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Q9QYY8

- SPAST_MOUSE

UniProt

Q9QYY8 - SPAST_MOUSE

Protein

Spastin

Gene

Spast

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 3 (24 Mar 2009)
      Previous versions | rss
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    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. ATP catabolic process Source: GOC
    2. axonogenesis Source: UniProtKB-HAMAP
    3. cytokinesis, completion of separation Source: UniProtKB
    4. ER to Golgi vesicle-mediated transport Source: UniProtKB
    5. microtubule bundle formation Source: UniProtKB
    6. microtubule severing Source: UniProtKB
    7. positive regulation of microtubule depolymerization Source: UniProtKB-HAMAP
    8. protein hexamerization Source: UniProtKB
    9. protein homooligomerization Source: UniProtKB

    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: 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

    GO - Cellular componenti

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

    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

    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...

    Transmembrane

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

    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

    MSSPAGRRKK KGSGGASPAP ARPPPPAAVP APAAGPAPAA GSPPKRNPSS    50
    FSSPLVVGFA LLRLLACHLG LLFAWLCQRF SRALMAAKRS SGTAPAPASP 100
    SPPEPGPGGE AESVRVFHKQ AFEYISIALR IDEEEKAGQK EQAVEWYKKG 150
    IEELEKGIAV IVTGQGEQYE RARRLQAKMM TNLVMAKDRL QLLEKLQPVL 200
    QFSKSQTDVY NESTNLTCRN GHLQSESGAV PKRKDPLTHA SNSLPRSKTV 250
    LKSGSAGLSG HHRAPSCSGL SMVSGARPGP GPAATTHKGT PKPNRTNKPS 300
    TPTTAVRKKK DLKNFRNVDS NLANLIMNEI VDNGTAVKFD DIAGQELAKQ 350
    ALQEIVILPS LRPELFTGLR APARGLLLFG PPGNGKTMLA KAVAAESNAT 400
    FFNISAASLT SKYVGEGEKL VRALFAVARE LQPSIIFIDE VDSLLCERRE 450
    GEHDASRRLK TEFLIEFDGV QSAGDDRVLV MGATNRPQEL DEAVLRRFIK 500
    RVYVSLPNEE TRLLLLKNLL CKQGSPLTQK ELAQLARMTD GYSGSDLTAL 550
    AKDAALGPIR ELKPEQVKNM SASEMRNIRL SDFTESLKKI KRSVSPQTLE 600
    AYIRWNKDFG DTTV 614
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK129282 mRNA. Translation: BAC98092.1 .
    BC046286 mRNA. Translation: AAH46286.1 .
    AK007793 mRNA. Translation: BAB25259.1 .
    AJ246002 mRNA. Translation: CAB60143.1 .
    CCDSi CCDS50181.1.
    RefSeqi NP_001156342.1. NM_001162870.1.
    NP_058658.2. NM_016962.2.
    UniGenei Mm.19804.

    3D structure databases

    ProteinModelPortali Q9QYY8.
    SMRi Q9QYY8. Positions 110-194, 322-610.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q9QYY8.

    Proteomic databases

    PaxDbi Q9QYY8.
    PRIDEi Q9QYY8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000024869 ; ENSMUSP00000024869 ; ENSMUSG00000024068 .
    GeneIDi 50850.
    KEGGi mmu:50850.
    UCSCi uc008dnz.2. mouse.

    Organism-specific databases

    CTDi 6683.
    MGIi MGI:1858896. Spast.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG0464.
    GeneTreei ENSGT00570000078874.
    HOGENOMi HOG000225146.
    HOVERGENi HBG108502.
    InParanoidi Q9QYY8.
    KOi K13254.
    OMAi SEMRNIK.
    OrthoDBi EOG7GXPCR.
    PhylomeDBi Q9QYY8.
    TreeFami TF105014.

    Miscellaneous databases

    NextBioi 307827.
    PROi Q9QYY8.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9QYY8.
    CleanExi MM_SPAST.
    Genevestigatori Q9QYY8.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    HAMAPi MF_03021. Spastin.
    InterProi IPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR003960. ATPase_AAA_CS.
    IPR007330. MIT.
    IPR027417. P-loop_NTPase.
    IPR017179. Spastin.
    [Graphical view ]
    Pfami PF00004. AAA. 1 hit.
    PF04212. MIT. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037338. Spastin. 1 hit.
    SMARTi SM00382. AAA. 1 hit.
    SM00745. MIT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    PROSITEi PS00674. AAA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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(2003) [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(2004) [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(2005) [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(2005) [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(2006) [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(2008) [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(2008) [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: October 1, 2014
    This is version 125 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