BAIT

ERF2

YLR246W
Subunit of a palmitoyltransferase; this complex adds a palmitoyl lipid moiety to heterolipidated substrates such as Ras1p and Ras2p through a thioester linkage; mutants partially mislocalize Ras2p to the vacuole; palmitoyltransferase is composed of Erf2p and Shr5p
GO Process (2)
GO Function (1)
GO Component (3)
Saccharomyces cerevisiae (S288c)
PREY

RAS2

CTN5, CYR3, GLC5, TSL7, Ras family GTPase RAS2, L000001583, YNL098C
GTP-binding protein; regulates nitrogen starvation response, sporulation, and filamentous growth; farnesylation and palmitoylation required for activity and localization to plasma membrane; homolog of mammalian Ras proto-oncogenes; RAS2 has a paralog, RAS1, that arose from the whole genome duplication
Saccharomyces cerevisiae (S288c)

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.

Publication

Regulation of RAS palmitoyltransferases by accessory proteins and palmitoylation.

Yang A, Liu S, Zhang Y, Chen J, Fan Y, Wang F, Zou Y, Feng S, Wu J, Hu Q

Palmitoylation of cysteine residues at the C-terminal hypervariable regions in human HRAS and NRAS, which is necessary for RAS signaling, is catalyzed by the acyltransferase DHHC9 in complex with its accessory protein GCP16. The molecular basis for the acyltransferase activity and the regulation of DHHC9 by GCP16 is not clear. Here we report the cryo-electron microscopy structures of the human ... [more]

Nat Struct Mol Biol Mar. 01, 2024; 31(3);436-446 [Pubmed: 38182928]

Throughput

  • Low Throughput

Additional Notes

  • Palmitoylation

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
ERF2 RAS2
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
697187
RAS2 ERF2
Co-localization
Co-localization

Interaction inferred from two proteins that co-localize in the cell by indirect immunofluorescence only when in addition, if one gene is deleted, the other protein becomes mis-localized. Also includes co-dependent association of proteins with promoter DNA in chromatin immunoprecipitation experiments.

Low-BioGRID
-
RAS2 ERF2
Synthetic Lethality
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.

Low-BioGRID
260337
RAS2 ERF2
Synthetic Rescue
Synthetic Rescue

A genetic interaction is inferred when mutations or deletions of one gene rescues the lethality or growth defect of a strain mutated or deleted for another gene.

Low-BioGRID
159410

Curated By

  • BioGRID