FIN1/YDR130C Summary 
FIN1 BASIC INFORMATION
| Standard Name | FIN1 1 |
|---|---|
| Systematic Name | YDR130C |
| Feature Type | ORF, Verified |
| Description | Spindle pole body-related intermediate filament protein, forms cell cycle-specific filaments between spindle pole bodies in mother and daughter cells, able to self-assemble, expression induced during S/G2, localization cell-cycle dependent (1, 2, 3 and see Summary Paragraph) 
|
| Name Description | Filaments In between Nuclei 1 |
| GO Annotations | All FIN1 GO evidence and references |
|---|---|
| View Computational GO annotations for FIN1 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated |
| Mutant Phenotype | All FIN1 Phenotype details and references |
|---|---|
| Classical genetics | |
| null | |
| overexpression | |
| Large-scale survey | |
| null |
| Interactions | FIN1 All interactions details and references |
|---|---|
| 18 total interaction(s) for 8 unique genes/features. | |
| Physical Interactions |
|
| Genetic Interactions |
|
| External Links | All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB |
|---|
| Primary SGDID | S000002537 |
|---|
FIN1 RESOURCES
| SGD ORF map | GBrowse |
|---|---|
|
Click on histogram for expression summary
Expression Summary
ADDITIONAL INFORMATION for FIN1
SUMMARY PARAGRAPH for FIN1
Fin1p is a spindle pole body-related intermediate filament protein that forms cell cycle-specific filaments between spindle pole bodies in mother and daughter cells, and is able to self-assemble in vitro (1, 3).
FIN1 expression is induced during the S/G2 phase of the cell cycle (2), and Fin1p is a Clb5p-Cdc28p specific substrate that is fully phosphorylated immediately after its synthesis in early S phase. The protein is then dephosphorylated after degradation of Clb5p during mitosis (4). This Fin1p dephosphorylation is dependent on Bmh1p and Bmh2p, as the protein cannot be dephosphorylated in a bmh1 bmh2 double null mutant (2). Fin1p has higher affinity for Bmh2p than for Bmh1p (3), and Bmh2p only interacts with phosphorylated forms of Fin1p (2). Phosphorylated Fin1p also interacts with the Glc7p catalytic subunit of the protein phosphatase type 1 complex, suggesting that Glc7p and Bmh1p/Bmh2p are involved in regulating the phosphorylation state of Fin1p (2).
In resting cells Fin1p is undetectable, in small-budded cells Fin1p is localized in the nucleus, and during late mitosis Fin1p localizes to the spindle pole bodies (1). fin1 null mutants are viable on both minimal and rich growth media. Overexpression of FIN1 in haploid cells is lethal, and in diploid cells it results in very poor growth, altered cell morphology, and an accumulation of filamentous structures that resemble the neurofibrillary tangles found in cells of patients with Alzheimer's disease (1).
Last updated: 2005-10-07
REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for FIN1]
| 1) | van Hemert MJ, et al. (2002) The Saccharomyces cerevisiae Fin1 protein forms cell cycle-specific filaments between spindle pole bodies. Proc Natl Acad Sci U S A 99(8):5390-3 |
| 2) | Mayordomo I and Sanz P (2002) The Saccharomyces cerevisiae 14-3-3 protein Bmh2 is required for regulation of the phosphorylation status of Fin1, a novel intermediate filament protein. Biochem J 365(Pt 1):51-6 |
| 3) | van Hemert MJ, et al. (2003) Self-association of the spindle pole body-related intermediate filament protein Fin1p and its phosphorylation-dependent interaction with 14-3-3 proteins in yeast. J Biol Chem 278(17):15049-55 |
| 4) | Loog M and Morgan DO (2005) Cyclin specificity in the phosphorylation of cyclin-dependent kinase substrates. Nature 434(7029):104-8 |
