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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P16278: Variant p.Ile51Thr

Beta-galactosidase
Gene: GLB1
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Variant information Variant position: help 51 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 Isoleucine (I) to Threonine (T) at position 51 (I51T, p.Ile51Thr). 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 (I) to medium size and polar (T) 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 GM1G3; no effect on catalytic activity; decreased protein stability. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 51 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 MFEIDYSRDSFLKDGQPFRY I SGSIHYSRVPRFYWKDRLLK 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                         MFEIDYSRDSFLKDGQPFRYISGSIHYSRVPRFYWKDRLLK

                              TFTIDYSHNRFLKDGQPFRYISGSIHYSRVPRFYWKDRLLK

Mouse                         TFKLDYSRDRFLKDGQPFRYISGSIHYFRIPRFYWEDRLLK

Bovine                        TFQIDYRRNRFLKDGQPFRYISGSIHYFRVPRFYWKDRLLK

Cat                           TFKIDYGHNRFLKDGQPFRYISGSIHYFRVPRFYWKDRLLK

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
Beta strand 51 – 54



Literature citations
Structural basis of pharmacological chaperoning for human beta-galactosidase.
Suzuki H.; Ohto U.; Higaki K.; Mena-Barragan T.; Aguilar-Moncayo M.; Ortiz Mellet C.; Nanba E.; Garcia Fernandez J.M.; Suzuki Y.; Shimizu T.;
J. Biol. Chem. 289:14560-14568(2014)
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 24-677 IN COMPLEX WITH GALACTOSE; CATALYTIC ACTIVITY; GLYCOSYLATION AT ASN-247; ASN-464; ASN-498 AND ASN-555; DISULFIDE BONDS; BIOPHYSICOCHEMICAL PROPERTIES; CHARACTERIZATION OF VARIANT GM1G3 THR-51; CHARACTERIZATION OF VARIANT GM1G1 AND GM1G2 CYS-201; 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; Human beta-galactosidase gene mutations in GM1-gangliosidosis: a common mutation among Japanese adult/chronic cases.
Yoshida K.; Oshima A.; Shimmoto M.; Fukuhara Y.; Sakuraba H.; Yanagisawa N.; Suzuki Y.;
Am. J. Hum. Genet. 49:435-442(1991)
Cited for: VARIANTS GM1G3 THR-51 AND GLN-457; VARIANTS GM1G1 ARG-123 AND CYS-316; VARIANT GM1G2 CYS-201;
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.