Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q76LX8: Variant p.Val88Met

A disintegrin and metalloproteinase with thrombospondin motifs 13
Gene: ADAMTS13
Feedback?
Variant information Variant position: help 88 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 Valine (V) to Methionine (M) at position 88 (V88M, p.Val88Met). 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 Similar physico-chemical property. Both residues are medium size and hydrophobic. 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 TTP; reduces protein secretion and proteolytic activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 88 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 1427 The length of the canonical sequence.
Location on the sequence: help QRQRQRRAAGGILHLELLVA V GPDVFQAHQEDTERYVLTNL 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                         QRQRQRRAAGGILHLELLVAVGPDVFQAHQEDTERYVLTNL

Mouse                         QRLRRRRTLEDILHLELLVAVGPDVSRAHQEDTERYVLTNL

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 75 – 1427 A disintegrin and metalloproteinase with thrombospondin motifs 13
Domain 80 – 286 Peptidase M12B
Binding site 83 – 83
Alternative sequence 2 – 329 Missing. In isoform 4.
Mutagenesis 71 – 71 R -> K. Abolishes pro-domain removal but no loss of proteolytic activity; when associated with D-73.
Mutagenesis 73 – 73 R -> D. Abolishes pro-domain removal but no loss of proteolytic activity; when associated with K-71.
Mutagenesis 83 – 83 E -> A. No change in calcium dependence for proteolysis.
Beta strand 80 – 88



Literature citations
Mechanisms of the interaction between two ADAMTS13 gene mutations leading to severe deficiency of enzymatic activity.
Peyvandi F.; Lavoretano S.; Palla R.; Valsecchi C.; Merati G.; De Cristofaro R.; Rossi E.; Mannuccio Mannucci P.;
Hum. Mutat. 27:330-336(2006)
Cited for: VARIANTS TTP MET-88 AND VAL-1239; CHARACTERIZATION OF VARIANTS TTP MET-88 AND VAL-1239;
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.