Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q68CP4: Variant p.Pro311Leu

Heparan-alpha-glucosaminide N-acetyltransferase
Gene: HGSNAT
Feedback?
Variant information Variant position: help 311 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 Proline (P) to Leucine (L) at position 311 (P311L, p.Pro311Leu). 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 Similar physico-chemical property. Both residues are medium size and hydrophobic. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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 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: help 311 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 663 The length of the canonical sequence.
Location on the sequence: help KYWYFKHASWNGLTVADLVF P WFVFIMGSSIFLSMTSILQR 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                         KYWYFKHASWNGLTVADLVFPWFVFIMGSSIFLSMTSILQR

Mouse                         KYWYFKHSSWNGLTVADLVFPWFVFIMGTSIFLSMTSILQR
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 – 663 Heparan-alpha-glucosaminide N-acetyltransferase
Transmembrane 303 – 323 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 VARIANTS MPS3C LEU-509 AND 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; LYS-510; GLU-517; PHE-546; GLN-551; CYS-567; LEU-569; VAL-590 AND LEU-599; Mutations in TMEM76 cause mucopolysaccharidosis IIIC (Sanfilippo C syndrome).
Hrebicek M.; Mrazova L.; Seyrantepe V.; Durand S.; Roslin N.M.; Noskova L.; Hartmannova H.; Ivanek R.; Cizkova A.; Poupetova H.; Sikora J.; Urinovska J.; Stranecky V.; Zeman J.; Lepage P.; Roquis D.; Verner A.; Ausseil J.; Beesley C.E.; Maire I.; Poorthuis B.J.H.M.; van de Kamp J.; van Diggelen O.P.; Wevers R.A.; Hudson T.J.; Fujiwara T.M.; Majewski J.; Morgan K.; Kmoch S.; Pshezhetsky A.V.;
Am. J. Hum. Genet. 79:807-819(2006)
Cited for: VARIANTS MPS3C PHE-104; GLN-265; LEU-311; CYS-372; HIS-372; CYS-431; SER-452; LYS-499; LYS-510; GLN-551; LEU-569; VAL-590; LEU-599 AND THR-643; FUNCTION; SUBCELLULAR LOCATION; TISSUE SPECIFICITY; Sanfilippo syndrome type C: mutation spectrum in the heparan sulfate acetyl-CoA: alpha-glucosaminide N-acetyltransferase (HGSNAT) gene.
Feldhammer M.; Durand S.; Mrazova L.; Boucher R.-M.; Laframboise R.; Steinfeld R.; Wraith J.E.; Michelakakis H.; van Diggelen O.P.; Hrebicek M.; Kmoch S.; Pshezhetsky A.V.;
Hum. Mutat. 30:918-925(2009)
Cited for: VARIANTS MPS3C PRO-165; GLN-265; LEU-311; CYS-372; CYS-431; LYS-499; LEU-509; GLU-514; GLU-517; PHE-546; GLN-551; LEU-569 AND THR-643; CHARACTERIZATION OF VARIANTS MPS3C GLN-265; CYS-431; LEU-509; GLN-551 AND THR-643; 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; GLN-265; ARG-290; LEU-311; CYS-372; CYS-431; SER-452; LYS-499; LEU-509; LYS-510; GLU-514; GLU-517; PHE-546; GLN-551; CYS-567; LEU-569; VAL-590; LEU-599 AND THR-643;
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.