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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P05186: Variant p.Ala40Val

Alkaline phosphatase, tissue-nonspecific isozyme
Gene: ALPL
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Variant information Variant position: help 40 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 Valine (V) at position 40 (A40V, p.Ala40Val). 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 hydrophobic (V) 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; 2% of activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 40 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 PEKEKDPKYWRDQAQETLKY A LELQKLNTNVAKNVIMFLGD 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                         PEKEKDPKYWRDQAQETLKYALELQKLNTNVAKNVIMFLGD

Mouse                         PEKERDPSYWRQQAQETLKNALKLQKLNTNVAKNVIMFLGD

Rat                           PEKEKDPSYWRQQAQETLKNALKLQKLNTNVAKNIIMFLGD

Bovine                        PEKEKDPKYWRDQAQQTLKNALRLQTLNTNVAKNVIMFLGD

Cat                           PEKEKDPKYWRDQAQQTLKNALRLQKLNTNVVKNVIMFLGD

Chicken                       PEREKDPEYWRQQAQETLRDALRLQHLNQNVAKNLILFLGD
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
Binding site 60 – 60
Binding site 60 – 60
Alternative sequence 1 – 99 MISPFLVLAIGTCLTNSLVPEKEKDPKYWRDQAQETLKYALELQKLNTNVAKNVIMFLGDGMGVSTVTAARILKGQLHHNPGEETRLEMDKFPFVALSK -> MPWSFRSSTPTWLRMSSCSWEM. In isoform 2.
Alternative sequence 1 – 55 Missing. In isoform 3.
Helix 26 – 42



Literature citations
Identification of fifteen novel mutations in the tissue-nonspecific alkaline phosphatase (TNSALP) gene in European patients with severe hypophosphatasia.
Mornet E.; Taillandier A.; Peyramaure S.; Kaper F.; Muller F.; Brenner R.; Bussiere P.; Freisinger P.; Godard J.; Le Merrer M.; Oury J.F.; Plauchu H.; Puddu R.; Rival J.M.; Superti-Furga A.; Touraine R.L.; Serre J.L.; Simon-Bouy B.;
Eur. J. Hum. Genet. 6:308-314(1998)
Cited for: VARIANTS HOPS PHE-17; VAL-40; SER-75; ARG-120; ARG-129; ASP-170; TRP-184; LYS-191; TRP-223; LYS-291; ASP-334; PRO-445; CYS-450; SER-473 AND ARG-491; VARIANT HIS-263; Correlations of genotype and phenotype in hypophosphatasia.
Zurutuza L.; Muller F.; Gibrat J.F.; Taillandier A.; Simon-Bouy B.; Serre J.L.; Mornet E.;
Hum. Mol. Genet. 8:1039-1046(1999)
Cited for: VARIANTS HOPS VAL-40; LEU-62; SER-75; THR-111; ARG-120; ARG-129; HIS-136; VAL-162; ASP-170; TYR-171; TRP-184; LYS-191; TRP-223; VAL-249; LYS-291; VAL-306; ASP-334; CYS-391; PRO-445; CYS-450; SER-473; LYS-476 AND ARG-491; 3D-STRUCTURE MODELING; CHARACTERIZATION OF VARIANTS; Fifteen new mutations (-195C>T, L-12X, 298-2A>G, T117N, A159T, R229S, 997+2T>A, E274X, A331T, H364R, D389G, 1256delC, R433H, N461I, C472S) in the tissue-nonspecific alkaline phosphatase (TNSALP) gene in patients with hypophosphatasia.
Taillandier A.; Cozien E.; Muller F.; Merrien Y.; Bonnin E.; Fribourg C.; Simon-Bouy B.; Serre J.L.; Bieth E.; Brenner R.; Cordier M.P.; De Bie S.; Fellmann F.; Freisinger P.; Hesse V.; Hennekam R.C.M.; Josifova D.; Kerzin-Storrar L.; Leporrier N.; Zabot M.-T.; Mornet E.;
Hum. Mutat. 15:293-293(2000)
Cited for: VARIANTS HOPS VAL-40; THR-111; ASN-134; THR-176; LYS-191; TYR-201; SER-246; THR-348; ARG-381; GLY-406; HIS-450; ILE-478 AND SER-489; 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;
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.