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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9UBP0: Variant p.Arg460Cys

Spastin
Gene: SPAST
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Variant information Variant position: help 460 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 Cysteine (C) at position 460 (R460C, p.Arg460Cys). 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 medium size and polar (C) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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 460 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 IDEVDSLLCERREGEHDASR R LKTEFLIEFDGVQSAGDDRV 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                         IDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGD-DRV

Mouse                         IDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGD-DR

Rat                           IDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGD-DR

Pig                           IDEVDSLLRERREGEHDASRRLKTEFLIEFDGVQSAGD-DR

Bovine                        IDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGD-DR

Chicken                       IDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSSGE-DR

Xenopus laevis                IDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSGGD-DR

Xenopus tropicalis            IDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSGGD-DR

Zebrafish                     IDEIDSLLCERREGEHDASRRLKTEFLIEFDGVQSGGD-ER

Caenorhabditis elegans        IDEIDSILCERSEKDAEVSRRMKTEFLVQFDGATSSAD-DR

Drosophila                    IDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGNPDGDR

Slime mold                    IDEIDSLLTERSSNESEASRRLKTEILVQFDGARTNGD-ER
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 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.
Mutagenesis 448 – 448 C -> AG. Abolishes ATPase activity.
Mutagenesis 448 – 448 C -> S. Does not affect ATPase activity.
Mutagenesis 451 – 451 R -> G. Abrogates binding to the tail of alpha-tubulin and beta-3-tubulin, impairs ATPase activity and abolishes microtubule severing.
Mutagenesis 457 – 457 A -> E. Abrogates binding to the tail of alpha-tubulin and beta-3-tubulin and abolishes microtubule severing.



Literature citations
Two novel mutations in the spastin gene (SPG4) found by DHPLC mutation analysis.
Falco M.; Scuderi C.; Musumeci S.; Sturnio M.; Neri M.; Bigoni S.; Caniatti L.; Fichera M.;
Neuromuscul. Disord. 14:750-753(2004)
Cited for: VARIANTS SPG4 GLY-459 AND CYS-460; Novel and recurrent spastin mutations in a large series of SPG4 Italian families.
Nanetti L.; Baratta S.; Panzeri M.; Tomasello C.; Lovati C.; Azzollini J.; Gellera C.; Di Bella D.; Taroni F.; Mariotti C.;
Neurosci. Lett. 528:42-45(2012)
Cited for: VARIANTS SPG4 THR-95; 112-GLU--VAL-616 DEL; 135-GLU--VAL-616 DEL; LEU-399; ARG-406; THR-409; VAL-426; 431-ARG--VAL-616 DEL; CYS-460; TRP-503; ARG-559 AND 562-ARG--VAL-616 DEL;
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.