Putative protein of unknown function containing WW and FF domains; overexpression causes accumulation of cells in G1 phase
GO Process (0)
GO Function (0)
GO Component (1)

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)


ribosomal 60S subunit protein L30, L30e, rp73, YL38, L32, L30, L000001726, YGL030W
Ribosomal 60S subunit protein L30; involved in pre-rRNA processing in the nucleolus; autoregulates splicing of its transcript; homologous to mammalian ribosomal protein L30, no bacterial homolog
Saccharomyces cerevisiae (S288c)


An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments.


Comparative analysis of Saccharomyces cerevisiae WW domains and their interacting proteins.

Hesselberth JR, Miller JP, Golob A, Stajich JE, Michaud GA, Fields S

BACKGROUND: The WW domain is found in a large number of eukaryotic proteins implicated in a variety of cellular processes. WW domains bind proline-rich protein and peptide ligands, but the protein interaction partners of many WW domain-containing proteins in Saccharomyces cerevisiae are largely unknown. RESULTS: We used protein microarray technology to generate a protein interaction map for 12 of the ... [more]

Genome Biol. Apr. 12, 2006; 7(4);R30 [Pubmed: 16606443]


  • High Throughput

Additional Notes

  • A protein microarray was probed with the WW domain from URN1 (YPR152C).
  • High Throughput: Each WW-domain was used as a probe for two separate protein microarrays. Only those in which four independent interactions were osbserved were considered high-confidence (i.e. significant signals found for proteins printed in duplicate on two separate microarrays).

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
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.


Curated By

  • BioGRID