BAIT

ELM1

LDB9, serine/threonine protein kinase ELM1, L000000548, YKL048C
Serine/threonine protein kinase that regulates cellular morphogenesis; septin behavior, and cytokinesis; required for the regulation of other kinases, such as Kin4p; forms part of the bud neck ring
Saccharomyces cerevisiae (S288c)
PREY

CDC28

CDK1, HSL5, SRM5, cyclin-dependent serine/threonine-protein kinase CDC28, L000000267, YBR160W
Cyclin-dependent kinase (CDK) catalytic subunit; master regulator of mitotic and meiotic cell cycles; alternately associates with G1 (CLNs), S and G2/M (CLBs) phase cyclins, which provide substrate specificity; regulates cell cycle and basal transcription, chromosome duplication and segregation, lipid biosynthesis, membrane trafficking, polarized growth, and morphogenesis; abundance increases in DNA replication stress; transcript induction in osmostress involves antisense RNA
GO Process (24)
GO Function (5)
GO Component (8)
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

Regulation of cytokinesis by the Elm1 protein kinase in Saccharomyces cerevisiae.

Bouquin N, Barral Y, Courbeyrette R, Blondel M, Snyder M, Mann C

A Saccharomyces cerevisiae mutant unable to grow in a cdc28-1N background was isolated and shown to be affected in the ELM1 gene. Elm1 is a protein kinase, thought to be a negative regulator of pseudo-hyphal growth. We show that Cdc11, one of the septins, is delocalised in the mutant, indicating that septin localisation is partly controlled by Elm1. Moreover, we ... [more]

J. Cell. Sci. Apr. 01, 2000; 113(0);1435-45 [Pubmed: 10725226]

Throughput

  • Low Throughput

Ontology Terms

  • phenotype: inviable (APO:0000112)

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
CDC28 ELM1
Biochemical Activity
Biochemical Activity

An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.

High-BioGRID
152085
ELM1 CDC28
Dosage Growth Defect
Dosage Growth Defect

A genetic interaction is inferred when over expression or increased dosage of one gene causes a growth defect in a strain that is mutated or deleted for another gene.

High-0.392BioGRID
908904
CDC28 ELM1
Negative Genetic
Negative Genetic

Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a more severe fitness defect or lethality under a given condition. This term is reserved for high or low throughput studies with scores.

High-0.1697BioGRID
358652
CDC28 ELM1
Negative Genetic
Negative Genetic

Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a more severe fitness defect or lethality under a given condition. This term is reserved for high or low throughput studies with scores.

High-0.3737BioGRID
1961823
ELM1 CDC28
Negative Genetic
Negative Genetic

Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a more severe fitness defect or lethality under a given condition. This term is reserved for high or low throughput studies with scores.

High-0.1826BioGRID
2053493
CDC28 ELM1
Negative Genetic
Negative Genetic

Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a more severe fitness defect or lethality under a given condition. This term is reserved for high or low throughput studies with scores.

High-0.17BioGRID
911132
CDC28 ELM1
PCA
PCA

A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay.

Low-BioGRID
662192

Curated By

  • BioGRID