs transport to cell surface; no enhancement of DKK1 binding by MESD resulting in impaired inhibition of Wnt signaling by DKK1. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 171 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 1615 The length of the canonical sequence.
Location on the sequence: help DQPRAIALDPAHGYMYWTDW G ETPRIERAGMDGSTRKIIVD 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                         DQPRAIALDPAHGYMYWTDWGETPRIERAGMDGSTRKIIVD

Mouse                         DQPRAIALDPAHGYMYWTDWGEAPRIERAGMDGSTRKIIVD
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 32 – 1615 Low-density lipoprotein receptor-related protein 5
Topological domain 32 – 1384 Extracellular
Repeat 163 – 206 LDL-receptor class B 3
Region 32 – 288 Beta-propeller 1



Literature citations
A cell-based Dkk1 binding assay reveals roles for extracellular domains of LRP5 in Dkk1 interaction and highlights differences between wild-type and the high bone mass mutant LRP5(G171V).
Murrills R.J.; Matteo J.J.; Bhat B.M.; Coleburn V.E.; Allen K.M.; Chen W.; Damagnez V.; Bhat R.A.; Bex F.J.; Bodine P.V.;
J. Cell. Biochem. 108:1066-1075(2009)
Cited for: INTERACTION WITH DKK1 AND MESD; CHARACTERIZATION OF VARIANT VAL-171; The LRP5 high-bone-mass G171V mutation disrupts LRP5 interaction with Mesd.
Zhang Y.; Wang Y.; Li X.; Zhang J.; Mao J.; Li Z.; Zheng J.; Li L.; Harris S.; Wu D.;
Mol. Cell. Biol. 24:4677-4684(2004)
Cited for: INTERACTION WITH MESD; CHARACTERIZATION OF VARIANT HBM VAL-171; A mutation in the LDL receptor-related protein 5 gene results in the autosomal dominant high-bone-mass trait.
Little R.D.; Carulli J.P.; Del Mastro R.G.; Dupuis J.; Osborne M.; Folz C.; Manning S.P.; Swain P.M.; Zhao S.-C.; Eustace B.; Lappe M.M.; Spitzer L.; Zweier S.; Braunschweiger K.; Benchekroun Y.; Hu X.; Adair R.; Chee L.; FitzGerald M.G.; Tulig C.; Caruso A.; Tzellas N.; Bawa A.; Franklin B.; McGuire S.; Nogues X.; Gong G.; Allen K.M.; Anisowicz A.; Morales A.J.; Lomedico P.T.; Recker S.M.; Van Eerdewegh P.; Recker R.R.; Johnson M.L.;
Am. J. Hum. Genet. 70:11-19(2002)
Cited for: VARIANT HBM VAL-171; POLYMORPHISM; High bone density due to a mutation in LDL-receptor-related protein 5.
Boyden L.M.; Mao J.; Belsky J.; Mitzner L.; Farhi A.; Mitnick M.A.; Wu D.; Insogna K.; Lifton R.P.;
N. Engl. J. Med. 346:1513-1521(2002)
Cited for: VARIANT HBM VAL-171; CHARACTERIZATION OF VARIANT HBM VAL-171;
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.