BAIT

BYSL

BYSTIN, RP5-973N23.2
bystin-like
GO Process (2)
GO Function (2)
GO Component (4)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Homo sapiens

Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Publication

The nucleoplasmic phase of pre-40S formation prior to nuclear export.

Cheng J, Lau B, Thoms M, Ameismeier M, Berninghausen O, Hurt E, Beckmann R

Biogenesis of the small ribosomal subunit in eukaryotes starts in the nucleolus with the formation of a 90S precursor and ends in the cytoplasm. Here, we elucidate the enigmatic structural transitions of assembly intermediates from human and yeast cells during the nucleoplasmic maturation phase. After dissociation of all 90S factors, the 40S body adopts a close-to-mature conformation, whereas the 3' ... [more]

Nucleic Acids Res Nov. 11, 2022; 50(20);11924-11937 [Pubmed: 36321656]

Throughput

  • Low Throughput

Additional Notes

  • cryoEM

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
BYSL RPS4X
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.

High-BioGRID
3348950
BYSL RPS4X
Co-fractionation
Co-fractionation

Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex.

High0.1206BioGRID
1271147

Curated By

  • BioGRID