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UniProtKB - Q8I0P1 (SPAST_DROME)

Entry version 146 (26 Feb 2020)
Sequence version 2 (24 Mar 2009)
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Protein

Spastin

Gene

spas

Organism
Drosophila melanogaster (Fruit fly)
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. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle (PubMed:15242610, PubMed:15562320, PubMed:15823537, PubMed:16276413, PubMed:17452528, PubMed:25875445, PubMed:18202664, PubMed:19341724). Regulates microtubule stability in the neuromuscular junction synapse (PubMed:15242610, PubMed:15562320, PubMed:19341724). Involved in lipid metabolism by regulating the size and distribution of lipid droplets (PubMed:25875445). Involved in axon regeneration by regulating microtubule severing (PubMed:23122959).UniRule annotation9 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

  • n ATP + n H(2)O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.UniRule annotation2 Publications EC:5.6.1.1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi523 – 530ATPUniRule annotation8

<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: FlyBase
  • ATP binding Source: UniProtKB-UniRule
  • isomerase activity Source: UniProtKB-KW
  • microtubule binding Source: UniProtKB
  • microtubule-severing ATPase activity Source: UniProtKB
Complete GO annotation on QuickGO ...

GO - Biological processi

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 functionDevelopmental protein, Isomerase
Biological processCell cycle, Cell division, Differentiation, Mitosis, Neurogenesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.6.4.3 1994

<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%5Fand%5Ftaxonomy%5Fsection">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:
SpastinUniRule annotation (EC:5.6.1.1UniRule annotation2 Publications)
Alternative name(s):
D-Spastin
Dm-Spastin
Dspastin1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:spasUniRule annotation
ORF Names:CG5977
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiDrosophila melanogaster (Fruit fly)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri7227 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Holometabola › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000000803 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 3R

Organism-specific databases

Drosophila genome database

More...FlyBasei		FBgn0039141 spas

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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 – 121CytoplasmicUniRule annotationAdd BLAST121
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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>Intramembranei122 – 142HelicalUniRule annotationAdd BLAST21
Topological domaini143 – 758CytoplasmicUniRule annotationAdd BLAST616

Keywords - Cellular componenti

Chromosome, Cytoplasm, Cytoskeleton, Lipid droplet, Membrane, Microtubule

<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 describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Loss of protein expression throughout the embryo leads to pupal lethality. Loss of protein expression specifically in the nervous system causes synaptic undergrowth and a reduction in total synaptic area. Neuromuscular junction boutons are smaller and more numerous. Microtubule stability appears to be enhanced within neuronal axons and at neuromuscular junctions and synaptic currents are increased. Older flies exhibit numerous vacuoles in the neuropil and cortex. Adult coordination and locomotory behavior are compromised and lifespan is reduced.3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi465L → A: Strongly impairs microtubule severing and weakly impairs ATPase activity; when associated with A-471 and A-472. 1 Publication1
Mutagenesisi465L → F: Strongly impairs microtubule severing and weakly impairs ATPase activity. 1 Publication1
Mutagenesisi469I → A: Strongly impairs microtubule severing and ATPase activity but does not affect interaction with microtubules; when associated with A-473 and A-474. 1 Publication1
Mutagenesisi471D → A: Strongly impairs microtubule severing and weakly impairs ATPase activity; when associated with A-465 and A-472. 1 Publication1
Mutagenesisi472E → A: Strongly impairs microtubule severing and weakly impairs ATPase activity; when associated with A-465 and A-471. 1 Publication1
Mutagenesisi473I → A: Strongly impairs microtubule severing and ATPase activity but does not affect interaction with microtubules; when associated with A-469 and A-474. 1 Publication1
Mutagenesisi474V → A: Strongly impairs microtubule severing and ATPase activity but does not affect interaction with microtubules; when associated with A-469 and A-473. 1 Publication1
Mutagenesisi503S → C: Impairs microtubule severing and ATPase activity. 1 Publication1
Mutagenesisi511G → R: Abrogates microtubule severing and strongly impairs ATPase activity. 1 Publication1
Mutagenesisi529K → R: Abrogates microtubule severing and ATPase activity. Induces accumulation of hyperstable microtubules at the neuromuscular junction presynpatic terminal and reduces synaptic area. Reduces adult lifespan and impairs climbing activity. 3 Publications1
Mutagenesisi555K → A: Abrogates microtubule severing. 1 Publication1
Mutagenesisi556Y → A: Abrogates microtubule severing. 1 Publication1
Mutagenesisi557V → A: Abrogates microtubule severing and impairs ATPase activity. 1 Publication1
Mutagenesisi558G → A or V: Abrogates microtubule severing. 1 Publication1
Mutagenesisi559D → A or R: Abrogates microtubule severing. 1 Publication1
Mutagenesisi560G → A: Impairs microtubule severing. 1 Publication1
Mutagenesisi560G → V: Abrogates microtubule severing. 1 Publication1
Mutagenesisi561E → A or R: Abrogates microtubule severing. 1 Publication1
Mutagenesisi562K → A or R: Abrogates microtubule severing. 1
Mutagenesisi583E → A: Abrogates microtubule severing and ATPase activity. 2 Publications1
Mutagenesisi583E → Q: Impairs interaction with microtubules and promotes hexamerization. 2 Publications1
Mutagenesisi589S → Y: Impairs microtubule severing. 1 Publication1
Mutagenesisi591R → A or E: Abrogates microtubule severing. 1 Publication1
Mutagenesisi595E → A: Impairs microtubule severing. 1 Publication1
Mutagenesisi595E → R: Abrogates microtubule severing. 1 Publication1
Mutagenesisi596H → A: Impairs microtubule severing. 1 Publication1
Mutagenesisi596H → D: Abrogates microtubule severing and impairs ATPase activity. 1 Publication1
Mutagenesisi596H → Y: Abrogates microtubule severing. 1 Publication1
Mutagenesisi597E → K: Impairs microtubule severing. 1 Publication1
Mutagenesisi598A → L: Abrogates microtubule severing. 1 Publication1
Mutagenesisi601R → E: Abrogates microtubule severing. 1 Publication1
Mutagenesisi601R → L: Abrogates microtubule severing and strongly impairs ATPase activity. 1 Publication1
Mutagenesisi631P → L: Abrogates microtubule severing. 1 Publication1
Mutagenesisi632Q → A: Strongly impairs microtubule severing and weakly impairs ATPase activity. 1 Publication1
Mutagenesisi633E → A: Weakly impairs microtubule severing and ATPase activity. 1 Publication1
Mutagenesisi633E → R: Impairs microtubule severing. 1 Publication1
Mutagenesisi697D → N: Weakly impairs microtubule severing and strongly impairs ATPase activity. 1 Publication1
Mutagenesisi704R → Q: Abrogates microtubule severing. 1 Publication1
Mutagenesisi753Y → A: Strongly impairs microtubule severing and ATPase activity. 1 Publication1

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003671441 – 758SpastinAdd BLAST758

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 residuei439Phosphothreonine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q8I0P1

PRoteomics IDEntifications database

More...PRIDEi		Q8I0P1

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q8I0P1

<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 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

Maternally expressed in early embryogenesis with high expression until blastoderm. At the cell formation stage, strongly expressed near the basal part of the cell layer underlying the surface. During germband extension and stomodeal plate formation, expressed in the ventral head and trunk ectoderm, as well as in cells near the cephalic furrow and in the invaginating hindgut and midgut primordia. After germband retraction and delamination of neuroblasts at stage 13, expressed in subsets of cells in all neuromeres of the CNS including those of the supraesophageal and subesophageal ganglia. In later embryonic stages expressed in cell clusters throughout the supraesophageal ganglion, with pronounced expression also seen in the subesophageal ganglion. In the ventral nerve cord (VNC), expressed in two broad longitudinal stripes located laterally, and weakly expressed in some midline cells. Also expressed in some sensory head organs of the peripheral nervous system (PNS), most probably the Bolwigs organs and/or the dorsal organs. Expressed in the developing larval neuromusculature, muscles and neuronal axons. Enriched in neuromuscular junctions throughout the muscles of the body wall. Enriched in punctate domains of synaptic boutons and excluded from interbouton axonal connections. Colocalizes with the synaptic vesicle pools.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		FBgn0039141 Expressed in female gonad and 45 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q8I0P1 differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q8I0P1 DM

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homohexamer. The homohexamer is stabilized by ATP-binding. The homohexamer may adopt a ring conformation through which microtubules pass prior to being severed (PubMed:18202664).

Interacts with microtubules (PubMed:15823537, PubMed:18202664).

Interacts with atl; may be involved in microtubule dynamics (PubMed:19341724).

UniRule annotation3 Publications

GO - Molecular functioni

  • alpha-tubulin binding Source: UniProtKB
  • microtubule binding Source: UniProtKB
Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		67781, 5 interactors

Database of interacting proteins

More...DIPi		DIP-59834N

Protein interaction database and analysis system

More...IntActi		Q8I0P1, 2 interactors

STRING: functional protein association networks

More...STRINGi		7227.FBpp0083918

<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

1758
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q8I0P1

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q8I0P1

<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%5Fand%5Fdomains%5Fsection">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>Domaini233 – 308MITSequence 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 – 210Required for localization to punctate cytoplasmic fociAdd BLAST210
Regioni1 – 159Interaction with atl1 PublicationAdd BLAST159
Regioni208 – 758Sufficient for interaction with microtubules and microtubule severing2 PublicationsAdd BLAST551
Regioni443 – 455Required for interaction with microtubules1 PublicationAdd BLAST13

<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

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q8I0P1

KEGG Orthology (KO)

More...KOi		K13254

Identification of Orthologs from Complete Genome Data

More...OMAi		YHKQAFE

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q8I0P1

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
IPR041569 AAA_lid_3
IPR003959 ATPase_AAA_core
IPR003960 ATPase_AAA_CS
IPR007330 MIT
IPR027417 P-loop_NTPase
IPR017179 Spastin

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00004 AAA, 1 hit
PF17862 AAA_lid_3, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

Q8I0P1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVRTKNQSSS SSASSSSTKS PIKSSSGAGS SGGGLGGRQS THRSSSASNV 
        60         70         80         90        100
AAVVAGGSSA AGGGSSSNRR SPGSSPDGDD DTTTTDDLTP TTCSPRSGHH 
       110        120        130        140        150
HSYGGYSSSV HKQNLYVVSF PIIFLFNVLR SLIYQLFCIF RYLYGASTKV 
       160        170        180        190        200
IYRPHRRDCN IEIVVQNSSK EQQQSLNHPS ELNREGDGQE QQLSNQPQRF 
       210        220        230        240        250
RPIQPLEMAA NRPGGGYSPG PGDPLLAKQK HHHRRAFEYI SKALKIDEEN 
       260        270        280        290        300
EGHKELAIEL YRKGIKELED GIAVDCWSGR GDVWDRAQRL HDKMQTNLSM 
       310        320        330        340        350
ARDRLHFLAL REQDLQMQRL SLKEKQKEEA QSKPQKTREP MLAGMTNEPM 
       360        370        380        390        400
KLRVRSSGYG PKATTSAQPT ASGRKLTIGS KRPVNLAVAN KSQTLPRNLG 
       410        420        430        440        450
SKTSVGAVQR QPAKTAATPP AVRRQFSSGR NTPPQRSRTP INNNGPSGSG 
       460        470        480        490        500
ASTPVVSVKG VEQKLVQLIL DEIVEGGAKV EWTDIAGQDV AKQALQEMVI 
       510        520        530        540        550
LPSVRPELFT GLRAPAKGLL LFGPPGNGKT LLARAVATEC SATFLNISAA 
       560        570        580        590        600
SLTSKYVGDG EKLVRALFAV ARHMQPSIIF IDEVDSLLSE RSSSEHEASR 
       610        620        630        640        650
RLKTEFLVEF DGLPGNPDGD RIVVLAATNR PQELDEAALR RFTKRVYVSL 
       660        670        680        690        700
PDEQTRELLL NRLLQKQGSP LDTEALRRLA KITDGYSGSD LTALAKDAAL 
       710        720        730        740        750
EPIRELNVEQ VKCLDISAMR AITEQDFHSS LKRIRRSVAP QSLNSYEKWS 

QDYGDITI
Length:758
Mass (Da):82,749
Last modified:March 24, 2009 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i406D075DCBD2A9CD
GO

<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 potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0B4LHJ5A0A0B4LHJ5_DROME
Spastin
spas D-spastin, Dmel\CG5977, Dspastin, Spas, Spastin
696Annotation 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>
A0A126GV10A0A126GV10_DROME
Spastin
spas D-spastin, Dmel\CG5977, Dspastin, Spas, Spastin
551Annotation 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>
A0A126GV13A0A126GV13_DROME
Spastin
spas D-spastin, Dmel\CG5977, Dspastin, Spas, Spastin
489Annotation 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>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAL39667 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti665Q → E in AAN71010 (PubMed:12537569).Curated1
Sequence conflicti665Q → E in AAN71106 (PubMed:12537569).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AE014297 Genomic DNA Translation: AAF56223.3
AE014297 Genomic DNA Translation: AAN13975.2
AY069522 mRNA Translation: AAL39667.1 Different initiation.
BT001254 mRNA Translation: AAN71010.1
BT001351 mRNA Translation: AAN71106.1
BT044258 mRNA Translation: ACH92323.1

NCBI Reference Sequences

More...RefSeqi		NP_001303438.1, NM_001316509.1
NP_651206.3, NM_142949.4
NP_732941.2, NM_170115.3

Genome annotation databases

Ensembl metazoan genome annotation project

More...EnsemblMetazoai		FBtr0084533; FBpp0083918; FBgn0039141
FBtr0084534; FBpp0083919; FBgn0039141

Database of genes from NCBI RefSeq genomes

More...GeneIDi		42846

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		dme:Dmel_CG5977

UCSC genome browser

More...UCSCi		CG5977-RA d. melanogaster

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA Translation: AAF56223.3
AE014297 Genomic DNA Translation: AAN13975.2
AY069522 mRNA Translation: AAL39667.1 Different initiation.
BT001254 mRNA Translation: AAN71010.1
BT001351 mRNA Translation: AAN71106.1
BT044258 mRNA Translation: ACH92323.1
RefSeqiNP_001303438.1, NM_001316509.1
NP_651206.3, NM_142949.4
NP_732941.2, NM_170115.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3B9PX-ray2.70A463-758[»]
6NYVX-ray2.42B445-758[»]
6NYWX-ray2.19B445-758[»]
6P10X-ray2.30B445-758[»]
6P11X-ray2.15B445-758[»]
6P12X-ray1.94B445-758[»]
6P13X-ray2.10B445-758[»]
6P14X-ray1.93A445-758[»]
SMRiQ8I0P1
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi67781, 5 interactors
DIPiDIP-59834N
IntActiQ8I0P1, 2 interactors
STRINGi7227.FBpp0083918

PTM databases

iPTMnetiQ8I0P1

Proteomic databases

PaxDbiQ8I0P1
PRIDEiQ8I0P1

Genome annotation databases

EnsemblMetazoaiFBtr0084533; FBpp0083918; FBgn0039141
FBtr0084534; FBpp0083919; FBgn0039141
GeneIDi42846
KEGGidme:Dmel_CG5977
UCSCiCG5977-RA d. melanogaster

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		42846
FlyBaseiFBgn0039141 spas

Phylogenomic databases

eggNOGiKOG0740 Eukaryota
COG0464 LUCA
GeneTreeiENSGT00940000156258
InParanoidiQ8I0P1
KOiK13254
OMAiYHKQAFE
PhylomeDBiQ8I0P1

Enzyme and pathway databases

BRENDAi3.6.4.3 1994

Miscellaneous databases

EvolutionaryTraceiQ8I0P1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		42846

Protein Ontology

More...PROi		PR:Q8I0P1

Gene expression databases

BgeeiFBgn0039141 Expressed in female gonad and 45 other tissues
ExpressionAtlasiQ8I0P1 differential
GenevisibleiQ8I0P1 DM

Family and domain databases

HAMAPiMF_03021 Spastin, 1 hit
InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR041569 AAA_lid_3
IPR003959 ATPase_AAA_core
IPR003960 ATPase_AAA_CS
IPR007330 MIT
IPR027417 P-loop_NTPase
IPR017179 Spastin
PfamiView protein in Pfam
PF00004 AAA, 1 hit
PF17862 AAA_lid_3, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 1 hit
SM00745 MIT, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS00674 AAA, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSPAST_DROME
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q8I0P1
Secondary accession number(s): Q8IMX5, Q8T066
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 24, 2009
Last modified: February 26, 2020
This is version 146 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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