BAIT

HSL1

ELM2, NIK1, protein kinase HSL1, L000003129, L000002839, YKL101W
Nim1p-related protein kinase; regulates the morphogenesis and septin checkpoints; associates with the assembled septin filament; required along with Hsl7p for bud neck recruitment, phosphorylation, and degradation of Swe1p
Kinome Project (Sc)
Saccharomyces cerevisiae (S288c)
PREY

GIN4

ERC47, protein kinase GIN4, L000002876, YDR507C
Protein kinase involved in bud growth and assembly of the septin ring; proposed to have kinase-dependent and kinase-independent activities; undergoes autophosphorylation; similar to Hsl1p; GIN4 has a paralog, KCC4, that arose from the whole genome duplication
Kinome Project (Sc)
GO Process (5)
GO Function (1)
GO Component (1)

Gene Ontology Biological Process

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

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)

Additional Notes

  • HSL1/GIN4/KCC4/ELM1 quadruple mutants show synthetic lethality

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
HSL1 GIN4
Affinity Capture-MS
Affinity Capture-MS

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.

High1BioGRID
-
HSL1 GIN4
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.

High-BioGRID
485947
GIN4 HSL1
Phenotypic Enhancement
Phenotypic Enhancement

A genetic interaction is inferred when mutation or overexpression of one gene results in enhancement of any phenotype (other than lethality/growth defect) associated with mutation or over expression of another gene.

Low-BioGRID
2543919
GIN4 HSL1
Phenotypic Enhancement
Phenotypic Enhancement

A genetic interaction is inferred when mutation or overexpression of one gene results in enhancement of any phenotype (other than lethality/growth defect) associated with mutation or over expression of another gene.

Low-BioGRID
3537234
GIN4 HSL1
Phenotypic Enhancement
Phenotypic Enhancement

A genetic interaction is inferred when mutation or overexpression of one gene results in enhancement of any phenotype (other than lethality/growth defect) associated with mutation or over expression of another gene.

Low-BioGRID
156260
GIN4 HSL1
Phenotypic Suppression
Phenotypic Suppression

A genetic interaction is inferred when mutation or over expression of one gene results in suppression of any phenotype (other than lethality/growth defect) associated with mutation or over expression of another gene.

Low-BioGRID
1029480

Curated By

  • BioGRID