Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q13586: Variant p.Phe108Ile

Stromal interaction molecule 1
Gene: STIM1
Feedback?
Variant information Variant position: help 108 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help From Phenylalanine (F) to Isoleucine (I) at position 108 (F108I, p.Phe108Ile). 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: help Change from large size and aromatic (F) to medium size and hydrophobic (I) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 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: help In TAM1; myoblasts with the mutation have significantly increased clustering of STIM1, regardless of calcium levels, indicating that calcium sensing in the sarcoplasmic reticulum is impaired. Any additional useful information about the variant.


Sequence information Variant position: help 108 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 685 The length of the canonical sequence.
Location on the sequence: help SDEFLREDLNYHDPTVKHST F HGEDKLISVEDLWKAWKSSE 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         SDEFLREDLNYH--DPTVKHSTFHGEDKLISVEDLWKAWKSSE

Mouse                         SDEFLREDLNYH--DPTVKHSTFHGEDKLISVEDLWKAWKS

Rat                           SDEFLREDLNYH--DPTVKHSTFHGEDKLISVEDLWKAWKA

Bovine                        SDEFLREDLNYH--DPTVKHSTFHGEDKLISVEDLWKAWKS

Caenorhabditis elegans        STGFMKEDMQMRGSERTRRENKFHGDDDAITVDDLWEAWFE
Sequence annotation in neighborhood: help 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.
TypePositionsDescription
Chain 23 – 685 Stromal interaction molecule 1
Topological domain 23 – 213 Extracellular
Domain 102 – 126 EF-hand 2
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.
Helix 102 – 108



Literature citations
Clinical, histological and genetic characterisation of patients with tubular aggregate myopathy caused by mutations in STIM1.
Boehm J.; Chevessier F.; Koch C.; Peche G.A.; Mora M.; Morandi L.; Pasanisi B.; Moroni I.; Tasca G.; Fattori F.; Ricci E.; Penisson-Besnier I.; Nadaj-Pakleza A.; Fardeau M.; Joshi P.R.; Deschauer M.; Romero N.B.; Eymard B.; Laporte J.;
J. Med. Genet. 51:824-833(2014)
Cited for: VARIANTS TAM1 THR-80; VAL-96; ILE-108; LEU-108 AND ASN-109; CHARACTERIZATION OF VARIANTS TAM1 THR-80; VAL-96; ILE-108; LEU-108 AND ASN-109; FUNCTION; SUBCELLULAR LOCATION;
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.