UniProtKB/Swiss-Prot P16278: Variant p.Arg59His

Beta-galactosidase
Gene: GLB1
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Variant information Variant position:

59 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

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:

From Arginine (R) to Histidine (H) at position 59 (R59H, p.Arg59His). 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 large size and basic (R) to medium size and polar (H) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

0 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 GM1G1; with cardiac involvement in some patients; loss of galactosidase activity; severe mutation. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs72555392 [ dbSNP | Ensembl ]

Sequence information Variant position:

59 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

677 The length of the canonical sequence.
Location on the sequence:

DSFLKDGQPFRYISGSIHYS R VPRFYWKDRLLKMKMAGLNA 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:

The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         DSFLKDGQPFRYISGSIHYSRVPRFYWKDRLLKMKMAGLNA

                              NRFLKDGQPFRYISGSIHYSRVPRFYWKDRLLKMKMAGLNA

Mouse                         DRFLKDGQPFRYISGSIHYFRIPRFYWEDRLLKMKMAGLNA

Bovine                        NRFLKDGQPFRYISGSIHYFRVPRFYWKDRLLKMKMAGLNA

Cat                           NRFLKDGQPFRYISGSIHYFRVPRFYWKDRLLKMKMAGLNA

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.

Type	Positions	Description
Chain	29 – 677	Beta-galactosidase
Helix	57 – 59

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; Identification of new mutations in six Italian patients affected by a variant form of infantile GM1-gangliosidosis with severe cardiomyopathy.
Morrone A.; Bardelli T.; Donati M.A.; Giorgi M.; Di Rocco R.; Gatti R.; Taddeucci G.; Ricci R.; D'Azzo A.; Zammarchi E.;
Cited for: VARIANTS GM1G1 HIS-59; ASN-591 AND CYS-591; 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; Beta-galactosidase gene mutations affecting the lysosomal enzyme and the elastin-binding protein in GM1-gangliosidosis patients with cardiac involvement.
Morrone A.; Bardelli T.; Donati M.A.; Giorgi M.; Di Rocco M.; Gatti R.; Parini R.; Ricci R.; Taddeucci G.; D'Azzo A.; Zammarchi E.;
Hum. Mutat. 15:354-366(2000)
Cited for: VARIANTS GM1G1 HIS-59; HIS-482; ASN-591 AND CYS-591; VARIANTS GM1G2 HIS-201 AND ASP-579; 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; Twenty-one novel mutations in the GLB1 gene identified in a large group of GM1-gangliosidosis and Morquio B patients: possible common origin for the prevalent p.R59H mutation among Gypsies.
Santamaria R.; Chabas A.; Coll M.J.; Miranda C.S.; Vilageliu L.; Grinberg D.;
Hum. Mutat. 27:1060-1060(2006)
Cited for: VARIANTS GM1G1 CYS-59; HIS-59; SER-136; VAL-151; PRO-173; CYS-199; ASP-272; ASN-346; CYS-347; PRO-420; ARG-422; ASN-441 AND CYS-590; VARIANT GM1G2 SER-264; VARIANTS GM1G3 HIS-201 AND LYS-420; VARIANTS MPS4B CYS-83; CYS-444; SER-494 AND ALA-500; VARIANTS PHE-436; CYS-521 AND GLY-532; 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; Expression and characterization of 14 GLB1 mutant alleles found in GM1-gangliosidosis and Morquio B patients.
Santamaria R.; Chabas A.; Callahan J.W.; Grinberg D.; Vilageliu L.;
J. Lipid Res. 48:2275-2282(2007)
Cited for: CHARACTERIZATION OF VARIANTS GM1G1 HIS-59; SER-162; PRO-173; HIS-201; PRO-420; ASN-441 AND CYS-590; CHARACTERIZATION OF VARIANTS MPS4B CYS-83; CYS-444 AND SER-494; CHARACTERIZATION OF VARIANT GM1G3 LYS-420 AND CYS-521; CHARACTERIZATION OF VARIANT GLY-532; GM1 gangliosidosis and Morquio B disease: expression analysis of missense mutations affecting the catalytic site of acid beta-galactosidase.
Hofer D.; Paul K.; Fantur K.; Beck M.; Buerger F.; Caillaud C.; Fumic K.; Ledvinova J.; Lugowska A.; Michelakakis H.; Radeva B.; Ramaswami U.; Plecko B.; Paschke E.;
Hum. Mutat. 30:1214-1221(2009)
Cited for: VARIANTS GM1G1 HIS-59; THR-132; ARG-184; ASP-190; CYS-201; HIS-201; MET-239; HIS-255; ILE-329; GLU-332; ASN-346; GLN-442 AND SER-597; VARIANTS GM1G2 GLN-68; ARG-155 AND HIS-333; VARIANTS GM1G3 MET-82; ASP-270 AND GLU-438; VARIANTS MPS4B PHE-149; TYR-198; LEU-273; ALA-397; PRO-408 AND ALA-500; CHARACTERIZATION OF VARIANTS GM1G1 THR-132; ARG-184; ASP-190; CYS-201; HIS-201; HIS-255; ILE-329; GLU-332 AND SER-597; CHARACTERIZATION OF VARIANTS GM1G2 GLN-68; ARG-155 AND HIS-333; CHARACTERIZATION OF VARIANTS GM1G3 ASP-270 AND GLU-438; CHARACTERIZATION OF VARIANTS MPS4B PHE-149; TYR-198; LEU-273; ALA-397; PRO-408 AND ALA-500; 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.