UniProtKB/SwissProt variant VAR

Variant information

Variant position:

115

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 Threonine (T) to Alanine (A) at position 115 (T115A, p.Thr115Ala).

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 medium size and polar (T) to small size and hydrophobic (A)

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

BLOSUM score:

0

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 SCN8; decreases expression levels; decreases GTPase activity; decreases neutrophil numbers and migration capacity.

Any additional useful information about the variant.

Sequence information

Variant position:

115

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

Protein sequence length:

504

The length of the canonical sequence.

Location on the sequence:

TPTKGKQNVIMFVGLQGSGK T TTCSKLAYYYQRKGWKTCLI

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                         TPTKGKQNVIMFVGLQGSGKTTTCSKLAYYYQRKGWKTCLI

                              TPTKGKQNVIMFVGLQGSGKTTTCSKLAYYYQRKGWKTCLI

Mouse                         TPTKGKQNVIMFVGLQGSGKTTTCSKLAYYYQRKGWKTCLI

Rat                           TPTKGKQNVIMFVGLQGSGKTTTCSKLAYFYQRKGWKTCLI

Bovine                        TPTKGKQNVIMFVGLQGSGKTTTCSKLAYYYQRKGWKTCLI

Zebrafish                     TPTKGKNNVIMFVGLQGSGKTTTCSKLAYYFQRKGWKTCLI

Slime mold                    KPTKGKSNIVMFVGLQGAGKTTSVTKLAYFYKKKGFSTAIV

Baker's yeast                 VPKKRKTNIIMFVGLQGSGKTTSCTKLAVYYSKRGFKVGLV

Fission yeast                 TPKKGRPSVIMMVGLQGSGKTTTCSKLALHYQRRGLKSCLV

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 – 504	Signal recognition particle 54 kDa protein
Nucleotide binding	108 – 115	GTP
Region	1 – 295	G-domain
Helix	114 – 127

Literature citations

Mutations in signal recognition particle SRP54 cause syndromic neutropenia with Shwachman-Diamond-like features.
Carapito R.; Konantz M.; Paillard C.; Miao Z.; Pichot A.; Leduc M.S.; Yang Y.; Bergstrom K.L.; Mahoney D.H.; Shardy D.L.; Alsaleh G.; Naegely L.; Kolmer A.; Paul N.; Hanauer A.; Rolli V.; Mueller J.S.; Alghisi E.; Sauteur L.; Macquin C.; Morlon A.; Sancho C.S.; Amati-Bonneau P.; Procaccio V.; Mosca-Boidron A.L.; Marle N.; Osmani N.; Lefebvre O.; Goetz J.G.; Unal S.; Akarsu N.A.; Radosavljevic M.; Chenard M.P.; Rialland F.; Grain A.; Bene M.C.; Eveillard M.; Vincent M.; Guy J.; Faivre L.; Thauvin-Robinet C.; Thevenon J.; Myers K.; Fleming M.D.; Shimamura A.; Bottollier-Lemallaz E.; Westhof E.; Lengerke C.; Isidor B.; Bahram S.;
J. Clin. Invest. 127:4090-4103(2017)
Cited for: VARIANTS SCN8 ALA-115; THR-117 DEL AND GLU-226; CHARACTERIZATION OF VARIANTS SCN8 ALA-115; THR-117 DEL AND GLU-226; CATALYTIC ACTIVITY; FUNCTION;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P61011: Variant p.Thr115Ala