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Information on EC 5.6.1.1 - microtubule-severing ATPase and Organism(s) Homo sapiens and UniProt Accession Q9BW62

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IUBMB Comments
A member of the AAA-ATPase family, active in splitting microtubules into tubulin dimers in the centrosome.
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This record set is specific for:
Homo sapiens
UNIPROT: Q9BW62
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
n
+
n
+
a microtubule
=
n
+
n
+
(n+1)
alpha/beta tubulin heterodimers
Synonyms
spastin, katanin, scinderin, kinesin spindle protein, mei-1, adseverin, katanin p60, microtubule-severing protein, microtubule-stimulated atpase, p60-katanin, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
katanin
kinesin spindle protein
-
-
microtuble severing AAA ATPase spastin
-
-
microtuble-severing AAA ATPase
-
-
microtuble-severing ATPase spastin
-
microtubule-severing AAA ATPase
-
-
microtubule-severing ATPase
microtubule-severing protein
-
MT-severing AAA ATPase
-
-
spastin
spastin AAA domain
-
-
vertebrate katanin
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (tubulin-dimerizing)
A member of the AAA-ATPase family, active in splitting microtubules into tubulin dimers in the centrosome.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O + microtubule
ADP + phosphate + alpha/beta tubulin heterodimers
show the reaction diagram
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
ATP + H2O + microtubule
ADP + phosphate + alpha/beta tubulin heterodimers
show the reaction diagram
GTP + H2O
GDP + phosphate
show the reaction diagram
additional information
?
-
-
enzyme activity regulates the number of microtubule end in mitotic spindle, enzyme inhibition slows the rate of spindle microtubule disassembly
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
ATP + H2O + microtubule
ADP + phosphate + alpha/beta tubulin heterodimers
show the reaction diagram
the enzyme plays important roles in various cellular events including axon regeneration, cytokinesis, and nuclear envelope sealing after mitosis
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
additional information
?
-
-
enzyme activity regulates the number of microtubule end in mitotic spindle, enzyme inhibition slows the rate of spindle microtubule disassembly
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-[3'-fluoro-4'-(trifluoromethyl)biphenyl-4-yl]methanamine
-
-
2-(4-tert-butylphenyl)pyridine
-
-
3'-fluoro-4'-(trifluoromethyl)biphenyl-4-amine
-
-
3'-fluoro-4'-(trifluoromethyl)biphenyl-4-carbaldehyde
-
-
3'-fluoro-4'-(trifluoromethyl)biphenyl-4-carbonitrile
-
-
3'-fluoro-4'-(trifluoromethyl)biphenyl-4-ol
-
-
3'-fluoro-4'-(trifluoromethyl)biphenyl-4-yl methyl sulfone
-
-
3'-fluoro-4'-(trifluoromethyl)biphenyl-4-yl methyl sulfoxide
-
-
3'-fluoro-N,N-dimethyl-4'-(trifluoromethyl)biphenyl-4-sulfonamide
-
-
3'-fluoro-N-methyl-4'-(trifluoromethyl)biphenyl-4-sulfonamide
-
-
3-(4-tert-butylphenyl)pyridine
-
-
3-fluoro-4'-(methoxymethyl)-4-(trifluoromethyl)biphenyl
-
-
3-[[3-(methylsulfanyl)phenyl]amino]-4-[4-(trifluoromethyl)phenyl]-1H-pyrrole-2,5-dione
-
inhibits microtubule-stimulated ATP hydrolysis by KSP
4'-(ethylsulfonyl)-3-fluoro-4-(trifluoromethyl)biphenyl
-
-
4'-(trifluoromethyl)biphenyl-4-carbonitrile
-
-
4'-tert-butylbiphenyl-4-carbonitrile
-
-
4-(2-tert-butylphenyl)pyridine
-
-
4-(3-tert-butylphenyl)pyridine
-
-
4-(4-tert-butylphenyl)pyridine
-
-
5'-adenylyl-beta,gamma-imidodiphosphate
-
purley competitive inhibitor
ATPgammaS
-
mixed inhibition of ATP turnover
ispinesib
-
SB-715992
methyl 3'-fluoro-4'-(trifluoromethyl)biphenyl-4-carboxylate
-
-
N-[3'-fluoro-4'-(trifluoromethyl)biphenyl-4-yl]methanesulfonamide
-
-
N-[3'-fluoro-4'-(trifluoromethyl)biphenyl-4-yl]sulfamide
-
-
N-[5-[3-fluoro-4-(trifluoromethyl)phenyl]pyridin-2-yl]sulfamide
-
-
N-[[3'-fluoro-4'-(trifluoromethyl)biphenyl-4-yl]methyl]sulfamide
-
-
PVZB1084
-
-
PVZB1194
-
inhibition only in presence of microtubules
spastin
the basal ATPase activity of spastin is negatively regulated by spastin concentration
-
tubulin
tubulin can inhibit severing activity by interfering with katanin binding to microtubules. The inhibition is mediated by the sequence of the tubulin and specifically depends on the carboxy-terminal tails. beta-Tubulin tails are the most effective at inhibiting severing, and detyrosinated alpha-tubulin tails are the least effective
-
[3'-fluoro-4'-(trifluoromethyl)biphenyl-4-yl]methanol
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-[[3-(methylsulfanyl)phenyl]amino]-4-[4-(trifluoromethyl)phenyl]-1H-pyrrole-2,5-dione
-
accelerates KSP-catalyzed ATP hydrolysis in the absence of microtubules circa 10fold
microtubule
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.014 - 2.2
ATP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2 - 13
ATP
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0012 - 0.006
3-[[3-(methylsulfanyl)phenyl]amino]-4-[4-(trifluoromethyl)phenyl]-1H-pyrrole-2,5-dione
0.11
ATPgammaS
-
pH 6.8, temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00247
3'-fluoro-4'-(trifluoromethyl)biphenyl-4-amine
Homo sapiens
-
-
0.00147
3'-fluoro-4'-(trifluoromethyl)biphenyl-4-carbaldehyde
Homo sapiens
-
-
0.0014
3'-fluoro-4'-(trifluoromethyl)biphenyl-4-carbonitrile
Homo sapiens
-
-
0.00214
3'-fluoro-4'-(trifluoromethyl)biphenyl-4-ol
Homo sapiens
-
-
0.00086
3'-fluoro-4'-(trifluoromethyl)biphenyl-4-yl methyl sulfone
Homo sapiens
-
-
0.0037
3'-fluoro-4'-(trifluoromethyl)biphenyl-4-yl methyl sulfoxide
Homo sapiens
-
-
0.00461
3'-fluoro-N-methyl-4'-(trifluoromethyl)biphenyl-4-sulfonamide
Homo sapiens
-
-
0.0068
3-(4-tert-butylphenyl)pyridine
Homo sapiens
-
-
0.00714
3-fluoro-4'-(methoxymethyl)-4-(trifluoromethyl)biphenyl
Homo sapiens
-
-
0.00549
4'-(trifluoromethyl)biphenyl-4-carbonitrile
Homo sapiens
-
-
0.00147
4'-tert-butylbiphenyl-4-carbonitrile
Homo sapiens
-
-
0.00042
4-(3-tert-butylphenyl)pyridine
Homo sapiens
-
-
0.001
4-(4-tert-butylphenyl)pyridine
Homo sapiens
-
-
0.00278
N-[3'-fluoro-4'-(trifluoromethyl)biphenyl-4-yl]methanesulfonamide
Homo sapiens
-
-
0.00002
N-[3'-fluoro-4'-(trifluoromethyl)biphenyl-4-yl]sulfamide
Homo sapiens
-
-
0.00004
N-[5-[3-fluoro-4-(trifluoromethyl)phenyl]pyridin-2-yl]sulfamide
Homo sapiens
-
-
0.00306
N-[[3'-fluoro-4'-(trifluoromethyl)biphenyl-4-yl]methyl]sulfamide
Homo sapiens
-
-
0.0007
PVZB1084
Homo sapiens
-
-
0.00012
PVZB1194
Homo sapiens
-
-
0.00363
[3'-fluoro-4'-(trifluoromethyl)biphenyl-4-yl]methanol
Homo sapiens
-
-
additional information
1-[3'-fluoro-4'-(trifluoromethyl)biphenyl-4-yl]methanamine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000045
His6-spastin
0.000046
GST-spastin
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
ATPase activity assay
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
microtubule severing assay
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
full-length isoform
Manually annotated by BRENDA team
-
synaptic terminal of neutrons
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
Katanin A subunit catalyzes the microtubule-severing activity during mitosis. It likely coordinates with KATNB1 to perform this function. KATNBL1 is a regulator of mammalian Katanin microtubule-severing
malfunction
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KATL1_HUMAN
490
0
55392
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
350000
-
hexamer, GST-free spastin, determined by gel filtration analysis and Western blotting
44000
-
full-length spastin without tag, determined by SDS-PAGE
530000
-
hexamer, GST-spastin, determined by gel filtration analysis and Western blotting
54400
58000
60000
62200
spastin isoform: 1st ATG, predicted molecular weight of the isoform tagged with His6
63600
67200
isoform, first ATG, + exon 4
69000
-
GST-spastin, determined by SDS-PAGE
88000
-
monomer, GST-spastin, determined by gel filtration analysis and Western blotting
95000
-
GST-spastin analyzed on a 12%-PAG
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotetramer
heterotetramer of KATNAL1/B1 (an ATPase associated with diverse cellular activities) and the regulatory subunit con80. It does not assemble beyond a dimer of heterodimers (heterotetramer), even at concentrations up to 0.05 mM
hexamer
homohexamer
-
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop method at 20°C, crystal structure of KATNAL1 AAA ATPase in the nucleotide-free state reveals a monomer
crystals of spastin are grown using the vapor diffusion method at 20°C
hanging drop method, the N-terminal residues (about 10000 Da) are clipped off during time of crystal formation (5-7 days)
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E308Q
inactive mutant enzyme
1-279STOP
-
deletion mutant, no severing of microtubules, no binding of microtubules
1-328STOP
-
deletion mutant, no severing of microtubules, but binding of microtubules
406-415del
-
localizes as wild type, but lacks microtubule severing activity
Delta1-132
-
YFP-spastin mutant, amino acids 1-132 deleted
DELTA1-226
-
full severing activity
DELTA1-227
-
deletion mutant, severs microtubules, binds microtubules
Delta116-194
-
YFP-spastin mutant, amino acids 116-194 deleted
Delta195-227
-
YFP-spastin mutant, amino acids 195-227 deleted
DELTAMTBD
-
deletion mutant lacking aa 1-227 and 270-328, neither binds nor severs microtubules
E356A
the basal ATPase activity is severely compromised to undetectable levels
E442Q
fragment 227-279
-
fragment consisting of aa 227-279, no severing of microtubules, no binding of microtubules
fragment 227-328
-
fragment consisting of aa 227-328, no severing of microtubules, but binding of microtubules
G370R
the basal ATPase activity is severely compromised to about 30%
I406V
-
mutant resembles wild type
K388A
-
mutant, no significant enzymatic activity
K388R
N386K
-
disease-associated mutation, no significant enzymatic activity
P45Q
leading to an early onset severe form of hereditary spastic paraplegia when present in heterozygosity with a mutant allele
R499C
R562Q
the basal ATPase activity is severely compromised to undetectable levels
S44L
leading to an early onset severe form of hereditary spastic paraplegia when present in heterozygosity with a mutant allele
spastin-DELTAAAA
-
spastin variant without AAA ATPase domain
spastin-DELTACT
-
C-terminal spastin deletion mutant, aa 398-583 deleted
spastin-DELTAexon4
-
spastin variant without exon4
spastin-DELTANT
-
N-terminal spastin deletion mutant, aa 1-300 deleted
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
GSH-Sepharose affinity chromatography, ion exchange chromatography, cleavage with precission protease, GSH-Sepharose affinity chromatography and gel filtration
-
GSTrap column chromatography, GST tag cleaved with PreScission Protease, GST-Sepharose chromatography, gel filtration
-
Ni-NTA column, glutathione-agarose beads
purification of recombinant protein using a glutathione-sepharose column, removing of the GST moiety with precision protease
-
using a glutathione-agarose column, the glutathione-S-transferase moiety is cleaved with thrombin
-
using a glutathione-Sepharose column, cleavage of the GST moiety with PreScission Protease
-
using Ni-NTA agarose affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21
coding sequence of spastin fused N-terminally to EGFP (pEGFP-N3 vector)
-
expressed in 293T HEK cells
expressed in NIH-3T3 cells
-
GST fusion of amino acid residues 228-616 containing the E442Q mutation (42500 Da for the 389 amino acid residues construct (amino acid residues 228-616)), expressed in Escherichia coli BL21-CodonPlus (DE3)-RIPL
-
His tagged variants and GST fusions expressed in Escherichia coli BL21 (RIL)
-
human cDNA PCR amplified
human katanin cloned and expressed in Escherichia coli
-
human spastin was cloned into the pGBK-T7 plasmid for yeast two-hybrid screening
-
into pQE30 vector, His-tag, and pGEX 4T3, GST-fusion, for expression in Escherichia coli
into the pGEX-6P-3 vector for expression in Escherichia coli BL21-CodonPlus DE3-RIPL cells
-
spastin cDNA is cloned into the pGEMT easy vector, for generating a bait construct for yeast two-hybrid analysis, the excised spastin fragment is cloned into the pGBKT7 vector, for expression analysis in mammalian cells, the fragment is cloned into the pCS2-myc and pEGFP-C1 vectors
-
spastin cDNA was cloned into pGEX6p-3 for production of recombinant protein in Escherichia coli or into pEYFP-C1
-
the human short isoform of spastin initiating from the alternative start codon is amplified by PCR and cloned into the pET41a vector for expression in Escherichia coli BL21DE3 cells
-
the motor domain of wild-type KSP monomer, aa 1-360, is expressed in Escherichia coli BL21DE3 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression and cellular distribution are increased in neoplastic glial phenotypes, especially in glioblastoma
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hartman, J.J.; Mahr, J.; McNally, K.; Okawa, K.; Iwamatsu, A.; Thomas, S.; Cheesman, S.; Heuser, J.; Vale, R.D.; McNally, F.J.
Katanin, a microtubule-severing protein, is a novel AAA ATPase that targets to the centrosome using a WD40-containing subunit
Cell
93
277-287
1998
Saccharomyces cerevisiae, Caenorhabditis elegans, Dictyostelium sp., Drosophila sp. (in: flies), Homo sapiens, Strongylocentrotus purpuratus, Xenopus laevis
Manually annotated by BRENDA team
Lohret, T.A.; McNally, F.J.; Quarmby, L.M.
A role for katanin-mediated axonemal severing during Chlamydomonas deflagellation
Mol. Biol.
9
1195-1207
1998
Chlamydomonas reinhardtii, Homo sapiens, Strongylocentrotus purpuratus, Xenopus laevis
Manually annotated by BRENDA team
McNally, F.J.; Thomas, S.
Katanin is responsible for the M-phase microtubule-severing activity in Xenopus eggs
Mol. Biol.
9
1847-1861
1998
Caenorhabditis elegans, Gallus gallus, Chlamydomonas reinhardtii, Mus musculus, Strongylocentrotus purpuratus, Xenopus laevis, Homo sapiens (O75449), Homo sapiens
Manually annotated by BRENDA team
Lohret, T.A.; Zhao, L.; Quarmby, L.M.
Cloning of Chlamydomonas p60 katanin and localization to the site of outer doublet severing during deflagellation
Cell Motil. Cytoskeleton
43
221-231
1999
Chlamydomonas reinhardtii, Homo sapiens, Strongylocentrotus purpuratus, Xenopus laevis
Manually annotated by BRENDA team
Ahmad, F.J.; Yu, W.; McNally, F.J.; Baas, P.W.
An essential role for katanin in severing microtubules in the neuron
J. Cell Biol.
145
305-315
1999
Homo sapiens, Rattus norvegicus, Strongylocentrotus purpuratus
Manually annotated by BRENDA team
Quarmby, L.
Cellular Samurai: katanin and the severing of microtubules
J. Cell Sci.
113
2821-2827
2000
Arabidopsis sp., Caenorhabditis elegans, Chlamydomonas reinhardtii, Drosophila sp. (in: flies), Homo sapiens, no activity in Saccharomyces cerevisiae, Xenopus laevis
Manually annotated by BRENDA team
Buster, D.; McNally, K.; McNally, F.J.
Katanin inhibition prevents the redistribution of gamma-tubulin at mitosis
J. Cell Sci.
115
1083-1092
2002
Homo sapiens
Manually annotated by BRENDA team
Evans, K.J.; Gomes, E.R.; Reisenweber, S.M.; Gundersen, G.G.; Lauring, B.P.
Linking axonal degeneration to microtubule remodeling by Spastin-mediated microtubule severing
J. Cell Biol.
168
599-606
2005
Homo sapiens
Manually annotated by BRENDA team
Salinas, S.; Carazo-Salas, R.E.; Proukakis, C.; Cooper, J.M.; Weston, A.E.; Schiavo, G.; Warner, T.T.
Human spastin has multiple microtubule-related functions
J. Neurochem.
95
1411-1420
2005
Homo sapiens (Q9UBP0), Homo sapiens
Manually annotated by BRENDA team
Schickel, J.; Beetz, C.; Froemmel, C.; Heide, G.; Sasse, A.; Hemmerich, P.; Deufel, T.
Unexpected pathogenic mechanism of a novel mutation in the coding sequence of SPG4 (spastin)
Neurology
66
421-423
2006
Homo sapiens
Manually annotated by BRENDA team
Evans, K.; Keller, C.; Pavur, K.; Glasgow, K.; Conn, B.; Lauring, B.
Interaction of two hereditary spastic paraplegia gene products, spastin and atlastin, suggests a common pathway for axonal maintenance
Proc. Natl. Acad. Sci. USA
103
10666-10671
2006
Homo sapiens
Manually annotated by BRENDA team
Luo, L.; Carson, J.D.; Molnar, K.S.; Tuske, S.J.; Coales, S.J.; Hamuro, Y.; Sung, C.M.; Sudakin, V.; Auger, K.R.; Dhanak, D.; Jackson, J.R.; Huang, P.S.; Tummino, P.J.; Copeland, R.A.
Conformation-dependent ligand regulation of ATP hydrolysis by human KSP - activation of basal hydrolysis and inhibition of microtubule-stimulated hydrolysis by a single, small molecule modulator
J. Am. Chem. Soc.
130
7584-7591
2008
Homo sapiens
Manually annotated by BRENDA team
White, S.R.; Evans, K.J.; Lary, J.; Cole, J.L.; Lauring, B.
Recognition of C-terminal amino acids in tubulin by pore loops in Spastin is important for microtubule severing
J. Cell Biol.
176
995-1005
2007
Homo sapiens
Manually annotated by BRENDA team
Pantakani, D.V.; Swapna, L.S.; Srinivasan, N.; Mannan, A.U.
Spastin oligomerizes into a hexamer and the mutant spastin (E442Q) redistribute the wild-type spastin into filamentous microtubule
J. Neurochem.
106
613-624
2008
Homo sapiens
Manually annotated by BRENDA team
Salinas, S.; Carazo-Salas, R.E.; Proukakis, C.; Schiavo, G.; Warner, T.T.
Spastin and microtubules - Functions in health and disease
J. Neurosci. Res.
85
2778-2782
2007
Homo sapiens (Q9UBP0)
Manually annotated by BRENDA team
Mannan, A.U.; Boehm, J.; Sauter, S.M.; Rauber, A.; Byrne, P.C.; Neesen, J.; Engel, W.
Spastin, the most commonly mutated protein in hereditary spastic paraplegia interacts with Reticulon 1 an endoplasmic reticulum protein
Neurogenetics
7
93-103
2006
Homo sapiens
Manually annotated by BRENDA team
Matsuno, K.; Sawada, J.; Sugimoto, M.; Ogo, N.; Asai, A.
Bis(hetero)aryl derivatives as unique kinesin spindle protein inhibitors
Bioorg. Med. Chem. Lett.
19
1058-1061
2009
Homo sapiens
Manually annotated by BRENDA team
Mancuso, G.; Rugarli, E.I.
A cryptic promoter in the first exon of the SPG4 gene directs the synthesis of the 60-kDa spastin isoform
BMC Biol.
6
31
2008
Homo sapiens (Q9UBP0)
Manually annotated by BRENDA team
Connell, J.W.; Lindon, C.; Luzio, J.P.; Reid, E.
Spastin couples microtubule severing to membrane traffic in completion of cytokinesis and secretion
Traffic
10
42-56
2009
Homo sapiens (Q9UBP0)
Manually annotated by BRENDA team
Lumb, J.H.; Connell, J.W.; Allison, R.; Reid, E.
The AAA ATPase spastin links microtubule severing to membrane modelling
Biochim. Biophys. Acta
1823
192-197
2012
Homo sapiens
Manually annotated by BRENDA team
Eckert, T.; Link, S.; Le, D.T.; Sobczak, J.P.; Gieseke, A.; Richter, K.; Woehlke, G.
Subunit interactions and cooperativity in the microtubule-severing AAA ATPase spastin
J. Biol. Chem.
287
26278-26290
2012
Homo sapiens
Manually annotated by BRENDA team
Draberova, E.; Vinopal, S.; Morfini, G.; Liu, P.S.; Sladkova, V.; Sulimenko, T.; Burns, M.R.; Solowska, J.; Kulandaivel, K.; de Chadarevian, J.P.; Legido, A.; Moerk, S.J.; Janacek, J.; Baas, P.W.; Draber, P.; Katsetos, C.D.
Microtubule-severing ATPase spastin in glioblastoma: increased expression in human glioblastoma cell lines and inverse roles in cell motility and proliferation
J. Neuropathol. Exp. Neurol.
70
811-826
2011
Homo sapiens (Q9UBP0), Homo sapiens
Manually annotated by BRENDA team
Taylor, J.; White, S.; Lauring, B.; Kull, F.
Crystal structure of the human spastin AAA domain
J. Struct. Biol.
179
133-137
2012
Homo sapiens
Manually annotated by BRENDA team
Bailey, M.E.; Sackett, D.L.; Ross, J.L.
Katanin severing and binding microtubules are inhibited by tubulin carboxy tails
Biophys. J.
109
2546-2561
2015
Homo sapiens (O75449), Homo sapiens, Xenopus laevis (Q9PUL2)
Manually annotated by BRENDA team
Fan, X.; Lin, Z.; Fan, G.; Lu, J.; Hou, Y.; Habai, G.; Sun, L.; Yu, P.; Shen, Y.; Wen, M.; Wang, C.
The AAA protein spastin possesses two levels of basal ATPase activity
FEBS Lett.
592
1625-1633
2018
Homo sapiens (Q9UBP0)
Manually annotated by BRENDA team
Nithianantham, S.; McNally, F.J.; Al-Bassam, J.
Structural basis for disassembly of katanin heterododecamers
J. Biol. Chem.
293
10590-10605
2018
Caenorhabditis elegans (P34808), Homo sapiens (Q9BW62)
Manually annotated by BRENDA team
Cheung, K.; Senese, S.; Kuang, J.; Bui, N.; Ongpipattanakul, C.; Gholkar, A.; Cohn, W.; Capri, J.; Whitelegge, J.P.; Torres, J.Z.
Proteomic analysis of the mammalian Katanin family of microtubule-severing enzymes defines Katanin p80 subunit B-like 1 (KATNBL1) as a regulator of mammalian Katanin microtubule-severing
Mol. Cell. Proteomics
15
1658-1669
2016
Homo sapiens (Q9BW62)
Manually annotated by BRENDA team