Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9UBP0: Variant p.Lys388Arg

Spastin
Gene: SPAST
Feedback?
Variant information Variant position: help 388 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 Lysine (K) to Arginine (R) at position 388 (K388R, p.Lys388Arg). 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 Similar physico-chemical property. Both residues are large size and basic. 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; abrogates ATPase activity, promotes microtubule binding and the formation of thick microtubule bundles and impairs traffic from the ER to Golgi. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 388 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 FTGLRAPARGLLLFGPPGNG K TMLAKAVAAESNATFFNISA 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                         FTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISA

Mouse                         FTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISA

Rat                           FTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISA

Pig                           FTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISA

Bovine                        FTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISA

Chicken                       FTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISA

Xenopus laevis                FTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISA

Xenopus tropicalis            FTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISA

Zebrafish                     FTGLRAPARGLLLFGPPGNGKTMLAKAVAMESNATFFNISA

Caenorhabditis elegans        FKGLRQPVKGILLFGPPGNGKTLLAKAVAGESKQMFFNISA

Drosophila                    FTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISA

Slime mold                    FTGLRAPPKGLLLFGPPGNGKTMIAKAVAYESKVTFFSISS
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
Binding site 382 – 389
Mutagenesis 388 – 388 K -> A. Abrogates ATPase activity and abolishes microtubule severing.
Helix 388 – 398



Literature citations
Spastin, the protein mutated in autosomal dominant hereditary spastic paraplegia, is involved in microtubule dynamics.
Errico A.; Ballabio A.; Rugarli E.I.;
Hum. Mol. Genet. 11:153-163(2002)
Cited for: FUNCTION; SUBCELLULAR LOCATION; CHARACTERIZATION OF VARIANTS SPG4 ARG-370; CYS-381; LYS-386; ARG-388; VAL-426; TYR-448; LEU-460; CYS-499 AND VAL-556; Linking axonal degeneration to microtubule remodeling by Spastin-mediated microtubule severing.
Evans K.J.; Gomes E.R.; Reisenweber S.M.; Gundersen G.G.; Lauring B.P.;
J. Cell Biol. 168:599-606(2005)
Cited for: FUNCTION; CATALYTIC ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES; INTERACTION WITH MICROTUBULES; SUBCELLULAR LOCATION; MUTAGENESIS OF LYS-388 AND GLU-442; CHARACTERIZATION OF VARIANTS SPG4 LYS-344; LYS-347; LYS-386; ARG-388 AND CYS-499; Subcellular localization of spastin: implications for the pathogenesis of hereditary spastic paraplegia.
Svenson I.K.; Kloos M.T.; Jacon A.; Gallione C.; Horton A.C.; Pericak-Vance M.A.; Ehlers M.D.; Marchuk D.A.;
Neurogenetics 6:135-141(2005)
Cited for: SUBCELLULAR LOCATION; CHARACTERIZATION OF VARIANT SPG4 ARG-388; Spastin and atlastin, two proteins mutated in autosomal-dominant hereditary spastic paraplegia, are binding partners.
Sanderson C.M.; Connell J.W.; Edwards T.L.; Bright N.A.; Duley S.; Thompson A.; Luzio J.P.; Reid E.;
Hum. Mol. Genet. 15:307-318(2006)
Cited for: INTERACTION WITH ATL1; CHARACTERIZATION OF VARIANT SPG4 ARG-388; Spastin couples microtubule severing to membrane traffic in completion of cytokinesis and secretion.
Connell J.W.; Lindon C.; Luzio J.P.; Reid E.;
Traffic 10:42-56(2009)
Cited for: FUNCTION; SUBCELLULAR LOCATION (ISOFORMS 1 AND 3); CHARACTERIZATION OF VARIANT SPG4 ARG-388; Spectrum of SPG4 mutations in autosomal dominant spastic paraplegia.
Fonknechten N.; Mavel D.; Byrne P.; Davoine C.-S.; Cruaud C.; Bonsch D.; Samson D.; Coutinho P.; Hutchinson M.; McMonagle P.; Burgunder J.-M.; Tartaglione A.; Heinzlef O.; Feki I.; Deufel T.; Parfrey N.; Brice A.; Fontaine B.; Prud'homme J.-F.; Weissenbach J.; Duerr A.; Hazan J.;
Hum. Mol. Genet. 9:637-644(2000)
Cited for: VARIANTS SPG4 CYS-362; ARG-370; CYS-381; LYS-386; ARG-388; VAL-426; TYR-448; LEU-460; CYS-499; ASN-555 AND VAL-556; Spastin gene mutation in Japanese with hereditary spastic paraplegia.
Yabe I.; Sasaki H.; Tashiro K.; Matsuura T.; Takegami T.; Satoh T.;
J. Med. Genet. 39:E46-E46(2002)
Cited for: VARIANTS SPG4 LYS-347; ARG-388 AND CYS-499;
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.