Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P16278: Variant p.Arg49Cys

Beta-galactosidase
Gene: GLB1
Feedback?
Variant information Variant position: help 49 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 49 (R49C, p.Arg49Cys). 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 and GM1G2; decrease in galactosidase activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 49 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 QRMFEIDYSRDSFLKDGQPF R YISGSIHYSRVPRFYWKDRL 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                         QRMFEIDYSRDSFLKDGQPFRYISGSIHYSRVPRFYWKDRL

                              QRTFTIDYSHNRFLKDGQPFRYISGSIHYSRVPRFYWKDRL

Mouse                         QRTFKLDYSRDRFLKDGQPFRYISGSIHYFRIPRFYWEDRL

Bovine                        QRTFQIDYRRNRFLKDGQPFRYISGSIHYFRVPRFYWKDRL

Cat                           QRTFKIDYGHNRFLKDGQPFRYISGSIHYFRVPRFYWKDRL
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



Literature citations
Human beta-galactosidase gene mutations in morquio B disease.
Oshima A.; Yoshida K.; Shimmoto M.; Fukuhara Y.; Sakuraba H.; Suzuki Y.;
Am. J. Hum. Genet. 49:1091-1093(1991)
Cited for: VARIANTS MPS4B LEU-273; HIS-482 AND CYS-509; VARIANT GM1G1 CYS-494; GM1-gangliosidosis (genetic beta-galactosidase deficiency): identification of four mutations in different clinical phenotypes among Japanese patients.
Nishimoto J.; Nanba E.; Inui K.; Okada S.; Suzuki K.;
Am. J. Hum. Genet. 49:566-574(1991)
Cited for: VARIANT GM1G1 CYS-49; VARIANT GM1G3 THR-51; VARIANT GM1G2 CYS-201; Recurrent and novel GLB1 mutations in India.
Bidchol A.M.; Dalal A.; Trivedi R.; Shukla A.; Nampoothiri S.; Sankar V.H.; Danda S.; Gupta N.; Kabra M.; Hebbar S.A.; Bhat R.Y.; Matta D.; Ekbote A.V.; Puri R.D.; Phadke S.R.; Gowrishankar K.; Aggarwal S.; Ranganath P.; Sharda S.; Kamate M.; Datar C.A.; Bhat K.; Kamath N.; Shah H.; Krishna S.; Gopinath P.M.; Verma I.C.; Nagarajaram H.A.; Satyamoorthy K.; Girisha K.M.;
Gene 567:173-181(2015)
Cited for: VARIANTS GM1G2 CYS-49; ARG-134; CYS-148; GLU-262; LEU-314; PRO-337; VAL-414; ASN-493; LEU-597 AND ILE-600; CHARACTERIZATION OF VARIANTS GM1G2 CYS-49; GLU-262; LEU-314; PRO-337; VAL-414; ASN-493; LEU-597 AND ILE-600; VARIANTS GM1G1 TRP-68; ARG-123; PRO-236; CYS-331; ASN-332; PRO-337; HIS-482 AND PRO-514; CHARACTERIZATION OF VARIANTS GM1G1 TRP-68; ARG-123; PRO-236; ASN-332; PRO-337; HIS-482 AND PRO-514; VARIANT GM1G3 PHE-297; CHARACTERIZATION OF VARIANT GM1G3 PHE-297; VARIANTS GLN-129 AND CYS-521; 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.