BAIT

DBF2

serine/threonine-protein kinase DBF2, L000000487, YGR092W
Ser/Thr kinase involved in transcription and stress response; functions as part of a network of genes in exit from mitosis; localization is cell cycle regulated; activated by Cdc15p during the exit from mitosis; also plays a role in regulating the stability of SWI5 and CLB2 mRNAs; phosphorylates Chs2p to regulate primary septum formation and Hof1p to regulate cytokinesis; DBF2 has a paralog, DBF20, that arose from the whole genome duplication
Kinome Project (Sc)
Saccharomyces cerevisiae (S288c)
PREY

PRE10

proteasome core particle subunit alpha 7, L000003146, YOR362C
Alpha 7 subunit of the 20S proteasome; protein abundance increases in response to DNA replication stress
UPS Project
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

Global analysis of protein phosphorylation in yeast.

Ptacek J, Devgan G, Michaud G, Zhu H, Zhu X, Fasolo J, Guo H, Jona G, Breitkreutz A, Sopko R, McCartney RR, Schmidt MC, Rachidi N, Lee SJ, Mah AS, Meng L, Stark MJ, Stern DF, De Virgilio C, Tyers M, Andrews B, Gerstein M, Schweitzer B, Predki PF, Snyder M

Protein phosphorylation is estimated to affect 30% of the proteome and is a major regulatory mechanism that controls many basic cellular processes. Until recently, our biochemical understanding of protein phosphorylation on a global scale has been extremely limited; only one half of the yeast kinases have known in vivo substrates and the phosphorylating kinase is known for less than 160 ... [more]

Nature Dec. 01, 2005; 438(7068);679-84 [Pubmed: 16319894]

Throughput

  • High Throughput

Additional Notes

  • 32P incorporation on protein chip

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
DBF2 PRE10
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
204968
PRE10 DBF2
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-0.1416BioGRID
1954414
DBF2 PRE10
Positive Genetic
Positive Genetic

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

High0.1928BioGRID
1896126

Curated By

  • BioGRID