UniProtKB - Q9UBP0 (SPAST_HUMAN)
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- BLAST
>sp|Q9UBP0|SPAST_HUMAN Spastin OS=Homo sapiens OX=9606 GN=SPAST PE=1 SV=1 MNSPGGRGKKKGSGGASNPVPPRPPPPCLAPAPPAAGPAPPPESPHKRNLYYFSYPLFVG FALLRLVAFHLGLLFVWLCQRFSRALMAAKRSSGAAPAPASASAPAPVPGGEAERVRVFH KQAFEYISIALRIDEDEKAGQKEQAVEWYKKGIEELEKGIAVIVTGQGEQCERARRLQAK MMTNLVMAKDRLQLLEKMQPVLPFSKSQTDVYNDSTNLACRNGHLQSESGAVPKRKDPLT HTSNSLPRSKTVMKTGSAGLSGHHRAPSYSGLSMVSGVKQGSGPAPTTHKGTPKTNRTNK PSTPTTATRKKKDLKNFRNVDSNLANLIMNEIVDNGTAVKFDDIAGQDLAKQALQEIVIL PSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE KLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRV LVMGATNRPQELDEAVLRRFIKRVYVSLPNEETRLLLLKNLLCKQGSPLTQKELAQLARM TDGYSGSDLTALAKDAALGPIRELKPEQVKNMSASEMRNIRLSDFTESLKKIKRSVSPQT LEAYIRWNKDFGDTTV
- Align
Protein
Spastin
Gene
SPAST
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
ATP-dependent microtubule severing protein that specifically recognizes and cuts microtubules that are polyglutamylated (PubMed:11809724, PubMed:15716377, PubMed:16219033, PubMed:17389232, PubMed:20530212, PubMed:22637577, PubMed:26875866). Preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (PubMed:26875866). Severing activity is not dependent on tubulin acetylation or detyrosination (PubMed:26875866). Microtubule severing promotes reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. It is critical for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia. SPAST is involved in abscission step of cytokinesis and nuclear envelope reassembly during anaphase in cooperation with the ESCRT-III complex (PubMed:19000169, PubMed:21310966, PubMed:26040712). Recruited at the midbody, probably by IST1, and participates in membrane fission during abscission together with the ESCRT-III complex (PubMed:21310966). Recruited to the nuclear membrane by IST1 and mediates microtubule severing, promoting nuclear envelope sealing and mitotic spindle disassembly during late anaphase (PubMed:26040712). Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and endosome recycling (PubMed:23897888). Recruited by IST1 to endosomes and regulates early endosomal tubulation and recycling by mediating microtubule severing (PubMed:23897888). Probably plays a role in axon growth and the formation of axonal branches (PubMed:15716377).UniRule annotation
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi
11 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.5"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) [PubMed] [Europe PMC] [Abstract]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. - Ref.11"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) [PubMed] [Europe PMC] [Abstract]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. - Ref.12"Human spastin has multiple microtubule-related functions."
Salinas S., Carazo-Salas R.E., Proukakis C., Cooper J.M., Weston A.E., Schiavo G., Warner T.T.
J. Neurochem. 95:1411-1420(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ASSOCIATION WITH MICROTUBULES. - Ref.18"Recognition of C-terminal amino acids in tubulin by pore loops in Spastin is important for microtubule severing."
White S.R., Evans K.J., Lary J., Cole J.L., Lauring B.P.
J. Cell Biol. 176:995-1005(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, HOMOHEXAMERIZATION, INTERACTION WITH TUBULIN AND MICROTUBULES, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-415; GLU-442; ARG-451 AND ALA-457, CHARACTERIZATION OF VARIANT SPG4 TYR-448. - Ref.23"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), CHARACTERIZATION OF VARIANT SPG4 ARG-388. - Ref.25"Tubulin polyglutamylation stimulates spastin-mediated microtubule severing."
Lacroix B., van Dijk J., Gold N.D., Guizetti J., Aldrian-Herrada G., Rogowski K., Gerlich D.W., Janke C.
J. Cell Biol. 189:945-954(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.28"Cortical constriction during abscission involves helices of ESCRT-III-dependent filaments."
Guizetti J., Schermelleh L., Maentler J., Maar S., Poser I., Leonhardt H., Mueller-Reichert T., Gerlich D.W.
Science 331:1616-1620(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.29"Subunit Interactions and cooperativity in the microtubule-severing AAA ATPase spastin."
Eckert T., Link S., Le D.T., Sobczak J.P., Gieseke A., Richter K., Woehlke G.
J. Biol. Chem. 287:26278-26290(2012) [PubMed] [Europe PMC] [Abstract]Cited for: HOMOHEXAMERIZATION, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, KINETIC PARAMETERS, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, COOPERATIVITY, MUTAGENESIS OF GLU-442. - Ref.33"An ESCRT-spastin interaction promotes fission of recycling tubules from the endosome."
Allison R., Lumb J.H., Fassier C., Connell J.W., Ten Martin D., Seaman M.N., Hazan J., Reid E.
J. Cell Biol. 202:527-543(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), INTERACTION WITH IST1. - Ref.37"Spastin and ESCRT-III coordinate mitotic spindle disassembly and nuclear envelope sealing."
Vietri M., Schink K.O., Campsteijn C., Wegner C.S., Schultz S.W., Christ L., Thoresen S.B., Brech A., Raiborg C., Stenmark H.
Nature 522:231-235(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), INTERACTION WITH IST1. - Ref.39"Graded control of microtubule severing by tubulin glutamylation."
Valenstein M.L., Roll-Mecak A.
Cell 164:911-921(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION.
Isoform 1: Involved in lipid metabolism by regulating the size and distribution of lipid droplets.1 Publication
Manual assertion based on experiment ini
- Ref.38"Spastin binds to lipid droplets and affects lipid metabolism."
Papadopoulos C., Orso G., Mancuso G., Herholz M., Gumeni S., Tadepalle N., Juengst C., Tzschichholz A., Schauss A., Hoening S., Trifunovic A., Daga A., Rugarli E.I.
PLoS Genet. 11:E1005149-E1005149(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (ISOFORM 1), SUBCELLULAR LOCATION (ISOFORM 1), MUTAGENESIS OF ARG-65 AND 81-ARG--ARG-84.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
ATP + H2O = ADP + phosphate.UniRule annotation
Manual assertion according to rulesi
6 PublicationsManual assertion based on experiment ini
- Ref.11"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) [PubMed] [Europe PMC] [Abstract]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. - Ref.12"Human spastin has multiple microtubule-related functions."
Salinas S., Carazo-Salas R.E., Proukakis C., Cooper J.M., Weston A.E., Schiavo G., Warner T.T.
J. Neurochem. 95:1411-1420(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ASSOCIATION WITH MICROTUBULES. - Ref.17"Interaction of two hereditary spastic paraplegia gene products, spastin and atlastin, suggests a common pathway for axonal maintenance."
Evans K.J., Keller C., Pavur K., Glasgow K., Conn B., Lauring B.P.
Proc. Natl. Acad. Sci. U.S.A. 103:10666-10671(2006) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, INTERACTION WITH ATL1, MUTAGENESIS OF GLU-442. - Ref.18"Recognition of C-terminal amino acids in tubulin by pore loops in Spastin is important for microtubule severing."
White S.R., Evans K.J., Lary J., Cole J.L., Lauring B.P.
J. Cell Biol. 176:995-1005(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, HOMOHEXAMERIZATION, INTERACTION WITH TUBULIN AND MICROTUBULES, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-415; GLU-442; ARG-451 AND ALA-457, CHARACTERIZATION OF VARIANT SPG4 TYR-448. - Ref.20"Spastin oligomerizes into a hexamer and the mutant spastin (E442Q) redistribute the wild-type spastin into filamentous microtubule."
Pantakani D.V.K., Swapna L.S., Srinivasan N., Mannan A.U.
J. Neurochem. 106:613-624(2008) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, HOMOHEXAMERIZATION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-442. - Ref.29"Subunit Interactions and cooperativity in the microtubule-severing AAA ATPase spastin."
Eckert T., Link S., Le D.T., Sobczak J.P., Gieseke A., Richter K., Woehlke G.
J. Biol. Chem. 287:26278-26290(2012) [PubMed] [Europe PMC] [Abstract]Cited for: HOMOHEXAMERIZATION, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, KINETIC PARAMETERS, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, COOPERATIVITY, MUTAGENESIS OF GLU-442.
<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi
Allosteric enzyme with a cooperative mechanism; at least two neighbor subunits influence each other strongly in spastin hexamers (PubMed:22637577). Microtubule binding promotes cooperative interactions among spastin subunits (PubMed:22637577). ATP-bound enzyme interacts strongly and cooperatively with microtubules; this interaction stimulates ATP hydrolysis (PubMed:23745751).UniRule annotation
Manual assertion according to rulesi
2 PublicationsManual assertion based on experiment ini
- Ref.29"Subunit Interactions and cooperativity in the microtubule-severing AAA ATPase spastin."
Eckert T., Link S., Le D.T., Sobczak J.P., Gieseke A., Richter K., Woehlke G.
J. Biol. Chem. 287:26278-26290(2012) [PubMed] [Europe PMC] [Abstract]Cited for: HOMOHEXAMERIZATION, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, KINETIC PARAMETERS, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, COOPERATIVITY, MUTAGENESIS OF GLU-442. - Ref.32"The nucleotide cycle of spastin correlates with its microtubule-binding properties."
Wen M., Wang C.
FEBS J. 280:3868-3877(2013) [PubMed] [Europe PMC] [Abstract]Cited for: ACTIVITY REGULATION, MUTAGENESIS OF GLU-442 AND CYS-448.
<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi
Kinetic parameters shown are for full-length enzyme. N-terminally truncated spastin (residues 228-616), which has been shown to exhibit full severing activity, shows a basal ATP turnover rate of 0.78 sec(-1) in the absence of microtubules, a KM of 0.16 mM for ATP, and the ATP turnover rate is extrapolated to 3.83 sec(-1) in the presence of microtubules. ATPase activity shows non-Michaelis-Menten kinetics in the presence of microtubules, but is close to non-cooperative behavior in their absence (PubMed:22637577).1 Publication
Manual assertion based on experiment ini
- Ref.29"Subunit Interactions and cooperativity in the microtubule-severing AAA ATPase spastin."
Eckert T., Link S., Le D.T., Sobczak J.P., Gieseke A., Richter K., Woehlke G.
J. Biol. Chem. 287:26278-26290(2012) [PubMed] [Europe PMC] [Abstract]Cited for: HOMOHEXAMERIZATION, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, KINETIC PARAMETERS, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, COOPERATIVITY, MUTAGENESIS OF GLU-442.
- KM=0.45 mM for ATP3 Publications
Manual assertion based on experiment ini
- Ref.11"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) [PubMed] [Europe PMC] [Abstract]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. - Ref.18"Recognition of C-terminal amino acids in tubulin by pore loops in Spastin is important for microtubule severing."
White S.R., Evans K.J., Lary J., Cole J.L., Lauring B.P.
J. Cell Biol. 176:995-1005(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, HOMOHEXAMERIZATION, INTERACTION WITH TUBULIN AND MICROTUBULES, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-415; GLU-442; ARG-451 AND ALA-457, CHARACTERIZATION OF VARIANT SPG4 TYR-448. - Ref.29"Subunit Interactions and cooperativity in the microtubule-severing AAA ATPase spastin."
Eckert T., Link S., Le D.T., Sobczak J.P., Gieseke A., Richter K., Woehlke G.
J. Biol. Chem. 287:26278-26290(2012) [PubMed] [Europe PMC] [Abstract]Cited for: HOMOHEXAMERIZATION, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, KINETIC PARAMETERS, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, COOPERATIVITY, MUTAGENESIS OF GLU-442.
- Vmax=1.2 nmol/min/µg enzyme3 Publications
Manual assertion based on experiment ini
- Ref.11"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) [PubMed] [Europe PMC] [Abstract]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. - Ref.18"Recognition of C-terminal amino acids in tubulin by pore loops in Spastin is important for microtubule severing."
White S.R., Evans K.J., Lary J., Cole J.L., Lauring B.P.
J. Cell Biol. 176:995-1005(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, HOMOHEXAMERIZATION, INTERACTION WITH TUBULIN AND MICROTUBULES, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-415; GLU-442; ARG-451 AND ALA-457, CHARACTERIZATION OF VARIANT SPG4 TYR-448. - Ref.29"Subunit Interactions and cooperativity in the microtubule-severing AAA ATPase spastin."
Eckert T., Link S., Le D.T., Sobczak J.P., Gieseke A., Richter K., Woehlke G.
J. Biol. Chem. 287:26278-26290(2012) [PubMed] [Europe PMC] [Abstract]Cited for: HOMOHEXAMERIZATION, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, KINETIC PARAMETERS, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, COOPERATIVITY, MUTAGENESIS OF GLU-442.
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 382 – 389 | ATPUniRule annotation Manual assertion according to rulesi 1 Publication<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 8 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- alpha-tubulin binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- ATP binding Source: UniProtKB-KW
- beta-tubulin binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- microtubule binding Source: UniProtKBInferred from direct assayi
- microtubule-severing ATPase activity Source: UniProtKBInferred from direct assayi
- protein-containing complex binding Source: ARUK-UCL <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
GO - Biological processi
- anterograde axonal transport Source: UniProtKB
- axonal transport of mitochondrion Source: UniProtKB
- cell differentiation Source: UniProtKB-KW
- cytokinetic process Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- cytoskeleton-dependent cytokinesis Source: ARUK-UCLTraceable author statementi
- ER to Golgi vesicle-mediated transport Source: UniProtKBInferred from mutant phenotypei
- exit from mitosis Source: UniProtKBInferred from mutant phenotypei
- membrane fission Source: UniProtKBInferred from mutant phenotypei
- metabolic process Source: UniProtKB-KW
- microtubule bundle formation Source: UniProtKBInferred from direct assayi
- microtubule severing Source: UniProtKBInferred from direct assayi
- mitotic cytokinesis Source: UniProtKBInferred from mutant phenotypei
- mitotic spindle disassembly Source: UniProtKBInferred from mutant phenotypei
- nervous system development Source: UniProtKB-KW
- nuclear envelope reassembly Source: UniProtKBInferred from mutant phenotypei
- positive regulation of cytokinesis Source: UniProtKBInferred from mutant phenotypei
- protein hexamerization Source: UniProtKBInferred from direct assayi
- protein homooligomerization Source: UniProtKBInferred from direct assayi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Allosteric enzyme, Developmental protein, Hydrolase |
| Biological process | Cell cycle, Cell division, Differentiation, Neurogenesis |
| Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.6.4.3 2681 |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | Q9UBP0 |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q9UBP0 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Spastin1 Publication<p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
Manual assertion according to rulesi (EC:3.6.4.3UniRule annotationManual assertion according to rulesi 6 PublicationsManual assertion based on experiment ini
Alternative name(s): Spastic paraplegia 4 protein |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:SPASTUniRule annotation Manual assertion according to rulesi Imported<p>Manually validated information which has been imported from another database.</p> <p><a href="/manual/evidences#ECO:0000312">More...</a></p> Manual assertion inferred from database entriesi Synonyms:ADPSP, FSP2, KIAA10831 Publication Manual assertion based on opinion ini
Manual assertion according to rulesi |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000021574.11 |
Human Gene Nomenclature Database More...HGNCi | HGNC:11233 SPAST |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 604277 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q9UBP0 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Endoplasmic reticulum
- Endoplasmic reticulum UniRule annotation
Manual assertion according to rulesi
1 PublicationManual assertion based on experiment ini
- Ref.16"Spastin, the most commonly mutated protein in hereditary spastic paraplegia interacts with Reticulon 1 an endoplasmic reticulum protein."
Mannan A.U., Boehm J., Sauter S.M., Rauber A., Byrne P.C., Neesen J., Engel W.
Neurogenetics 7:93-103(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RTN1, SUBCELLULAR LOCATION.
- Endoplasmic reticulum UniRule annotation
Nucleus
- Nucleus UniRule annotation
Manual assertion according to rulesi
2 PublicationsManual assertion based on experiment ini
- Ref.7"Identification of nuclear localisation sequences in spastin (SPG4) using a novel Tetra-GFP reporter system."
Beetz C., Brodhun M., Moutzouris K., Kiehntopf M., Berndt A., Lehnert D., Deufel T., Bastmeyer M., Schickel J.
Biochem. Biophys. Res. Commun. 318:1079-1084(2004) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL. - Ref.9"Spastin subcellular localization is regulated through usage of different translation start sites and active export from the nucleus."
Claudiani P., Riano E., Errico A., Andolfi G., Rugarli E.I.
Exp. Cell Res. 309:358-369(2005) [PubMed] [Europe PMC] [Abstract]Cited for: ALTERNATIVE INITIATION, SUBCELLULAR LOCATION, NUCLEAR EXPORT SIGNALS, MUTAGENESIS OF MET-1 AND MET-87.
- Nucleus UniRule annotation
Cytoskeleton
- centrosome UniRule annotation
Manual assertion according to rulesi
1 PublicationManual assertion based on experiment ini
- Ref.13"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) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT SPG4 ARG-388.
- cytoskeleton UniRule annotation
Manual assertion according to rulesi
5 PublicationsManual assertion based on experiment ini
- Ref.11"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) [PubMed] [Europe PMC] [Abstract]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. - Ref.18"Recognition of C-terminal amino acids in tubulin by pore loops in Spastin is important for microtubule severing."
White S.R., Evans K.J., Lary J., Cole J.L., Lauring B.P.
J. Cell Biol. 176:995-1005(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, HOMOHEXAMERIZATION, INTERACTION WITH TUBULIN AND MICROTUBULES, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-415; GLU-442; ARG-451 AND ALA-457, CHARACTERIZATION OF VARIANT SPG4 TYR-448. - Ref.20"Spastin oligomerizes into a hexamer and the mutant spastin (E442Q) redistribute the wild-type spastin into filamentous microtubule."
Pantakani D.V.K., Swapna L.S., Srinivasan N., Mannan A.U.
J. Neurochem. 106:613-624(2008) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, HOMOHEXAMERIZATION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-442. - Ref.23"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), CHARACTERIZATION OF VARIANT SPG4 ARG-388. - Ref.24"Hereditary spastic paraplegia proteins REEP1, spastin, and atlastin-1 coordinate microtubule interactions with the tubular ER network."
Park S.H., Zhu P.P., Parker R.L., Blackstone C.
J. Clin. Invest. 120:1097-1110(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH REEP1, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), TOPOLOGY (ISOFORM 1).
- spindle UniRule annotation
Manual assertion according to rulesi
1 PublicationManual assertion based on experiment ini
- Ref.8"Spastin interacts with the centrosomal protein NA14, and is enriched in the spindle pole, the midbody and the distal axon."
Errico A., Claudiani P., D'Addio M., Rugarli E.I.
Hum. Mol. Genet. 13:2121-2132(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SSNA1 AND MICROTUBULES, SUBCELLULAR LOCATION.
- centrosome UniRule annotation
Other locations
- Membrane UniRule annotation
Manual assertion according to rulesi
1 PublicationManual assertion based on experiment ini
- Ref.23"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), CHARACTERIZATION OF VARIANT SPG4 ARG-388.
Manual assertion according to rulesi
1 PublicationManual assertion inferred by curator fromi
- Ref.24"Hereditary spastic paraplegia proteins REEP1, spastin, and atlastin-1 coordinate microtubule interactions with the tubular ER network."
Park S.H., Zhu P.P., Parker R.L., Blackstone C.
J. Clin. Invest. 120:1097-1110(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH REEP1, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), TOPOLOGY (ISOFORM 1).
- Midbody UniRule annotation
Manual assertion according to rulesi
2 PublicationsManual assertion based on experiment ini
- Ref.28"Cortical constriction during abscission involves helices of ESCRT-III-dependent filaments."
Guizetti J., Schermelleh L., Maentler J., Maar S., Poser I., Leonhardt H., Mueller-Reichert T., Gerlich D.W.
Science 331:1616-1620(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.40"Structural basis for midbody targeting of spastin by the ESCRT-III protein CHMP1B."
Yang D., Rismanchi N., Renvoise B., Lippincott-Schwartz J., Blackstone C., Hurley J.H.
Nat. Struct. Mol. Biol. 15:1278-1286(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 112-196 IN COMPLEX WITH CHMP1B, INTERACTION WITH CHMP1B, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-120 AND PHE-124.
- perinuclear region UniRule annotation
Manual assertion according to rulesi
3 PublicationsManual assertion based on experiment ini
- Ref.5"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) [PubMed] [Europe PMC] [Abstract]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. - Ref.8"Spastin interacts with the centrosomal protein NA14, and is enriched in the spindle pole, the midbody and the distal axon."
Errico A., Claudiani P., D'Addio M., Rugarli E.I.
Hum. Mol. Genet. 13:2121-2132(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SSNA1 AND MICROTUBULES, SUBCELLULAR LOCATION. - Ref.10"The hereditary spastic paraplegia protein spastin interacts with the ESCRT-III complex-associated endosomal protein CHMP1B."
Reid E., Connell J.W., Edwards T.L., Duley S., Brown S.E., Sanderson C.M.
Hum. Mol. Genet. 14:19-38(2005) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CHMP1B, SUBCELLULAR LOCATION.
- Cytoplasm UniRule annotation
Manual assertion according to rulesi
2 PublicationsManual assertion based on experiment ini
- Ref.9"Spastin subcellular localization is regulated through usage of different translation start sites and active export from the nucleus."
Claudiani P., Riano E., Errico A., Andolfi G., Rugarli E.I.
Exp. Cell Res. 309:358-369(2005) [PubMed] [Europe PMC] [Abstract]Cited for: ALTERNATIVE INITIATION, SUBCELLULAR LOCATION, NUCLEAR EXPORT SIGNALS, MUTAGENESIS OF MET-1 AND MET-87. - Ref.24"Hereditary spastic paraplegia proteins REEP1, spastin, and atlastin-1 coordinate microtubule interactions with the tubular ER network."
Park S.H., Zhu P.P., Parker R.L., Blackstone C.
J. Clin. Invest. 120:1097-1110(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH REEP1, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), TOPOLOGY (ISOFORM 1).
Note: Forms a intramembrane hairpin-like structure in the membrane (PubMed:20200447). Localization to the centrosome is independent of microtubules (PubMed:15891913). Localizes to the midbody of dividing cells, and this requires CHMP1B (PubMed:18997780). Enriched in the distal axons and branches of postmitotic neurons (PubMed:15269182).UniRule annotation- Membrane UniRule annotation
- Ref.24"Hereditary spastic paraplegia proteins REEP1, spastin, and atlastin-1 coordinate microtubule interactions with the tubular ER network."
Park S.H., Zhu P.P., Parker R.L., Blackstone C.
J. Clin. Invest. 120:1097-1110(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH REEP1, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), TOPOLOGY (ISOFORM 1). - Ref.8"Spastin interacts with the centrosomal protein NA14, and is enriched in the spindle pole, the midbody and the distal axon."
Errico A., Claudiani P., D'Addio M., Rugarli E.I.
Hum. Mol. Genet. 13:2121-2132(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SSNA1 AND MICROTUBULES, SUBCELLULAR LOCATION. - Ref.13"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) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT SPG4 ARG-388. - Ref.40"Structural basis for midbody targeting of spastin by the ESCRT-III protein CHMP1B."
Yang D., Rismanchi N., Renvoise B., Lippincott-Schwartz J., Blackstone C., Hurley J.H.
Nat. Struct. Mol. Biol. 15:1278-1286(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 112-196 IN COMPLEX WITH CHMP1B, INTERACTION WITH CHMP1B, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-120 AND PHE-124.
Manual assertion according to rulesi
1 PublicationManual assertion inferred by curator fromi
Manual assertion based on experiment ini
Isoform 1 :
Endosome
- Endosome 1 Publication
Manual assertion based on experiment ini
- Ref.33"An ESCRT-spastin interaction promotes fission of recycling tubules from the endosome."
Allison R., Lumb J.H., Fassier C., Connell J.W., Ten Martin D., Seaman M.N., Hazan J., Reid E.
J. Cell Biol. 202:527-543(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), INTERACTION WITH IST1.
- Endosome 1 Publication
Endoplasmic reticulum
- Endoplasmic reticulum membrane 2 Publications
Manual assertion based on experiment ini
- Ref.23"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), CHARACTERIZATION OF VARIANT SPG4 ARG-388. - Ref.35"Protrudin binds atlastins and endoplasmic reticulum-shaping proteins and regulates network formation."
Chang J., Lee S., Blackstone C.
Proc. Natl. Acad. Sci. U.S.A. 110:14954-14959(2013) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ZFYVE27.
Manual assertion inferred by curator fromi
- Ref.24"Hereditary spastic paraplegia proteins REEP1, spastin, and atlastin-1 coordinate microtubule interactions with the tubular ER network."
Park S.H., Zhu P.P., Parker R.L., Blackstone C.
J. Clin. Invest. 120:1097-1110(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH REEP1, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), TOPOLOGY (ISOFORM 1).
- Endoplasmic reticulum membrane 2 Publications
Cytoskeleton
- cytoskeleton 2 Publications
Manual assertion based on experiment ini
- Ref.23"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), CHARACTERIZATION OF VARIANT SPG4 ARG-388. - Ref.24"Hereditary spastic paraplegia proteins REEP1, spastin, and atlastin-1 coordinate microtubule interactions with the tubular ER network."
Park S.H., Zhu P.P., Parker R.L., Blackstone C.
J. Clin. Invest. 120:1097-1110(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH REEP1, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), TOPOLOGY (ISOFORM 1).
- cytoskeleton 2 Publications
Nucleus
- Nucleus membrane 1 Publication
Manual assertion based on experiment ini
- Ref.37"Spastin and ESCRT-III coordinate mitotic spindle disassembly and nuclear envelope sealing."
Vietri M., Schink K.O., Campsteijn C., Wegner C.S., Schultz S.W., Christ L., Thoresen S.B., Brech A., Raiborg C., Stenmark H.
Nature 522:231-235(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), INTERACTION WITH IST1.
- Nucleus membrane 1 Publication
Other locations
- Lipid droplet 1 Publication
Manual assertion based on experiment ini
- Ref.38"Spastin binds to lipid droplets and affects lipid metabolism."
Papadopoulos C., Orso G., Mancuso G., Herholz M., Gumeni S., Tadepalle N., Juengst C., Tzschichholz A., Schauss A., Hoening S., Trifunovic A., Daga A., Rugarli E.I.
PLoS Genet. 11:E1005149-E1005149(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (ISOFORM 1), SUBCELLULAR LOCATION (ISOFORM 1), MUTAGENESIS OF ARG-65 AND 81-ARG--ARG-84.
Note: Forms a intramembrane hairpin-like structure in the membrane (PubMed:20200447). Recruited to nuclear membrane by IST1 during late anaphase (PubMed:26040712). Localizes to endoplasmic reticulum tubular network (PubMed:23969831).1 Publication- Lipid droplet 1 Publication
- Ref.24"Hereditary spastic paraplegia proteins REEP1, spastin, and atlastin-1 coordinate microtubule interactions with the tubular ER network."
Park S.H., Zhu P.P., Parker R.L., Blackstone C.
J. Clin. Invest. 120:1097-1110(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH REEP1, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), TOPOLOGY (ISOFORM 1). - Ref.35"Protrudin binds atlastins and endoplasmic reticulum-shaping proteins and regulates network formation."
Chang J., Lee S., Blackstone C.
Proc. Natl. Acad. Sci. U.S.A. 110:14954-14959(2013) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ZFYVE27. - Ref.37"Spastin and ESCRT-III coordinate mitotic spindle disassembly and nuclear envelope sealing."
Vietri M., Schink K.O., Campsteijn C., Wegner C.S., Schultz S.W., Christ L., Thoresen S.B., Brech A., Raiborg C., Stenmark H.
Nature 522:231-235(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), INTERACTION WITH IST1.
Manual assertion inferred by curator fromi
Manual assertion based on experiment ini
Isoform 3 :
Endosome
- Endosome 2 Publications
Manual assertion based on experiment ini
- Ref.23"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), CHARACTERIZATION OF VARIANT SPG4 ARG-388. - Ref.33"An ESCRT-spastin interaction promotes fission of recycling tubules from the endosome."
Allison R., Lumb J.H., Fassier C., Connell J.W., Ten Martin D., Seaman M.N., Hazan J., Reid E.
J. Cell Biol. 202:527-543(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), INTERACTION WITH IST1.
- Endosome 2 Publications
Nucleus
- Nucleus membrane 2 Publications
Manual assertion based on experiment ini
- Ref.9"Spastin subcellular localization is regulated through usage of different translation start sites and active export from the nucleus."
Claudiani P., Riano E., Errico A., Andolfi G., Rugarli E.I.
Exp. Cell Res. 309:358-369(2005) [PubMed] [Europe PMC] [Abstract]Cited for: ALTERNATIVE INITIATION, SUBCELLULAR LOCATION, NUCLEAR EXPORT SIGNALS, MUTAGENESIS OF MET-1 AND MET-87. - Ref.37"Spastin and ESCRT-III coordinate mitotic spindle disassembly and nuclear envelope sealing."
Vietri M., Schink K.O., Campsteijn C., Wegner C.S., Schultz S.W., Christ L., Thoresen S.B., Brech A., Raiborg C., Stenmark H.
Nature 522:231-235(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), INTERACTION WITH IST1.
- Nucleus membrane 2 Publications
Other locations
- Cytoplasm 2 Publications
Manual assertion based on experiment ini
- Ref.24"Hereditary spastic paraplegia proteins REEP1, spastin, and atlastin-1 coordinate microtubule interactions with the tubular ER network."
Park S.H., Zhu P.P., Parker R.L., Blackstone C.
J. Clin. Invest. 120:1097-1110(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH REEP1, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), TOPOLOGY (ISOFORM 1). - Ref.35"Protrudin binds atlastins and endoplasmic reticulum-shaping proteins and regulates network formation."
Chang J., Lee S., Blackstone C.
Proc. Natl. Acad. Sci. U.S.A. 110:14954-14959(2013) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ZFYVE27.
Note: Constitutes the main endosomal form (PubMed:19000169). Recruited to nuclear membrane by IST1 during late anaphase (PubMed:26040712).2 Publications- Cytoplasm 2 Publications
- Ref.23"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), CHARACTERIZATION OF VARIANT SPG4 ARG-388. - Ref.37"Spastin and ESCRT-III coordinate mitotic spindle disassembly and nuclear envelope sealing."
Vietri M., Schink K.O., Campsteijn C., Wegner C.S., Schultz S.W., Christ L., Thoresen S.B., Brech A., Raiborg C., Stenmark H.
Nature 522:231-235(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), INTERACTION WITH IST1.
Manual assertion based on experiment ini
Cytoskeleton
- microtubule Source: UniProtKB-KW
- microtubule organizing center Source: UniProtKB-SubCell
- spindle Source: UniProtKB-SubCell
Cytosol
- cytosol Source: HPA
Endoplasmic reticulum
- endoplasmic reticulum membrane Source: UniProtKB-SubCell
- endoplasmic reticulum tubular network Source: UniProtKBInferred from direct assayi
Endosome
- endosome Source: UniProtKB-SubCell
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
Nucleus
- nuclear membrane Source: UniProtKBInferred from direct assayi
- nucleoplasm Source: HPA
- nucleus Source: UniProtKBInferred from direct assayi
Other locations
- axon cytoplasm Source: GOC
- cytoplasm Source: UniProtKBInferred from direct assayi
- cytoplasmic vesicle Source: MGIInferred from direct assayi
- lipid droplet Source: UniProtKB-SubCell
- midbody Source: UniProtKBInferred from direct assayi
- perinuclear region of cytoplasm Source: UniProtKB-SubCell
Topology
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 1 – 56 | CytoplasmicUniRule annotation Manual assertion according to rulesi 1 PublicationManual assertion inferred by curator fromi
| 56 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei | 57 – 77 | HelicalUniRule annotation Manual assertion according to rulesi 1 PublicationManual assertion inferred by curator fromi
| 21 | |
| Topological domaini | 78 – 616 | CytoplasmicUniRule annotation Manual assertion according to rulesi 1 PublicationManual assertion inferred by curator fromi
| 539 |
Keywords - Cellular componenti
Cytoplasm, Cytoskeleton, Endoplasmic reticulum, Endosome, Lipid droplet, Membrane, Microtubule, Nucleus<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Spastic paraplegia 4, autosomal dominant (SPG4)43 PublicationsManual assertion based on experiment ini
- Ref.1"Spastin, a new AAA protein, is altered in the most frequent form of autosomal dominant spastic paraplegia."
Hazan J., Fonknechten N., Mavel D., Paternotte C., Samson D., Artiguenave F., Davoine C.-S., Cruaud C., Durr A., Wincker P., Brottier P., Cattolico L., Barbe V., Burgunder J.-M., Prud'homme J.-F., Brice A., Fontaine B., Heilig R., Weissenbach J.
Nat. Genet. 23:296-303(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, VARIANTS SPG4 CYS-362; TYR-448 AND CYS-499. - Ref.5"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) [PubMed] [Europe PMC] [Abstract]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. - Ref.11"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) [PubMed] [Europe PMC] [Abstract]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. - Ref.13"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) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT SPG4 ARG-388. - Ref.15"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) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ATL1, CHARACTERIZATION OF VARIANT SPG4 ARG-388. - Ref.18"Recognition of C-terminal amino acids in tubulin by pore loops in Spastin is important for microtubule severing."
White S.R., Evans K.J., Lary J., Cole J.L., Lauring B.P.
J. Cell Biol. 176:995-1005(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, HOMOHEXAMERIZATION, INTERACTION WITH TUBULIN AND MICROTUBULES, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-415; GLU-442; ARG-451 AND ALA-457, CHARACTERIZATION OF VARIANT SPG4 TYR-448. - Ref.23"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), CHARACTERIZATION OF VARIANT SPG4 ARG-388. - Ref.42"Hereditary spastic paraplegia caused by mutations in the SPG4 gene."
Buerger J., Fonknechten N., Hoeltzenbein M., Neumann L., Bratanoff E., Hazan J., Reis A.
Eur. J. Hum. Genet. 8:771-776(2000) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT SPG4 GLY-441. - Ref.43"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) [PubMed] [Europe PMC] [Abstract]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. - Ref.44"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) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS SPG4 GLY-424 AND HIS-584, VARIANT LEU-44. - Ref.45"Novel mutations in spastin gene and absence of correlation with age at onset of symptoms."
Hentati A., Deng H.-X., Zhai H., Chen W., Yang Y., Hung W.-Y., Azim A.C., Bohlega S., Tandan R., Warner C., Laing N.G., Cambi F., Mitsumoto H., Roos R.P., Boustany R.-M.N., Ben-Hamida M., Hentati F., Siddique T.
Neurology 55:1388-1390(2000) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS SPG4 PHE-436 AND ASP-559. - Ref.46"Identification and expression analysis of spastin gene mutations in hereditary spastic paraplegia."
Svenson I.K., Ashley-Koch A.E., Gaskell P.C., Riney T.J., Cumming W.J.K., Kingston H.M., Hogan E.L., Boustany R.-M.N., Vance J.M., Nance M.A., Pericak-Vance M.A., Marchuk D.A.
Am. J. Hum. Genet. 68:1077-1085(2001) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS SPG4 CYS-499 AND GLY-562. - Ref.47"A Japanese SPG4 family with a novel missense mutation of the SPG4 gene: intrafamilial variability in age at onset and clinical severity."
Namekawa M., Takiyama Y., Sakoe K., Nagaki H., Shimazaki H., Yoshimura M., Ikeguchi K., Nakano I., Nishizawa M.
Acta Neurol. Scand. 106:387-391(2002) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT SPG4 VAL-485. - Ref.48"Spectrum of SPG4 mutations in a large collection of North American families with hereditary spastic paraplegia."
Meijer I.A., Hand C.K., Cossette P., Figlewicz D.A., Rouleau G.A.
Arch. Neurol. 59:281-286(2002) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS SPG4 LEU-399; VAL-426; LEU-489; ASP-559 AND GLN-562. - Ref.49"Mutation analysis of the spastin gene (SPG4) in patients in Germany with autosomal dominant hereditary spastic paraplegia."
Sauter S.M., Miterski B., Klimpe S., Boensch D., Schoels L., Visbeck A., Papke T., Hopf H.C., Engel W., Deufel T., Epplen J.T., Neesen J.
Hum. Mutat. 20:127-132(2002) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS SPG4 ARG-407; TYR-551 AND ILE-615. - Ref.50"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) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS SPG4 LYS-347; ARG-388 AND CYS-499. - Ref.51"Missense and splice site mutations in SPG4 suggest loss-of-function in dominant spastic paraplegia."
Patrono C., Casali C., Tessa A., Cricchi F., Fortini D., Carrozzo R., Siciliano G., Bertini E., Santorelli F.M.
J. Neurol. 249:200-205(2002) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT SPG4 ASP-512. - Ref.52"Three novel spastin (SPG4) mutations in families with autosomal dominant hereditary spastic paraplegia."
Proukakis C., Hart P.E., Cornish A., Warner T.T., Crosby A.H.
J. Neurol. Sci. 201:65-69(2002) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT SPG4 PHE-404 DEL. - Ref.53"A novel missense mutation (I344K) in the SPG4gene in a Korean family with autosomal-dominant hereditary spastic paraplegia."
Ki C.S., Lee W.Y., Han do H., Sung D.H., Lee K.B., Lee K.A., Cho S.S., Cho S., Hwang H., Sohn K.M., Choi Y.J., Kim J.W.
J. Hum. Genet. 47:473-477(2002) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT SPG4 LYS-344. - Ref.54"Screening of patients with hereditary spastic paraplegia reveals seven novel mutations in the SPG4 (Spastin) gene."
Proukakis C., Auer-Grumbach M., Wagner K., Wilkinson P.A., Reid E., Patton M.A., Warner T.T., Crosby A.H.
Hum. Mutat. 21:170-170(2003) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT SPG4 LEU-503. - Ref.55"Novel spastin mutations and their expression analysis in two Italian families."
Molon A., Montagna P., Angelini C., Pegoraro E.
Eur. J. Hum. Genet. 11:710-713(2003) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT SPG4 PRO-534. - Ref.56"Three novel mutations of the spastin gene in Chinese patients with hereditary spastic paraplegia."
Tang B., Zhao G., Xia K., Pan Q., Luo W., Shen L., Long Z., Dai H., Zi X., Jiang H.
Arch. Neurol. 61:49-55(2004) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS SPG4 GLN-378; VAL-390 AND LEU-515 DEL. - Ref.57"Hereditary spastic paraplegia: clinical genetic study of 15 families."
Orlacchio A., Kawarai T., Totaro A., Errico A., St George-Hyslop P.H., Rugarli E.I., Bernardi G.
Arch. Neurol. 61:849-855(2004) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT SPG4 SER-386. - Ref.58"Hereditary spastic paraplegia with cerebellar ataxia: a complex phenotype associated with a new SPG4 gene mutation."
Nielsen J.E., Johnsen B., Koefoed P., Scheuer K.H., Groenbech-Jensen M., Law I., Krabbe K., Noerremoelle A., Eiberg H., Soendergaard H., Dam M., Rehfeld J.F., Krarup C., Paulson O.B., Hasholt L., Soerensen S.A.
Eur. J. Neurol. 11:817-824(2004) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT SPG4 GLN-490 DEL. - Ref.59"Intragenic modifiers of hereditary spastic paraplegia due to spastin gene mutations."
Svenson I.K., Kloos M.T., Gaskell P.C., Nance M.A., Garbern J.Y., Hisanaga S., Pericak-Vance M.A., Ashley-Koch A.E., Marchuk D.A.
Neurogenetics 5:157-164(2004) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS SPG4 VAL-470 AND GLY-562, VARIANTS LEU-44 AND GLN-45. - Ref.60"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) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS SPG4 GLY-459 AND CYS-460. - Ref.61"A new SPG4 mutation in a variant form of spastic paraplegia with congenital arachnoid cysts."
Orlacchio A., Gaudiello F., Totaro A., Floris R., St George-Hyslop P.H., Bernardi G., Kawarai T.
Neurology 62:1875-1878(2004) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT SPG4 ILE-614. - Ref.62"Infantile hereditary spastic paraparesis due to codominant mutations in the spastin gene."
Chinnery P.F., Keers S.M., Holden M.J., Ramesh V., Dalton A.
Neurology 63:710-712(2004) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT SPG4 LEU-361, VARIANT LEU-44. - Ref.63"Eight novel mutations in SPG4 in a large sample of patients with hereditary spastic paraplegia."
Crippa F., Panzeri C., Martinuzzi A., Arnoldi A., Redaelli F., Tonelli A., Baschirotto C., Vazza G., Mostacciuolo M.L., Daga A., Orso G., Profice P., Trabacca A., D'Angelo M.G., Comi G.P., Galbiati S., Lamperti C., Bonato S. , Pandolfo M., Meola G., Musumeci O., Toscano A., Trevisan C.P., Bresolin N., Bassi M.T.
Arch. Neurol. 63:750-755(2006) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS SPG4 VAL-195; VAL-406; GLY-493; HIS-499; TRP-503 AND CYS-607. - Ref.64"Novel spastin (SPG4) mutations in Italian patients with hereditary spastic paraplegia."
Magariello A., Muglia M., Patitucci A., Mazzei R., Conforti F.L., Gabriele A.L., Sprovieri T., Ungaro C., Gambardella A., Mancuso M., Siciliano G., Branca D., Aguglia U., de Angelis M.V., Longo K., Quattrone A.
Neuromuscul. Disord. 16:387-390(2006) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT SPG4 LEU-435. - Ref.66"Seven novel mutations and four exon deletions in a collection of Norwegian patients with SPG4 hereditary spastic paraplegia."
Erichsen A.K., Inderhaug E., Mattingsdal M., Eiklid K., Tallaksen C.M.
Eur. J. Neurol. 14:809-814(2007) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS SPG4 THR-364; HIS-380 AND HIS-579, VARIANT LEU-44. - Ref.67"Unique spectrum of SPAST variants in Estonian HSP patients: presence of benign missense changes but lack of exonic rearrangements."
Braschinsky M., Tamm R., Beetz C., Sachez-Ferrero E., Raukas E., Luus S.M., Gross-Paju K., Boillot C., Canzian F., Metspalu A., Haldre S.
BMC Neurol. 10:17-17(2010) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS LEU-44 AND GLY-229, VARIANTS SPG4 ILE-162; PHE-426 AND SER-460. - Ref.68"Mutational spectrum of the SPG4 (SPAST) and SPG3A (ATL1) genes in Spanish patients with hereditary spastic paraplegia."
Alvarez V., Sanchez-Ferrero E., Beetz C., Diaz M., Alonso B., Corao A.I., Gamez J., Esteban J., Gonzalo J.F., Pascual-Pascual S.I., Lopez de Munain A., Moris G., Ribacoba R., Marquez C., Rosell J., Marin R., Garcia-Barcina M.J., Del Castillo E., Benito C., Coto E.
BMC Neurol. 10:89-89(2010) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS SPG4 THR-287 DEL; LEU-293; LEU-328; ARG-378; HIS-380; PRO-391; 393-LYS--ALA-396 DEL; THR-409; ARG-410; PRO-436; ASN-441; SER-460; ALA-463; PHE-492; GLY-498; ARG-503 INS; GLY-514 AND THR-580. - Ref.69"Hereditary spastic paraplegia due to SPAST mutations in 151 Dutch patients: new clinical aspects and 27 novel mutations."
de Bot S.T., van den Elzen R.T., Mensenkamp A.R., Schelhaas H.J., Willemsen M.A., Knoers N.V., Kremer H.P., van de Warrenburg B.P., Scheffer H.
J. Neurol. Neurosurg. Psych. 81:1073-1078(2010) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS SPG4 ILE-162; LYS-356; SER-365; ARG-382; ILE-; PHE-422; ASN-445; SER-460; LEU-482; GLU-512 DEL; VAL-534 AND PRO-562, VARIANT LEU-44. - Ref.70"Mutation screening of spastin, atlastin, and REEP1 in hereditary spastic paraplegia."
McCorquodale D.S. III, Ozomaro U., Huang J., Montenegro G., Kushman A., Citrigno L., Price J., Speziani F., Pericak-Vance M.A., Zuchner S.
Clin. Genet. 79:523-530(2011) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS SPG4 THR-97; ASP-201; SER-314; VAL-360; ALA-464; GLY-498 AND ILE-550. - Ref.71"Clinical and genetic findings in a series of Italian children with pure hereditary spastic paraplegia."
Battini R., Fogli A., Borghetti D., Michelucci A., Perazza S., Baldinotti F., Conidi M.E., Ferreri M.I., Simi P., Cioni G.
Eur. J. Neurol. 18:150-157(2011) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS SPG4 LEU-413 AND LYS-454. - Ref.72"Detection of novel mutations and review of published data suggests that hereditary spastic paraplegia caused by spastin (SPAST) mutations is found more often in males."
Proukakis C., Moore D., Labrum R., Wood N.W., Houlden H.
J. Neurol. Sci. 306:62-65(2011) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS SPG4 MET-364; LEU-368; GLU-377 AND SER-450. - Ref.73"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) [PubMed] [Europe PMC] [Abstract]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. - Ref.74"First mutation in the nuclear localization signal sequence of spastin protein identified in a patient with hereditary spastic paraplegia."
Magariello A., Tortorella C., Patitucci A., Tortelli R., Liguori M., Mazzei R., Conforti F.L., Citrigno L., Ungaro C., Simone I.L., Muglia M.
Eur. J. Neurol. 20:E22-E23(2013) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT SPG4 HIS-309. - Ref.75"High frequency of SPG4 in Taiwanese families with autosomal dominant hereditary spastic paraplegia."
Lan M.Y., Chang Y.Y., Yeh T.H., Lai S.C., Liou C.W., Kuo H.C., Wu Y.R., Lyu R.K., Hung J.W., Chang Y.C., Lu C.S.
BMC Neurol. 14:216-216(2014) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS SPG4 244-ASN--VAL-616 DEL; PRO-461; GLY-555 AND 581-ARG--VAL-616 DEL. - Ref.76"Mutation analysis of SPAST, ATL1, and REEP1 in Korean Patients with Hereditary Spastic Paraplegia."
Kim T.H., Lee J.H., Park Y.E., Shin J.H., Nam T.S., Kim H.S., Jang H.J., Semenov A., Kim S.J., Kim D.S.
J. Clin. Neurol. 10:257-261(2014) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS SPG4 44-SER--VAL-616 DEL; 245-SER--VAL-616 DEL; 254-LYS--VAL-616 DEL; GLY-372; LEU-399; ARG-451 DEL; ARG-458; HIS-499 AND 581-ARG--VAL-616 DEL. - Ref.77"Spastin mutation screening in Chinese patients with pure hereditary spastic paraplegia."
Wei Q.Q., Chen Y., Zheng Z.Z., Chen X., Huang R., Yang Y., Burgunder J., Shang H.F.
Parkinsonism Relat. Disord. 20:845-849(2014) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS SPG4 PRO-363; LEU-399; VAL-441 AND ARG-595. - Ref.78"Truncating mutations in SPAST patients are associated with a high rate of psychiatric comorbidities in hereditary spastic paraplegia."
Chelban V., Tucci A., Lynch D.S., Polke J.M., Santos L., Jonvik H., Groppa S., Wood N.W., Houlden H.
J. Neurol. Neurosurg. Psych. 88:681-687(2017) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS SPG4 LYS-328; LYS-366; LEU-368; VAL-368; THR-372; TYR-386; THR-390; ALA-418; TYR-470; THR-485; MET-498 AND 546-GLY--VAL-616 DEL.
Ref.1
"Spastin, a new AAA protein, is altered in the most frequent form of autosomal dominant spastic paraplegia."
Hazan J., Fonknechten N., Mavel D., Paternotte C., Samson D., Artiguenave F., Davoine C.-S., Cruaud C., Durr A., Wincker P., Brottier P., Cattolico L., Barbe V., Burgunder J.-M., Prud'homme J.-F., Brice A., Fontaine B., Heilig R., Weissenbach J.
Nat. Genet. 23:296-303(1999) [PubMed] [Europe PMC] [Abstract]
Hazan J., Fonknechten N., Mavel D., Paternotte C., Samson D., Artiguenave F., Davoine C.-S., Cruaud C., Durr A., Wincker P., Brottier P., Cattolico L., Barbe V., Burgunder J.-M., Prud'homme J.-F., Brice A., Fontaine B., Heilig R., Weissenbach J.
Nat. Genet. 23:296-303(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, VARIANTS SPG4 CYS-362; TYR-448 AND CYS-499.
Ref.5
"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) [PubMed] [Europe PMC] [Abstract]
Errico A., Ballabio A., Rugarli E.I.
Hum. Mol. Genet. 11:153-163(2002) [PubMed] [Europe PMC] [Abstract]
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.
Ref.11
"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) [PubMed] [Europe PMC] [Abstract]
Evans K.J., Gomes E.R., Reisenweber S.M., Gundersen G.G., Lauring B.P.
J. Cell Biol. 168:599-606(2005) [PubMed] [Europe PMC] [Abstract]
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.
Ref.13
"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) [PubMed] [Europe PMC] [Abstract]
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) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT SPG4 ARG-388.
Ref.15
"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) [PubMed] [Europe PMC] [Abstract]
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) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATL1, CHARACTERIZATION OF VARIANT SPG4 ARG-388.
Ref.18
"Recognition of C-terminal amino acids in tubulin by pore loops in Spastin is important for microtubule severing."
White S.R., Evans K.J., Lary J., Cole J.L., Lauring B.P.
J. Cell Biol. 176:995-1005(2007) [PubMed] [Europe PMC] [Abstract]
White S.R., Evans K.J., Lary J., Cole J.L., Lauring B.P.
J. Cell Biol. 176:995-1005(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, HOMOHEXAMERIZATION, INTERACTION WITH TUBULIN AND MICROTUBULES, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-415; GLU-442; ARG-451 AND ALA-457, CHARACTERIZATION OF VARIANT SPG4 TYR-448.
Ref.23
"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) [PubMed] [Europe PMC] [Abstract]
Connell J.W., Lindon C., Luzio J.P., Reid E.
Traffic 10:42-56(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), CHARACTERIZATION OF VARIANT SPG4 ARG-388.
Ref.42
"Hereditary spastic paraplegia caused by mutations in the SPG4 gene."
Buerger J., Fonknechten N., Hoeltzenbein M., Neumann L., Bratanoff E., Hazan J., Reis A.
Eur. J. Hum. Genet. 8:771-776(2000) [PubMed] [Europe PMC] [Abstract]
Buerger J., Fonknechten N., Hoeltzenbein M., Neumann L., Bratanoff E., Hazan J., Reis A.
Eur. J. Hum. Genet. 8:771-776(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG4 GLY-441.
Ref.43
"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) [PubMed] [Europe PMC] [Abstract]
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) [PubMed] [Europe PMC] [Abstract]
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.
Ref.44
"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) [PubMed] [Europe PMC] [Abstract]
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) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 GLY-424 AND HIS-584, VARIANT LEU-44.
Ref.45
"Novel mutations in spastin gene and absence of correlation with age at onset of symptoms."
Hentati A., Deng H.-X., Zhai H., Chen W., Yang Y., Hung W.-Y., Azim A.C., Bohlega S., Tandan R., Warner C., Laing N.G., Cambi F., Mitsumoto H., Roos R.P., Boustany R.-M.N., Ben-Hamida M., Hentati F., Siddique T.
Neurology 55:1388-1390(2000) [PubMed] [Europe PMC] [Abstract]
Hentati A., Deng H.-X., Zhai H., Chen W., Yang Y., Hung W.-Y., Azim A.C., Bohlega S., Tandan R., Warner C., Laing N.G., Cambi F., Mitsumoto H., Roos R.P., Boustany R.-M.N., Ben-Hamida M., Hentati F., Siddique T.
Neurology 55:1388-1390(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 PHE-436 AND ASP-559.
Ref.46
"Identification and expression analysis of spastin gene mutations in hereditary spastic paraplegia."
Svenson I.K., Ashley-Koch A.E., Gaskell P.C., Riney T.J., Cumming W.J.K., Kingston H.M., Hogan E.L., Boustany R.-M.N., Vance J.M., Nance M.A., Pericak-Vance M.A., Marchuk D.A.
Am. J. Hum. Genet. 68:1077-1085(2001) [PubMed] [Europe PMC] [Abstract]
Svenson I.K., Ashley-Koch A.E., Gaskell P.C., Riney T.J., Cumming W.J.K., Kingston H.M., Hogan E.L., Boustany R.-M.N., Vance J.M., Nance M.A., Pericak-Vance M.A., Marchuk D.A.
Am. J. Hum. Genet. 68:1077-1085(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 CYS-499 AND GLY-562.
Ref.47
"A Japanese SPG4 family with a novel missense mutation of the SPG4 gene: intrafamilial variability in age at onset and clinical severity."
Namekawa M., Takiyama Y., Sakoe K., Nagaki H., Shimazaki H., Yoshimura M., Ikeguchi K., Nakano I., Nishizawa M.
Acta Neurol. Scand. 106:387-391(2002) [PubMed] [Europe PMC] [Abstract]
Namekawa M., Takiyama Y., Sakoe K., Nagaki H., Shimazaki H., Yoshimura M., Ikeguchi K., Nakano I., Nishizawa M.
Acta Neurol. Scand. 106:387-391(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG4 VAL-485.
Ref.48
"Spectrum of SPG4 mutations in a large collection of North American families with hereditary spastic paraplegia."
Meijer I.A., Hand C.K., Cossette P., Figlewicz D.A., Rouleau G.A.
Arch. Neurol. 59:281-286(2002) [PubMed] [Europe PMC] [Abstract]
Meijer I.A., Hand C.K., Cossette P., Figlewicz D.A., Rouleau G.A.
Arch. Neurol. 59:281-286(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 LEU-399; VAL-426; LEU-489; ASP-559 AND GLN-562.
Ref.49
"Mutation analysis of the spastin gene (SPG4) in patients in Germany with autosomal dominant hereditary spastic paraplegia."
Sauter S.M., Miterski B., Klimpe S., Boensch D., Schoels L., Visbeck A., Papke T., Hopf H.C., Engel W., Deufel T., Epplen J.T., Neesen J.
Hum. Mutat. 20:127-132(2002) [PubMed] [Europe PMC] [Abstract]
Sauter S.M., Miterski B., Klimpe S., Boensch D., Schoels L., Visbeck A., Papke T., Hopf H.C., Engel W., Deufel T., Epplen J.T., Neesen J.
Hum. Mutat. 20:127-132(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 ARG-407; TYR-551 AND ILE-615.
Ref.50
"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) [PubMed] [Europe PMC] [Abstract]
Yabe I., Sasaki H., Tashiro K., Matsuura T., Takegami T., Satoh T.
J. Med. Genet. 39:E46-E46(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 LYS-347; ARG-388 AND CYS-499.
Ref.51
"Missense and splice site mutations in SPG4 suggest loss-of-function in dominant spastic paraplegia."
Patrono C., Casali C., Tessa A., Cricchi F., Fortini D., Carrozzo R., Siciliano G., Bertini E., Santorelli F.M.
J. Neurol. 249:200-205(2002) [PubMed] [Europe PMC] [Abstract]
Patrono C., Casali C., Tessa A., Cricchi F., Fortini D., Carrozzo R., Siciliano G., Bertini E., Santorelli F.M.
J. Neurol. 249:200-205(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG4 ASP-512.
Ref.52
"Three novel spastin (SPG4) mutations in families with autosomal dominant hereditary spastic paraplegia."
Proukakis C., Hart P.E., Cornish A., Warner T.T., Crosby A.H.
J. Neurol. Sci. 201:65-69(2002) [PubMed] [Europe PMC] [Abstract]
Proukakis C., Hart P.E., Cornish A., Warner T.T., Crosby A.H.
J. Neurol. Sci. 201:65-69(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG4 PHE-404 DEL.
Ref.53
"A novel missense mutation (I344K) in the SPG4gene in a Korean family with autosomal-dominant hereditary spastic paraplegia."
Ki C.S., Lee W.Y., Han do H., Sung D.H., Lee K.B., Lee K.A., Cho S.S., Cho S., Hwang H., Sohn K.M., Choi Y.J., Kim J.W.
J. Hum. Genet. 47:473-477(2002) [PubMed] [Europe PMC] [Abstract]
Ki C.S., Lee W.Y., Han do H., Sung D.H., Lee K.B., Lee K.A., Cho S.S., Cho S., Hwang H., Sohn K.M., Choi Y.J., Kim J.W.
J. Hum. Genet. 47:473-477(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG4 LYS-344.
Ref.54
"Screening of patients with hereditary spastic paraplegia reveals seven novel mutations in the SPG4 (Spastin) gene."
Proukakis C., Auer-Grumbach M., Wagner K., Wilkinson P.A., Reid E., Patton M.A., Warner T.T., Crosby A.H.
Hum. Mutat. 21:170-170(2003) [PubMed] [Europe PMC] [Abstract]
Proukakis C., Auer-Grumbach M., Wagner K., Wilkinson P.A., Reid E., Patton M.A., Warner T.T., Crosby A.H.
Hum. Mutat. 21:170-170(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG4 LEU-503.
Ref.55
"Novel spastin mutations and their expression analysis in two Italian families."
Molon A., Montagna P., Angelini C., Pegoraro E.
Eur. J. Hum. Genet. 11:710-713(2003) [PubMed] [Europe PMC] [Abstract]
Molon A., Montagna P., Angelini C., Pegoraro E.
Eur. J. Hum. Genet. 11:710-713(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG4 PRO-534.
Ref.56
"Three novel mutations of the spastin gene in Chinese patients with hereditary spastic paraplegia."
Tang B., Zhao G., Xia K., Pan Q., Luo W., Shen L., Long Z., Dai H., Zi X., Jiang H.
Arch. Neurol. 61:49-55(2004) [PubMed] [Europe PMC] [Abstract]
Tang B., Zhao G., Xia K., Pan Q., Luo W., Shen L., Long Z., Dai H., Zi X., Jiang H.
Arch. Neurol. 61:49-55(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 GLN-378; VAL-390 AND LEU-515 DEL.
Ref.57
"Hereditary spastic paraplegia: clinical genetic study of 15 families."
Orlacchio A., Kawarai T., Totaro A., Errico A., St George-Hyslop P.H., Rugarli E.I., Bernardi G.
Arch. Neurol. 61:849-855(2004) [PubMed] [Europe PMC] [Abstract]
Orlacchio A., Kawarai T., Totaro A., Errico A., St George-Hyslop P.H., Rugarli E.I., Bernardi G.
Arch. Neurol. 61:849-855(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG4 SER-386.
Ref.58
"Hereditary spastic paraplegia with cerebellar ataxia: a complex phenotype associated with a new SPG4 gene mutation."
Nielsen J.E., Johnsen B., Koefoed P., Scheuer K.H., Groenbech-Jensen M., Law I., Krabbe K., Noerremoelle A., Eiberg H., Soendergaard H., Dam M., Rehfeld J.F., Krarup C., Paulson O.B., Hasholt L., Soerensen S.A.
Eur. J. Neurol. 11:817-824(2004) [PubMed] [Europe PMC] [Abstract]
Nielsen J.E., Johnsen B., Koefoed P., Scheuer K.H., Groenbech-Jensen M., Law I., Krabbe K., Noerremoelle A., Eiberg H., Soendergaard H., Dam M., Rehfeld J.F., Krarup C., Paulson O.B., Hasholt L., Soerensen S.A.
Eur. J. Neurol. 11:817-824(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG4 GLN-490 DEL.
Ref.59
"Intragenic modifiers of hereditary spastic paraplegia due to spastin gene mutations."
Svenson I.K., Kloos M.T., Gaskell P.C., Nance M.A., Garbern J.Y., Hisanaga S., Pericak-Vance M.A., Ashley-Koch A.E., Marchuk D.A.
Neurogenetics 5:157-164(2004) [PubMed] [Europe PMC] [Abstract]
Svenson I.K., Kloos M.T., Gaskell P.C., Nance M.A., Garbern J.Y., Hisanaga S., Pericak-Vance M.A., Ashley-Koch A.E., Marchuk D.A.
Neurogenetics 5:157-164(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 VAL-470 AND GLY-562, VARIANTS LEU-44 AND GLN-45.
Ref.60
"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) [PubMed] [Europe PMC] [Abstract]
Falco M., Scuderi C., Musumeci S., Sturnio M., Neri M., Bigoni S., Caniatti L., Fichera M.
Neuromuscul. Disord. 14:750-753(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 GLY-459 AND CYS-460.
Ref.61
"A new SPG4 mutation in a variant form of spastic paraplegia with congenital arachnoid cysts."
Orlacchio A., Gaudiello F., Totaro A., Floris R., St George-Hyslop P.H., Bernardi G., Kawarai T.
Neurology 62:1875-1878(2004) [PubMed] [Europe PMC] [Abstract]
Orlacchio A., Gaudiello F., Totaro A., Floris R., St George-Hyslop P.H., Bernardi G., Kawarai T.
Neurology 62:1875-1878(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG4 ILE-614.
Ref.62
"Infantile hereditary spastic paraparesis due to codominant mutations in the spastin gene."
Chinnery P.F., Keers S.M., Holden M.J., Ramesh V., Dalton A.
Neurology 63:710-712(2004) [PubMed] [Europe PMC] [Abstract]
Chinnery P.F., Keers S.M., Holden M.J., Ramesh V., Dalton A.
Neurology 63:710-712(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG4 LEU-361, VARIANT LEU-44.
Ref.63
"Eight novel mutations in SPG4 in a large sample of patients with hereditary spastic paraplegia."
Crippa F., Panzeri C., Martinuzzi A., Arnoldi A., Redaelli F., Tonelli A., Baschirotto C., Vazza G., Mostacciuolo M.L., Daga A., Orso G., Profice P., Trabacca A., D'Angelo M.G., Comi G.P., Galbiati S., Lamperti C., Bonato S. , Pandolfo M., Meola G., Musumeci O., Toscano A., Trevisan C.P., Bresolin N., Bassi M.T.
Arch. Neurol. 63:750-755(2006) [PubMed] [Europe PMC] [Abstract]
Crippa F., Panzeri C., Martinuzzi A., Arnoldi A., Redaelli F., Tonelli A., Baschirotto C., Vazza G., Mostacciuolo M.L., Daga A., Orso G., Profice P., Trabacca A., D'Angelo M.G., Comi G.P., Galbiati S., Lamperti C., Bonato S. , Pandolfo M., Meola G., Musumeci O., Toscano A., Trevisan C.P., Bresolin N., Bassi M.T.
Arch. Neurol. 63:750-755(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 VAL-195; VAL-406; GLY-493; HIS-499; TRP-503 AND CYS-607.
Ref.64
"Novel spastin (SPG4) mutations in Italian patients with hereditary spastic paraplegia."
Magariello A., Muglia M., Patitucci A., Mazzei R., Conforti F.L., Gabriele A.L., Sprovieri T., Ungaro C., Gambardella A., Mancuso M., Siciliano G., Branca D., Aguglia U., de Angelis M.V., Longo K., Quattrone A.
Neuromuscul. Disord. 16:387-390(2006) [PubMed] [Europe PMC] [Abstract]
Magariello A., Muglia M., Patitucci A., Mazzei R., Conforti F.L., Gabriele A.L., Sprovieri T., Ungaro C., Gambardella A., Mancuso M., Siciliano G., Branca D., Aguglia U., de Angelis M.V., Longo K., Quattrone A.
Neuromuscul. Disord. 16:387-390(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG4 LEU-435.
Ref.66
"Seven novel mutations and four exon deletions in a collection of Norwegian patients with SPG4 hereditary spastic paraplegia."
Erichsen A.K., Inderhaug E., Mattingsdal M., Eiklid K., Tallaksen C.M.
Eur. J. Neurol. 14:809-814(2007) [PubMed] [Europe PMC] [Abstract]
Erichsen A.K., Inderhaug E., Mattingsdal M., Eiklid K., Tallaksen C.M.
Eur. J. Neurol. 14:809-814(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 THR-364; HIS-380 AND HIS-579, VARIANT LEU-44.
Ref.67
"Unique spectrum of SPAST variants in Estonian HSP patients: presence of benign missense changes but lack of exonic rearrangements."
Braschinsky M., Tamm R., Beetz C., Sachez-Ferrero E., Raukas E., Luus S.M., Gross-Paju K., Boillot C., Canzian F., Metspalu A., Haldre S.
BMC Neurol. 10:17-17(2010) [PubMed] [Europe PMC] [Abstract]
Braschinsky M., Tamm R., Beetz C., Sachez-Ferrero E., Raukas E., Luus S.M., Gross-Paju K., Boillot C., Canzian F., Metspalu A., Haldre S.
BMC Neurol. 10:17-17(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LEU-44 AND GLY-229, VARIANTS SPG4 ILE-162; PHE-426 AND SER-460.
Ref.68
"Mutational spectrum of the SPG4 (SPAST) and SPG3A (ATL1) genes in Spanish patients with hereditary spastic paraplegia."
Alvarez V., Sanchez-Ferrero E., Beetz C., Diaz M., Alonso B., Corao A.I., Gamez J., Esteban J., Gonzalo J.F., Pascual-Pascual S.I., Lopez de Munain A., Moris G., Ribacoba R., Marquez C., Rosell J., Marin R., Garcia-Barcina M.J., Del Castillo E., Benito C., Coto E.
BMC Neurol. 10:89-89(2010) [PubMed] [Europe PMC] [Abstract]
Alvarez V., Sanchez-Ferrero E., Beetz C., Diaz M., Alonso B., Corao A.I., Gamez J., Esteban J., Gonzalo J.F., Pascual-Pascual S.I., Lopez de Munain A., Moris G., Ribacoba R., Marquez C., Rosell J., Marin R., Garcia-Barcina M.J., Del Castillo E., Benito C., Coto E.
BMC Neurol. 10:89-89(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 THR-287 DEL; LEU-293; LEU-328; ARG-378; HIS-380; PRO-391; 393-LYS--ALA-396 DEL; THR-409; ARG-410; PRO-436; ASN-441; SER-460; ALA-463; PHE-492; GLY-498; ARG-503 INS; GLY-514 AND THR-580.
Ref.69
"Hereditary spastic paraplegia due to SPAST mutations in 151 Dutch patients: new clinical aspects and 27 novel mutations."
de Bot S.T., van den Elzen R.T., Mensenkamp A.R., Schelhaas H.J., Willemsen M.A., Knoers N.V., Kremer H.P., van de Warrenburg B.P., Scheffer H.
J. Neurol. Neurosurg. Psych. 81:1073-1078(2010) [PubMed] [Europe PMC] [Abstract]
de Bot S.T., van den Elzen R.T., Mensenkamp A.R., Schelhaas H.J., Willemsen M.A., Knoers N.V., Kremer H.P., van de Warrenburg B.P., Scheffer H.
J. Neurol. Neurosurg. Psych. 81:1073-1078(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 ILE-162; LYS-356; SER-365; ARG-382; ILE-; PHE-422; ASN-445; SER-460; LEU-482; GLU-512 DEL; VAL-534 AND PRO-562, VARIANT LEU-44.
Ref.70
"Mutation screening of spastin, atlastin, and REEP1 in hereditary spastic paraplegia."
McCorquodale D.S. III, Ozomaro U., Huang J., Montenegro G., Kushman A., Citrigno L., Price J., Speziani F., Pericak-Vance M.A., Zuchner S.
Clin. Genet. 79:523-530(2011) [PubMed] [Europe PMC] [Abstract]
McCorquodale D.S. III, Ozomaro U., Huang J., Montenegro G., Kushman A., Citrigno L., Price J., Speziani F., Pericak-Vance M.A., Zuchner S.
Clin. Genet. 79:523-530(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 THR-97; ASP-201; SER-314; VAL-360; ALA-464; GLY-498 AND ILE-550.
Ref.71
"Clinical and genetic findings in a series of Italian children with pure hereditary spastic paraplegia."
Battini R., Fogli A., Borghetti D., Michelucci A., Perazza S., Baldinotti F., Conidi M.E., Ferreri M.I., Simi P., Cioni G.
Eur. J. Neurol. 18:150-157(2011) [PubMed] [Europe PMC] [Abstract]
Battini R., Fogli A., Borghetti D., Michelucci A., Perazza S., Baldinotti F., Conidi M.E., Ferreri M.I., Simi P., Cioni G.
Eur. J. Neurol. 18:150-157(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 LEU-413 AND LYS-454.
Ref.72
"Detection of novel mutations and review of published data suggests that hereditary spastic paraplegia caused by spastin (SPAST) mutations is found more often in males."
Proukakis C., Moore D., Labrum R., Wood N.W., Houlden H.
J. Neurol. Sci. 306:62-65(2011) [PubMed] [Europe PMC] [Abstract]
Proukakis C., Moore D., Labrum R., Wood N.W., Houlden H.
J. Neurol. Sci. 306:62-65(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 MET-364; LEU-368; GLU-377 AND SER-450.
Ref.73
"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) [PubMed] [Europe PMC] [Abstract]
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) [PubMed] [Europe PMC] [Abstract]
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.
Ref.74
"First mutation in the nuclear localization signal sequence of spastin protein identified in a patient with hereditary spastic paraplegia."
Magariello A., Tortorella C., Patitucci A., Tortelli R., Liguori M., Mazzei R., Conforti F.L., Citrigno L., Ungaro C., Simone I.L., Muglia M.
Eur. J. Neurol. 20:E22-E23(2013) [PubMed] [Europe PMC] [Abstract]
Magariello A., Tortorella C., Patitucci A., Tortelli R., Liguori M., Mazzei R., Conforti F.L., Citrigno L., Ungaro C., Simone I.L., Muglia M.
Eur. J. Neurol. 20:E22-E23(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG4 HIS-309.
Ref.75
"High frequency of SPG4 in Taiwanese families with autosomal dominant hereditary spastic paraplegia."
Lan M.Y., Chang Y.Y., Yeh T.H., Lai S.C., Liou C.W., Kuo H.C., Wu Y.R., Lyu R.K., Hung J.W., Chang Y.C., Lu C.S.
BMC Neurol. 14:216-216(2014) [PubMed] [Europe PMC] [Abstract]
Lan M.Y., Chang Y.Y., Yeh T.H., Lai S.C., Liou C.W., Kuo H.C., Wu Y.R., Lyu R.K., Hung J.W., Chang Y.C., Lu C.S.
BMC Neurol. 14:216-216(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 244-ASN--VAL-616 DEL; PRO-461; GLY-555 AND 581-ARG--VAL-616 DEL.
Ref.76
"Mutation analysis of SPAST, ATL1, and REEP1 in Korean Patients with Hereditary Spastic Paraplegia."
Kim T.H., Lee J.H., Park Y.E., Shin J.H., Nam T.S., Kim H.S., Jang H.J., Semenov A., Kim S.J., Kim D.S.
J. Clin. Neurol. 10:257-261(2014) [PubMed] [Europe PMC] [Abstract]
Kim T.H., Lee J.H., Park Y.E., Shin J.H., Nam T.S., Kim H.S., Jang H.J., Semenov A., Kim S.J., Kim D.S.
J. Clin. Neurol. 10:257-261(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 44-SER--VAL-616 DEL; 245-SER--VAL-616 DEL; 254-LYS--VAL-616 DEL; GLY-372; LEU-399; ARG-451 DEL; ARG-458; HIS-499 AND 581-ARG--VAL-616 DEL.
Ref.77
"Spastin mutation screening in Chinese patients with pure hereditary spastic paraplegia."
Wei Q.Q., Chen Y., Zheng Z.Z., Chen X., Huang R., Yang Y., Burgunder J., Shang H.F.
Parkinsonism Relat. Disord. 20:845-849(2014) [PubMed] [Europe PMC] [Abstract]
Wei Q.Q., Chen Y., Zheng Z.Z., Chen X., Huang R., Yang Y., Burgunder J., Shang H.F.
Parkinsonism Relat. Disord. 20:845-849(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 PRO-363; LEU-399; VAL-441 AND ARG-595.
Ref.78
"Truncating mutations in SPAST patients are associated with a high rate of psychiatric comorbidities in hereditary spastic paraplegia."
Chelban V., Tucci A., Lynch D.S., Polke J.M., Santos L., Jonvik H., Groppa S., Wood N.W., Houlden H.
J. Neurol. Neurosurg. Psych. 88:681-687(2017) [PubMed] [Europe PMC] [Abstract]
Chelban V., Tucci A., Lynch D.S., Polke J.M., Santos L., Jonvik H., Groppa S., Wood N.W., Houlden H.
J. Neurol. Neurosurg. Psych. 88:681-687(2017) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 LYS-328; LYS-366; LEU-368; VAL-368; THR-372; TYR-386; THR-390; ALA-418; TYR-470; THR-485; MET-498 AND 546-GLY--VAL-616 DEL.
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body.
See also OMIM:182601| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_075827 | 44 – 616 | Missing in SPG4. 1 Publication Manual assertion based on experiment ini
| 573 | |
| Natural variantiVAR_075828 | 95 | A → T in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067628 | 97 | P → T in SPG4; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_075829 | 112 – 616 | Missing in SPG4. 1 Publication Manual assertion based on experiment ini
| 505 | |
| Natural variantiVAR_075830 | 135 – 616 | Missing in SPG4. 1 Publication Manual assertion based on experiment ini
| 482 | |
| Natural variantiVAR_067563 | 162 | V → I in SPG4; unknown pathological significance. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_026758 | 195 | L → V in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067629 | 201 | V → D in SPG4; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_075831 | 244 – 616 | Missing in SPG4. 1 Publication Manual assertion based on experiment ini
| 373 | |
| Natural variantiVAR_075832 | 245 – 616 | Missing in SPG4. 1 Publication Manual assertion based on experiment ini
| 372 | |
| Natural variantiVAR_075833 | 254 – 616 | Missing in SPG4. 1 Publication Manual assertion based on experiment ini
| 363 | |
| Natural variantiVAR_067631 | 287 | Missing in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067632 | 293 | P → L in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_075834 | 309 | R → H in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067633 | 314 | L → S in SPG4; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_079314 | 328 | I → K in SPG4; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067634 | 328 | I → L in SPG4; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_019448 | 344 | I → K in SPG4; abrogates ATPase activity and promotes microtubule binding. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_027206 | 347 | Q → K in SPG4; promotes microtubule binding. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067564 | 356 | E → K in SPG4; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067635 | 360 | L → V in SPG4; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_027207 | 361 | P → L in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_010195 | 362 | S → C in SPG4. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_075835 | 363 | L → P in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_075836 | 364 | R → M in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067636 | 364 | R → T in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067565 | 365 | P → S in SPG4; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_079315 | 366 | E → K in SPG4; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_075837 | 368 | F → L in SPG4. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_079316 | 368 | F → V in SPG4; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_027208 | 370 | G → R in SPG4; promotes microtubule binding and the formation of thick microtubule bundles. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_075838 | 372 | R → G in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_079317 | 372 | R → T in SPG4; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_075839 | 377 | G → E in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_019439 | 378 | L → Q in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067637 | 378 | L → R in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067638 | 380 | L → H in SPG4. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_027209 | 381 | F → C in SPG4; promotes microtubule binding and the formation of thick microtubule bundles. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067566 | 382 | G → R in SPG4; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_027210 | 386 | N → K in SPG4; abrogates ATPase activity, promotes microtubule binding and the formation of thick microtubule bundles. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_019440 | 386 | N → S in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_079318 | 386 | N → Y in SPG4; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_027211 | 388 | K → R in SPG4; abrogates ATPase activity, promotes microtubule binding and the formation of thick microtubule bundles and impairs traffic from the ER to Golgi. 7 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_079319 | 390 | M → T in SPG4; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_019441 | 390 | M → V in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067639 | 391 | L → P in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067640 | 393 – 396 | Missing in SPG4. 1 Publication Manual assertion based on experiment ini
| 4 | |
| Natural variantiVAR_027212 | 399 | S → L in SPG4. 4 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_019449 | 404 | Missing in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_075840 | 406 | I → R in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_026759 | 406 | I → V in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067567 | 407 | S → I in SPG4; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_019450 | 407 | S → R in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067641 | 409 | A → T in SPG4. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067642 | 410 | S → R in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067568 | 413 | S → L in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_079320 | 418 | E → A in SPG4; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067569 | 422 | L → F in SPG4; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_010196 | 424 | R → G in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067643 | 426 | L → F in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_027213 | 426 | L → V in SPG4; promotes microtubule binding and the formation of thick microtubule bundles. 4 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_075841 | 431 – 616 | Missing in SPG4. 1 Publication Manual assertion based on experiment ini
| 186 | |
| Natural variantiVAR_027214 | 435 | P → L in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_027215 | 436 | S → F in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067644 | 436 | S → P in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_027216 | 441 | D → G in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067645 | 441 | D → N in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_075842 | 441 | D → V in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067570 | 445 | S → N in SPG4; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_010197 | 448 | C → Y in SPG4; abrogates binding to the tail of beta-3-tubulin, abolishes microtubule severing and promotes the formation of thick microtubule bundles. 4 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_075843 | 450 | R → S in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_075844 | 451 | Missing in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067571 | 454 | E → K in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_075845 | 458 | S → R in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_027217 | 459 | R → G in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_027218 | 460 | R → C in SPG4. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_027219 | 460 | R → L in SPG4; promotes microtubule binding and the formation of thick microtubule bundles. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067572 | 460 | R → S in SPG4. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_075846 | 461 | L → P in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067646 | 463 | T → A in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067647 | 464 | E → A in SPG4; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_027220 | 470 | D → V in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_079321 | 470 | D → Y in SPG4; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067573 | 482 | V → L in SPG4; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_079322 | 485 | A → T in SPG4; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_027221 | 485 | A → V in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_027222 | 489 | P → L in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_075847 | 490 – 616 | Missing in SPG4. 1 Publication Manual assertion based on experiment ini
| 127 | |
| Natural variantiVAR_067648 | 492 | L → F in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_026760 | 493 | D → G in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067649 | 498 | R → G in SPG4. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_079323 | 498 | R → M in SPG4; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_010198 | 499 | R → C in SPG4; abrogates ATPase activity, promotes microtubule binding and the formation of thick microtubule bundles. 6 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_026761 | 499 | R → H in SPG4. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_019442 | 503 | R → L in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067650 | 503 | R → RR in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_026762 | 503 | R → W in SPG4. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_027223 | 512 | E → D in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067574 | 512 | Missing in SPG4; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067651 | 514 | R → G in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_019443 | 515 | Missing in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_019444 | 534 | L → P in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067575 | 534 | L → V in SPG4; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_079324 | 546 – 616 | Missing in SPG4. 1 Publication Manual assertion based on experiment ini
| 71 | |
| Natural variantiVAR_067652 | 550 | T → I in SPG4; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_019451 | 551 | A → Y in SPG4; requires 2 nucleotide substitutions. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_075848 | 555 | D → G in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_027224 | 555 | D → N in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_027225 | 556 | A → V in SPG4; promotes microtubule binding and the formation of thick microtubule bundles. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_027226 | 559 | G → D in SPG4. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_075849 | 559 | G → R in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_075850 | 562 – 616 | Missing in SPG4. 1 Publication Manual assertion based on experiment ini
| 55 | |
| Natural variantiVAR_027227 | 562 | R → G in SPG4. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067576 | 562 | R → P in SPG4; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_027228 | 562 | R → Q in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067653 | 579 | N → H in SPG4; unknown pathological significance. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_067654 | 580 | I → T in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_075851 | 581 – 616 | Missing in SPG4. 2 Publications Manual assertion based on experiment ini
| 36 | |
| Natural variantiVAR_010199 | 584 | D → H in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_075852 | 595 | S → R in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_026763 | 607 | W → C in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_019445 | 614 | T → I in SPG4; variant form with congenital arachnoid cysts. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_019452 | 615 | T → I in SPG4. 1 Publication Manual assertion based on experiment ini
| 1 |
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 1 | M → V: Cytoplasmic and nuclear. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 65 | R → G: Abolishes localization to lipid droplets. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 81 – 84 | RFSR → GFSG: Does not affect localization to lipid droplets. 1 Publication Manual assertion based on experiment ini
| 4 | |
| Mutagenesisi | 87 | M → V: Exclusively cytoplasmic. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 120 | H → D: Impairs binding to CHMP1B. Impairs midbody localization; when associated with D-124. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 124 | F → A: Impairs binding to CHMP1B. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 124 | F → D: Impairs binding to CHMP1B. Impairs midbody localization; when associated with D-120. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 310 – 312 | KKK → QQQ: Loss of microtubule-binding. 1 Publication Manual assertion based on experiment ini
| 3 | |
| Mutagenesisi | 388 | K → A: Abrogates ATPase activity and abolishes microtubule severing. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 415 | Y → A: Abrogates binding to the tail of alpha-tubulin and beta-3-tubulin, impairs ATPase activity and abolishes microtubule severing. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 442 | E → Q: Abrogates ATP hydrolysis, abolishes microtubule severing, stabilizes the homohexameric form, and promotes microtubule binding and redistribution from the endosome to microtubules. 8 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 448 | C → A or G: Abolishes ATPase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 448 | C → S: Does not affect ATPase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 451 | R → G: Abrogates binding to the tail of alpha-tubulin and beta-3-tubulin, impairs ATPase activity and abolishes microtubule severing. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 457 | A → E: Abrogates binding to the tail of alpha-tubulin and beta-3-tubulin and abolishes microtubule severing. 1 Publication Manual assertion based on experiment ini
| 1 |
Keywords - Diseasei
Disease mutation, Hereditary spastic paraplegia, NeurodegenerationOrganism-specific databases
DisGeNET More...DisGeNETi | 6683 |
GeneReviews a resource of expert-authored, peer-reviewed disease descriptions. More...GeneReviewsi | SPAST |
MalaCards human disease database More...MalaCardsi | SPAST |
| MIMi | 182601 phenotype |
Open Targets More...OpenTargetsi | ENSG00000021574 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 100985 Autosomal dominant spastic paraplegia type 4 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA36063 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | SPAST |
Domain mapping of disease mutations (DMDM) More...DMDMi | 12230611 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000084763 | 1 – 616 | SpastinAdd BLAST | 616 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 245 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| Modified residuei | 268 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| Modified residuei | 306 | PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| Modified residuei | 597 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 |
Keywords - PTMi
PhosphoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q9UBP0 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q9UBP0 |
PeptideAtlas More...PeptideAtlasi | Q9UBP0 |
PRoteomics IDEntifications database More...PRIDEi | Q9UBP0 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 84020 84021 [Q9UBP0-2] 84022 [Q9UBP0-3] 84023 [Q9UBP0-4] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q9UBP0 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q9UBP0 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
Expressed in brain, heart, kidney, liver, lung, pancreas, placenta and skeletal muscle. The short isoforms may predominate in brain and spinal cord.1 Publication
Manual assertion based on experiment ini
- Ref.1"Spastin, a new AAA protein, is altered in the most frequent form of autosomal dominant spastic paraplegia."
Hazan J., Fonknechten N., Mavel D., Paternotte C., Samson D., Artiguenave F., Davoine C.-S., Cruaud C., Durr A., Wincker P., Brottier P., Cattolico L., Barbe V., Burgunder J.-M., Prud'homme J.-F., Brice A., Fontaine B., Heilig R., Weissenbach J.
Nat. Genet. 23:296-303(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, VARIANTS SPG4 CYS-362; TYR-448 AND CYS-499.
<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei
Expressed in fetal brain, heart, kidney, liver, lung, skeletal muscle, spleen and thymus.1 Publication
Manual assertion based on experiment ini
- Ref.1"Spastin, a new AAA protein, is altered in the most frequent form of autosomal dominant spastic paraplegia."
Hazan J., Fonknechten N., Mavel D., Paternotte C., Samson D., Artiguenave F., Davoine C.-S., Cruaud C., Durr A., Wincker P., Brottier P., Cattolico L., Barbe V., Burgunder J.-M., Prud'homme J.-F., Brice A., Fontaine B., Heilig R., Weissenbach J.
Nat. Genet. 23:296-303(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, VARIANTS SPG4 CYS-362; TYR-448 AND CYS-499.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000021574 Expressed in 219 organ(s), highest expression level in cerebral cortex |
CleanEx database of gene expression profiles More...CleanExi | HS_SPAST |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q9UBP0 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q9UBP0 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA017311 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Homohexamer (PubMed:17389232, PubMed:22637577). Mostly monomeric, but assembles into hexameric structure for short periods of time. Oligomerization seems to be a prerequisite for catalytic activity (PubMed:17389232, PubMed:22637577). Binding to ATP in a cleft between two adjacent subunits stabilizes the homohexameric form (PubMed:17389232, PubMed:22637577). Binds to microtubules at least in part via the alpha-tubulin and beta-tubulin tails (PubMed:15269182, PubMed:15716377, PubMed:23272056). The hexamer adopts a ring conformation through which microtubules pass prior to being severed (PubMed:17389232, PubMed:22637577). Does not interact strongly with tubulin heterodimers (PubMed:15269182, PubMed:15716377, PubMed:23272056). Interacts (via MIT domain) with CHMP1B; the interaction is direct (PubMed:15537668, PubMed:18997780). Interacts with SSNA1 (PubMed:15269182). Interacts with ATL1 (PubMed:16339213, PubMed:16815977). Interacts with RTN1 (PubMed:16602018). Interacts with ZFYVE27 (PubMed:16826525, PubMed:23969831). Isoform 1 but not isoform 3 interacts with RTN2 (PubMed:22232211). Interacts with REEP1 (PubMed:20200447). Interacts (via MIT domain) with IST1 (PubMed:23897888, PubMed:26040712).UniRule annotation
Manual assertion according to rulesi
16 PublicationsManual assertion based on experiment ini
- Ref.8"Spastin interacts with the centrosomal protein NA14, and is enriched in the spindle pole, the midbody and the distal axon."
Errico A., Claudiani P., D'Addio M., Rugarli E.I.
Hum. Mol. Genet. 13:2121-2132(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SSNA1 AND MICROTUBULES, SUBCELLULAR LOCATION. - Ref.10"The hereditary spastic paraplegia protein spastin interacts with the ESCRT-III complex-associated endosomal protein CHMP1B."
Reid E., Connell J.W., Edwards T.L., Duley S., Brown S.E., Sanderson C.M.
Hum. Mol. Genet. 14:19-38(2005) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CHMP1B, SUBCELLULAR LOCATION. - Ref.11"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) [PubMed] [Europe PMC] [Abstract]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. - Ref.14"ZFYVE27 (SPG33), a novel spastin-binding protein, is mutated in hereditary spastic paraplegia."
Mannan A.U., Krawen P., Sauter S.M., Boehm J., Chronowska A., Paulus W., Neesen J., Engel W.
Am. J. Hum. Genet. 79:351-357(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ZFYVE27. - Ref.15"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) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ATL1, CHARACTERIZATION OF VARIANT SPG4 ARG-388. - Ref.16"Spastin, the most commonly mutated protein in hereditary spastic paraplegia interacts with Reticulon 1 an endoplasmic reticulum protein."
Mannan A.U., Boehm J., Sauter S.M., Rauber A., Byrne P.C., Neesen J., Engel W.
Neurogenetics 7:93-103(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RTN1, SUBCELLULAR LOCATION. - Ref.17"Interaction of two hereditary spastic paraplegia gene products, spastin and atlastin, suggests a common pathway for axonal maintenance."
Evans K.J., Keller C., Pavur K., Glasgow K., Conn B., Lauring B.P.
Proc. Natl. Acad. Sci. U.S.A. 103:10666-10671(2006) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, INTERACTION WITH ATL1, MUTAGENESIS OF GLU-442. - Ref.18"Recognition of C-terminal amino acids in tubulin by pore loops in Spastin is important for microtubule severing."
White S.R., Evans K.J., Lary J., Cole J.L., Lauring B.P.
J. Cell Biol. 176:995-1005(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, HOMOHEXAMERIZATION, INTERACTION WITH TUBULIN AND MICROTUBULES, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-415; GLU-442; ARG-451 AND ALA-457, CHARACTERIZATION OF VARIANT SPG4 TYR-448. - Ref.24"Hereditary spastic paraplegia proteins REEP1, spastin, and atlastin-1 coordinate microtubule interactions with the tubular ER network."
Park S.H., Zhu P.P., Parker R.L., Blackstone C.
J. Clin. Invest. 120:1097-1110(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH REEP1, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), TOPOLOGY (ISOFORM 1). - Ref.29"Subunit Interactions and cooperativity in the microtubule-severing AAA ATPase spastin."
Eckert T., Link S., Le D.T., Sobczak J.P., Gieseke A., Richter K., Woehlke G.
J. Biol. Chem. 287:26278-26290(2012) [PubMed] [Europe PMC] [Abstract]Cited for: HOMOHEXAMERIZATION, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, KINETIC PARAMETERS, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, COOPERATIVITY, MUTAGENESIS OF GLU-442. - Ref.30"Mutations in the ER-shaping protein reticulon 2 cause the axon-degenerative disorder hereditary spastic paraplegia type 12."
Montenegro G., Rebelo A.P., Connell J., Allison R., Babalini C., D'Aloia M., Montieri P., Schule R., Ishiura H., Price J., Strickland A., Gonzalez M.A., Baumbach-Reardon L., Deconinck T., Huang J., Bernardi G., Vance J.M., Rogers M.T. , Tsuji S., De Jonghe P., Pericak-Vance M.A., Schols L., Orlacchio A., Reid E., Zuchner S.
J. Clin. Invest. 122:538-544(2012) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RTN2. - Ref.31"Spastin's microtubule-binding properties and comparison to katanin."
Eckert T., Le D.T., Link S., Friedmann L., Woehlke G.
PLoS ONE 7:E50161-E50161(2012) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH MICROTUBULES, OLIGOMERIZATION, MUTAGENESIS OF 310-LYS--LYS-312 AND GLU-442. - Ref.33"An ESCRT-spastin interaction promotes fission of recycling tubules from the endosome."
Allison R., Lumb J.H., Fassier C., Connell J.W., Ten Martin D., Seaman M.N., Hazan J., Reid E.
J. Cell Biol. 202:527-543(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), INTERACTION WITH IST1. - Ref.35"Protrudin binds atlastins and endoplasmic reticulum-shaping proteins and regulates network formation."
Chang J., Lee S., Blackstone C.
Proc. Natl. Acad. Sci. U.S.A. 110:14954-14959(2013) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ZFYVE27. - Ref.37"Spastin and ESCRT-III coordinate mitotic spindle disassembly and nuclear envelope sealing."
Vietri M., Schink K.O., Campsteijn C., Wegner C.S., Schultz S.W., Christ L., Thoresen S.B., Brech A., Raiborg C., Stenmark H.
Nature 522:231-235(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), INTERACTION WITH IST1. - Ref.40"Structural basis for midbody targeting of spastin by the ESCRT-III protein CHMP1B."
Yang D., Rismanchi N., Renvoise B., Lippincott-Schwartz J., Blackstone C., Hurley J.H.
Nat. Struct. Mol. Biol. 15:1278-1286(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 112-196 IN COMPLEX WITH CHMP1B, INTERACTION WITH CHMP1B, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-120 AND PHE-124.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| ATL1 | Q8WXF7-1 | 4 | EBI-1222832,EBI-15590227 |
GO - Molecular functioni
- alpha-tubulin binding Source: UniProtKBInferred from physical interactioni
- beta-tubulin binding Source: UniProtKBInferred from direct assayi
- microtubule binding Source: UniProtKBInferred from direct assayi
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 112562, 29 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q9UBP0 |
Database of interacting proteins More...DIPi | DIP-38418N |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | Q9UBP0 |
Protein interaction database and analysis system More...IntActi | Q9UBP0, 14 interactors |
Molecular INTeraction database More...MINTi | Q9UBP0 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000320885 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 112 – 136 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 25 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 139 – 141 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 142 – 144 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 146 – 161 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 16 | |
| Helixi | 169 – 195 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 27 | |
| Helixi | 328 – 330 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 341 – 343 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 348 – 357 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Helixi | 359 – 363 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 365 – 367 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 370 – 372 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 376 – 383 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Helixi | 388 – 398 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| Beta strandi | 402 – 406 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 420 – 432 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| Beta strandi | 433 – 441 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Helixi | 443 – 446 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 458 – 472 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| Beta strandi | 480 – 487 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Helixi | 489 – 491 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 494 – 497 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 502 – 505 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 511 – 522 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| Helixi | 531 – 540 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Turni | 541 – 543 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 546 – 556 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| Helixi | 559 – 562 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 573 – 575 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 582 – 591 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Helixi | 598 – 610 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 13 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q9UBP0 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9UBP0 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q9UBP0 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 120 – 195 | MITSequence analysisAdd BLAST | 76 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 1 – 300 | Required for interaction with RTN11 Publication Manual assertion based on experiment ini
| 300 | |
| Regioni | 1 – 194 | Required for midbody localization1 Publication Manual assertion based on experiment ini
| 194 | |
| Regioni | 1 – 80 | Required for interaction with ATL12 Publications Manual assertion based on experiment ini
| 80 | |
| Regioni | 1 – 50 | Required for nuclear localization1 Publication Manual assertion based on experiment ini
| 50 | |
| Regioni | 50 – 87 | Required for interaction with SSNA1 and microtubules1 Publication Manual assertion based on experiment ini
| 38 | |
| Regioni | 112 – 196 | Sufficient for interaction with CHMP1B1 Publication Manual assertion based on experiment ini
| 85 | |
| Regioni | 114 – 200 | Required for interaction with microtubules1 Publication Manual assertion based on experiment ini
| 87 | |
| Regioni | 228 – 616 | Sufficient for microtubule severing1 Publication Manual assertion based on experiment ini
| 389 | |
| Regioni | 270 – 328 | Required for interaction with microtubules and microtubule severing1 Publication Manual assertion based on experiment ini
| 59 | |
| Regioni | 310 – 312 | Required for interaction with microtubules1 Publication Manual assertion based on experiment ini
| 3 |
Motif
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi | 4 – 11 | Nuclear localization signalUniRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| 8 | |
| Motifi | 59 – 67 | Nuclear export signalUniRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| 9 | |
| Motifi | 309 – 312 | Nuclear localization signalUniRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| 4 |
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Belongs to the AAA ATPase family. Spastin subfamily.UniRule annotation
Manual assertion according to rulesi
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0740 Eukaryota COG0464 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00570000078874 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000225146 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG108502 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9UBP0 |
KEGG Orthology (KO) More...KOi | K13254 |
Identification of Orthologs from Complete Genome Data More...OMAi | SEMRNIK |
Database of Orthologous Groups More...OrthoDBi | EOG091G0Q8J |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q9UBP0 |
TreeFam database of animal gene trees More...TreeFami | TF105014 |
Family and domain databases
HAMAP database of protein families More...HAMAPi | MF_03021 Spastin, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR003593 AAA+_ATPase IPR003959 ATPase_AAA_core IPR003960 ATPase_AAA_CS IPR007330 MIT IPR027417 P-loop_NTPase IPR017179 Spastin IPR035106 Spastin_chordate IPR015415 Vps4_C |
Pfam protein domain database More...Pfami | View protein in Pfam PF00004 AAA, 1 hit PF09336 Vps4_C, 1 hit |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF037338 Spastin, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00382 AAA, 1 hit SM00745 MIT, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF52540 SSF52540, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00674 AAA, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4+)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
This entry describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative promoter usage, alternative splicing and alternative initiation. AlignAdd to basketAdded to basketNote: Alternative promoter usage of a cryptic promoter in exon 1 can direct the synthesis of N-terminally truncated isoforms, which may also arise from alternative initiation.2 Publications
Manual assertion based on experiment ini
- Ref.9"Spastin subcellular localization is regulated through usage of different translation start sites and active export from the nucleus."
Claudiani P., Riano E., Errico A., Andolfi G., Rugarli E.I.
Exp. Cell Res. 309:358-369(2005) [PubMed] [Europe PMC] [Abstract]Cited for: ALTERNATIVE INITIATION, SUBCELLULAR LOCATION, NUCLEAR EXPORT SIGNALS, MUTAGENESIS OF MET-1 AND MET-87. - Ref.19"A cryptic promoter in the first exon of the SPG4 gene directs the synthesis of the 60-kDa spastin isoform."
Mancuso G., Rugarli E.I.
BMC Biol. 6:31-31(2008) [PubMed] [Europe PMC] [Abstract]Cited for: ALTERNATIVE PROMOTER USAGE, CHARACTERIZATION OF VARIANT LEU-44.
This entry has 4 described isoforms and 12 potential isoforms that are <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>computationally mapped.iShow all