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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P10253: Variant p.Pro522Ala

Lysosomal alpha-glucosidase
Gene: GAA
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Variant information Variant position: help 522 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 Proline (P) to Alanine (A) at position 522 (P522A, p.Pro522Ala). 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 medium size and hydrophobic (P) to small size and hydrophobic (A) 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 GSD2; no residual enzymatic activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 522 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 952 The length of the canonical sequence.
Location on the sequence: help MVAEFHDQVPFDGMWIDMNE P SNFIRGSEDGCPNNELENPP 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                         MVAEFHDQVPFDGMWIDMNEPSNFIRGSEDGCPNNELENPP

Mouse                         MVSEFHAQVPFDGMWLDMNEPSNFVRGSQQGCPNNELENPP

Rat                           MVSEFHAQVPFDGMWIDMNEPSNFIRGSQQGCPDNELENPP

Bovine                        MVTEFHAQVPFDGMWIDMNEPSNFVRGSVDGCPDNSLENPP
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 70 – 952 Lysosomal alpha-glucosidase
Chain 123 – 952 76 kDa lysosomal alpha-glucosidase
Chain 204 – 952 70 kDa lysosomal alpha-glucosidase
Active site 518 – 518 Nucleophile
Active site 521 – 521
Mutagenesis 516 – 516 W -> R. Loss of activity.
Mutagenesis 518 – 518 D -> GNE. Loss of activity.
Turn 520 – 522



Literature citations
Late onset Pompe disease: clinical and neurophysiological spectrum of 38 patients including long-term follow-up in 18 patients.
Muller-Felber W.; Horvath R.; Gempel K.; Podskarbi T.; Shin Y.; Pongratz D.; Walter M.C.; Baethmann M.; Schlotter-Weigel B.; Lochmuller H.; Schoser B.;
Neuromuscul. Disord. 17:698-706(2007)
Cited for: VARIANTS GSD2 PRO-355; ALA-522 AND VAL-610; VARIANT ARG-359; Molecular and functional characterization of eight novel GAA mutations in Italian infants with Pompe disease.
Pittis M.G.; Donnarumma M.; Montalvo A.L.E.; Dominissini S.; Kroos M.; Rosano C.; Stroppiano M.; Bianco M.G.; Donati M.A.; Parenti G.; D'Amico A.; Ciana G.; Di Rocco M.; Reuser A.; Bembi B.; Filocamo M.;
Hum. Mutat. 29:E27-E36(2008)
Cited for: VARIANTS GSD2 GLY-103; CYS-191; ARG-219; TRP-224; LYS-262; ARG-293; PRO-355; LEU-375; ARG-401; ASN-489; ALA-522; PRO-552; TYR-599; TRP-638; ARG-643 AND ASN-645; CHARACTERIZATION OF VARIANTS GSD2 CYS-191; LEU-375; ARG-401; ALA-522 AND TYR-599; FUNCTION; CATALYTIC ACTIVITY;
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.