UniProtKB/Swiss-Prot Q12879: Variant p.Arg370Trp

Glutamate receptor ionotropic, NMDA 2A
Gene: GRIN2A
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Variant information Variant position:

370 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

US 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 Arginine (R) to Tryptophan (W) at position 370 (R370W, p.Arg370Trp). 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 large size and basic (R) to large size and aromatic (W) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

-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:

In FESD; uncertain significance; no effect on function in ion transmembrane transport when expressed in Xenopus oocytes; has no effect on channel basal gating properties and activation by glutamate and glycine; mutant channels are more responsive to inhibition by Zn(2+) than wild-type channels. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs761168789 [ dbSNP | Ensembl ]

Sequence information Variant position:

370 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

1464 The length of the canonical sequence.
Location on the sequence:

FTEEGYQVHPRLVVIVLNKD R EWEKVGKWENHTLSLRHAVW 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                         FTEEGYQVHPRLVVIVLNKDREWEKVGKWENHTLSLRHAVW

Chimpanzee                    FTEEGYQVHPRLVVIVLNKDREWEKVGKWENHTLSLRHAVW

Mouse                         FTEEGYQVHPRLVVIVLNKDREWEKVGKWENQTLSLRHAVW

Rat                           FTEEGYQVHPRLVVIVLNKDREWEKVGKWENQTLSLRHAVW

Xenopus laevis                FTEDGYQANPKLVVLLLNMEREWEKVGKWENKSLNMKYPVW

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.

Type	Positions	Description
Chain	23 – 1464	Glutamate receptor ionotropic, NMDA 2A
Topological domain	23 – 555	Extracellular
Glycosylation	380 – 380	N-linked (GlcNAc...) asparagine

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;

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.