Variant position: 67 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:
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 NEGFEWDLKGIPLDQGSELH VVVKDHETMGRNRFLGEAKVP
Mouse NEGFEWDLKGIPLDQSSELL VVVKDHETMGRNRFLGEAKIP
Bovine NEGFEWDLKGIPLDQGSELL VVVKDHETMGRNRFLGEANIP
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
1 – 2080 Dysferlin
1 – 2046 Cytoplasmic
1 – 85 C2 1
71 – 71 D -> A. Fails to bind calcium.
79 – 79 R -> D. Moderately increased calcium affinity.
80 – 80 F -> A. Reduced calcium affinity.
64 – 71
Calcium-sensitive phospholipid binding properties of normal and mutant ferlin C2 domains.
Davis D.B.; Doherty K.R.; Delmonte A.J.; McNally E.M.;
J. Biol. Chem. 277:22883-22888(2002)
Cited for: TISSUE SPECIFICITY; CHARACTERIZATION OF VARIANT MMD1 ASP-67;
AHNAK, a novel component of the dysferlin protein complex, redistributes to the cytoplasm with dysferlin during skeletal muscle regeneration.
Huang Y.; Laval S.H.; van Remoortere A.; Baudier J.; Benaud C.; Anderson L.V.; Straub V.; Deelder A.; Frants R.R.; den Dunnen J.T.; Bushby K.; van der Maarel S.M.;
FASEB J. 21:732-742(2007)
Cited for: INTERACTION WITH AHNAK AND AHNAK2; SUBCELLULAR LOCATION; CHARACTERIZATION OF VARIANT LGMD2B ASP-67; TISSUE SPECIFICITY; IDENTIFICATION BY MASS SPECTROMETRY;
Identical dysferlin mutation in limb-girdle muscular dystrophy type 2B and distal myopathy.
Illarioshkin S.N.; Ivanova-Smolenskaya I.A.; Greenberg C.R.; Nylen E.; Sukhorukov V.S.; Poleshchuk V.V.; Markova E.D.; Wrogemann K.;
Cited for: VARIANT MMD1 ASP-67; VARIANT LGMD2B ASP-67;
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