Home  |  Contact

UniProtKB/Swiss-Prot Q9NP73: Variant p.Asn107Ser

Putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13
Gene: ALG13
Variant information

Variant position:  107
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 Asparagine (N) to Serine (S) at position 107 (N107S, p.Asn107Ser).
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 medium size and polar (N) to small size and polar (S)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  1
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:  Epileptic encephalopathy, early infantile, 36 (EIEE36) [MIM:300884]: A form of epileptic encephalopathy, a heterogeneous group of severe childhood onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. Some EIEE36 patients may present with an abnormal isoelectric focusing of serum transferrin, consistent with a diagnostic classification of congenital disorder of glycosylation type I. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions. {ECO:0000269|PubMed:22492991, ECO:0000269|PubMed:23033978, ECO:0000269|PubMed:23934111, ECO:0000269|PubMed:26138355, ECO:0000269|PubMed:27476654}. 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 EIEE36; de novo mutation detected in unrelated patients.
Any additional useful information about the variant.

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

Sequence information

Variant position:  107
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  1137
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 – 1137 Putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13
Region 1 – 125 Glycosyltransferase activity

Literature citations

De novo mutations in epileptic encephalopathies.
Allen A.S.; Berkovic S.F.; Cossette P.; Delanty N.; Dlugos D.; Eichler E.E.; Epstein M.P.; Glauser T.; Goldstein D.B.; Han Y.; Heinzen E.L.; Hitomi Y.; Howell K.B.; Johnson M.R.; Kuzniecky R.; Lowenstein D.H.; Lu Y.F.; Madou M.R.; Marson A.G.; Mefford H.C.; Esmaeeli Nieh S.; O'Brien T.J.; Ottman R.; Petrovski S.; Poduri A.; Ruzzo E.K.; Scheffer I.E.; Sherr E.H.; Yuskaitis C.J.; Abou-Khalil B.; Alldredge B.K.; Bautista J.F.; Berkovic S.F.; Boro A.; Cascino G.D.; Consalvo D.; Crumrine P.; Devinsky O.; Dlugos D.; Epstein M.P.; Fiol M.; Fountain N.B.; French J.; Friedman D.; Geller E.B.; Glauser T.; Glynn S.; Haut S.R.; Hayward J.; Helmers S.L.; Joshi S.; Kanner A.; Kirsch H.E.; Knowlton R.C.; Kossoff E.H.; Kuperman R.; Kuzniecky R.; Lowenstein D.H.; McGuire S.M.; Motika P.V.; Novotny E.J.; Ottman R.; Paolicchi J.M.; Parent J.M.; Park K.; Poduri A.; Scheffer I.E.; Shellhaas R.A.; Sherr E.H.; Shih J.J.; Singh R.; Sirven J.; Smith M.C.; Sullivan J.; Lin Thio L.; Venkat A.; Vining E.P.; Von Allmen G.K.; Weisenberg J.L.; Widdess-Walsh P.; Winawer M.R.;
Nature 501:217-221(2013)

Whole-exome sequencing improves the diagnosis yield in sporadic infantile spasm syndrome.
Dimassi S.; Labalme A.; Ville D.; Calender A.; Mignot C.; Boutry-Kryza N.; de Bellescize J.; Rivier-Ringenbach C.; Bourel-Ponchel E.; Cheillan D.; Simonet T.; Maincent K.; Rossi M.; Till M.; Mougou-Zerelli S.; Edery P.; Saad A.; Heron D.; des Portes V.; Sanlaville D.; Lesca G.;
Clin. Genet. 89:198-204(2016)

Diagnostic exome sequencing in persons with severe intellectual disability.
de Ligt J.; Willemsen M.H.; van Bon B.W.; Kleefstra T.; Yntema H.G.; Kroes T.; Vulto-van Silfhout A.T.; Koolen D.A.; de Vries P.; Gilissen C.; del Rosario M.; Hoischen A.; Scheffer H.; de Vries B.B.; Brunner H.G.; Veltman J.A.; Vissers L.E.;
N. Engl. J. Med. 367:1921-1929(2012)
Cited for: VARIANT EIEE36 SER-107;

De novo mutations in SLC1A2 and CACNA1A are important causes of epileptic encephalopathies.
Epi4K Consortium;
Am. J. Hum. Genet. 99:287-298(2016)
Cited for: VARIANT EIEE36 SER-107;

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.