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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9UBP0: Variant p.Arg424Gly

Spastin
Gene: SPAST
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Variant information Variant position: help 424 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 Arginine (R) to Glycine (G) at position 424 (R424G, p.Arg424Gly). 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 large size and basic (R) to glycine (G) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 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 SPG4. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 424 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 616 The length of the canonical sequence.
Location on the sequence: help FNISAASLTSKYVGEGEKLV R ALFAVARELQPSIIFIDEVD 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                         FNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVD

Mouse                         FNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVD

Rat                           FNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVD

Pig                           FNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVD

Bovine                        FNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVD

Chicken                       FNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVD

Xenopus laevis                FNISAASLTSKYVGEGEKLVRALFSVARELQPSIIFIDEVD

Xenopus tropicalis            FNISAASLTSKYVGEGEKLVRALFSVARELQPSIIFIDEVD

Zebrafish                     FNISAATLTSKYVGEGEKLVRALFAVARELQPSIIFIDEID

Caenorhabditis elegans        FNISASSLTSKWVGDSEKTIRGLFQIARNAQPSIIFIDEID

Drosophila                    LNISAASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVD

Slime mold                    FSISSSSLTSKYVGDGEKLVRALFAVATHFQPSIIFIDEID
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 1 – 616 Spastin
Topological domain 78 – 616 Cytoplasmic
Region 228 – 616 Sufficient for microtubule severing
Mutagenesis 415 – 415 Y -> A. Abrogates binding to the tail of alpha-tubulin and beta-3-tubulin, impairs ATPase activity and abolishes microtubule severing.
Mutagenesis 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.



Literature citations
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;
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.