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UniProtKB/Swiss-Prot P28472: Variant p.Asp120Asn

Gamma-aminobutyric acid receptor subunit beta-3
Gene: GABRB3
Variant information

Variant position:  120
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 Aspartate (D) to Asparagine (N) at position 120 (D120N, p.Asp120Asn).
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 acidic (D) to medium size and polar (N)
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

Variant description:  In DEE43; no effect on localization to the plasma membrane; decreased GABA-gated chloride ion channel activity; decreased single channel open probability.
Any additional useful information about the variant.

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

Sequence information

Variant position:  120
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  473
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.


Mouse                         S------------GIPLNLTLDNRVADQLWVPDTYFLNDKK

Rat                           S------------GIPLNLTLDNRVADQLWVPDTYFLNDKK

Chicken                       A------------GIPLNLTLDNRVADQLWVPDTYFLNDKK


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 26 – 473 Gamma-aminobutyric acid receptor subunit beta-3
Topological domain 26 – 245 Extracellular
Region 120 – 122 Benzamidine binding; agonist
Glycosylation 105 – 105 N-linked (GlcNAc...) asparagine

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)

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: INVOLVEMENT IN DEE43; VARIANTS DEE43 ASN-120; MET-157; PHE-182; LYS-249; GLN-256; HIS-293 AND THR-305;

Epileptic encephalopathy de novo GABRB mutations impair GABAA receptor function.
Janve V.S.; Hernandez C.C.; Verdier K.M.; Hu N.; Macdonald R.L.;
Ann. Neurol. 79:806-825(2016)

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.