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UniProtKB/Swiss-Prot P17661: Variant p.Ala360Pro

Desmin
Gene: DES
Variant information

Variant position:  360
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 Alanine (A) to Proline (P) at position 360 (A360P, p.Ala360Pro).
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 small size and hydrophobic (A) to medium size and hydrophobic (P)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -1
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 MFM1; heterozygous with I-393 gives a severe childhood-onset; unable to form a functional filamentous network in the presence of I-393; abolishes binding to MTM1.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  360
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  470
The length of the canonical sequence.

Location on the sequence:   GTNDSLMRQMRELEDRFASE  A SGYQDNIARLEEEIRHLKDE
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                         GTNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDE

Mouse                         GTNDSLMRQMRELEDRFASEANGYQDNIARLEEEIRHLKDE

Rat                           GTNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDE

Pig                           GTNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDE

Bovine                        GTNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDE

Chicken                       GTNDSLMRQMREMEERFAGEAGGYQDTIARLEEEIRHLKDE

Xenopus laevis                GTNDSLMRQMRDLEEKFSGEAAGYQDTIGRLEEEIRNMKDE

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.

TypePositionsDescription
Chain 2 – 470 Desmin
Domain 108 – 416 IF rod
Region 268 – 415 Interaction with NEB
Region 296 – 412 Coil 2B
Modified residue 358 – 358 Phosphoserine
Modified residue 361 – 361 Phosphoserine


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;

Myotubularin controls desmin intermediate filament architecture and mitochondrial dynamics in human and mouse skeletal muscle.
Hnia K.; Tronchere H.; Tomczak K.K.; Amoasii L.; Schultz P.; Beggs A.H.; Payrastre B.; Mandel J.L.; Laporte J.;
J. Clin. Invest. 121:70-85(2011)
Cited for: INTERACTION WITH MTM1; CHARACTERIZATION OF VARIANTS ASP-342; PRO-357; PRO-360 AND PRO-370; SUBUNIT;

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.