UniProtKB/SwissProt variant VAR

Variant information

Variant position:

126

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 Arginine (R) to Cysteine (C) at position 126 (R126C, p.Arg126Cys).

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 medium size and polar (C)

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 GLUT1DS1, GLUT1DS2 and DYT9; reduced transporter activity.

Any additional useful information about the variant.

Other resources:

Links to websites of interest for the variant.

Variant rs80359818 [ dbSNP | Ensembl ]

Sequence information

Variant position:

126

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

Protein sequence length:

492

The length of the canonical sequence.

Location on the sequence:

SAVLMGFSKLGKSFEMLILG R FIIGVYCGLTTGFVPMYVGE

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                         SAVLMGFSKLGKSFEMLILGRFIIGVY-CGLTTGFVPMYVGE

Mouse                         AAVLMGFSKLGKSFEMLILGRFIIGVY-CGLTTGFVPMYVG

Rat                           SAVLMGFSKLGKSFEMLILGRFIIGVY-CGLTTGFVPMYVG

Pig                           SAVLMGFSKLGKSFEMLILGRFIIGVY-CGLTTGFVPMYVG

Bovine                        SAVLMGFSKLGKSFEMLILGRFIIGVY-CGLTTGFVPMYVG

Rabbit                        SAVLMGFSKLAKSFEMLILGRFIIGVY-CGLTTGFVPMYVG

Sheep                         SAVLMGFSKLGKSFEMLILGRFIIGVY-CGLTTGFVPMYVG

Chicken                       AAVLMGFSKMALSFEMLILGRFIIGLY-SGLTTGFVPMYVG

Drosophila                    GACLMGFTKVSHSYEMLFLGRFIIGVN-CGLNTSLVPMYIS

Baker's yeast                 TRRLGATIDVEHSH-LRFLGNMTLNLWDCGGQDVFMENYFT

Fission yeast                 TRRLGATIDIEHSH-VRFLGNLVLNLWDCGGQEAFMENYLS

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	1 – 492	Solute carrier family 2, facilitated glucose transporter member 1
Transmembrane	121 – 144	Helical; Name=4
Binding site	137 – 137	Cytochalasin b inhibitor
Helix	119 – 145

Literature citations

Imaging the metabolic footprint of Glut1 deficiency on the brain.
Pascual J.M.; van Heertum R.L.; Wang D.; Engelstad K.; De Vivo D.C.;
Ann. Neurol. 52:458-464(2002)
Cited for: VARIANTS GLUT1DS1 CYS-126; HIS-126; LYS-146; CYS-153 AND TRP-333;

Early-onset absence epilepsy caused by mutations in the glucose transporter GLUT1.
Suls A.; Mullen S.A.; Weber Y.G.; Verhaert K.; Ceulemans B.; Guerrini R.; Wuttke T.V.; Salvo-Vargas A.; Deprez L.; Claes L.R.; Jordanova A.; Berkovic S.F.; Lerche H.; De Jonghe P.; Scheffer I.E.;
Ann. Neurol. 66:415-419(2009)
Cited for: VARIANT EIG12 PRO-223; VARIANTS GLUT1DS2 CYS-126 AND LEU-324; CHARACTERIZATION OF VARIANT EIG12 PRO-223; CHARACTERIZATION OF VARIANTS GLUT1DS2 CYS-126 AND LEU-324;

Paroxysmal choreoathetosis/spasticity (DYT9) is caused by a GLUT1 defect.
Weber Y.G.; Kamm C.; Suls A.; Kempfle J.; Kotschet K.; Schule R.; Wuttke T.V.; Maljevic S.; Liebrich J.; Gasser T.; Ludolph A.C.; Van Paesschen W.; Schols L.; De Jonghe P.; Auburger G.; Lerche H.;
Neurology 77:959-964(2011)
Cited for: VARIANTS DYT9 CYS-126 AND CYS-212;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P11166: Variant p.Arg126Cys