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Protein

Filament protein FIN1

Gene

FIN1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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 - Molecular functioni

  • microtubule binding Source: SGD
  • structural constituent of cytoskeleton Source: SGD

GO - Biological processi

Enzyme and pathway databases

BioCyciYEAST:G3O-29729-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Filament protein FIN1
Alternative name(s):
Filaments in between nuclei protein 1
Gene namesi
Name:FIN1
Ordered Locus Names:YDR130C
ORF Names:YD9302.05C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR130C
SGDiS000002537 FIN1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000872571 – 291Filament protein FIN1Add BLAST291

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei54PhosphoserineCombined sources1
Modified residuei68PhosphothreonineCombined sources1
Modified residuei74PhosphoserineCombined sources1
Modified residuei88PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated by CDC28. Phosphorylation is required for BMH1 and BMH2 interaction. Dephosphorylation by GLC7 depends on the presence of BMH1 and BMH2.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ03898
PaxDbiQ03898
PRIDEiQ03898

PTM databases

iPTMnetiQ03898

Expressioni

Inductioni

Induced during G2-M transition.1 Publication

Interactioni

Subunit structurei

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 GLC7.1 Publication

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi32186, 195 interactors
DIPiDIP-1342N
IntActiQ03898, 8 interactors
MINTiQ03898
STRINGi4932.YDR130C

Structurei

3D structure databases

ProteinModelPortaliQ03898
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili254 – 284Sequence analysisAdd BLAST31

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi153 – 158Poly-Gln6

Domaini

The coiled coil domain is essential for dimerization.

Keywords - Domaini

Coiled coil

Phylogenomic databases

HOGENOMiHOG000074700
InParanoidiQ03898
OMAiTRTIFAN
OrthoDBiEOG092C3WXG

Family and domain databases

InterProiView protein in InterPro
IPR035260 Fin1
PfamiView protein in Pfam
PF17300 FIN1, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD127795 PD127795, 1 hit

Sequencei

Sequence statusi: Complete.

Q03898-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSNKSNRRSL RDIGNTIGRN NIPSDKDNVF VRLSMSPLRT TSQKEFLKPP
60 70 80 90 100
MRISPNKTDG MKHSIQVTPR RIMSPECLKG YVSKETQSLD RPQFKNSNKN
110 120 130 140 150
VKIQNSDHIT NIIFPTSPTK LTFSNENKIG GDGSLTRIRA RFKNGLMSPE
160 170 180 190 200
RIQQQQQQHI LPSDAKSNTD LCSNTELKDA PFENDLPRAK LKGKNLLVEL
210 220 230 240 250
KKEEEDVGNG IESLTKSNTK LNSMLANEGK IHKASFQKSV KFKLPDNIVT
260 270 280 290
EETVELKEIK DLLLQMLRRQ REIESRLSNI ELQLTEIPKH K
Length:291
Mass (Da):33,186
Last modified:November 1, 1996 - v1
Checksum:iFD4DB73A50F50172
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48179 Genomic DNA Translation: CAA88211.1
AY557684 Genomic DNA Translation: AAS56010.1
BK006938 Genomic DNA Translation: DAA11976.1
PIRiS51857
RefSeqiNP_010415.1, NM_001180438.1

Genome annotation databases

EnsemblFungiiYDR130C; YDR130C; YDR130C
GeneIDi851708
KEGGisce:YDR130C

Similar proteinsi

Entry informationi

Entry nameiFIN1_YEAST
AccessioniPrimary (citable) accession number: Q03898
Secondary accession number(s): D6VSB6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: November 1, 1996
Last modified: September 12, 2018
This is version 140 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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