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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q13586: Variant p.His72Gln

Stromal interaction molecule 1
Gene: STIM1
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Variant information Variant position: help 72 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 Histidine (H) to Glutamine (Q) at position 72 (H72Q, p.His72Gln). 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 Similar physico-chemical property. Both residues are medium size and polar. 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.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 72 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 DKPLCHSEDEKLSFEAVRNI H KLMDDDANGDVDVEESDEFL 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                         DKPLCHSEDEKLSFEAVRNIHKLMDDDANGDVDVEESDEFL

Mouse                         DKPLCHSEDEKLSFEAVRNIHKLMDDDANGDVDVEESDEFL

Rat                           DKPLCHSEDEKLSFEAVRNIHKLMDDDANGDVDVEESDEFL

Bovine                        DKPLCHSEDEKLSFDAVRSIHKLMDDDANGDVDVEESDEFL

Caenorhabditis elegans        ---------DKLGYEAIRDIHRDMDDDHSGSIDRNESTGFM
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 64 – 97 EF-hand 1
Binding site 76 – 76
Binding site 78 – 78
Binding site 80 – 80
Binding site 82 – 82
Binding site 87 – 87
Mutagenesis 76 – 76 D -> AN. Increases Ca(2+) influx even when Ca(2+) stores are not depleted. Promotes constitutive activation of the Ca2+ release-activated Ca2+ (CRAC) channel.
Mutagenesis 78 – 78 D -> N. Increases Ca(2+) influx even when Ca(2+) stores are not depleted.
Mutagenesis 87 – 87 E -> AQ. Increases Ca(2+) influx through activation of CRAC channels, even when Ca(2+) stores are not depleted.
Helix 64 – 73



Literature citations
Constitutive activation of the calcium sensor STIM1 causes tubular-aggregate myopathy.
Boehm J.; Chevessier F.; Maues De Paula A.; Koch C.; Attarian S.; Feger C.; Hantai D.; Laforet P.; Ghorab K.; Vallat J.M.; Fardeau M.; Figarella-Branger D.; Pouget J.; Romero N.B.; Koch M.; Ebel C.; Levy N.; Krahn M.; Eymard B.; Bartoli M.; Laporte J.;
Am. J. Hum. Genet. 92:271-278(2013)
Cited for: VARIANTS TAM1 GLN-72; GLY-84; ARG-109 AND ASN-109; CHARACTERIZATION OF VARIANTS TAM1 GLN-72; GLY-84; ARG-109 AND ASN-109;
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.