O94488 · MBO1_SCHPO

Function

function

Spindle pole body (SPB) component that acts as the gamma-tubulin complex-binding protein of the SPB outer plaque (PubMed:15120067, PubMed:15659644, PubMed:19001497).
Promotes nucleation of all cytoplasmic microtubules by recruiting the gamma-tubulin complex to the spindle pole body (SPB), to the interphase microtubule organizing center (iMTOC), and to the equatorial MTOC (eMTOC) during anaphase (PubMed:15004232, PubMed:15120067, PubMed:15659644, PubMed:19001497).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentequatorial microtubule organizing center
Cellular Componenthalf bridge of mitotic spindle pole body
Cellular Componentinterphase microtubule organizing center
Cellular Componentmicrotubule
Cellular Componentmicrotubule cytoskeleton
Cellular Componentmicrotubule organizing center
Cellular Componentmitotic actomyosin contractile ring, proximal layer
Cellular Componentmitotic spindle pole body
Cellular Componentouter plaque of mitotic spindle pole body
Cellular Componentstatic microtubule bundle
Molecular Functioncalmodulin binding
Biological Processastral microtubule nucleation
Biological Processcentromere clustering at the mitotic interphase nuclear envelope
Biological Processdynein-driven meiotic oscillatory nuclear movement
Biological Processestablishment of mitotic spindle orientation
Biological Processkaryogamy involved in conjugation with cellular fusion
Biological Processmicrotubule nucleation by interphase microtubule organizing center
Biological Processnuclear migration by microtubule mediated pushing forces
Biological Processspindle pole body-led chromosome movement during mitotic interphase

Names & Taxonomy

Protein names

  • Recommended name
    Gamma tubulin complex adapter mto1
  • Alternative names
    • Microtubule organizer protein 1
    • Morphology defective protein 20

Gene names

    • Name
      mto1
    • Synonyms
      mbo1
      , mod20
    • ORF names
      SPCC417.07c

Organism names

Accessions

  • Primary accession
    O94488

Proteomes

Organism-specific databases

Phenotypes & Variants

Disruption phenotype

Abolishes cytoplasmic microtubule (MT) nucleation from SPB and non-SPB sites (PubMed:15120067, PubMed:19001497).
Leads to MTs escaping from the nucleus to form fewer and thicker cytoplasmic MT bundles that curve around the cell tip (PubMed:15659644, PubMed:19001497).
Curved cell shape (PubMed:15659644, PubMed:19001497).
Leads to unclustering of centromeres at the nuclear periphery; normally, the centromeres cluster at the SPB during interphase (PubMed:17881496).

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis259-267Abolishes cytoplasmic microtubule (MT) nucleation and leads to MTs escaping from the nucleus to form abnormal MT bundles that curve around the cell tip and a curved cell shape. Abolishes interactions with gamma-tubulin complex components.
Mutagenesis267-275Abolishes cytoplasmic microtubule (MT) nucleation and leads to MTs escaping from the nucleus to form abnormal MT bundles that curve around the cell tip and a curved cell shape. Abolishes interactions with gamma-tubulin complex components.
Mutagenesis288-296Mildly curved cell shape. Phenotypically mostly normal.
Mutagenesis523-537Abolishes interaction with mto2 and with components of the gamma-tubulin complex. Abolishes cytoplasmic microtubule nucleation from non-SPB (spindle pole body) sites, but not from the SPB. Morphologically, cells are curved.

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00003561691-1115Gamma tubulin complex adapter mto1
Modified residue94Phosphoserine
Modified residue1005Phosphoserine
Modified residue1009Phosphoserine

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Interacts with mto2; the interaction is direct and required for efficient binding to the gamma-tubulin complex (PubMed:15659644, PubMed:15800064, PubMed:19001497).
Interacts with gamma tubulin complex subunits alp4, alp6 and gtb1 (PubMed:19001497).
Interacts with mcp6 (PubMed:15120067).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, coiled coil.

Type
IDPosition(s)Description
Region25-180Disordered
Compositional bias30-74Basic and acidic residues
Compositional bias75-178Polar residues
Coiled coil445-915
Region523-537Required for interaction with mto2
Region1001-1037Disordered
Compositional bias1067-1101Basic and acidic residues
Region1067-1115Disordered
Coiled coil1072-1102

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,115
  • Mass (Da)
    128,469
  • Last updated
    1999-05-01 v1
  • Checksum
    8CA5503EC141E3E0
MEENSSELDSNNFNVLVDNLAGLSLTDEEVRRILSPRKEGSRQLPSSTSKDEDSEEASHKYDFEIDRDSLKSDSGSPRLHQNATAPTSSTPLQSPDESVNKLNSEDEEGNSSVAPFFLDTTNFDRLNDNITTDDEQLSPVLTANQGFQSQEQYEEDSYNNYDYTSDPSSPNYISSSLDQLPHLDDEDDLQLTPIKEERNYLHSQDAPTTNALSKKISDILIPASAMKDLKDRKNALAKEFEESQPGSSLTLKEQANVIDNLRKEVFGLKLKCYFLYDQLNKFHDQEVQDIMKQNIDLKTLTMELQRAVAGYEKKISGLESRIKPDQSFNLSTPSPAPSNLITLQSRYSQALSELETTKRAFAALRKEKSKKTNYSVGAYNEDRNVLSNMLDNERREKEALLQELESLRVQLSKKVPMPAKNTDERVIETLQRSNELLRMDISMQNEALLLRKQENDRLVKQVEELTVALNSGKMNAIVEAESSKNELWDSMMVSRMKTQEQSIELTRLYKQLQDIEEDYENKLMRMEQQWREDVDQLQEYVEEITQELQDTKEVLSKSSKESDDYEEVVGKLRTEAEREIEKFEKTIRENEESISLFKEEVEKLTDEITQLSERYNDKCHEFDELQKRLQTLEEENNKAKEDSTSKTSNLLEQLKMTEAEVDSLRKENEENKQVIALKESELVKSNDNKLLLNEQIESLNDQLSQLKTEMESVTTSKESLADYLSNLKERHNDELDSLNKKLREFEGILSSNSSLKSEIEERNNQYVTLRENFDSLQNAIMETFDKQVTHCSVNHLVQQIRKLKDENKKDQSGTDKLMKKIYHCEQSLKEKTNSLETLVSEKKELKNLLDAERRSKKAIQLELENLSSQAFRRNLSGSSSPSERSQSRELKLLQASEKRLKEQVEERNSLIKNIVTRFTQLNTGSKPVNTNVEALTTISSMNQAVNMNFRELDKSIQEFKRKCQSMEREFKTELRKLDGVLEARSKRLSQLEERVKLLGAGSTSSIPNSPRASKRVSLDSEDKKLVPASPDKSAVQRGITALKRDAEGMSHIWQLRLREMEFQLKAEQEGRKRDKLGARERLQDLIRQNRSLSRQIKTDKESNSRSPSISSQEHK

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias30-74Basic and acidic residues
Compositional bias75-178Polar residues
Compositional bias1067-1101Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CU329672
EMBL· GenBank· DDBJ
CAA22653.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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