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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9H9S5: Variant p.Ser221Arg

Ribitol 5-phosphate transferase FKRP
Gene: FKRP
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Variant information Variant position: help 221 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 Serine (S) to Arginine (R) at position 221 (S221R, p.Ser221Arg). 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 small size and polar (S) to large size and basic (R) 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 MDDGB5; severe form; brain involvement; intellectual disability and cerebellar cysts on cranial MRI; affects tetramer assembly; decreases the ribitol 5-phosphate transferase activity of about 95%. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 221 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 495 The length of the canonical sequence.
Location on the sequence: help LLRARDLFNLSAPLARPVGT S LFLQTALRGWAVQLLDLTFA 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                         LLRARDLFNLSAPLARPVGTSLFLQTALRGWAVQLLDLTFA

Mouse                         LMRSRDLFNLSVPLARPLATSLFLQTALRGWAVQLLDLTFA
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 1 – 495 Ribitol 5-phosphate transferase FKRP
Topological domain 30 – 495 Lumenal
Glycosylation 209 – 209 N-linked (GlcNAc...) asparagine
Helix 218 – 228



Literature citations
Crystal structures of fukutin-related protein (FKRP), a ribitol-phosphate transferase related to muscular dystrophy.
Kuwabara N.; Imae R.; Manya H.; Tanaka T.; Mizuno M.; Tsumoto H.; Kanagawa M.; Kobayashi K.; Toda T.; Senda T.; Endo T.; Kato R.;
Nat. Commun. 11:303-303(2020)
Cited for: X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 45-495 IN COMPLEXES WITH CDP-L-RIBITOL; MAGNESIUM AND ZINC; SUBUNIT; DISULFIDE BOND; GLYCOSYLATION AT ASN-172 AND ASN-209; REGION; MUTAGENESIS OF TYR-88; ASP-360; ASP-362; ASP-364 AND ASP-416; VARIANT MDDGB5 ARG-221; VARIANT MDDGC5 ILE-276; CHARACTERIZATION OF VARIANT MDDGB5 ARG-221; CHARACTERIZATION OF VARIANT MDDGC5 ILE-276; COFACTOR; CATALYTIC ACTIVITY; FUNCTION; FKRP gene mutations cause congenital muscular dystrophy, mental retardation, and cerebellar cysts.
Topaloglu H.; Brockington M.; Yuva Y.; Talim B.; Haliloglu G.; Blake D.J.; Torelli S.; Brown S.C.; Muntoni F.;
Neurology 60:988-992(2003)
Cited for: VARIANTS MDDGB5 ARG-221 AND THR-315;
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.