UniProtKB/Swiss-Prot O75923: Variant p.Ala170Glu

Dysferlin
Gene: DYSF
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Variant information Variant position:

170 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

LB/B 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 Glutamate (E) at position 170 (A170E, p.Ala170Glu). 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 acidic (E) 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
Other resources:

Links to websites of interest for the variant.

Variant rs34999029 [ dbSNP | Ensembl ]

Sequence information Variant position:

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

2080 The length of the canonical sequence.
Location on the sequence:

VVADTGGEEDTEDQGLTGDE A EPFLDQSGGPGAPTTPRKLP 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                         VVADTGGEEDTEDQGLTGDEAEPFLDQSG--GPGAPTTPRKLP

Mouse                         LVPDTGGEEDTEDQGLTGDEAEPFLDQSAAVGPGGPTTPRK

Bovine                        TVADTGGEEDTEDQGLTGDEAEPFLDQSGALGPGAPSTPKK

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	1 – 2080	Dysferlin
Topological domain	1 – 2046	Cytoplasmic
Region	132 – 215	Disordered
Compositional bias	155 – 172	Acidic residues
Modified residue	166 – 166	Phosphothreonine
Alternative sequence	152 – 152	A -> AGGGQSRAETWSLLSDSTMDTRYSGKKWPAPT. In isoform 2, isoform 5, isoform 7, isoform 8, isoform 11 and isoform 13.

Literature citations
Dysferlin mutations in LGMD2B, Miyoshi myopathy, and atypical dysferlinopathies.
Nguyen K.; Bassez G.; Bernard R.; Krahn M.; Labelle V.; Figarella-Branger D.; Pouget J.; Hammouda el H.; Beroud C.; Urtizberea A.; Eymard B.; Leturcq F.; Ben-Yaou R.; Levy N.;
Hum. Mutat. 26:165-165(2005)
Cited for: VARIANTS GLU-170 AND TRP-253; VARIANTS LGMDR2 TRP-555 AND MET-1208; VARIANTS MMD1 GLU-299; TRP-456; TRP-555; HIS-1046 AND GLN-1693; VARIANT PROXIMODISTAL MYOPATHY VAL-1276; VARIANT PSEUDOMETABOLIC MYOPATHY PRO-266; VARIANTS VAL-189; LEU-1331; SER-1351 AND VAL-1748; Mutation finding in patients with dysferlin deficiency and role of the dysferlin interacting proteins annexin A1 and A2 in muscular dystrophies.
Cagliani R.; Magri F.; Toscano A.; Merlini L.; Fortunato F.; Lamperti C.; Rodolico C.; Prelle A.; Sironi M.; Aguennouz M.; Ciscato P.; Uncini A.; Moggio M.; Bresolin N.; Comi G.P.;
Hum. Mutat. 26:283-283(2005)
Cited for: VARIANTS MMD1 TRP-959; TRP-1693; ASN-1837 AND GLY-1942 AND CYS-2042; VARIANTS LGMDR2 ARG-621; TRP-959; GLN-1038; LYS-1335 AND CYS-2042; VARIANTS GLU-170; LEU-374 AND SER-1678; Analysis of the DYSF mutational spectrum in a large cohort of patients.
Krahn M.; Beroud C.; Labelle V.; Nguyen K.; Bernard R.; Bassez G.; Figarella-Branger D.; Fernandez C.; Bouvenot J.; Richard I.; Ollagnon-Roman E.; Bevilacqua J.A.; Salvo E.; Attarian S.; Chapon F.; Pellissier J.-F.; Pouget J.; Hammouda el H.; Laforet P.; Urtizberea J.A.; Eymard B.; Leturcq F.; Levy N.;
Hum. Mutat. 30:E345-E375(2009)
Cited for: VARIANTS LGMDR2 ARG-52; ARG-155; GLU-234; THR-284; TRP-555; ARG-618; ARG-731; CYS-930; PRO-1228; THR-1526; ASP-1543; TRP-1768; SER-1970 AND CYS-2042; VARIANTS MMD1 GLU-299; 386-PHE--ASP-390 DELINS TYR; ARG-426; TRP-456; TRP-555; LEU-1029; HIS-1046; HIS-1046; GLN-1693; 1938-THR-ALA-1939 DEL AND CYS-2042; VARIANTS GLU-170; TRP-253 AND TRP-555; VARIANTS PROXIMODISTAL MYOPATHY ARG-299; ARG-340; VAL-1748; TRP-1768 AND CYS-2042; VARIANT PSEUDOMETABOLIC MYOPATHY PRO-266; VARIANTS VAL-84; VAL-189; ALA-335; LEU-374; ASN-390; GLN-819; GLN-1022; GLN-1038; VAL-1276; VAL-1325; ASN-1837 AND SER-1967;

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