BAIT

MIH1

putative tyrosine protein phosphatase MIH1, L000001111, YMR036C
Protein tyrosine phosphatase involved in cell cycle control; regulates the phosphorylation state of Cdc28p; homolog of S. pombe cdc25
GO Process (2)
GO Function (1)
GO Component (2)
Saccharomyces cerevisiae (S288c)
PREY

PTP1

tyrosine protein phosphatase PTP1, L000001525, YDL230W
Phosphotyrosine-specific protein phosphatase; dephosphorylates a broad range of substrates in vivo, including Fpr3p; localized to the cytoplasm and the mitochondria; proposed to be a negative regulator of filamentation
GO Process (3)
GO Function (1)
GO Component (2)

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)

Synthetic Lethality

A genetic interaction is inferred when mutations or deletions in separate genes, each of which alone causes a minimal phenotype, result in lethality when combined in the same cell under a given condition.

Publication

Redundant Regulation of Cdk1 Tyrosine Dephosphorylation in Saccharomyces cerevisiae.

Kennedy EK, Dysart M, Lianga N, Williams EC, Pilon S, Dore C, Deneault JS, Rudner AD

Cdk1 activity drives both mitotic entry and the metaphase-to-anaphase transition in all eukaryotes. The kinase Wee1, and the phosphatase Cdc25, regulate the mitotic activity of Cdk1 by the reversible phosphorylation of a conserved tyrosine residue. Mutation of cdc25 in Schizosaccharomyces pombe blocks Cdk1 dephosphorylation and causes cell cycle arrest. In contrast, deletion of MIH1, the cdc25 homologue in Saccharomyces cerevisiae, ... [more]

Genetics Dec. 29, 2015; 0(0); [Pubmed: 26715668]

Throughput

  • Low Throughput

Ontology Terms

  • phenotype: inviable (APO:0000112)

Additional Notes

  • genetic complex
  • mih1 ptp1 rts1 triple mutant

Curated By

  • BioGRID