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:
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 NIWQGEFPVTNTGEDGFQGT APVDAFPPNGYGLYNIVGNAW
Mouse NIWQGKFPVSNTGEDGFQGT APVDAFPPNGYGLYNIVGNVW
Bovine NIWQGEFPVTNTGEDGFRGT APVDAFPPNGYGLYNIVGNAW
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
34 – 374 Formylglycine-generating enzyme
259 – 259 Calcium 1
260 – 260 Calcium 1; via carbonyl oxygen
273 – 273 Calcium 1
275 – 275 Calcium 1; via carbonyl oxygen
293 – 293 Calcium 2; via carbonyl oxygen
296 – 296 Calcium 2; via carbonyl oxygen
298 – 298 Calcium 2; via carbonyl oxygen
218 – 365
235 – 346
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.;
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;
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