Variant position: 424 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 616 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 FNISAASLTSKYVGEGEKLV RALFAVARELQPSIIFIDEVD
Mouse FNISAASLTSKYVGEGEKLV RALFAVARELQPSIIFIDEVD
Rat FNISAASLTSKYVGEGEKLV RALFAVARELQPSIIFIDEVD
Pig FNISAASLTSKYVGEGEKLV RALFAVARELQPSIIFIDEVD
Bovine FNISAASLTSKYVGEGEKLV RALFAVARELQPSIIFIDEVD
Chicken FNISAASLTSKYVGEGEKLV RALFAVARELQPSIIFIDEVD
Xenopus laevis FNISAASLTSKYVGEGEKLV RALFSVARELQPSIIFIDEVD
Xenopus tropicalis FNISAASLTSKYVGEGEKLV RALFSVARELQPSIIFIDEVD
Zebrafish FNISAATLTSKYVGEGEKLV RALFAVARELQPSIIFIDEID
Caenorhabditis elegans FNISASSLTSKWVGDSEKTI RGLFQIARNAQPSIIFIDEID
Drosophila LNISAASLTSKYVGDGEKLV RALFAVARHMQPSIIFIDEVD
Slime mold FSISSSSLTSKYVGDGEKLV RALFAVATHFQPSIIFIDEID
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 – 616 Spastin
78 – 616 Cytoplasmic
228 – 616 Sufficient for microtubule severing
415 – 415 Y -> A. Abrogates binding to the tail of alpha-tubulin and beta-3-tubulin, impairs ATPase activity and abolishes microtubule severing.
442 – 442 E -> Q. Abrogates ATP hydrolysis, abolishes microtubule severing, stabilizes the homohexameric form, and promotes microtubule binding and redistribution from the endosome to microtubules.
Mutation analysis of the spastin gene (SPG4) in patients with hereditary spastic paraparesis.
Lindsey J.C.; Lusher M.E.; McDermott C.J.; White K.D.; Reid E.; Rubinsztein D.C.; Bashir R.; Hazan J.; Shaw P.J.; Bushby K.M.D.;
J. Med. Genet. 37:759-765(2000)
Cited for: VARIANTS SPG4 GLY-424 AND HIS-584; VARIANT LEU-44;
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