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UniProtKB - Q9UBP0 (SPAST_HUMAN)

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>

<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 annotation11 Publications
Isoform 1: Involved in lipid metabolism by regulating the size and distribution of lipid droplets.1 Publication

<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. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<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 annotation2 Publications

<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
  1. KM=0.45 mM for ATP3 Publications
  1. Vmax=1.2 nmol/min/µg enzyme3 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bindingi382 – 389ATPUniRule annotation1 Publication8

<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
  • ATPase activity Source: GO_Central
  • ATP binding Source: UniProtKB-UniRule
  • beta-tubulin binding Source: UniProtKB
  • isomerase activity Source: UniProtKB-KW
  • microtubule binding Source: UniProtKB
  • microtubule-severing ATPase activity Source: UniProtKB
  • protein-containing complex binding Source: ARUK-UCL
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<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 functionAllosteric enzyme, Developmental protein, Isomerase
Biological processCell cycle, Cell division, Differentiation, Neurogenesis
LigandATP-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

Protein family/group databases

Transport Classification Database

More...TCDBi		1.R.1.1.1 the membrane contact site (mcs) family

<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 PublicationUniRule annotation (EC:5.6.1.1UniRule annotation6 Publications)
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 annotationImported
Synonyms:ADPSP, FSP2, KIAA10831 Publication, SPG4UniRule annotation
<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>OrganismiHomo 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 identifieri9606 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2

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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 domaini1 – 56CytoplasmicUniRule annotation1 PublicationAdd BLAST56
<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>Intramembranei57 – 77HelicalUniRule annotation1 PublicationAdd BLAST21
Topological domaini78 – 616CytoplasmicUniRule annotation1 PublicationAdd BLAST539

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 Publications
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 keyPosition(s)DescriptionActionsGraphical viewLength
<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_07582744 – 616Missing in SPG4. 1 PublicationAdd BLAST573
Natural variantiVAR_07582895A → T in SPG4. 1 PublicationCorresponds to variant dbSNP:rs1343258361Ensembl.1
Natural variantiVAR_06762897P → T in SPG4; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs372005558EnsemblClinVar.1
Natural variantiVAR_075829112 – 616Missing in SPG4. 1 PublicationAdd BLAST505
Natural variantiVAR_075830135 – 616Missing in SPG4. 1 PublicationAdd BLAST482
Natural variantiVAR_067563162V → I in SPG4; unknown pathological significance. 2 PublicationsCorresponds to variant dbSNP:rs141944844EnsemblClinVar.1
Natural variantiVAR_026758195L → V in SPG4. 1 Publication1
Natural variantiVAR_067629201V → D in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_075831244 – 616Missing in SPG4. 1 PublicationAdd BLAST373
Natural variantiVAR_075832245 – 616Missing in SPG4. 1 PublicationAdd BLAST372
Natural variantiVAR_075833254 – 616Missing in SPG4. 1 PublicationAdd BLAST363
Natural variantiVAR_067631287Missing in SPG4. 1 Publication1
Natural variantiVAR_067632293P → L in SPG4. 1 PublicationCorresponds to variant dbSNP:rs773193617Ensembl.1
Natural variantiVAR_075834309R → H in SPG4. 1 PublicationCorresponds to variant dbSNP:rs202152835Ensembl.1
Natural variantiVAR_067633314L → S in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_079314328I → K in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_067634328I → L in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_019448344I → K in SPG4; abrogates ATPase activity and promotes microtubule binding. 2 PublicationsCorresponds to variant dbSNP:rs121908513EnsemblClinVar.1
Natural variantiVAR_027206347Q → K in SPG4; promotes microtubule binding. 2 Publications1
Natural variantiVAR_067564356E → K in SPG4; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1057519181Ensembl.1
Natural variantiVAR_067635360L → V in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_027207361P → L in SPG4. 1 Publication1
Natural variantiVAR_010195362S → C in SPG4. 2 PublicationsCorresponds to variant dbSNP:rs121908509EnsemblClinVar.1
Natural variantiVAR_075835363L → P in SPG4. 1 Publication1
Natural variantiVAR_075836364R → M in SPG4. 1 Publication1
Natural variantiVAR_067636364R → T in SPG4. 1 Publication1
Natural variantiVAR_067565365P → S in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_079315366E → K in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_075837368F → L in SPG4. 2 Publications1
Natural variantiVAR_079316368F → V in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_027208370G → R in SPG4; promotes microtubule binding and the formation of thick microtubule bundles. 2 Publications1
Natural variantiVAR_075838372R → G in SPG4. 1 Publication1
Natural variantiVAR_079317372R → T in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_075839377G → E in SPG4. 1 Publication1
Natural variantiVAR_019439378L → Q in SPG4. 1 Publication1
Natural variantiVAR_067637378L → R in SPG4. 1 Publication1
Natural variantiVAR_067638380L → H in SPG4. 2 Publications1
Natural variantiVAR_027209381F → C in SPG4; promotes microtubule binding and the formation of thick microtubule bundles. 2 Publications1
Natural variantiVAR_067566382G → R in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_027210386N → K in SPG4; abrogates ATPase activity, promotes microtubule binding and the formation of thick microtubule bundles. 3 Publications1
Natural variantiVAR_019440386N → S in SPG4. 1 PublicationCorresponds to variant dbSNP:rs121908514EnsemblClinVar.1
Natural variantiVAR_079318386N → Y in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_027211388K → 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 Publications1
Natural variantiVAR_079319390M → T in SPG4; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1131691977Ensembl.1
Natural variantiVAR_019441390M → V in SPG4. 1 PublicationCorresponds to variant dbSNP:rs797044850EnsemblClinVar.1
Natural variantiVAR_067639391L → P in SPG4. 1 Publication1
Natural variantiVAR_067640393 – 396Missing in SPG4. 1 Publication4
Natural variantiVAR_027212399S → L in SPG4. 4 Publications1
Natural variantiVAR_019449404Missing in SPG4. 1 Publication1
Natural variantiVAR_075840406I → R in SPG4. 1 Publication1
Natural variantiVAR_026759406I → V in SPG4. 1 PublicationCorresponds to variant dbSNP:rs587777757EnsemblClinVar.1
Natural variantiVAR_067567407S → I in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_019450407S → R in SPG4. 1 Publication1
Natural variantiVAR_067641409A → T in SPG4. 2 PublicationsCorresponds to variant dbSNP:rs1064793273Ensembl.1
Natural variantiVAR_067642410S → R in SPG4. 1 Publication1
Natural variantiVAR_067568413S → L in SPG4. 1 Publication1
Natural variantiVAR_079320418E → A in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_067569422L → F in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_010196424R → G in SPG4. 1 Publication1
Natural variantiVAR_067643426L → F in SPG4. 1 Publication1
Natural variantiVAR_027213426L → V in SPG4; promotes microtubule binding and the formation of thick microtubule bundles. 4 PublicationsCorresponds to variant dbSNP:rs1060502227Ensembl.1
Natural variantiVAR_075841431 – 616Missing in SPG4. 1 PublicationAdd BLAST186
Natural variantiVAR_027214435P → L in SPG4. 1 Publication1
Natural variantiVAR_027215436S → F in SPG4. 1 Publication1
Natural variantiVAR_067644436S → P in SPG4. 1 Publication1
Natural variantiVAR_027216441D → G in SPG4. 1 PublicationCorresponds to variant dbSNP:rs121908512EnsemblClinVar.1
Natural variantiVAR_067645441D → N in SPG4. 1 Publication1
Natural variantiVAR_075842441D → V in SPG4. 1 Publication1
Natural variantiVAR_067570445S → N in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_010197448C → Y in SPG4; abrogates binding to the tail of beta-3-tubulin, abolishes microtubule severing and promotes the formation of thick microtubule bundles. 4 PublicationsCorresponds to variant dbSNP:rs121908510EnsemblClinVar.1
Natural variantiVAR_075843450R → S in SPG4. 1 Publication1
Natural variantiVAR_075844451Missing in SPG4. 1 Publication1
Natural variantiVAR_067571454E → K in SPG4. 1 Publication1
Natural variantiVAR_075845458S → R in SPG4. 1 Publication1
Natural variantiVAR_027217459R → G in SPG4. 1 Publication1
Natural variantiVAR_027218460R → C in SPG4. 2 PublicationsCorresponds to variant dbSNP:rs878854990EnsemblClinVar.1
Natural variantiVAR_027219460R → L in SPG4; promotes microtubule binding and the formation of thick microtubule bundles. 2 Publications1
Natural variantiVAR_067572460R → S in SPG4. 3 Publications1
Natural variantiVAR_075846461L → P in SPG4. 1 Publication1
Natural variantiVAR_067646463T → A in SPG4. 1 Publication1
Natural variantiVAR_067647464E → A in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_027220470D → V in SPG4. 1 PublicationCorresponds to variant dbSNP:rs121908516EnsemblClinVar.1
Natural variantiVAR_079321470D → Y in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_067573482V → L in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_079322485A → T in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_027221485A → V in SPG4. 1 Publication1
Natural variantiVAR_027222489P → L in SPG4. 1 Publication1
Natural variantiVAR_075847490 – 616Missing in SPG4. 1 PublicationAdd BLAST127
Natural variantiVAR_067648492L → F in SPG4. 1 Publication1
Natural variantiVAR_026760493D → G in SPG4. 1 Publication1
Natural variantiVAR_067649498R → G in SPG4. 2 Publications1
Natural variantiVAR_079323498R → M in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_010198499R → C in SPG4; abrogates ATPase activity, promotes microtubule binding and the formation of thick microtubule bundles. 6 PublicationsCorresponds to variant dbSNP:rs121908511EnsemblClinVar.1
Natural variantiVAR_026761499R → H in SPG4. 2 PublicationsCorresponds to variant dbSNP:rs878854991EnsemblClinVar.1
Natural variantiVAR_019442503R → L in SPG4. 1 Publication1
Natural variantiVAR_067650503R → RR in SPG4. 1 Publication1
Natural variantiVAR_026762503R → W in SPG4. 2 PublicationsCorresponds to variant dbSNP:rs864622162EnsemblClinVar.1
Natural variantiVAR_027223512E → D in SPG4. 1 Publication1
Natural variantiVAR_067574512Missing in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_067651514R → G in SPG4. 1 Publication1
Natural variantiVAR_019443515Missing in SPG4. 1 Publication1
Natural variantiVAR_019444534L → P in SPG4. 1 Publication1
Natural variantiVAR_067575534L → V in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_079324546 – 616Missing in SPG4. 1 PublicationAdd BLAST71
Natural variantiVAR_067652550T → I in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_019451551A → Y in SPG4; requires 2 nucleotide substitutions. 1 Publication1
Natural variantiVAR_075848555D → G in SPG4. 1 Publication1
Natural variantiVAR_027224555D → N in SPG4. 1 Publication1
Natural variantiVAR_027225556A → V in SPG4; promotes microtubule binding and the formation of thick microtubule bundles. 2 Publications1
Natural variantiVAR_027226559G → D in SPG4. 2 PublicationsCorresponds to variant dbSNP:rs864622179EnsemblClinVar.1
Natural variantiVAR_075849559G → R in SPG4. 1 PublicationCorresponds to variant dbSNP:rs878854992EnsemblClinVar.1
Natural variantiVAR_075850562 – 616Missing in SPG4. 1 PublicationAdd BLAST55
Natural variantiVAR_027227562R → G in SPG4. 2 PublicationsCorresponds to variant dbSNP:rs121908518EnsemblClinVar.1
Natural variantiVAR_067576562R → P in SPG4; unknown pathological significance. 1 Publication1
Natural variantiVAR_027228562R → Q in SPG4. 1 PublicationCorresponds to variant dbSNP:rs863224923EnsemblClinVar.1
Natural variantiVAR_067653579N → H in SPG4; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs144594804EnsemblClinVar.1
Natural variantiVAR_067654580I → T in SPG4. 1 Publication1
Natural variantiVAR_075851581 – 616Missing in SPG4. 2 PublicationsAdd BLAST36
Natural variantiVAR_010199584D → H in SPG4. 1 Publication1
Natural variantiVAR_075852595S → R in SPG4. 1 Publication1
Natural variantiVAR_026763607W → C in SPG4. 1 Publication1
Natural variantiVAR_019445614T → I in SPG4; variant form with congenital arachnoid cysts. 1 Publication1
Natural variantiVAR_019452615T → I in SPG4. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Mutagenesisi1M → V: Cytoplasmic and nuclear. 1 Publication1
Mutagenesisi65R → G: Abolishes localization to lipid droplets. 1 Publication1
Mutagenesisi81 – 84RFSR → GFSG: Does not affect localization to lipid droplets. 1 Publication4
Mutagenesisi87M → V: Exclusively cytoplasmic. 1 Publication1
Mutagenesisi120H → D: Impairs binding to CHMP1B. Impairs midbody localization; when associated with D-124. 1 Publication1
Mutagenesisi124F → A: Impairs binding to CHMP1B. 1 Publication1
Mutagenesisi124F → D: Impairs binding to CHMP1B. Impairs midbody localization; when associated with D-120. 1 Publication1
Mutagenesisi310 – 312KKK → QQQ: Loss of microtubule-binding. 1 Publication3
Mutagenesisi388K → A: Abrogates ATPase activity and abolishes microtubule severing. 1 Publication1
Mutagenesisi415Y → A: Abrogates binding to the tail of alpha-tubulin and beta-3-tubulin, impairs ATPase activity and abolishes microtubule severing. 1 Publication1
Mutagenesisi442E → Q: Abrogates ATP hydrolysis, abolishes microtubule severing, stabilizes the homohexameric form, and promotes microtubule binding and redistribution from the endosome to microtubules. 8 Publications1
Mutagenesisi448C → A or G: Abolishes ATPase activity. 1 Publication1
Mutagenesisi448C → S: Does not affect ATPase activity. 1 Publication1
Mutagenesisi451R → G: Abrogates binding to the tail of alpha-tubulin and beta-3-tubulin, impairs ATPase activity and abolishes microtubule severing. 1 Publication1
Mutagenesisi457A → E: Abrogates binding to the tail of alpha-tubulin and beta-3-tubulin and abolishes microtubule severing. 1 Publication1

Keywords - Diseasei

Disease mutation, Hereditary spastic paraplegia, Neurodegeneration

Organism-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
MIMi182601 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 keyPosition(s)DescriptionActionsGraphical viewLength
<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_00000847631 – 616SpastinAdd BLAST616

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei245PhosphoserineCombined sources1
Modified residuei268PhosphoserineCombined sources1
Modified residuei306PhosphothreonineCombined sources1
Modified residuei597PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic 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

<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

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 annotation16 Publications

<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

WithEntry#Exp.IntActNotes
ATL1Q8WXF7-14EBI-1222832,EBI-15590227

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

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

1616
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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 keyPosition(s)DescriptionActionsGraphical viewLength
<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>Domaini120 – 195MITSequence analysisAdd BLAST76

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Regioni1 – 300Required for interaction with RTN11 PublicationAdd BLAST300
Regioni1 – 194Required for midbody localization1 PublicationAdd BLAST194
Regioni1 – 80Required for interaction with ATL12 PublicationsAdd BLAST80
Regioni1 – 50Required for nuclear localization1 PublicationAdd BLAST50
Regioni50 – 87Required for interaction with SSNA1 and microtubules1 PublicationAdd BLAST38
Regioni112 – 196Sufficient for interaction with CHMP1B1 PublicationAdd BLAST85
Regioni114 – 200Required for interaction with microtubules1 PublicationAdd BLAST87
Regioni228 – 616Sufficient for microtubule severing1 PublicationAdd BLAST389
Regioni270 – 328Required for interaction with microtubules and microtubule severing1 PublicationAdd BLAST59
Regioni310 – 312Required for interaction with microtubules1 Publication3

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Motifi4 – 11Nuclear localization signalUniRule annotation1 Publication8
Motifi59 – 67Nuclear export signalUniRule annotation1 Publication9
Motifi309 – 312Nuclear localization signalUniRule annotation1 Publication4

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0740 Eukaryota
COG0464 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000156258

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. Align