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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P05186: Variant p.Ala116Thr

Alkaline phosphatase, tissue-nonspecific isozyme
Gene: ALPL
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Variant information Variant position: help 116 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 Alanine (A) to Threonine (T) at position 116 (A116T, p.Ala116Thr). 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 small size and hydrophobic (A) to medium size and polar (T) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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 HOPS; loss of alkaline phosphatase activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 116 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 524 The length of the canonical sequence.
Location on the sequence: help ALSKTYNTNAQVPDSAGTAT A YLCGVKANEGTVGVSAATER 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                         ALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATER

Mouse                         ALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATER

Rat                           ALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATER

Bovine                        ALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATQR

Cat                           ALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATQR

Chicken                       ALAKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAGVTR
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 18 – 501 Alkaline phosphatase, tissue-nonspecific isozyme
Active site 110 – 110 Phosphoserine intermediate
Binding site 110 – 110
Modified residue 110 – 110 Phosphoserine
Helix 110 – 119



Literature citations
A molecular approach to dominance in hypophosphatasia.
Lia-Baldini A.S.; Muller F.; Taillandier A.; Gibrat J.F.; Mouchard M.; Robin B.; Simon-Bouy B.; Serre J.L.; Aylsworth A.S.; Bieth E.; Delanote S.; Freisinger P.; Hu J.C.-C.; Krohn H.-P.; Nunes M.E.; Mornet E.;
Hum. Genet. 109:99-108(2001)
Cited for: CHARACTERIZATION OF VARIANTS HOPS VAL-40; VAL-63; THR-116; LEU-181; TRP-184; TRP-223; VAL-249; VAL-378; ILE-478 AND PHE-490; Twelve novel mutations in the tissue-nonspecific alkaline phosphatase gene (ALPL) in patients with various forms of hypophosphatasia.
Taillandier A.; Lia-Baldini A.S.; Mouchard M.; Robin B.; Muller F.; Simon-Bouy B.; Serre J.L.; Bera-Louville A.; Bonduelle M.; Eckhardt J.; Gaillard D.; Myhre A.G.; Koertge-Jung S.; Larget-Piet L.; Malou E.; Sillence D.; Temple I.K.; Viot G.; Mornet E.;
Hum. Mutat. 18:83-84(2001)
Cited for: VARIANTS HPPI CYS-28 AND MET-459; VARIANTS HOPS VAL-40; VAL-51; HIS-71; THR-116; HIS-136; HIS-152; THR-176; THR-179; LYS-191; ASP-211; VAL-220; GLY-235; TYR-294; GLY-327; SER-399 AND ALA-423; Molecular study of three cases of odontohypophosphatasia resulting from heterozygosity for mutations in the tissue non-specific alkaline phosphatase gene.
Herasse M.; Spentchian M.; Taillandier A.; Keppler-Noreuil K.; Fliorito A.N.M.; Bergoffen J.; Wallerstein R.; Muti C.; Simon-Bouy B.; Mornet E.;
J. Med. Genet. 40:605-609(2003)
Cited for: VARIANTS HOPS LEU-108; THR-116 AND MET-414; CHARACTERIZATION OF VARIANT HOPS LEU-108;
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.