Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P16278: Variant p.Arg208Cys

Beta-galactosidase
Gene: GLB1
Feedback?
Variant information Variant position: help 208 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 Arginine (R) to Cysteine (C) at position 208 (R208C, p.Arg208Cys). 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 large size and basic (R) to medium size and polar (C) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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 GM1G1. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 208 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 677 The length of the canonical sequence.
Location on the sequence: help EYGSYFACDFDYLRFLQKRF R HHLGDDVVLFTTDGAHKTFL 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                         EYGSYFACDFDYLRFLQKRFRHHLGDDVVLFTTDGAHKTFL

                              EYGSYFTCDYDYLRFLQKLFHHHLGNDVLLFTTDGANEKFL

Mouse                         EYGSYFACDYDYLRFLVHRFRYHLGNDVILFTTDGASEKML

Bovine                        EYGSYLSCDYDYLRFLQKRFHDHLGEDVLLFTTDGVNERLL

Cat                           EYGSYFTCDYDYLRFLQRRFRDHLGGDVLLFTTDGAHEKFL
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 29 – 677 Beta-galactosidase
Active site 188 – 188 Proton donor
Disulfide bond 195 – 230
Alternative sequence 83 – 244 YVPWNFHEPWPGQYQFSEDHDVEYFLRLAHELGLLVILRPGPYICAEWEMGGLPAWLLEKESILLRSSDPDYLAAVDKWLGVLLPKMKPLLYQNGGPVITVQVENEYGSYFACDFDYLRFLQKRFRHHLGDDVVLFTTDGAHKTFLKCGALQGLYTTVDFGT -> LPGSCGQVVGSPSAQDEASPLSEWRASYNSA. In isoform 2.
Helix 197 – 211



Literature citations
Mutations in acid beta-galactosidase cause GM1-gangliosidosis in American patients.
Boustany R.-M.N.; Qian W.-H.; Suzuki K.;
Am. J. Hum. Genet. 53:881-888(1993)
Cited for: VARIANTS GM1G1 CYS-208 AND ARG-578; VARIANTS GM1G2 HIS-590 AND GLY-632; Six novel beta-galactosidase gene mutations in Brazilian patients with GM1-gangliosidosis.
Silva C.M.D.; Severini M.H.; Sopelsa A.; Coelho J.C.; Zaha A.; d'Azzo A.; Giugliani R.;
Hum. Mutat. 13:401-409(1999)
Cited for: VARIANTS GM1G1 HIS-59; SER-121; CYS-208; MET-240 AND ASN-491; VARIANTS LEU-10; CYS-521 AND GLY-532; Role of beta-galactosidase and elastin binding protein in lysosomal and nonlysosomal complexes of patients with GM1-gangliosidosis.
Caciotti A.; Donati M.A.; Boneh A.; d'Azzo A.; Federico A.; Parini R.; Antuzzi D.; Bardelli T.; Nosi D.; Kimonis V.; Zammarchi E.; Morrone A.;
Hum. Mutat. 25:285-292(2005)
Cited for: VARIANTS GM1G1 HIS-59; CYS-59; CYS-208; MET-239; TYR-281; HIS-482; ASP-579; ASN-591 AND CYS-591; VARIANT GM1G2 HIS-201; VARIANT GM1G3 CYS-521; CHARACTERIZATION OF VARIANTS GM1G1 HIS-59; CYS-59; CYS-208; MET-239; TYR-281; HIS-482; ASP-579; ASN-591 AND CYS-591; CHARACTERIZATION OF VARIANT GM1G2 HIS-201; CHARACTERIZATION OF VARIANT GM1G3 CYS-521; FUNCTION; CATALYTIC ACTIVITY; Identification of 14 novel GLB1 mutations, including five deletions, in 19 patients with GM1 gangliosidosis from South America.
Santamaria R.; Blanco M.; Chabas A.; Grinberg D.; Vilageliu L.;
Clin. Genet. 71:273-279(2007)
Cited for: VARIANTS GM1G1 CYS-59; HIS-59; VAL-134; LEU-147 DEL; SER-162; CYS-208; ASP-272; 377-VAL--LYS-381 DEL; TYR-491; LEU-549 AND CYS-590; VARIANT GM1G2 HIS-201; VARIANT GM1G3 ARG-155; VARIANTS GM1-GANGLIOSIDOSIS LEU-434 AND GLU-554;
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.