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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q8NBK3: Variant p.Arg349Gln

Formylglycine-generating enzyme
Gene: SUMF1
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Variant information Variant position: help 349 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 Arginine (R) to Glutamine (Q) at position 349 (R349Q, p.Arg349Gln). 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 large size and basic (R) to medium size and polar (Q) 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 MSD; loss of activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 349 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 374 The length of the canonical sequence.
Location on the sequence: help KKGGSYMCHRSYCYRYRCAA R SQNTPDSSASNLGFRCAADR 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                         KKGGSYMCHRSYCYRYRCAARSQNTPDSSASNLGFRCAADR

Mouse                         KKGGSYMCHKSYCYRYRCAARSQNTPDSSASNLGFRCAADH

Bovine                        KKGGSYMCHKSYCYRYRCAARSQNTPDSSASNLGFRCAADH
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 34 – 374 Formylglycine-generating enzyme
Region 341 – 360 Interaction with sulfatases
Binding site 336 – 336
Binding site 341 – 341
Disulfide bond 218 – 365
Alternative sequence 340 – 374 YCYRYRCAARSQNTPDSSASNLGFRCAADRLPTMD -> QEYYDPYFQDVASEMLRRHTASRWKAFSSLEPCCSIRRHQQYAAIERLTCGKFELRCASLRKIDCLNTNIACSYSMRQHGPRLHCVD. In isoform 3.
Mutagenesis 333 – 333 S -> A. Loss of activity.
Mutagenesis 333 – 333 S -> T. Reduces activity by 99%.
Mutagenesis 336 – 336 C -> S. Loss of activity.
Mutagenesis 337 – 337 H -> A. Reduces activity 5-fold.
Mutagenesis 340 – 340 Y -> F. No effect.
Mutagenesis 341 – 341 C -> S. Loss of activity.



Literature citations
Multiple sulfatase deficiency is caused by mutations in the gene encoding the Homo sapiens C-alpha-formyglycine-generating enzyme.
Dierks T.; Schmidt B.; Borissenko L.V.; Peng J.; Preusser A.; Mariappan M.; von Figura K.;
Cell 113:435-444(2003)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); VARIANTS MSD VAL-279; ARG-336; GLN-349 AND TRP-349; VARIANT ASN-63; The multiple sulfatase deficiency gene encodes an essential and limiting factor for the activity of sulfatases.
Cosma M.P.; Pepe S.; Annunziata I.; Newbold R.F.; Grompe M.; Parenti G.; Ballabio A.;
Cell 113:445-456(2003)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); VARIANTS MSD PRO-155; TYR-218; ARG-336; CYS-345; PRO-348; GLN-349 AND TRP-349; FUNCTION; Molecular and functional analysis of SUMF1 mutations in multiple sulfatase deficiency.
Cosma M.P.; Pepe S.; Parenti G.; Settembre C.; Annunziata I.; Wade-Martins R.; Domenico C.D.; Natale P.D.; Mankad A.; Cox B.; Uziel G.; Mancini G.M.; Zammarchi E.; Donati M.A.; Kleijer W.J.; Filocamo M.; Carrozzo R.; Carella M.; Ballabio A.;
Hum. Mutat. 23:576-581(2004)
Cited for: VARIANTS MSD PHE-20; PRO-177; TRP-224; ILE-259 AND LEU-266; CHARACTERIZATION OF VARIANTS MSD PHE-20; PRO-155; PRO-177; TYR-218; TRP-224; ILE-259; LEU-266; VAL-279; ARG-336; CYS-345; PRO-348; TRP-349 AND GLN-349;
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.