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UniProtKB/Swiss-Prot Q8NBK3: Variant p.Ala279Val

Formylglycine-generating enzyme
Gene: SUMF1
Variant information

Variant position:  279
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 Alanine (A) to Valine (V) at position 279 (A279V, p.Ala279Val).
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 small size and hydrophobic (A) to medium size and hydrophobic (V)
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 MSD; loss of activity; decreases its specific enzyme activity to about 23%; does not affect localization of the protein in the endoplasmic reticulum of MSD fibroblasts; protein stability is decreased.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  279
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  374
The length of the canonical sequence.

Location on the sequence:   NIWQGEFPVTNTGEDGFQGT  A PVDAFPPNGYGLYNIVGNAW
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                         NIWQGEFPVTNTGEDGFQGTAPVDAFPPNGYGLYNIVGNAW

Mouse                         NIWQGKFPVSNTGEDGFQGTAPVDAFPPNGYGLYNIVGNVW

Bovine                        NIWQGEFPVTNTGEDGFRGTAPVDAFPPNGYGLYNIVGNAW

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.

TypePositionsDescription
Chain 34 – 374 Formylglycine-generating enzyme
Metal binding 259 – 259 Calcium 1
Metal binding 260 – 260 Calcium 1; via carbonyl oxygen
Metal binding 273 – 273 Calcium 1
Metal binding 275 – 275 Calcium 1; via carbonyl oxygen
Metal binding 293 – 293 Calcium 2; via carbonyl oxygen
Metal binding 296 – 296 Calcium 2; via carbonyl oxygen
Metal binding 298 – 298 Calcium 2; via carbonyl oxygen
Disulfide bond 218 – 365
Disulfide bond 235 – 346


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;

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;

Molecular analysis of SUMF1 mutations: stability and residual activity of mutant formylglycine-generating enzyme determine disease severity in multiple sulfatase deficiency.
Schlotawa L.; Steinfeld R.; von Figura K.; Dierks T.; Gaertner J.;
Hum. Mutat. 29:205-205(2008)
Cited for: CHARACTERIZATION OF VARIANTS MSD PRO-177; SER-179; VAL-279 AND TRP-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.