BAIT

MPS1

PAC8, RPK1, serine/threonine/tyrosine protein kinase MPS1, L000001698, YDL028C
Dual-specificity kinase; autophosphorylation required for function; required for spindle pole body (SPB) duplication and spindle checkpoint function; contributes to bi-orientation by promoting formation of force-generating kinetochore-microtubule attachments in meiosis I; substrates include SPB proteins Spc42p, Spc110p, and Spc98p, mitotic exit network protein Mob1p, kinetochore protein Cnn1p, and checkpoint protein Mad1p; substrate of APCC(Cdh1); similar to human Mps1p
Kinome Project (Sc)
Saccharomyces cerevisiae (S288c)
PREY

SPC110

NUF1, XCM1, L000001285, YDR356W
Inner plaque spindle pole body (SPB) component; ortholog of human kendrin; involved in connecting nuclear microtubules to SPB; interacts with Tub4p-complex and calmodulin; phosphorylated by Mps1p in cell cycle-dependent manner
GO Process (2)
GO Function (1)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)

Biochemical Activity (Phosphorylation)

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.

Publication

Yeast Mps1p phosphorylates the spindle pole component Spc110p in the N-terminal domain.

Friedman DB, Kern JW, Huneycutt BJ, Vinh DB, Crawford DK, Steiner E, Scheiltz D, Yates J, Resing KA, Ahn NG, Winey M, Davis TN

The yeast spindle pole body (SPB) component Spc110p (Nuf1p) undergoes specific serine/threonine phosphorylation as the mitotic spindle apparatus forms, and this phosphorylation persists until cells enter anaphase. We demonstrate that the dual-specificity kinase Mps1p is essential for the mitosis-specific phosphorylation of Spc110p in vivo and that Mps1p phosphorylates Spc110p in vitro. Phosphopeptides generated by proteolytic cleavage were identified and sequenced ... [more]

J. Biol. Chem. May. 25, 2001; 276(21);17958-67 [Pubmed: 11278681]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
MPS1 SPC110
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
-
MPS1 SPC110
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.

Low-BioGRID
947945
MPS1 SPC110
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-0.1408BioGRID
1922973

Curated By

  • BioGRID