UniProtKB/Swiss-Prot P16278 : Variant p.Arg201His
Beta-galactosidase
Gene: GLB1
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Variant information
Variant position:
201
The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:
LP/P [Disclaimer : Variants classification is intended for research purposes only, not for clinical and diagnostic use . The label disease variant is assigned according to literature reports on probable disease-association that can be based on theoretical reasons. This label must not be considered as a definitive proof for the pathogenic role of a variant. ]
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 201 (R201H, p.Arg201His).
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 and GM1G2; also in a patient with a slowly progressive GM1-gangliosidosis form; 36.2% of wild-type galactosidase activity.
Any additional useful information about the variant.
Other resources:
Links to websites of interest for the variant.
Sequence information
Variant position:
201
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:
ITVQVENEYGSYFACDFDYL
R FLQKRFRHHLGDDVVLFTTD
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 ITVQVENEYGSYFACDFDYLR FLQKRFRHHLGDDVVLFTTD
ITMQVENEYGSYFTCDYDYLR FLQKLFHHHLGNDVLLFTTD
Mouse ITVQVENEYGSYFACDYDYLR FLVHRFRYHLGNDVILFTTD
Bovine ITVQVENEYGSYLSCDYDYLR FLQKRFHDHLGEDVLLFTTD
Cat ITVQVENEYGSYFTCDYDYLR FLQRRFRDHLGGDVLLFTTD
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
Active site
188 – 188
Proton donor
Binding site
187 – 187
Disulfide bond
195 – 230
Alternative sequence
83 – 244
YVPWNFHEPWPGQYQFSEDHDVEYFLRLAHELGLLVILRPGPYICAEWEMGGLPAWLLEKESILLRSSDPDYLAAVDKWLGVLLPKMKPLLYQNGGPVITVQVENEYGSYFACDFDYLRFLQKRFRHHLGDDVVLFTTDGAHKTFLKCGALQGLYTTVDFGT -> LPGSCGQVVGSPSAQDEASPLSEWRASYNSA. In isoform 2.
Helix
197 – 211
Literature citations
Beta-Galactosidase gene mutations in patients with slowly progressive GM1 gangliosidosis.
Kaye E.M.; Shalish C.; Livermore J.; Taylor H.A.; Stevenson R.E.; Breakefield X.O.;
J. Child Neurol. 12:242-247(1997)
Cited for: VARIANTS SLOWLY PROGRESSIVE GM1-GANGLIOSIDOSIS HIS-201; SER-266 AND CYS-509;
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;
Elastogenesis in cultured dermal fibroblasts from patients with lysosomal beta-galactosidase, protective protein/cathepsin A and neuraminidase-1 deficiencies.
Tatano Y.; Takeuchi N.; Kuwahara J.; Sakuraba H.; Takahashi T.; Takada G.; Itoh K.;
J. Med. Invest. 53:103-112(2006)
Cited for: VARIANTS MPS4B LEU-273; HIS-482 AND CYS-509; VARIANTS GM1G1 CYS-201; HIS-201 AND HIS-318;
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.