Home  |  Contact

UniProtKB/Swiss-Prot P06280: Variant p.Gly35Glu

Alpha-galactosidase A
Gene: GLA
Variant information

Variant position:  35
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  US
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:  From Glycine (G) to Glutamate (E) at position 35 (G35E, p.Gly35Glu).
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:  Change from glycine (G) to medium size and acidic (E)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -2
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:  In FD; unknown pathological significance; decreased enzyme activity.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.

Sequence information

Variant position:  35
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  429
The length of the canonical sequence.

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.

Sequence annotation in neighborhood:  
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.

Chain 32 – 429 Alpha-galactosidase A

Literature citations

A sensitive mutation screening strategy for Fabry disease: detection of nine mutations in the alpha-galactosidase A gene.
Blanch L.C.; Meaney C.; Morris C.P.;
Hum. Mutat. 8:38-43(1996)
Cited for: VARIANTS FD ARG-52; GLU-128; THR-205; THR-284; LYS-298 AND GLU-358 DEL;

Screening and detection of gene mutations in Japanese patients with Fabry disease by non-radioactive single-stranded conformation polymorphism analysis.
Takata T.; Okumiya T.; Hayashibe H.; Shimmoto M.; Kase R.; Itoh K.; Utsumi K.; Kamei S.; Sakuraba H.;
Brain Dev. 19:111-116(1997)
Cited for: VARIANTS FD PRO-20; SER-40; GLN-66; VAL-72; CYS-112; TYR-142; VAL-156; VAL-166; ASN-242; ALA-260; ASP-261; GLU-279; ILE-296; GLN-301; LYS-320; ARG-328; GLU-358 DEL AND SER-373;

Twenty novel mutations in the alpha-galactosidase A gene causing Fabry disease.
Topaloglu A.K.; Ashley G.A.; Tong B.; Shabbeer J.; Astrin K.H.; Eng C.M.; Desnick R.J.;
Mol. Med. 5:806-811(1999)
Cited for: VARIANTS FD VAL-42; CYS-112; ARG-142; ARG-148; VAL-165; ASP-183; SER-215; CYS-235; LEU-236; HIS-244; LEU-259; ILE-267; PHE-289; GLU-321; GLU-358 DEL AND TYR-378;

Detection of alpha-galactosidase a mutations causing Fabry disease by denaturing high performance liquid chromatography.
Shabbeer J.; Robinson M.; Desnick R.J.;
Hum. Mutat. 25:299-305(2005)
Cited for: VARIANTS FD VAL-31; LEU-42; ARG-43; ASN-93; CYS-112; HIS-112; SER-112; SER-134; VAL-135; ASP-171; PHE-201; SER-215; GLU-234; ASP-261; TYR-264; VAL-264; GLY-276; PRO-285; PHE-300; ALA-328; VAL-328; LYS-338; ALA-358; GLU-358 DEL; ARG-404 DEL AND SER-414;

Functional and clinical consequences of novel alpha-galactosidase A mutations in Fabry disease.
Lukas J.; Scalia S.; Eichler S.; Pockrandt A.M.; Dehn N.; Cozma C.; Giese A.K.; Rolfs A.;
Hum. Mutat. 37:43-51(2016)
Cited for: CHARACTERIZATION OF VARIANTS FD ASP-20; PRO-20; PRO-21; GLY-33; GLU-35; TRP-36; SER-40; THR-42; PRO-45; ASP-48; TYR-56; LEU-60; PHE-64; ASP-80; HIS-86; ASN-91; THR-91; SER-94; TYR-94; ILE-113; THR-121; LEU-164; GLY-164; GLN-167; PHE-180; VAL-187; SER-196; THR-198; TYR-202; ARG-204; ARG-213; LEU-214; MET-219; PRO-227; SER-228; VAL-242; PHE-243; PRO-247; LYS-249; THR-253; ALA-254; ARG-259; ARG-262; GLY-269; GLY-276; VAL-309; ASN-315; ALA-316; SER-317; TYR-320; ARG-323; ARG-327; LEU-327; ARG-328; ARG-330; PRO-342; GLY-352; PRO-356; LYS-358; SER-360; ALA-375; SER-392; SER-399 AND ARG-404 DEL; CHARACTERIZATION OF VARIANTS PRO-3; VAL-3; GLY-71; THR-154; VAL-289 AND ASN-313; CATALYTIC ACTIVITY; FUNCTION;

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.