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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q12879: Variant p.Pro79Arg

Glutamate receptor ionotropic, NMDA 2A
Gene: GRIN2A
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Variant information Variant position: help 79 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 Arginine (R) at position 79 (P79R, p.Pro79Arg). 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 Change from medium size and hydrophobic (P) to large size and basic (R) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -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: help In FESD; decreased function in ion transmembrane transport when expressed in Xenopus oocytes; decreased localization to cell membrane; mutant channels are less responsive to inhibition by Zn(2+) than wild-type channels. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 79 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 1464 The length of the canonical sequence.
Location on the sequence: help QAAGLPLDVNVVALLMNRTD P KSLITHVCDLMSGARIHGLV 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                         QAAGLPLDVNVVALLMNRTDPKSLITHVCDLMSGARIHGLV

Chimpanzee                    QAAGLPLDVNVVALLMNRTDPKSLITHVCDLMSGARIHGLV

Mouse                         QATGLPLDVNVVALLMNRTDPKSLITHVCDLMSGARIHGLV

Rat                           QATGLPLDVNVVALLMNRTDPKSLITHVCDLMSGARIHGLV

Xenopus laevis                MS--LDFDVNVVTLLVNQTDPKSIITHVCDLMSGTKIHGVV
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 23 – 1464 Glutamate receptor ionotropic, NMDA 2A
Topological domain 23 – 555 Extracellular
Glycosylation 75 – 75 N-linked (GlcNAc...) asparagine
Helix 79 – 91



Literature citations
Mutations in GRIN2A cause idiopathic focal epilepsy with rolandic spikes.
Lemke J.R.; Lal D.; Reinthaler E.M.; Steiner I.; Nothnagel M.; Alber M.; Geider K.; Laube B.; Schwake M.; Finsterwalder K.; Franke A.; Schilhabel M.; Jahn J.A.; Muhle H.; Boor R.; Van Paesschen W.; Caraballo R.; Fejerman N.; Weckhuysen S.; De Jonghe P.; Larsen J.; Moller R.S.; Hjalgrim H.; Addis L.; Tang S.; Hughes E.; Pal D.K.; Veri K.; Vaher U.; Talvik T.; Dimova P.; Guerrero Lopez R.; Serratosa J.M.; Linnankivi T.; Lehesjoki A.E.; Ruf S.; Wolff M.; Buerki S.; Wohlrab G.; Kroell J.; Datta A.N.; Fiedler B.; Kurlemann G.; Kluger G.; Hahn A.; Haberlandt D.E.; Kutzer C.; Sperner J.; Becker F.; Weber Y.G.; Feucht M.; Steinbock H.; Neophythou B.; Ronen G.M.; Gruber-Sedlmayr U.; Geldner J.; Harvey R.J.; Hoffmann P.; Herms S.; Altmuller J.; Toliat M.R.; Thiele H.; Nurnberg P.; Wilhelm C.; Stephani U.; Helbig I.; Lerche H.; Zimprich F.; Neubauer B.A.; Biskup S.; von Spiczak S.;
Nat. Genet. 45:1067-1072(2013)
Cited for: VARIANTS FESD ARG-79; ILE-183; TYR-231; VAL-243; VAL-290; TRP-370; ARG-436; SER-547 DEL; SER-699; VAL-705; LYS-714; THR-727; LEU-734; GLU-772; THR-814; PHE-904 AND SER-976; CHARACTERIZATION OF VARIANT FESD VAL-243; Altered zinc sensitivity of NMDA receptors harboring clinically-relevant mutations.
Serraz B.; Grand T.; Paoletti P.;
Neuropharmacology 109:196-204(2016)
Cited for: CHARACTERIZATION OF VARIANTS ARG-79; ILE-183; SER-184; TYR-231; VAL-243; VAL-290; SER-295; TRP-370 AND ARG-436; ACTIVITY REGULATION; Epilepsy-associated GRIN2A mutations reduce NMDA receptor trafficking and agonist potency - molecular profiling and functional rescue.
Addis L.; Virdee J.K.; Vidler L.R.; Collier D.A.; Pal D.K.; Ursu D.;
Sci. Rep. 7:66-66(2017)
Cited for: CHARACTERIZATION OF VARIANTS ARG-79; TYR-231; ARG-436; ARG-483; VAL-705; LYS-714; ASN-731; THR-814; ASN-933 AND SER-976; 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.