Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Spastin

Gene

Spast

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity). Required for development of axonal processes and for axonal branching.By similarity2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.UniRule annotation

Enzyme regulationi

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 (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi380 – 3878ATPUniRule annotation

GO - Molecular functioni

  1. alpha-tubulin binding Source: UniProtKB
  2. ATP binding Source: UniProtKB-HAMAP
  3. beta-tubulin binding Source: UniProtKB
  4. microtubule binding Source: UniProtKB
  5. microtubule-severing ATPase activity Source: UniProtKB

GO - Biological processi

  1. axonogenesis Source: UniProtKB-HAMAP
  2. cell cycle Source: UniProtKB-KW
  3. cell division Source: UniProtKB-KW
  4. cytoplasmic microtubule organization Source: GO_Central
  5. ER to Golgi vesicle-mediated transport Source: UniProtKB
  6. microtubule bundle formation Source: UniProtKB
  7. microtubule severing Source: UniProtKB
  8. positive regulation of microtubule depolymerization Source: UniProtKB-HAMAP
  9. protein hexamerization Source: UniProtKB
  10. protein homooligomerization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Hydrolase

Keywords - Biological processi

Cell cycle, Cell division, Differentiation, Neurogenesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
SpastinUniRule annotation (EC:3.6.4.3UniRule annotation)
Gene namesi
Name:Spast
Synonyms:Kiaa1083, Spg4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1858896. Spast.

Subcellular locationi

Membrane UniRule annotation; Single-pass membrane protein UniRule annotation. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome UniRule annotation. Cytoplasmcytoskeleton UniRule annotation. Cytoplasmperinuclear region UniRule annotation. Endoplasmic reticulum UniRule annotation. Endosome UniRule annotation. Nucleus UniRule annotation. Cytoplasmcytoskeletonspindle UniRule annotation
Note: Localization to the centrosome is independent of microtubules. Localizes to the midbody of dividing cells, and this requires CHMP1B (By similarity). Evenly distributed along early axons and concentrates in the growth cone of the axons of late stage 3 neurons.By similarity1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei55 – 7723HelicalUniRule annotationAdd
BLAST

GO - Cellular componenti

  1. centrosome Source: UniProtKB-HAMAP
  2. cytoplasm Source: MGI
  3. cytoplasmic vesicle Source: MGI
  4. endoplasmic reticulum Source: UniProtKB-SubCell
  5. endosome Source: UniProtKB-SubCell
  6. extracellular vesicular exosome Source: MGI
  7. integral component of membrane Source: UniProtKB-KW
  8. microtubule Source: UniProtKB-HAMAP
  9. microtubule cytoskeleton Source: MGI
  10. midbody Source: UniProtKB-HAMAP
  11. nucleus Source: UniProtKB
  12. perinuclear region of cytoplasm Source: UniProtKB-SubCell
  13. spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Endoplasmic reticulum, Endosome, Membrane, Microtubule, Nucleus

Pathology & Biotechi

Disruption phenotypei

Progressive axonal degeneration characterized by focal axonal swellings and the accumulation of organelles and cytoskeletal components, which is suggestive of impaired axonal transport. Late development of mild motor defects. Adults are sterile. Primary cortical neurons develop swellings at the border between stable and dynamic microtubules.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 614614SpastinPRO_0000084764Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei243 – 2431PhosphoserineBy similarity
Modified residuei266 – 2661PhosphoserineBy similarity
Modified residuei304 – 3041PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9QYY8.
PaxDbiQ9QYY8.
PRIDEiQ9QYY8.

PTM databases

PhosphoSiteiQ9QYY8.

Expressioni

Tissue specificityi

Expressed in brain, heart, liver, lung, skeletal muscle, spinal cord, spleen and testis.2 Publications

Inductioni

Expressed is decreased following activation of the Notch pathway by JAG1/Jagged1.1 Publication

Gene expression databases

BgeeiQ9QYY8.
CleanExiMM_SPAST.
GenevestigatoriQ9QYY8.

Interactioni

Subunit structurei

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 (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9QYY8.
SMRiQ9QYY8. Positions 110-194, 322-610.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini118 – 19376MITUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 298298Required for interaction with RTN1By similarityAdd
BLAST
Regioni1 – 192192Required for midbody localizationBy similarityAdd
BLAST
Regioni1 – 7878Required for interaction with ATL1By similarityAdd
BLAST
Regioni1 – 4848Required for nuclear localizationBy similarityAdd
BLAST
Regioni48 – 8538Required for interaction with SSNA1 and microtubulesBy similarityAdd
BLAST
Regioni110 – 19485Sufficient for interaction with CHMP1BBy similarityAdd
BLAST
Regioni112 – 19887Required for interaction with microtubulesBy similarityAdd
BLAST
Regioni224 – 326103Sufficient for interaction with microtubulesBy similarityAdd
BLAST
Regioni226 – 614389Sufficient for microtubule severingBy similarityAdd
BLAST
Regioni268 – 32659Required for interaction with microtubules and microtubule severingBy similarityAdd
BLAST
Regioni308 – 3103Required for interaction with microtubules

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi4 – 118Nuclear localization signalUniRule annotation
Motifi57 – 659Nuclear export signalUniRule annotation
Motifi307 – 3104Nuclear localization signalUniRule annotation

Sequence similaritiesi

Belongs to the AAA ATPase family. Spastin subfamily.UniRule annotation
Contains 1 MIT domain.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0464.
GeneTreeiENSGT00570000078874.
HOGENOMiHOG000225146.
HOVERGENiHBG108502.
InParanoidiQ9QYY8.
KOiK13254.
OMAiSEMRNIK.
OrthoDBiEOG7GXPCR.
PhylomeDBiQ9QYY8.
TreeFamiTF105014.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_03021. Spastin.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR007330. MIT.
IPR027417. P-loop_NTPase.
IPR017179. Spastin.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF04212. MIT. 1 hit.
[Graphical view]
PIRSFiPIRSF037338. Spastin. 1 hit.
SMARTiSM00382. AAA. 1 hit.
SM00745. MIT. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9QYY8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSPAGRRKK KGSGGASPAP ARPPPPAAVP APAAGPAPAA GSPPKRNPSS
60 70 80 90 100
FSSPLVVGFA LLRLLACHLG LLFAWLCQRF SRALMAAKRS SGTAPAPASP
110 120 130 140 150
SPPEPGPGGE AESVRVFHKQ AFEYISIALR IDEEEKAGQK EQAVEWYKKG
160 170 180 190 200
IEELEKGIAV IVTGQGEQYE RARRLQAKMM TNLVMAKDRL QLLEKLQPVL
210 220 230 240 250
QFSKSQTDVY NESTNLTCRN GHLQSESGAV PKRKDPLTHA SNSLPRSKTV
260 270 280 290 300
LKSGSAGLSG HHRAPSCSGL SMVSGARPGP GPAATTHKGT PKPNRTNKPS
310 320 330 340 350
TPTTAVRKKK DLKNFRNVDS NLANLIMNEI VDNGTAVKFD DIAGQELAKQ
360 370 380 390 400
ALQEIVILPS LRPELFTGLR APARGLLLFG PPGNGKTMLA KAVAAESNAT
410 420 430 440 450
FFNISAASLT SKYVGEGEKL VRALFAVARE LQPSIIFIDE VDSLLCERRE
460 470 480 490 500
GEHDASRRLK TEFLIEFDGV QSAGDDRVLV MGATNRPQEL DEAVLRRFIK
510 520 530 540 550
RVYVSLPNEE TRLLLLKNLL CKQGSPLTQK ELAQLARMTD GYSGSDLTAL
560 570 580 590 600
AKDAALGPIR ELKPEQVKNM SASEMRNIRL SDFTESLKKI KRSVSPQTLE
610
AYIRWNKDFG DTTV
Length:614
Mass (Da):66,456
Last modified:March 24, 2009 - v3
Checksum:iC0D235031A7E4C8F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti104 – 1041E → A in BAC98092 (PubMed:14621295).Curated
Sequence conflicti104 – 1041E → A in AAH46286 (PubMed:15489334).Curated
Sequence conflicti137 – 1371Missing in AAH46286 (PubMed:15489334).Curated
Sequence conflicti137 – 1371Missing in BAB25259 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129282 mRNA. Translation: BAC98092.1.
BC046286 mRNA. Translation: AAH46286.1.
AK007793 mRNA. Translation: BAB25259.1.
AJ246002 mRNA. Translation: CAB60143.1.
CCDSiCCDS50181.1.
RefSeqiNP_001156342.1. NM_001162870.1.
NP_058658.2. NM_016962.2.
UniGeneiMm.19804.

Genome annotation databases

EnsembliENSMUST00000024869; ENSMUSP00000024869; ENSMUSG00000024068.
GeneIDi50850.
KEGGimmu:50850.
UCSCiuc008dnz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129282 mRNA. Translation: BAC98092.1.
BC046286 mRNA. Translation: AAH46286.1.
AK007793 mRNA. Translation: BAB25259.1.
AJ246002 mRNA. Translation: CAB60143.1.
CCDSiCCDS50181.1.
RefSeqiNP_001156342.1. NM_001162870.1.
NP_058658.2. NM_016962.2.
UniGeneiMm.19804.

3D structure databases

ProteinModelPortaliQ9QYY8.
SMRiQ9QYY8. Positions 110-194, 322-610.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ9QYY8.

Proteomic databases

MaxQBiQ9QYY8.
PaxDbiQ9QYY8.
PRIDEiQ9QYY8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000024869; ENSMUSP00000024869; ENSMUSG00000024068.
GeneIDi50850.
KEGGimmu:50850.
UCSCiuc008dnz.2. mouse.

Organism-specific databases

CTDi6683.
MGIiMGI:1858896. Spast.
RougeiSearch...

Phylogenomic databases

eggNOGiCOG0464.
GeneTreeiENSGT00570000078874.
HOGENOMiHOG000225146.
HOVERGENiHBG108502.
InParanoidiQ9QYY8.
KOiK13254.
OMAiSEMRNIK.
OrthoDBiEOG7GXPCR.
PhylomeDBiQ9QYY8.
TreeFamiTF105014.

Miscellaneous databases

NextBioi307827.
PROiQ9QYY8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QYY8.
CleanExiMM_SPAST.
GenevestigatoriQ9QYY8.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_03021. Spastin.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR007330. MIT.
IPR027417. P-loop_NTPase.
IPR017179. Spastin.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF04212. MIT. 1 hit.
[Graphical view]
PIRSFiPIRSF037338. Spastin. 1 hit.
SMARTiSM00382. AAA. 1 hit.
SM00745. MIT. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryonic tail.
  2. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N-3.
    Tissue: Mammary tumor.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 58-614.
    Strain: C57BL/6J.
    Tissue: Pancreas.
  4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 111-614, TISSUE SPECIFICITY.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  6. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  7. "A mutation of spastin is responsible for swellings and impairment of transport in a region of axon characterized by changes in microtubule composition."
    Tarrade A., Fassier C., Courageot S., Charvin D., Vitte J., Peris L., Thorel A., Mouisel E., Fonknechten N., Roblot N., Seilhean D., Dierich A., Hauw J.J., Melki J.
    Hum. Mol. Genet. 15:3544-3558(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  8. "The microtubule-severing proteins spastin and katanin participate differently in the formation of axonal branches."
    Yu W., Qiang L., Solowska J.M., Karabay A., Korulu S., Baas P.W.
    Mol. Biol. Cell 19:1485-1498(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. "Microtubule stabilizing effect of notch activation in primary cortical neurons."
    Ferrari-Toninelli G., Bonini S.A., Bettinsoli P., Uberti D., Memo M.
    Neuroscience 154:946-952(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  10. Cited for: FUNCTION.

Entry informationi

Entry nameiSPAST_MOUSE
AccessioniPrimary (citable) accession number: Q9QYY8
Secondary accession number(s): Q6ZPY6, Q80VE0, Q9CVK0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: March 24, 2009
Last modified: April 1, 2015
This is version 130 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.