Version 5.4
Bos taurus Protein: SPAST
Summary
InnateDB Protein IDBP-683546.2
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol SPAST
Protein Name Spastin
Synonyms SPG4;
Species Bos taurus
Ensembl Protein ENSBTAP00000044166
InnateDB Gene IDBG-631955 (SPAST)
Protein Structure
UniProt Annotation
Function ATP-dependent microtubule severing protein. Microtubule severing may promote reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and for completion of the abscission stage of cytokinesis. Also plays a role in axon growth and the formation of axonal branches. {ECO:0000255HAMAP-Rule:MF_03021}.
Subcellular Localization Membrane {ECO:0000255HAMAP-Rule:MF_03021}; Single-pass membrane protein {ECO:0000255HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255HAMAP-Rule:MF_03021}. Cytoplasm, perinuclear region {ECO:0000255HAMAP-Rule:MF_03021}. Endoplasmic reticulum {ECO:0000255HAMAP-Rule:MF_03021}. Endosome {ECO:0000255HAMAP- Rule:MF_03021}. Nucleus {ECO:0000255HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, spindle {ECO:0000255HAMAP- Rule:MF_03021}. Note=Localization to the centrosome is independent of microtubules. Localizes to the midbody of dividing cells, and this requires CHMP1B. Enriched in the distal axons and branches of postmitotic neurons. {ECO:0000255HAMAP-Rule:MF_03021}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
They are also associated with 5 interaction(s) predicted by orthology.
Predicted by orthology
Total 5 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0000166 nucleotide binding
GO:0003824 catalytic activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0008017 microtubule binding
GO:0008568 microtubule-severing ATPase activity
GO:0009378 four-way junction helicase activity
GO:0016787 hydrolase activity
GO:0017111 nucleoside-triphosphatase activity
GO:0043014 alpha-tubulin binding
GO:0048487 beta-tubulin binding
Biological Process
GO:0001578 microtubule bundle formation
GO:0006200 ATP catabolic process
GO:0006281 DNA repair
GO:0006310 DNA recombination
GO:0006888 ER to Golgi vesicle-mediated transport
GO:0007049 cell cycle
GO:0007109 cytokinesis, completion of separation
GO:0007275 multicellular organismal development
GO:0007399 nervous system development
GO:0007409 axonogenesis
GO:0008152 metabolic process
GO:0030154 cell differentiation
GO:0031117 positive regulation of microtubule depolymerization
GO:0034214 protein hexamerization
GO:0051013 microtubule severing
GO:0051260 protein homooligomerization
GO:0051301 cell division
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005768 endosome
GO:0005783 endoplasmic reticulum
GO:0005813 centrosome
GO:0005815 microtubule organizing center
GO:0005819 spindle
GO:0005856 cytoskeleton
GO:0005874 microtubule
GO:0015630 microtubule cytoskeleton
GO:0016020 membrane
GO:0016021 integral component of membrane
GO:0030496 midbody
GO:0031410 cytoplasmic vesicle
GO:0048471 perinuclear region of cytoplasm
GO:0070062 extracellular vesicular exosome
Protein Structure and Domains
PDB ID
InterPro IPR003593 AAA+ ATPase domain
IPR003959 ATPase, AAA-type, core
IPR007330 MIT
IPR008824 DNA helicase, Holliday junction RuvB type, N-terminal
IPR017179 Spastin
IPR027417 P-loop containing nucleoside triphosphate hydrolase
PFAM PF00004
PF07724
PF13304
PF04212
PF05496
PRINTS
PIRSF PIRSF037338
SMART SM00382
SM00745
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt A2VDN5
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 521442
UniGene Bt.46123
RefSeq NP_001075060
HUGO
OMIM
CCDS
HPRD
IMGT
EMBL BC133327
GenPept AAI33328

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

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Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca