UniProtKB/SwissProt variant VAR

Variant information

Variant position:

760

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 Glutamine (Q) at position 760 (R760Q, p.Arg760Gln).

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 (Q)

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 SPH4; Prague II; induces abnormal cations sodium and potassium fluxes; decreases anion chloride transport.

Any additional useful information about the variant.

Other resources:

Links to websites of interest for the variant.

Variant rs121912755 [ dbSNP | Ensembl ]

Sequence information

Variant position:

760

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

Protein sequence length:

911

The length of the canonical sequence.

Location on the sequence:

VMGKASTPGAAAQIQEVKEQ R ISGLLVAVLVGLSILMEPIL

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                         VMGKASTPGAAAQIQEVKEQRISGLLVAVLVGLSILMEPIL

Mouse                         VMGKASGPGAAAQIQEVKEQRISGLLVSVLVGLSILMEPIL

Rat                           VMGKASGPGAAAQIQEVKEQRISGLLVSVLVGLSILMEPIL

Chicken                       VVGKSAVPGERAHIVEVKEQRLSGLLVAVLIGVSILMEPIL

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 – 911	Band 3 anion transport protein
Topological domain	738 – 760	Cytoplasmic

Literature citations

Mutations of conserved arginines in the membrane domain of erythroid band 3 lead to a decrease in membrane-associated band 3 and to the phenotype of hereditary spherocytosis.
Jarolim P.; Rubin H.L.; Brabec V.; Chrobak L.; Zolotarev A.S.; Alper S.L.; Brugnara C.; Wichterle H.; Palek J.;
Blood 85:634-640(1995)
Cited for: VARIANTS SPH4 GLN-760; TRP-760; CYS-808 AND TRP-870;

Characteristic features of the genotype and phenotype of hereditary spherocytosis in the Japanese population.
Yawata Y.; Kanzaki A.; Yawata A.; Doerfler W.; Oezcan R.; Eber S.W.;
Int. J. Hematol. 71:118-135(2000)
Cited for: VARIANTS SPH4 ARG-130; ARG-455; ARG-714; TRP-760; GLN-760; HIS-808; ARG-837 AND MET-837; VARIANTS ALA-38; GLU-56; ASP-72 AND LEU-854;

Trafficking and folding defects in hereditary spherocytosis mutants of the human red cell anion exchanger.
Quilty J.A.; Reithmeier R.A.;
Traffic 1:987-998(2000)
Cited for: CHARACTERIZATION OF VARIANTS PRO-707; GLN-760; TRP-760; CYS-808; PRO-834; MET-837 AND TRP-870;

Monovalent cation leaks in human red cells caused by single amino-acid substitutions in the transport domain of the band 3 chloride-bicarbonate exchanger, AE1.
Bruce L.J.; Robinson H.C.; Guizouarn H.; Borgese F.; Harrison P.; King M.-J.; Goede J.S.; Coles S.E.; Gore D.M.; Lutz H.U.; Ficarella R.; Layton D.M.; Iolascon A.; Ellory J.C.; Stewart G.W.;
Nat. Genet. 37:1258-1263(2005)
Cited for: INVOLVEMENT IN CHC AND SPH4; VARIANT GLU-56; VARIANTS CHC PRO-687; PRO-731 AND ARG-734; VARIANTS SPH4 TYR-705 AND GLN-760; CHARACTERIZATION OF VARIANTS CHC PRO-687; PRO-731 AND ARG-734; CHARACTERIZATION OF VARIANTS SPH4 TYR-705 AND GLN-760;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P02730: Variant p.Arg760Gln