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Q9UBP0 (SPAST_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Spastin

EC=3.6.4.3
Alternative name(s):
Spastic paraplegia 4 protein
Gene names
Name:SPAST
Synonyms:ADPSP, FSP2, KIAA1083, SPG4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length616 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. May also play a role in axon growth and the formation of axonal branches. Ref.5 Ref.6 Ref.11 Ref.12 Ref.18 Ref.23 Ref.27

Catalytic activity

ATP + H2O = ADP + phosphate. Ref.11 Ref.12 Ref.17 Ref.18 Ref.20 Ref.27

Enzyme regulation

Allosteric enzyme with a cooperative mechanism; at least two neighbor subunits influence each other strongly in spastin hexamers. Microtubule binding promotes cooperative interactions among spastin subunits. Ref.27

Subunit structure

Homohexamer. Mostly monomeric, but assembles into hexameric structure for short periods of time. Oligomerization seems to be a prerequisite for catalytic activity. Binding to ATP in a cleft between two adjacent subunits stabilizes the homohexameric form. Binds to microtubules at least in part via the alpha-tubulin and beta-tubulin tails. The hexamer adopts a ring conformation through which microtubules pass prior to being severed. Does not interact strongly with tubulin heterodimers. Interacts (via MIT domain) with CHMP1B; the interaction is direct. Interacts with ATL1, RTN1, SSNA1 and ZFYVE27. Isoform 1 but not isoform 3 interacts with RTN2. Interacts with REEP1. Ref.8 Ref.10 Ref.11 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.24 Ref.27 Ref.28 Ref.29 Ref.30

Subcellular location

Membrane; Single-pass membrane protein Potential. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeleton. Cytoplasmperinuclear region. Endoplasmic reticulum. Endosome. Nucleus. Cytoplasmcytoskeletonspindle. 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. Isoform 3 is the main endosomal form. Ref.5 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.23 Ref.30

Tissue specificity

Expressed in brain, heart, kidney, liver, lung, pancreas, placenta and skeletal muscle. The short isoforms may predominate in brain and spinal cord. Ref.1

Developmental stage

Expressed in fetal brain, heart, kidney, liver, lung, skeletal muscle, spleen and thymus. Ref.1

Involvement in disease

Spastic paraplegia 4, autosomal dominant (SPG4) [MIM:182601]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.5 Ref.11 Ref.13 Ref.15 Ref.18 Ref.23 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47 Ref.48 Ref.49 Ref.50 Ref.51 Ref.52 Ref.54 Ref.55 Ref.56 Ref.57 Ref.58 Ref.59

Sequence similarities

Belongs to the AAA ATPase family. Spastin subfamily.

Contains 1 MIT domain.

Biophysicochemical properties

Kinetic parameters:

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 (Ref.27).

KM=0.45 mM for ATP Ref.11 Ref.18 Ref.27

Vmax=1.2 nmol/min/µg enzyme

Ontologies

Keywords
   Biological processCell cycle
Cell division
Differentiation
Neurogenesis
   Cellular componentCytoplasm
Cytoskeleton
Endoplasmic reticulum
Endosome
Membrane
Microtubule
Nucleus
   Coding sequence diversityAlternative initiation
Alternative promoter usage
Alternative splicing
Polymorphism
   DiseaseHereditary spastic paraplegia
Neurodegeneration
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Hydrolase
   PTMPhosphoprotein
   Technical term3D-structure
Allosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.11Ref.12Ref.18. Source: GOC

ER to Golgi vesicle-mediated transport

Inferred from mutant phenotype Ref.23. Source: UniProtKB

axonogenesis

Inferred from electronic annotation. Source: UniProtKB-HAMAP

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

cytokinesis, completion of separation

Inferred from mutant phenotype Ref.23. Source: UniProtKB

microtubule bundle formation

Inferred from direct assay Ref.12. Source: UniProtKB

microtubule severing

Inferred from direct assay Ref.11Ref.12Ref.18. Source: UniProtKB

positive regulation of microtubule depolymerization

Inferred from electronic annotation. Source: UniProtKB-HAMAP

protein hexamerization

Inferred from direct assay Ref.18. Source: UniProtKB

protein homooligomerization

Inferred from direct assay Ref.18. Source: UniProtKB

   Cellular_componentcentrosome

Inferred from electronic annotation. Source: UniProtKB-HAMAP

cytoplasm

Inferred from direct assay Ref.9Ref.23. Source: UniProtKB

cytoplasmic vesicle

Inferred from direct assay PubMed 21545838. Source: MGI

endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule

Inferred from electronic annotation. Source: UniProtKB-HAMAP

midbody

Inferred from electronic annotation. Source: UniProtKB-HAMAP

nucleus

Inferred from direct assay Ref.9Ref.23. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

spindle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

alpha-tubulin binding

Inferred from physical interaction Ref.18. Source: UniProtKB

beta-tubulin binding

Inferred from physical interaction Ref.18. Source: UniProtKB

microtubule binding

Inferred from direct assay Ref.11Ref.12Ref.18. Source: UniProtKB

microtubule-severing ATPase activity

Inferred from direct assay Ref.11Ref.12Ref.18. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.17Ref.24PubMed 20719964Ref.28. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative promoter usage, alternative splicing and alternative initiation. [Align] [Select]

Note: Alternative promoter usage of a cryptic promoter in exon 1 can direct the synthesis of N-terminally truncated isoforms, which may also arise from alternative initiation.
Isoform 1 (identifier: Q9UBP0-1)

Also known as: Long; Long variant 1;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9UBP0-2)

Also known as: Long variant 2;

The sequence of this isoform differs from the canonical sequence as follows:
     197-228: Missing.
Isoform 3 (identifier: Q9UBP0-3)

Also known as: Short; Short variant 1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-86: Missing.
Note: Produced by alternative promoter usage. May also be produced by alternative initiation at Met-87 of isoform 1. Major isoform.
Isoform 4 (identifier: Q9UBP0-4)

Also known as: Short variant 2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-86: Missing.
     197-228: Missing.
Note: Produced by alternative promoter usage and alternative splicing. May also be produced by alternative initiation at Met-87 of isoform 2.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 616616Spastin HAMAP-Rule MF_03021
PRO_0000084763

Regions

Transmembrane57 – 7721Helical; Potential
Domain120 – 19576MIT
Nucleotide binding382 – 3898ATP Probable
Region1 – 300300Required for interaction with RTN1 HAMAP-Rule MF_03021
Region1 – 194194Required for midbody localization HAMAP-Rule MF_03021
Region1 – 8080Required for interaction with ATL1 HAMAP-Rule MF_03021
Region1 – 5050Required for nuclear localization HAMAP-Rule MF_03021
Region50 – 8738Required for interaction with SSNA1 and microtubules HAMAP-Rule MF_03021
Region112 – 19685Sufficient for interaction with CHMP1B HAMAP-Rule MF_03021
Region114 – 20087Required for interaction with microtubules HAMAP-Rule MF_03021
Region226 – 328103Sufficient for interaction with microtubules By similarity
Region228 – 616389Sufficient for microtubule severing HAMAP-Rule MF_03021
Region270 – 32859Required for interaction with microtubules and microtubule severing HAMAP-Rule MF_03021
Region310 – 3123Required for interaction with microtubules HAMAP-Rule MF_03021
Motif4 – 118Nuclear localization signal Ref.7
Motif59 – 679Nuclear export signal HAMAP-Rule MF_03021
Motif309 – 3124Nuclear localization signal Ref.7

Amino acid modifications

Modified residue2451Phosphoserine Ref.26
Modified residue2681Phosphoserine Ref.21 Ref.22 Ref.25
Modified residue3061Phosphothreonine Ref.21

Natural variations

Alternative sequence1 – 8686Missing in isoform 3 and isoform 4.
VSP_036650
Alternative sequence197 – 22832Missing in isoform 2 and isoform 4.
VSP_000024
Natural variant441S → L Rare polymorphism which modifies the phenotype of SPG4 disease; may decrease the activity of the alternative promoter which directs the synthesis of isoform 3 and isoform 4. Ref.19 Ref.33 Ref.47 Ref.50 Ref.54 Ref.55 Ref.57
Corresponds to variant rs121908515 [ dbSNP | Ensembl ].
VAR_010194
Natural variant451P → Q Rare polymorphism which modifies the phenotype of SPG4 disease. Ref.47
VAR_027205
Natural variant971P → T in a patient with hereditary spastic paraplegia; unknown pathological significance. Ref.58
VAR_067628
Natural variant1621V → I in a patient with hereditary spastic paraplegia; unknown pathological significance. Ref.55 Ref.57
Corresponds to variant rs141944844 [ dbSNP | Ensembl ].
VAR_067563
Natural variant1951L → V in SPG4. Ref.51
VAR_026758
Natural variant2011V → D in a patient with hereditary spastic paraplegia; unknown pathological significance. Ref.58
VAR_067629
Natural variant2291S → G. Ref.55
VAR_067630
Natural variant2871Missing in SPG4. Ref.56
VAR_067631
Natural variant2931P → L in SPG4. Ref.56
VAR_067632
Natural variant3141L → S in a patient with hereditary spastic paraplegia; unknown pathological significance. Ref.58
VAR_067633
Natural variant3281I → L in a patient with hereditary spastic paraplegia; unknown pathological significance. Ref.56
VAR_067634
Natural variant3441I → K in SPG4; abrogates ATPase activity and promotes microtubule binding. Ref.11 Ref.42
VAR_019448
Natural variant3471Q → K in SPG4; promotes microtubule binding. Ref.11 Ref.39
VAR_027206
Natural variant3561E → K in a patient with hereditary spastic paraplegia; unknown pathological significance. Ref.57
VAR_067564
Natural variant3601L → V in a patient with hereditary spastic paraplegia; unknown pathological significance. Ref.58
VAR_067635
Natural variant3611P → L in SPG4. Ref.50
VAR_027207
Natural variant3621S → C in SPG4. Ref.1 Ref.32
VAR_010195
Natural variant3641R → T in SPG4. Ref.54
VAR_067636
Natural variant3651P → S in a patient with hereditary spastic paraplegia; unknown pathological significance. Ref.57
VAR_067565
Natural variant3701G → R in SPG4; promotes microtubule binding and the formation of thick microtubule bundles. Ref.5 Ref.32
VAR_027208
Natural variant3781L → Q in SPG4. Ref.45
VAR_019439
Natural variant3781L → R in SPG4. Ref.56
VAR_067637
Natural variant3801L → H in SPG4. Ref.54 Ref.56
VAR_067638
Natural variant3811F → C in SPG4; promotes microtubule binding and the formation of thick microtubule bundles. Ref.5 Ref.32
VAR_027209
Natural variant3821G → R in a patient with hereditary spastic paraplegia; unknown pathological significance. Ref.57
VAR_067566
Natural variant3861N → K in SPG4; abrogates ATPase activity, promotes microtubule binding and the formation of thick microtubule bundles. Ref.5 Ref.11 Ref.32
VAR_027210
Natural variant3861N → S in SPG4. Ref.46
VAR_019440
Natural variant3881K → R in SPG4; abrogates ATPase activity, promotes microtubule binding and the formation of thick microtubule bundles and impairs traffic from the ER to Golgi. Ref.5 Ref.11 Ref.13 Ref.15 Ref.23 Ref.32 Ref.39
VAR_027211
Natural variant3901M → V in SPG4. Ref.45
VAR_019441
Natural variant3911L → P in SPG4. Ref.56
VAR_067639
Natural variant393 – 3964Missing in SPG4.
VAR_067640
Natural variant3991S → L in SPG4. Ref.37
VAR_027212
Natural variant4041Missing in SPG4. Ref.41
VAR_019449
Natural variant4061I → V in SPG4. Ref.51
VAR_026759
Natural variant4071S → I in a patient with hereditary spastic paraplegia; unknown pathological significance. Ref.57
VAR_067567
Natural variant4071S → R in SPG4. Ref.38
VAR_019450
Natural variant4091A → T in SPG4. Ref.56
VAR_067641
Natural variant4101S → R in SPG4. Ref.56
VAR_067642
Natural variant4131S → L in SPG4. Ref.59
VAR_067568
Natural variant4221L → F in a patient with hereditary spastic paraplegia; unknown pathological significance. Ref.57
VAR_067569
Natural variant4231V → L in a breast cancer sample; somatic mutation. Ref.53
VAR_035902
Natural variant4241R → G in SPG4. Ref.33
VAR_010196
Natural variant4261L → F in SPG4. Ref.55
VAR_067643
Natural variant4261L → V in SPG4; promotes microtubule binding and the formation of thick microtubule bundles. Ref.5 Ref.32 Ref.37
VAR_027213
Natural variant4351P → L in SPG4. Ref.52
VAR_027214
Natural variant4361S → F in SPG4. Ref.34
VAR_027215
Natural variant4361S → P in SPG4. Ref.56
VAR_067644
Natural variant4411D → G in SPG4. Ref.31
VAR_027216
Natural variant4411D → N in SPG4. Ref.56
VAR_067645
Natural variant4451S → N in a patient with hereditary spastic paraplegia; unknown pathological significance. Ref.57
VAR_067570
Natural variant4481C → Y in SPG4; abrogates binding to the tail of beta-3-tubulin, abolishes microtubule severing and promotes the formation of thick microtubule bundles. Ref.1 Ref.5 Ref.18 Ref.32
VAR_010197
Natural variant4541E → K in SPG4. Ref.59
VAR_067571
Natural variant4591R → G in SPG4. Ref.48
VAR_027217
Natural variant4601R → C in SPG4; promotes microtubule binding and the formation of thick microtubule bundles. Ref.48
VAR_027218
Natural variant4601R → L in SPG4. Ref.5 Ref.32
VAR_027219
Natural variant4601R → S in SPG4. Ref.55 Ref.56 Ref.57
VAR_067572
Natural variant4631T → A in SPG4. Ref.56
VAR_067646
Natural variant4641E → A in a patient with hereditary spastic paraplegia; unknown pathological significance. Ref.58
VAR_067647
Natural variant4701D → V in SPG4. Ref.47
Corresponds to variant rs28939368 [ dbSNP | Ensembl ].
VAR_027220
Natural variant4821V → L in a patient with hereditary spastic paraplegia; unknown pathological significance. Ref.57
VAR_067573
Natural variant4851A → V in SPG4. Ref.36
VAR_027221
Natural variant4891P → L in SPG4. Ref.37
VAR_027222
Natural variant4921L → F in SPG4. Ref.56
VAR_067648
Natural variant4931D → G in SPG4. Ref.51
VAR_026760
Natural variant4981R → G in SPG4. Ref.56 Ref.58
VAR_067649
Natural variant4991R → C in SPG4; abrogates ATPase activity, promotes microtubule binding and the formation of thick microtubule bundles. Ref.1 Ref.5 Ref.11 Ref.32 Ref.35 Ref.39
VAR_010198
Natural variant4991R → H in SPG4. Ref.51
VAR_026761
Natural variant5031R → L in SPG4. Ref.43
VAR_019442
Natural variant5031R → RR in SPG4. Ref.56
VAR_067650
Natural variant5031R → W in SPG4. Ref.51
VAR_026762
Natural variant5121E → D in SPG4. Ref.40
VAR_027223
Natural variant5121Missing in a patient with hereditary spastic paraplegia; unknown pathological significance. Ref.57
VAR_067574
Natural variant5141R → G in SPG4. Ref.56
VAR_067651
Natural variant5151Missing in SPG4. Ref.45
VAR_019443
Natural variant5341L → P in SPG4. Ref.44
VAR_019444
Natural variant5341L → V Found at homozygosity in two children with hereditary spastic paraplegia; unknown pathological significance. Ref.57
VAR_067575
Natural variant5501T → I in a patient with hereditary spastic paraplegia; unknown pathological significance. Ref.58
VAR_067652
Natural variant5511A → Y in SPG4; requires 2 nucleotide substitutions. Ref.38
VAR_019451
Natural variant5551D → N in SPG4. Ref.32
VAR_027224
Natural variant5561A → V in SPG4; promotes microtubule binding and the formation of thick microtubule bundles. Ref.5 Ref.32
VAR_027225
Natural variant5591G → D in SPG4. Ref.34 Ref.37
VAR_027226
Natural variant5621R → G in SPG4. Ref.35 Ref.47
VAR_027227
Natural variant5621R → P in a patient with hereditary spastic paraplegia; unknown pathological significance. Ref.57
VAR_067576
Natural variant5621R → Q in SPG4. Ref.37
VAR_027228
Natural variant5791N → H Found in patients with hereditary spastic paraplegia; unknown pathological significance. Ref.54
Corresponds to variant rs144594804 [ dbSNP | Ensembl ].
VAR_067653
Natural variant5801I → T in SPG4. Ref.56
VAR_067654
Natural variant5841D → H in SPG4. Ref.33
VAR_010199
Natural variant6071W → C in SPG4. Ref.51
VAR_026763
Natural variant6141T → I in SPG4; variant form with congenital arachnoid cysts. Ref.49
VAR_019445
Natural variant6151T → I in SPG4. Ref.38
VAR_019452

Experimental info

Mutagenesis11M → V: Cytoplasmic and nuclear. Ref.9
Mutagenesis871M → V: Exclusively cytoplasmic. Ref.9
Mutagenesis1201H → D: Impairs binding to CHMP1B. Impairs midbody localization; when associated with D-124. Ref.30
Mutagenesis1241F → A: Impairs binding to CHMP1B. Ref.30
Mutagenesis1241F → D: Impairs binding to CHMP1B. Impairs midbody localization; when associated with D-120. Ref.30
Mutagenesis310 – 3123KKK → QQQ: Loss of microtubule-binding. Ref.29
Mutagenesis3881K → A: Abrogates ATPase activity and abolishes microtubule severing. Ref.11
Mutagenesis4151Y → A: Abrogates binding to the tail of alpha-tubulin and beta-3-tubulin, impairs ATPase activity and abolishes microtubule severing. Ref.18
Mutagenesis4421E → Q: Abrogates ATP hydrolysis, abolishes microtubule severing, stabilizes the homohexameric form, and promotes microtubule binding and redistribution from the endosome to microtubules. Ref.11 Ref.17 Ref.18 Ref.20 Ref.27 Ref.29
Mutagenesis4511R → G: Abrogates binding to the tail of alpha-tubulin and beta-3-tubulin, impairs ATPase activity and abolishes microtubule severing. Ref.18
Mutagenesis4571A → E: Abrogates binding to the tail of alpha-tubulin and beta-3-tubulin and abolishes microtubule severing. Ref.18

Secondary structure

.......................................................... 616
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Long) (Long variant 1) [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 75E5FC5787132B4C

FASTA61667,197
        10         20         30         40         50         60 
MNSPGGRGKK KGSGGASNPV PPRPPPPCLA PAPPAAGPAP PPESPHKRNL YYFSYPLFVG 

        70         80         90        100        110        120 
FALLRLVAFH LGLLFVWLCQ RFSRALMAAK RSSGAAPAPA SASAPAPVPG GEAERVRVFH 

       130        140        150        160        170        180 
KQAFEYISIA LRIDEDEKAG QKEQAVEWYK KGIEELEKGI AVIVTGQGEQ CERARRLQAK 

       190        200        210        220        230        240 
MMTNLVMAKD RLQLLEKMQP VLPFSKSQTD VYNDSTNLAC RNGHLQSESG AVPKRKDPLT 

       250        260        270        280        290        300 
HTSNSLPRSK TVMKTGSAGL SGHHRAPSYS GLSMVSGVKQ GSGPAPTTHK GTPKTNRTNK 

       310        320        330        340        350        360 
PSTPTTATRK KKDLKNFRNV DSNLANLIMN EIVDNGTAVK FDDIAGQDLA KQALQEIVIL 

       370        380        390        400        410        420 
PSLRPELFTG LRAPARGLLL FGPPGNGKTM LAKAVAAESN ATFFNISAAS LTSKYVGEGE 

       430        440        450        460        470        480 
KLVRALFAVA RELQPSIIFI DEVDSLLCER REGEHDASRR LKTEFLIEFD GVQSAGDDRV 

       490        500        510        520        530        540 
LVMGATNRPQ ELDEAVLRRF IKRVYVSLPN EETRLLLLKN LLCKQGSPLT QKELAQLARM 

       550        560        570        580        590        600 
TDGYSGSDLT ALAKDAALGP IRELKPEQVK NMSASEMRNI RLSDFTESLK KIKRSVSPQT 

       610 
LEAYIRWNKD FGDTTV 

« Hide

Isoform 2 (Long variant 2) [UniParc].

Checksum: 502F0FCB78ECED14
Show »

FASTA58463,606
Isoform 3 (Short) (Short variant 1) [UniParc].

Checksum: 0A4DB33B07801675
Show »

FASTA53058,009
Isoform 4 (Short variant 2) [UniParc].

Checksum: F8BB32A6C8CB1D73
Show »

FASTA49854,418

References

« Hide 'large scale' references
[1]"Spastin, a new AAA protein, is altered in the most frequent form of autosomal dominant spastic paraplegia."
Hazan J., Fonknechten N., Mavel D., Paternotte C., Samson D., Artiguenave F., Davoine C.-S., Cruaud C., Durr A., Wincker P., Brottier P., Cattolico L., Barbe V., Burgunder J.-M., Prud'homme J.-F., Brice A., Fontaine B., Heilig R., Weissenbach J.
Nat. Genet. 23:296-303(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, VARIANTS SPG4 CYS-362; TYR-448 AND CYS-499.
[2]"Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[5]"Spastin, the protein mutated in autosomal dominant hereditary spastic paraplegia, is involved in microtubule dynamics."
Errico A., Ballabio A., Rugarli E.I.
Hum. Mol. Genet. 11:153-163(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS SPG4 ARG-370; CYS-381; LYS-386; ARG-388; VAL-426; TYR-448; LEU-460; CYS-499 AND VAL-556.
[6]"The identification of a conserved domain in both spartin and spastin, mutated in hereditary spastic paraplegia."
Ciccarelli F.D., Proukakis C., Patel H., Cross H., Azam S., Patton M.A., Bork P., Crosby A.H.
Genomics 81:437-441(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN MIT, PROBABLE FUNCTION.
[7]"Identification of nuclear localisation sequences in spastin (SPG4) using a novel Tetra-GFP reporter system."
Beetz C., Brodhun M., Moutzouris K., Kiehntopf M., Berndt A., Lehnert D., Deufel T., Bastmeyer M., Schickel J.
Biochem. Biophys. Res. Commun. 318:1079-1084(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL.
[8]"Spastin interacts with the centrosomal protein NA14, and is enriched in the spindle pole, the midbody and the distal axon."
Errico A., Claudiani P., D'Addio M., Rugarli E.I.
Hum. Mol. Genet. 13:2121-2132(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SSNA1 AND MICROTUBULES, SUBCELLULAR LOCATION.
[9]"Spastin subcellular localization is regulated through usage of different translation start sites and active export from the nucleus."
Claudiani P., Riano E., Errico A., Andolfi G., Rugarli E.I.
Exp. Cell Res. 309:358-369(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE INITIATION, SUBCELLULAR LOCATION, NUCLEAR EXPORT SIGNALS, MUTAGENESIS OF MET-1 AND MET-87.
[10]"The hereditary spastic paraplegia protein spastin interacts with the ESCRT-III complex-associated endosomal protein CHMP1B."
Reid E., Connell J.W., Edwards T.L., Duley S., Brown S.E., Sanderson C.M.
Hum. Mol. Genet. 14:19-38(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CHMP1B, SUBCELLULAR LOCATION.
[11]"Linking axonal degeneration to microtubule remodeling by Spastin-mediated microtubule severing."
Evans K.J., Gomes E.R., Reisenweber S.M., Gundersen G.G., Lauring B.P.
J. Cell Biol. 168:599-606(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-388 AND GLU-442, CHARACTERIZATION OF VARIANTS SPG4 LYS-344; LYS-347; LYS-386; ARG-388 AND CYS-499.
[12]"Human spastin has multiple microtubule-related functions."
Salinas S., Carazo-Salas R.E., Proukakis C., Cooper J.M., Weston A.E., Schiavo G., Warner T.T.
J. Neurochem. 95:1411-1420(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, ASSOCIATION WITH MICROTUBULES, SUBCELLULAR LOCATION.
[13]"Subcellular localization of spastin: implications for the pathogenesis of hereditary spastic paraplegia."
Svenson I.K., Kloos M.T., Jacon A., Gallione C., Horton A.C., Pericak-Vance M.A., Ehlers M.D., Marchuk D.A.
Neurogenetics 6:135-141(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT SPG4 ARG-388.
[14]"ZFYVE27 (SPG33), a novel spastin-binding protein, is mutated in hereditary spastic paraplegia."
Mannan A.U., Krawen P., Sauter S.M., Boehm J., Chronowska A., Paulus W., Neesen J., Engel W.
Am. J. Hum. Genet. 79:351-357(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZFYVE27.
[15]"Spastin and atlastin, two proteins mutated in autosomal-dominant hereditary spastic paraplegia, are binding partners."
Sanderson C.M., Connell J.W., Edwards T.L., Bright N.A., Duley S., Thompson A., Luzio J.P., Reid E.
Hum. Mol. Genet. 15:307-318(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATL1, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT SPG4 ARG-388.
[16]"Spastin, the most commonly mutated protein in hereditary spastic paraplegia interacts with Reticulon 1 an endoplasmic reticulum protein."
Mannan A.U., Boehm J., Sauter S.M., Rauber A., Byrne P.C., Neesen J., Engel W.
Neurogenetics 7:93-103(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RTN1, SUBCELLULAR LOCATION.
[17]"Interaction of two hereditary spastic paraplegia gene products, spastin and atlastin, suggests a common pathway for axonal maintenance."
Evans K.J., Keller C., Pavur K., Glasgow K., Conn B., Lauring B.P.
Proc. Natl. Acad. Sci. U.S.A. 103:10666-10671(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, INTERACTION WITH ATL1, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-442.
[18]"Recognition of C-terminal amino acids in tubulin by pore loops in Spastin is important for microtubule severing."
White S.R., Evans K.J., Lary J., Cole J.L., Lauring B.P.
J. Cell Biol. 176:995-1005(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, HOMOHEXAMERIZATION, INTERACTION WITH TUBULIN AND MICROTUBULES, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-415; GLU-442; ARG-451 AND ALA-457, CHARACTERIZATION OF VARIANT SPG4 TYR-448.
[19]"A cryptic promoter in the first exon of the SPG4 gene directs the synthesis of the 60-kDa spastin isoform."
Mancuso G., Rugarli E.I.
BMC Biol. 6:31-31(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE PROMOTER USAGE, CHARACTERIZATION OF VARIANT LEU-44.
[20]"Spastin oligomerizes into a hexamer and the mutant spastin (E442Q) redistribute the wild-type spastin into filamentous microtubule."
Pantakani D.V.K., Swapna L.S., Srinivasan N., Mannan A.U.
J. Neurochem. 106:613-624(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, HOMOHEXAMERIZATION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-442.
[21]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268 AND THR-306, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[23]"Spastin couples microtubule severing to membrane traffic in completion of cytokinesis and secretion."
Connell J.W., Lindon C., Luzio J.P., Reid E.
Traffic 10:42-56(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT SPG4 ARG-388.
[24]"Hereditary spastic paraplegia proteins REEP1, spastin, and atlastin-1 coordinate microtubule interactions with the tubular ER network."
Park S.H., Zhu P.P., Parker R.L., Blackstone C.
J. Clin. Invest. 120:1097-1110(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH REEP1.
[25]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[26]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"Subunit Interactions and cooperativity in the microtubule-severing AAA ATPase spastin."
Eckert T., Link S., Le D.T., Sobczak J.P., Gieseke A., Richter K., Woehlke G.
J. Biol. Chem. 287:26278-26290(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: HOMOHEXAMERIZATION, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, KINETIC PARAMETERS, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, COOPERATIVITY, MUTAGENESIS OF GLU-442.
[28]"Mutations in the ER-shaping protein reticulon 2 cause the axon-degenerative disorder hereditary spastic paraplegia type 12."
Montenegro G., Rebelo A.P., Connell J., Allison R., Babalini C., D'Aloia M., Montieri P., Schule R., Ishiura H., Price J., Strickland A., Gonzalez M.A., Baumbach-Reardon L., Deconinck T., Huang J., Bernardi G., Vance J.M., Rogers M.T. expand/collapse author list , Tsuji S., De Jonghe P., Pericak-Vance M.A., Schols L., Orlacchio A., Reid E., Zuchner S.
J. Clin. Invest. 122:538-544(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RTN2.
[29]"Spastin's microtubule-binding properties and comparison to katanin."
Eckert T., Le D.T., Link S., Friedmann L., Woehlke G.
PLoS ONE 7:E50161-E50161(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MICROTUBULES, OLIGOMERIZATION, MUTAGENESIS OF 310-LYS--LYS-312 AND GLU-442.
[30]"Structural basis for midbody targeting of spastin by the ESCRT-III protein CHMP1B."
Yang D., Rismanchi N., Renvoise B., Lippincott-Schwartz J., Blackstone C., Hurley J.H.
Nat. Struct. Mol. Biol. 15:1278-1286(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 112-196 IN COMPLEX WITH CHMP1B, INTERACTION WITH CHMP1B, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-120 AND PHE-124.
[31]"Hereditary spastic paraplegia caused by mutations in the SPG4 gene."
Buerger J., Fonknechten N., Hoeltzenbein M., Neumann L., Bratanoff E., Hazan J., Reis A.
Eur. J. Hum. Genet. 8:771-776(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG4 GLY-441.
[32]"Spectrum of SPG4 mutations in autosomal dominant spastic paraplegia."
Fonknechten N., Mavel D., Byrne P., Davoine C.-S., Cruaud C., Bonsch D., Samson D., Coutinho P., Hutchinson M., McMonagle P., Burgunder J.-M., Tartaglione A., Heinzlef O., Feki I., Deufel T., Parfrey N., Brice A., Fontaine B. expand/collapse author list , Prud'homme J.-F., Weissenbach J., Duerr A., Hazan J.
Hum. Mol. Genet. 9:637-644(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 CYS-362; ARG-370; CYS-381; LYS-386; ARG-388; VAL-426; TYR-448; LEU-460; CYS-499; ASN-555 AND VAL-556.
[33]"Mutation analysis of the spastin gene (SPG4) in patients with hereditary spastic paraparesis."
Lindsey J.C., Lusher M.E., McDermott C.J., White K.D., Reid E., Rubinsztein D.C., Bashir R., Hazan J., Shaw P.J., Bushby K.M.D.
J. Med. Genet. 37:759-765(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 LEU-44; GLY-424 AND HIS-584.
[34]"Novel mutations in spastin gene and absence of correlation with age at onset of symptoms."
Hentati A., Deng H.-X., Zhai H., Chen W., Yang Y., Hung W.-Y., Azim A.C., Bohlega S., Tandan R., Warner C., Laing N.G., Cambi F., Mitsumoto H., Roos R.P., Boustany R.-M.N., Ben-Hamida M., Hentati F., Siddique T.
Neurology 55:1388-1390(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 PHE-436 AND ASP-559.
[35]"Identification and expression analysis of spastin gene mutations in hereditary spastic paraplegia."
Svenson I.K., Ashley-Koch A.E., Gaskell P.C., Riney T.J., Cumming W.J.K., Kingston H.M., Hogan E.L., Boustany R.-M.N., Vance J.M., Nance M.A., Pericak-Vance M.A., Marchuk D.A.
Am. J. Hum. Genet. 68:1077-1085(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 CYS-499 AND GLY-562.
[36]"A Japanese SPG4 family with a novel missense mutation of the SPG4 gene: intrafamilial variability in age at onset and clinical severity."
Namekawa M., Takiyama Y., Sakoe K., Nagaki H., Shimazaki H., Yoshimura M., Ikeguchi K., Nakano I., Nishizawa M.
Acta Neurol. Scand. 106:387-391(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG4 VAL-485.
[37]"Spectrum of SPG4 mutations in a large collection of North American families with hereditary spastic paraplegia."
Meijer I.A., Hand C.K., Cossette P., Figlewicz D.A., Rouleau G.A.
Arch. Neurol. 59:281-286(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 LEU-399; VAL-426; LEU-489; ASP-559 AND GLN-562.
[38]"Mutation analysis of the spastin gene (SPG4) in patients in Germany with autosomal dominant hereditary spastic paraplegia."
Sauter S.M., Miterski B., Klimpe S., Boensch D., Schoels L., Visbeck A., Papke T., Hopf H.C., Engel W., Deufel T., Epplen J.T., Neesen J.
Hum. Mutat. 20:127-132(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 ARG-407; TYR-551 AND ILE-615.
[39]"Spastin gene mutation in Japanese with hereditary spastic paraplegia."
Yabe I., Sasaki H., Tashiro K., Matsuura T., Takegami T., Satoh T.
J. Med. Genet. 39:E46-E46(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 LYS-347; ARG-388 AND CYS-499.
[40]"Missense and splice site mutations in SPG4 suggest loss-of-function in dominant spastic paraplegia."
Patrono C., Casali C., Tessa A., Cricchi F., Fortini D., Carrozzo R., Siciliano G., Bertini E., Santorelli F.M.
J. Neurol. 249:200-205(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG4 ASP-512.
[41]"Three novel spastin (SPG4) mutations in families with autosomal dominant hereditary spastic paraplegia."
Proukakis C., Hart P.E., Cornish A., Warner T.T., Crosby A.H.
J. Neurol. Sci. 201:65-69(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG4 PHE-404 DEL.
[42]"A novel missense mutation (I344K) in the SPG4gene in a Korean family with autosomal-dominant hereditary spastic paraplegia."
Ki C.S., Lee W.Y., Han do H., Sung D.H., Lee K.B., Lee K.A., Cho S.S., Cho S., Hwang H., Sohn K.M., Choi Y.J., Kim J.W.
J. Hum. Genet. 47:473-477(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG4 LYS-344.
[43]"Screening of patients with hereditary spastic paraplegia reveals seven novel mutations in the SPG4 (Spastin) gene."
Proukakis C., Auer-Grumbach M., Wagner K., Wilkinson P.A., Reid E., Patton M.A., Warner T.T., Crosby A.H.
Hum. Mutat. 21:170-170(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG4 LEU-503.
[44]"Novel spastin mutations and their expression analysis in two Italian families."
Molon A., Montagna P., Angelini C., Pegoraro E.
Eur. J. Hum. Genet. 11:710-713(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG4 PRO-534.
[45]"Three novel mutations of the spastin gene in Chinese patients with hereditary spastic paraplegia."
Tang B., Zhao G., Xia K., Pan Q., Luo W., Shen L., Long Z., Dai H., Zi X., Jiang H.
Arch. Neurol. 61:49-55(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 GLN-378; VAL-390 AND LEU-515 DEL.
[46]"Hereditary spastic paraplegia: clinical genetic study of 15 families."
Orlacchio A., Kawarai T., Totaro A., Errico A., St George-Hyslop P.H., Rugarli E.I., Bernardi G.
Arch. Neurol. 61:849-855(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG4 SER-386.
[47]"Intragenic modifiers of hereditary spastic paraplegia due to spastin gene mutations."
Svenson I.K., Kloos M.T., Gaskell P.C., Nance M.A., Garbern J.Y., Hisanaga S., Pericak-Vance M.A., Ashley-Koch A.E., Marchuk D.A.
Neurogenetics 5:157-164(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 VAL-470 AND GLY-562, VARIANTS LEU-44 AND GLN-45.
[48]"Two novel mutations in the spastin gene (SPG4) found by DHPLC mutation analysis."
Falco M., Scuderi C., Musumeci S., Sturnio M., Neri M., Bigoni S., Caniatti L., Fichera M.
Neuromuscul. Disord. 14:750-753(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 GLY-459 AND CYS-460.
[49]"A new SPG4 mutation in a variant form of spastic paraplegia with congenital arachnoid cysts."
Orlacchio A., Gaudiello F., Totaro A., Floris R., St George-Hyslop P.H., Bernardi G., Kawarai T.
Neurology 62:1875-1878(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG4 ILE-614.
[50]"Infantile hereditary spastic paraparesis due to codominant mutations in the spastin gene."
Chinnery P.F., Keers S.M., Holden M.J., Ramesh V., Dalton A.
Neurology 63:710-712(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 LEU-44 AND LEU-361.
[51]"Eight novel mutations in SPG4 in a large sample of patients with hereditary spastic paraplegia."
Crippa F., Panzeri C., Martinuzzi A., Arnoldi A., Redaelli F., Tonelli A., Baschirotto C., Vazza G., Mostacciuolo M.L., Daga A., Orso G., Profice P., Trabacca A., D'Angelo M.G., Comi G.P., Galbiati S., Lamperti C., Bonato S. expand/collapse author list , Pandolfo M., Meola G., Musumeci O., Toscano A., Trevisan C.P., Bresolin N., Bassi M.T.
Arch. Neurol. 63:750-755(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 VAL-195; VAL-406; GLY-493; HIS-499; TRP-503 AND CYS-607.
[52]"Novel spastin (SPG4) mutations in Italian patients with hereditary spastic paraplegia."
Magariello A., Muglia M., Patitucci A., Mazzei R., Conforti F.L., Gabriele A.L., Sprovieri T., Ungaro C., Gambardella A., Mancuso M., Siciliano G., Branca D., Aguglia U., de Angelis M.V., Longo K., Quattrone A.
Neuromuscul. Disord. 16:387-390(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG4 LEU-435.
[53]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-423.
[54]"Seven novel mutations and four exon deletions in a collection of Norwegian patients with SPG4 hereditary spastic paraplegia."
Erichsen A.K., Inderhaug E., Mattingsdal M., Eiklid K., Tallaksen C.M.
Eur. J. Neurol. 14:809-814(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 THR-364 AND HIS-380, VARIANTS LEU-44 AND HIS-579.
[55]"Unique spectrum of SPAST variants in Estonian HSP patients: presence of benign missense changes but lack of exonic rearrangements."
Braschinsky M., Tamm R., Beetz C., Sachez-Ferrero E., Raukas E., Luus S.M., Gross-Paju K., Boillot C., Canzian F., Metspalu A., Haldre S.
BMC Neurol. 10:17-17(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LEU-44; ILE-162 AND GLY-229, VARIANTS SPG4 PHE-426 AND SER-460.
[56]"Mutational spectrum of the SPG4 (SPAST) and SPG3A (ATL1) genes in Spanish patients with hereditary spastic paraplegia."
Alvarez V., Sanchez-Ferrero E., Beetz C., Diaz M., Alonso B., Corao A.I., Gamez J., Esteban J., Gonzalo J.F., Pascual-Pascual S.I., Lopez de Munain A., Moris G., Ribacoba R., Marquez C., Rosell J., Marin R., Garcia-Barcina M.J., Del Castillo E., Benito C., Coto E.
BMC Neurol. 10:89-89(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 THR-287 DEL; LEU-293; ARG-378; HIS-380; PRO-391; 393-LYS--ALA-396 DEL; THR-409; ARG-410; PRO-436; ASN-441; SER-460; ALA-463; PHE-492; GLY-498; ARG-503 INS; GLY-514 AND THR-580, VARIANT LEU-328.
[57]"Hereditary spastic paraplegia due to SPAST mutations in 151 Dutch patients: new clinical aspects and 27 novel mutations."
de Bot S.T., van den Elzen R.T., Mensenkamp A.R., Schelhaas H.J., Willemsen M.A., Knoers N.V., Kremer H.P., van de Warrenburg B.P., Scheffer H.
J. Neurol. Neurosurg. Psych. 81:1073-1078(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG4 SER-460, VARIANTS LEU-44; ILE-162; LYS-356; SER-365; ARG-382; ILE-407; PHE-422; ASN-445; LEU-482; GLU-512 DEL; VAL-534 AND PRO-562.
[58]"Mutation screening of spastin, atlastin, and REEP1 in hereditary spastic paraplegia."
McCorquodale D.S. III, Ozomaro U., Huang J., Montenegro G., Kushman A., Citrigno L., Price J., Speziani F., Pericak-Vance M.A., Zuchner S.
Clin. Genet. 79:523-530(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS THR-97; ASP-201; SER-314; VAL-360; ALA-464 AND ILE-550, VARIANT SPG4 GLY-498.
[59]"Clinical and genetic findings in a series of Italian children with pure hereditary spastic paraplegia."
Battini R., Fogli A., Borghetti D., Michelucci A., Perazza S., Baldinotti F., Conidi M.E., Ferreri M.I., Simi P., Cioni G.
Eur. J. Neurol. 18:150-157(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG4 LEU-413 AND LYS-454.
+Additional computationally mapped references.

Web resources

Protein Spotlight

The making of crooked - Issue 104 of April 2009

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ246001 mRNA. Translation: CAB60141.1.
AJ246003 Genomic DNA. Translation: CAB60208.1.
AB029006 mRNA. Translation: BAA83035.1.
CH471053 Genomic DNA. Translation: EAX00462.1.
BC150260 mRNA. Translation: AAI50261.1.
CCDSCCDS1778.1. [Q9UBP0-1]
CCDS1779.1. [Q9UBP0-2]
RefSeqNP_055761.2. NM_014946.3. [Q9UBP0-1]
NP_955468.1. NM_199436.1. [Q9UBP0-2]
UniGeneHs.468091.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3EABX-ray2.50A/B/C/D/E/F112-196[»]
3VFDX-ray3.30A228-616[»]
ProteinModelPortalQ9UBP0.
SMRQ9UBP0. Positions 112-196, 324-612.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112562. 7 interactions.
IntActQ9UBP0. 2 interactions.
STRING9606.ENSP00000320885.

PTM databases

PhosphoSiteQ9UBP0.

Polymorphism databases

DMDM12230611.

Proteomic databases

MaxQBQ9UBP0.
PaxDbQ9UBP0.
PeptideAtlasQ9UBP0.
PRIDEQ9UBP0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000315285; ENSP00000320885; ENSG00000021574. [Q9UBP0-1]
ENST00000345662; ENSP00000340817; ENSG00000021574. [Q9UBP0-2]
GeneID6683.
KEGGhsa:6683.
UCSCuc002roc.3. human. [Q9UBP0-1]

Organism-specific databases

CTD6683.
GeneCardsGC02P032288.
GeneReviewsSPAST.
HGNCHGNC:11233. SPAST.
HPAHPA017311.
MIM182601. phenotype.
604277. gene.
neXtProtNX_Q9UBP0.
Orphanet100985. Autosomal dominant spastic paraplegia type 4.
PharmGKBPA36063.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0464.
HOGENOMHOG000225146.
HOVERGENHBG108502.
InParanoidQ9UBP0.
KOK13254.
OMASEMRNIK.
OrthoDBEOG7GXPCR.
PhylomeDBQ9UBP0.
TreeFamTF105014.

Gene expression databases

ArrayExpressQ9UBP0.
BgeeQ9UBP0.
CleanExHS_SPAST.
GenevestigatorQ9UBP0.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
HAMAPMF_03021. Spastin.
InterProIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR007330. MIT.
IPR027417. P-loop_NTPase.
IPR017179. Spastin.
[Graphical view]
PfamPF00004. AAA. 1 hit.
PF04212. MIT. 1 hit.
[Graphical view]
PIRSFPIRSF037338. Spastin. 1 hit.
SMARTSM00382. AAA. 1 hit.
SM00745. MIT. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSPAST. human.
EvolutionaryTraceQ9UBP0.
GeneWikiSpastin.
GenomeRNAi6683.
NextBio26047.
PROQ9UBP0.
SOURCESearch...

Entry information

Entry nameSPAST_HUMAN
AccessionPrimary (citable) accession number: Q9UBP0
Secondary accession number(s): A7E2A7, Q9UPR9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM