Q03898 · FIN1_YEAST

Function

function

Forms cell-cycle specific filaments between the spindle pole bodies of dividing yeast cells.

Miscellaneous

Strong overexpression results in the accumulation of filamentous structures resembling the neurofibrillary tangles found in cells of patients with Alzheimer disease.
Overexpression is lethal in haploids and causes very poor growth in diploids.

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 Componentastral microtubule
Cellular Componentcytoplasm
Cellular Componentintermediate filament
Cellular Componentkinetochore
Cellular Componentmitotic spindle
Cellular Componentnucleus
Cellular Componentprotein phosphatase type 1 complex
Cellular Componentspindle microtubule
Cellular Componentspindle pole
Cellular Componentspindle pole body
Molecular Functionmicrotubule binding
Molecular Functionstructural constituent of cytoskeleton
Biological Processdeactivation of mitotic spindle assembly checkpoint
Biological Processintermediate filament cytoskeleton organization
Biological Processmitotic sister chromatid segregation
Biological Processmitotic spindle organization
Biological Processprotein localization to kinetochore

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Filament protein FIN1
  • Alternative names
    • Filaments in between nuclei protein 1

Gene names

    • Name
      FIN1
    • ORF names
      YD9302.05C
    • Ordered locus names
      YDR130C

Organism names

Accessions

  • Primary accession
    Q03898
  • Secondary accessions
    • D6VSB6

Proteomes

Organism-specific databases

Subcellular Location

Nucleus
Cytoplasm
Note: Nuclear during early bud formation, located at the spindle poles during late mitosis, very low abundance in resting cells.

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000872571-291Filament protein FIN1
Modified residue54Phosphoserine
Modified residue68Phosphothreonine
Modified residue74Phosphoserine
Modified residue88Phosphoserine

Post-translational modification

Phosphorylated by CDC28. Phosphorylation is required for BMH1 and BMH2 interaction. Dephosphorylation by GLC7 depends on the presence of BMH1 and BMH2.

Keywords

Proteomic databases

PTM databases

Expression

Induction

Induced during G2-M transition.

Interaction

Subunit

Homooligomer; in vitro, FIN1 self-assembles into 10 nm diameter filaments. Interacts with the 14-3-3 proteins BMH1 and BMH2, and the protein phosphatase 1 complex catalytic subunit GLC7.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q03898CDC14 Q006842EBI-32941, EBI-4192
BINARY Q03898CLB2 P248692EBI-32941, EBI-4515
BINARY Q03898GLC7 P325983EBI-32941, EBI-13715

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for coiled coil.

TypeIDPosition(s)Description
Coiled coil254-284

Domain

The coiled coil domain is essential for dimerization.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    291
  • Mass (Da)
    33,186
  • Last updated
    1996-11-01 v1
  • Checksum
    FD4DB73A50F50172
MSNKSNRRSLRDIGNTIGRNNIPSDKDNVFVRLSMSPLRTTSQKEFLKPPMRISPNKTDGMKHSIQVTPRRIMSPECLKGYVSKETQSLDRPQFKNSNKNVKIQNSDHITNIIFPTSPTKLTFSNENKIGGDGSLTRIRARFKNGLMSPERIQQQQQQHILPSDAKSNTDLCSNTELKDAPFENDLPRAKLKGKNLLVELKKEEEDVGNGIESLTKSNTKLNSMLANEGKIHKASFQKSVKFKLPDNIVTEETVELKEIKDLLLQMLRRQREIESRLSNIELQLTEIPKHK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Z48179
EMBL· GenBank· DDBJ
CAA88211.1
EMBL· GenBank· DDBJ
Genomic DNA
AY557684
EMBL· GenBank· DDBJ
AAS56010.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006938
EMBL· GenBank· DDBJ
DAA11976.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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