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UniProtKB/Swiss-Prot Q68CP4: Variant p.Gly290Arg

Heparan-alpha-glucosaminide N-acetyltransferase
Variant information

Variant position:  290
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 Glycine (G) to Arginine (R) at position 290 (G290R, p.Gly290Arg).
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 glycine (G) to large size and basic (R)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -2
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 MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum.
Any additional useful information about the variant.

Sequence information

Variant position:  290
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  663
The length of the canonical 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.



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.

Chain 1 – 663 Heparan-alpha-glucosaminide N-acetyltransferase
Transmembrane 276 – 296 Helical
Active site 297 – 297
Disulfide bond 151 – 462
Mutagenesis 297 – 297 H -> A. Loss of enzymatic activity, but correctly targeted and processed.

Literature citations

Protein misfolding as an underlying molecular defect in mucopolysaccharidosis III type C.
Feldhammer M.; Durand S.; Pshezhetsky A.V.;
PLoS ONE 4:E7434-E7434(2009)
Cited for: FUNCTION; GLYCOSYLATION; CHARACTERIZATION OF VARIANT MPS3C THR-643; CHARACTERIZATION OF VARIANTS PHE-104; PRO-165; GLN-265; ARG-290; LYS-301; LEU-311; HIS-372; CYS-431; SER-452; LYS-499; LEU-509; LYS-510; GLU-517; PHE-546; GLN-551; CYS-567; LEU-569; VAL-590 AND LEU-599;

Functional analysis of the HGSNAT gene in patients with mucopolysaccharidosis IIIC (Sanfilippo C Syndrome).
Fedele A.O.; Hopwood J.J.;
Hum. Mutat. 31:E1574-E1586(2010)
Cited for: CHARACTERIZATION OF VARIANTS MPS3C PHE-104; PRO-165; ARG-290; LEU-311; CYS-372; CYS-431; SER-452; LYS-499; LYS-510; GLU-514; GLU-517; PHE-546; CYS-567; LEU-569; VAL-590; LEU-599 AND THR-643; CHARACTERIZATION OF VARIANTS GLN-265; LEU-509 AND GLN-551;

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.