UniProtKB/SwissProt variant VAR

Variant information

Variant position:

178

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 Glycine (G) to Arginine (R) at position 178 (G178R, p.Gly178Arg).

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 glycine (G) to large size and basic (R)

The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:

-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:

In CF; loss of bicarbonate transport; no effect on protein maturation, subcellular location at the plasma membrane, nor on chloride channel activity.

Any additional useful information about the variant.

Other resources:

Links to websites of interest for the variant.

Variant rs80282562 [ dbSNP | Ensembl ]

Sequence information

Variant position:

178

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

Protein sequence length:

1480

The length of the canonical sequence.

Location on the sequence:

SLIYKKTLKLSSRVLDKISI G QLVSLLSNNLNKFDEGLALA

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                         SLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALA

Gorilla                       SLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALA

Rhesus macaque                SLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALA

Chimpanzee                    SLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALA

Mouse                         SLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALA

Rat                           SLIYKKTLKLSSRVLDKISIGQLISLLSNNLNKFDEGLALA

Pig                           SLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALA

Bovine                        SLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALA

Rabbit                        SLIYKKTLKLSSRVLDKISIGQLISLLSNNLNKFDEGLALA

Sheep                         SLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALA

Horse                         SLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALA

Xenopus laevis                SLIYKKTLKLSSKVLDKISTGQLVSLLSNNLNKFDEGLALA

Zebrafish                     SIIYKKTLKLSSRVLDKISTGQLVSLMSANLGKFDQSLGMA

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 – 1480	Cystic fibrosis transmembrane conductance regulator
Topological domain	147 – 195	Cytoplasmic
Domain	81 – 365	ABC transmembrane type-1 1
Helix	177 – 185

Literature citations

Molecular characterization of cystic fibrosis: 16 novel mutations identified by analysis of the whole cystic fibrosis conductance transmembrane regulator (CFTR) coding regions and splice site junctions.
Fanen P.; Ghanem N.; Vidaud M.; Besmond C.; Martin J.; Costes B.; Plassa F.; Goossens M.;
Genomics 13:770-776(1992)
Cited for: VARIANTS VAL-44; MET-470; VAL-506; CYS-508; ALA-576; CYS-668; PHE-997; THR-1027 AND LEU-1162; VARIANTS CF GLY-44; ARG-178; ARG-225; TRP-334; PHE-508 DEL; 542-GLY--LEU-1480 DEL; ASP-551; ILE-562; ARG-628; 710-LYS--LEU-1480 DEL; 846-TRP--LEU-1480 DEL; CYS-913; 1063-TRP--LEU-1480 DEL; CYS-1066; 1092-TYR--LEU-1480 DEL; 1162-ARG--LEU-1480 DEL; GLU-1200; 1282-TRP--LEU-1480 DEL AND LYS-1303;

Aberrant CFTR-dependent HCO3- transport in mutations associated with cystic fibrosis.
Choi J.Y.; Muallem D.; Kiselyov K.; Lee M.G.; Thomas P.J.; Muallem S.;
Nature 410:94-97(2001)
Cited for: CHARACTERIZATION OF VARIANTS CF HIS-117; THR-148; ARG-178; LYS-193; ASP-551; SER-551; GLN-620; VAL-648; GLY-800; TYR-949; THR-1067; GLN-1070; GLU-1244; PRO-1255 AND ASP-1349;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P13569: Variant p.Gly178Arg