UniProtKB/SwissProt variant VAR

Stromal interaction molecule 1
Gene: STIM1
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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 Isoleucine (I) to Phenylalanine (F) at position 115 (I115F, p.Ile115Phe). 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 hydrophobic (I) to large size and aromatic (F) 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 STRMK and TAM1. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs527236030 [ dbSNP | Ensembl ]

Sequence information Variant position:

115 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

685 The length of the canonical sequence.
Location on the sequence:

DLNYHDPTVKHSTFHGEDKL I SVEDLWKAWKSSEVYNWTVD 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                         DLNYH--DPTVKHSTFHGEDKLISVEDLWKAWKSSEVYNWTVD

Mouse                         DLNYH--DPTVKHSTFHGEDKLISVEDLWKAWKSSEVYNWT

Rat                           DLNYH--DPTVKHSTFHGEDKLISVEDLWKAWKASEVYNWT

Bovine                        DLNYH--DPTVKHSTFHGEDKLISVEDLWKAWKSSEVYNWT

Caenorhabditis elegans        DMQMRGSERTRRENKFHGDDDAITVDDLWEAWFESIERTWT

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	23 – 685	Stromal interaction molecule 1
Topological domain	23 – 213	Extracellular
Domain	102 – 126	EF-hand 2
Glycosylation	131 – 131	N-linked (GlcNAc...) asparagine
Mutagenesis	108 – 108	F -> D. Constitutive localization in punctae at the cell membrane and constitutive activation of CRAC channels; when associated with D-110.
Mutagenesis	110 – 110	G -> D. Constitutive localization in punctae at the cell membrane and constitutive activation of CRAC channels; when associated with D-108.
Mutagenesis	131 – 131	N -> Q. Impairs ORAI1 ARC channel currents; when associated with Q-171.

Literature citations
Childhood onset tubular aggregate myopathy associated with de novo STIM1 mutations.
Hedberg C.; Niceta M.; Fattori F.; Lindvall B.; Ciolfi A.; D'Amico A.; Tasca G.; Petrini S.; Tulinius M.; Tartaglia M.; Oldfors A.; Bertini E.;
J. Neurol. 261:870-876(2014)
Cited for: VARIANTS TAM1 ARG-109 AND PHE-115; York platelet syndrome is a CRAC channelopathy due to gain-of-function mutations in STIM1.
Markello T.; Chen D.; Kwan J.Y.; Horkayne-Szakaly I.; Morrison A.; Simakova O.; Maric I.; Lozier J.; Cullinane A.R.; Kilo T.; Meister L.; Pakzad K.; Bone W.; Chainani S.; Lee E.; Links A.; Boerkoel C.; Fischer R.; Toro C.; White J.G.; Gahl W.A.; Gunay-Aygun M.;
Mol. Genet. Metab. 114:474-482(2015)
Cited for: VARIANTS STRMK PHE-115 AND TRP-304;

Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q13586: Variant p.Ile115Phe