BAIT

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
Kinome Project (Sc)
GO Process (24)
GO Function (5)
GO Component (8)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

NCL1

TRM4, YBL024W
S-adenosyl-L-methionine-dependent tRNA: m5C-methyltransferase; methylates cytosine to m5C at several positions in tRNAs and intron-containing pre-tRNAs; increases proportion of tRNALeu(CAA) with m5C at wobble position in response to hydrogen peroxide, causing selective translation of mRNA from genes enriched in TTG codon; loss of NCL1 confers hypersensitivity to oxidative stress; similar to Nop2p and human proliferation associated nucleolar protein p120
GO Process (3)
GO Function (2)
GO Component (1)

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

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
  • complex to CLN2

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
CDC28 NCL1
Dosage Lethality
Dosage Lethality

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

Low-BioGRID
2452001

Curated By

  • BioGRID