UniProtKB/Swiss-Prot P16278: Variant p.Arg201Cys

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] 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 Cysteine (C) at position 201 (R201C, p.Arg201Cys). 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 (C) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

-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:

In GM1G1 and GM1G2; no effect on intrinsic catalytic activity; decreased protein stability; 8.4% of wild-type galactosidase activity; activity severely reduced in transfection with variant F-436. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs72555360 [ dbSNP | Ensembl ]

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                         ITVQVENEYGSYFACDFDYLRFLQKRFRHHLGDDVVLFTTD

                              ITMQVENEYGSYFTCDYDYLRFLQKLFHHHLGNDVLLFTTD

Mouse                         ITVQVENEYGSYFACDYDYLRFLVHRFRYHLGNDVILFTTD

Bovine                        ITVQVENEYGSYLSCDYDYLRFLQKRFHDHLGEDVLLFTTD

Cat                           ITVQVENEYGSYFTCDYDYLRFLQRRFRDHLGGDVLLFTTD

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
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; Modulating action of the new polymorphism L436F detected in the GLB1 gene of a type-II GM1 gangliosidosis patient.
Caciotti A.; Bardelli T.; Cunningham J.; D'Azzo A.; Zammarchi E.; Morrone A.;
Hum. Genet. 113:44-50(2003)
Cited for: VARIANTS GM1G2 TRP-68 AND CYS-201; CHARACTERIZATION OF VARIANTS GM1G2 TRP-68 AND CYS-201; VARIANT PHE-436; MODULATING ACTION OF VARIANT PHE-436; 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; 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.