UniProtKB/SwissProt variant VAR

Variant information

Variant position:

560

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 Threonine (T) at position 560 (R560T, p.Arg560Thr).

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 (T)

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 CF; impairs maturation and trafficking to the cell membrane; decrease in channel activity.

Any additional useful information about the variant.

Other resources:

Links to websites of interest for the variant.

Variant rs80055610 [ dbSNP | Ensembl ]

Sequence information

Variant position:

560

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:

VLGEGGITLSGGQRARISLA R AVYKDADLYLLDSPFGYLDV

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                         VLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV

Gorilla                       VLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV

                              VLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV

Rhesus macaque                VLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV

Chimpanzee                    VLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV

Mouse                         VLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV

Rat                           VLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV

Pig                           VLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV

Bovine                        VLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV

Rabbit                        VLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV

Sheep                         VLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV

Horse                         VLGEGGIQLSGGQRARISLARAVYKDADLYLLDSPFGYLDV

Xenopus laevis                VLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFSYLDL

Zebrafish                     PMAEGGLNLSGGQKARVALARAVYRDADLYLLDAPFTHLDI

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	359 – 858	Cytoplasmic
Domain	423 – 646	ABC transporter 1
Modified residue	549 – 549	Phosphoserine
Helix	550 – 563

Literature citations

Revertant mutants G550E and 4RK rescue cystic fibrosis mutants in the first nucleotide-binding domain of CFTR by different mechanisms.
Roxo-Rosa M.; Xu Z.; Schmidt A.; Neto M.; Cai Z.; Soares C.M.; Sheppard D.N.; Amaral M.D.;
Proc. Natl. Acad. Sci. U.S.A. 103:17891-17896(2006)
Cited for: CHARACTERIZATION OF VARIANTS CF PHE-508 DEL; THR-560; GLU-561 AND ILE-562;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P13569: Variant p.Arg560Thr