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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P17661: Variant p.Asn393Ile

Desmin
Gene: DES
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Variant information Variant position: help 393 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 Asparagine (N) to Isoleucine (I) at position 393 (N393I, p.Asn393Ile). 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 medium size and polar (N) to medium size and hydrophobic (I) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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 MFM1; heterozygous with P-360 gives a severe childhood-onset; filamentous network is not affected however several spots indicate focal disorganization. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 393 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 470 The length of the canonical sequence.
Location on the sequence: help EIRHLKDEMARHLREYQDLL N VKMALDVEIATYRKLLEGEE 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                         EIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEE

                              EIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEE

Mouse                         EIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEE

Rat                           EIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEE

Pig                           EIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEE

Bovine                        EIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEE

Chicken                       EIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEE

Xenopus laevis                EIRNMKDEMARHLREYQDLLNVKMALDMEIATYRKLLEGEE
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 2 – 470 Desmin
Domain 108 – 416 IF rod
Region 268 – 415 Interaction with NEB
Region 296 – 412 Coil 2B



Literature citations
Missense mutations in desmin associated with familial cardiac and skeletal myopathy.
Goldfarb L.G.; Park K.-Y.; Cervenakova L.; Gorokhova S.; Lee H.-S.; Vasconcelos O.; Nagle J.W.; Semino-Mora C.; Sivakumar K.; Dalakas M.C.;
Nat. Genet. 19:402-403(1998)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; VARIANTS MFM1 PRO-337; PRO-360 AND ILE-393; Desmin myopathy, a skeletal myopathy with cardiomyopathy caused by mutations in the desmin gene.
Dalakas M.C.; Park K.-Y.; Semino-Mora C.; Lee H.S.; Sivakumar K.; Goldfarb L.G.;
N. Engl. J. Med. 342:770-780(2000)
Cited for: VARIANTS MFM1 PRO-337; ASP-342; PRO-360; ILE-393; TRP-406 AND MET-451; CHARACTERIZATION OF VARIANTS MFM1 PRO-337; ASP-342; PRO-360; ILE-393; TRP-406 AND MET-451; Variable pathogenic potentials of mutations located in the desmin alpha-helical domain.
Goudeau B.; Rodrigues-Lima F.; Fischer D.; Casteras-Simon M.; Sambuughin N.; de Visser M.; Laforet P.; Ferrer X.; Chapon F.; Sjoberg G.; Kostareva A.; Sejersen T.; Dalakas M.C.; Goldfarb L.G.; Vicart P.;
Hum. Mutat. 27:906-913(2006)
Cited for: VARIANTS MFM1 ARG-338; TYR-399 AND LYS-401; VARIANT VAL-213; CHARACTERIZATION OF VARIANTS MFM1 ARG-338; PRO-360; ILE-393; TYR-399 AND LYS-401; CHARACTERIZATION OF VARIANT VAL-213;
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.