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UniProtKB/Swiss-Prot Q9UJJ9: Variant p.Gly106Ser

N-acetylglucosamine-1-phosphotransferase subunit gamma
Gene: GNPTG
Chromosomal location: 16p13.3
Variant information

Variant position:  106
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Disease [Disclaimer]
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Glycine (G) to Serine (S) at position 106 (G106S, p.Gly106Ser).
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 small size and polar (S)
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

Involvement in disease:  Mucolipidosis type III complementation group C (MLIIIC) [MIM:252605]: Autosomal recessive disease of lysosomal hydrolase trafficking. Unlike the related diseases, mucolipidosis II and IIIA, the enzyme affected in mucolipidosis IIIC (GlcNAc-phosphotransferase) retains full transferase activity on synthetic substrates but lacks activity on lysosomal hydrolases. Typical clinical findings include stiffness of the hands and shoulders, claw-hand deformity, scoliosis, short stature, coarse facies, and mild mental retardation. Radiographically, severe dysostosis multiplex of the hip is characteristic and frequently disabling. The clinical diagnosis can be confirmed by finding elevated serum lysosomal enzyme levels and/or decreased lysosomal enzyme levels in cultured fibroblasts. {ECO:0000269|PubMed:10712439, ECO:0000269|PubMed:15060128, ECO:0000269|PubMed:15532026, ECO:0000269|PubMed:19370764, ECO:0000269|PubMed:24316125, ECO:0000269|PubMed:26108976, ECO:0000269|PubMed:27038293}. Note=The disease is caused by mutations affecting the gene represented in this entry.
The name and a short description of the disease associated with the variant. For more information about the disease, the user can refer to OMIM, following the link provided after the disease acronym.

Variant description:  In MLIIIC; decreased localization to Golgi apparatus.
Any additional useful information about the variant.

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



Sequence information

Variant position:  106
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  305
The length of the canonical sequence.

Location on the sequence:   FHNVTQHEQTFRWNAYSGIL  G IWHEWEIANNTFTGMWMRDG
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                         FHNVTQHEQTFRWNAYSGILGIWHEWEIANNTFTGMWMRDG

Mouse                         FHNVTQHEQTFRWNAYSGILGIWHEWEIINNTFKGMWMTDG

Bovine                        FHNVTQHEQTFRWNAYSGILGIWHEWEITNNTFRGMWMRDG

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 25 – 305 N-acetylglucosamine-1-phosphotransferase subunit gamma
Domain 69 – 126 PRKCSH
Glycosylation 88 – 88 N-linked (GlcNAc...) asparagine
Glycosylation 115 – 115 N-linked (GlcNAc...) asparagine


Literature citations

Genomic organisation of the UDP-N-acetylglucosamine-1-phosphotransferase gamma subunit (GNPTAG) and its mutations in mucolipidosis III.
Raas-Rothschild A.; Bargal R.; Goldman O.; Ben-Asher E.; Groener J.E.; Toutain A.; Stemmer E.; Ben-Neriah Z.; Flusser H.; Beemer F.A.; Penttinen M.; Olender T.; Rein A.J.; Bach G.; Zeigler M.;
J. Med. Genet. 41:E52-E52(2004)
Cited for: INVOLVEMENT IN MLIIIC; VARIANT MLIIIC SER-106;

Identification and molecular characterization of six novel mutations in the UDP-N-acetylglucosamine-1-phosphotransferase gamma subunit (GNPTG) gene in patients with mucolipidosis III gamma.
Persichetti E.; Chuzhanova N.A.; Dardis A.; Tappino B.; Pohl S.; Thomas N.S.; Rosano C.; Balducci C.; Paciotti S.; Dominissini S.; Montalvo A.L.; Sibilio M.; Parini R.; Rigoldi M.; Di Rocco M.; Parenti G.; Orlacchio A.; Bembi B.; Cooper D.N.; Filocamo M.; Beccari T.;
Hum. Mutat. 30:978-984(2009)
Cited for: VARIANTS MLIIIC SER-106 AND ASN-115 DEL; VARIANT MET-286;

Mucolipidosis III GNPTG missense mutations cause misfolding of the gamma subunit of GlcNAc-1-phosphotransferase.
van Meel E.; Kornfeld S.;
Hum. Mutat. 37:623-626(2016)
Cited for: CHARACTERIZATION OF VARIANT MLIIIC SER-106 AND TYR-142; CHARACTERIZATION OF VARIANT MET-286; SUBCELLULAR LOCATION;

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.